PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
9741955-17	1998	The data are consistent with two distinct pathways of metabolism for BOX, (1) reduction to an imine, hydrolysis and subsequent conversion of butyraldehyde to 14CO2 and (2) CYP3A-catalysed dehydration of BOX to butyronitrile followed by CYP2E1-catalysed release of cyanide.	Cyanides	264-271	cytochrome P450, family 3, subfamily a, polypeptide 62	Rattus norvegicus	172-177
9724695-0	1998	Cyanide restores N gene-mediated resistance to tobacco mosaic virus in transgenic tobacco expressing salicylic acid hydroxylase Salicylhydroxamic acid (SHAM), an inhibitor of alternative oxidase (AOX), blocks salicylic acid-induced resistance to tobacco mosaic virus (TMV) but does not inhibit pathogenesis-related PR-1 protein synthesis or resistance to fungal and bacterial pathogens.	Cyanides	0-7	acyl-CoA oxidase 1	Homo sapiens	197-200
9705279-6	1998	Transient expression studies in Chinese hamster ovary cells with wild-type and mutated recombinant N-methyl-D-aspartate subunits (NR) demonstrated that cyanide selectively potentiated NR1/NR2A receptors, presumably via the chemical reduction of NR2A.	Cyanides	152-159	glutamate ionotropic receptor NMDA type subunit 1	Rattus norvegicus	184-187
9705279-8	1998	Some of the effects of cyanide on NR1/NR2B receptors may be mediated by the formation of a thiocyanate adduct with a cysteine residue located in NR1.	Cyanides	23-30	glutamate ionotropic receptor NMDA type subunit 1	Rattus norvegicus	34-37
9705279-8	1998	Some of the effects of cyanide on NR1/NR2B receptors may be mediated by the formation of a thiocyanate adduct with a cysteine residue located in NR1.	Cyanides	23-30	glutamate ionotropic receptor NMDA type subunit 2B	Rattus norvegicus	38-42
9705279-8	1998	Some of the effects of cyanide on NR1/NR2B receptors may be mediated by the formation of a thiocyanate adduct with a cysteine residue located in NR1.	Cyanides	23-30	glutamate ionotropic receptor NMDA type subunit 1	Rattus norvegicus	145-148
9761325-3	1998	Once epileptogenicity was established in these animals, activity of cyanide-sensitive Cu,Zn-SOD was maintained at significantly lower levels than in control mice.	Cyanides	68-75	superoxide dismutase 1, soluble	Mus musculus	86-95
9761325-4	1998	However, cyanide-insensitive Mn-SOD activity was not different from non-epileptic controls.	Cyanides	9-16	superoxide dismutase 2, mitochondrial	Mus musculus	29-35
9698817-4	1998	This review is focused on the oxidase side of the respiratory chain that presents a cyanide-resistant energy-dissipating alternative oxidase (AOX) besides the cytochrome pathway.	Cyanides	84-91	acyl-CoA oxidase 1	Homo sapiens	121-140
9698817-4	1998	This review is focused on the oxidase side of the respiratory chain that presents a cyanide-resistant energy-dissipating alternative oxidase (AOX) besides the cytochrome pathway.	Cyanides	84-91	acyl-CoA oxidase 1	Homo sapiens	142-145
9630731-3	1998	The average value of the change of heat capacity (DeltaCpd) of Lba.CN is between such values for apoMb and Mb.CN suggesting for some stabilisation role of the cyanide ion (CN-) on the protein molecule.	Cyanides	159-166	leghemoglobin A	Glycine max	63-66
9536016-0	1998	Cyanide-induced generation of oxidative species: involvement of nitric oxide synthase and cyclooxygenase-2.	Cyanides	0-7	prostaglandin-endoperoxide synthase 2	Homo sapiens	90-106
9536016-13	1998	These findings show that activation of phospholipase A2 and subsequent metabolism of arachidonic acid by the COX-2 and LOX pathways and NOS contribute to cyanide-induced ROS production.	Cyanides	154-161	phospholipase A2 group IB	Homo sapiens	39-55
9536016-13	1998	These findings show that activation of phospholipase A2 and subsequent metabolism of arachidonic acid by the COX-2 and LOX pathways and NOS contribute to cyanide-induced ROS production.	Cyanides	154-161	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	109-114
9514863-1	1998	We tested the effect of the GTS1 gene of the yeast Saccharomyces cerevisiae on the cyanide-induced ultradian oscillation of the glycolytic metabolite NADH in cell suspension of strains with different copy numbers of the gene, that is, the wild-type, GTS1-disrupted and GTS1-overexpressing strains.	Cyanides	83-90	Gts1p	Saccharomyces cerevisiae S288C	28-32
9639344-5	1998	Washing out cyanide during the development of the rigor contracture led to a rapid relaxation of the contracture, a fall in cytosolic Ca2+ and a rapid, partial reversal of the cytosolic acidosis.	Cyanides	12-19	carbonic anhydrase 2	Rattus norvegicus	134-137
11670334-3	1998	The cyanide (HCN/CN(-)) exchange kinetics on the trans-dioxotetracyanometalate complexes and protonated/substituted ([MO(X)(CN)(4)](n)()(-)) forms thereof were studied in aqueous medium.	Cyanides	4-11	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	13-16
9514863-1	1998	We tested the effect of the GTS1 gene of the yeast Saccharomyces cerevisiae on the cyanide-induced ultradian oscillation of the glycolytic metabolite NADH in cell suspension of strains with different copy numbers of the gene, that is, the wild-type, GTS1-disrupted and GTS1-overexpressing strains.	Cyanides	83-90	Gts1p	Saccharomyces cerevisiae S288C	250-254
9401734-2	1997	MetHb was determined as the difference in absorption caused by cyanide in the absence of potassium ferricyanide divided by the difference in absorption caused by cyanide in the presence of the ferricyanide.	Cyanides	63-70	hemoglobin subunit gamma 2	Homo sapiens	0-5
9514863-1	1998	We tested the effect of the GTS1 gene of the yeast Saccharomyces cerevisiae on the cyanide-induced ultradian oscillation of the glycolytic metabolite NADH in cell suspension of strains with different copy numbers of the gene, that is, the wild-type, GTS1-disrupted and GTS1-overexpressing strains.	Cyanides	83-90	Gts1p	Saccharomyces cerevisiae S288C	250-254
9609319-3	1998	The increased lipid peroxidation induced by cyanide was inhibited by piperonyl butoxide (1 mM), an inhibitor of mixed function oxidase, but not by allopurinol (0.1 mM), an inhibitor of xanthine oxidase.	Cyanides	44-51	xanthine dehydrogenase	Mus musculus	185-201
9460794-10	1998	TGF-beta maintains survival of chick telencephalic neurons made hypoxic by treatment with cyanide and decreases the area of infarction when administered in animal models of cerebral ischemia.	Cyanides	90-97	transforming growth factor alpha	Gallus gallus	0-8
9587916-3	1998	Using D-[2,3-3H]aspartic acid ([3H]D-Asp) as a tracer, it was found that corticosterone (CORT, the physiological GC in rat) enhanced the overflow of extracellular [3H]D-Asp in astrocyte cultures and, to a lesser extent, in neuron-enriched cultures during cyanide-induced ischemia.	Cyanides	255-262	cortistatin	Rattus norvegicus	89-93
9587916-4	1998	Analysis of [3H]D-Asp uptake kinetics indicates that CORT reduced the maximum uptake rate in cultured astrocyte, but not in neurons, after cyanide exposure.	Cyanides	139-146	cortistatin	Rattus norvegicus	53-57
9587916-5	1998	It is concluded that, during cyanide-induced ischemia, CORT might mainly the ability of astrocytes to clear excitatory amino acids from the synapse, thus exacerbating the damaging cascade of these amino acids.	Cyanides	29-36	cortistatin	Rattus norvegicus	55-59
9401734-2	1997	MetHb was determined as the difference in absorption caused by cyanide in the absence of potassium ferricyanide divided by the difference in absorption caused by cyanide in the presence of the ferricyanide.	Cyanides	104-111	hemoglobin subunit gamma 2	Homo sapiens	0-5
9399123-0	1997	Multicomponent spectroscopic assay for hemoglobin and ferrihemoglobin species in methemoglobin treatment of cyanide poisoning.	Cyanides	108-115	hemoglobin subunit gamma 2	Homo sapiens	81-94
9356097-3	1997	We developed a new spectrophotometric assay to measure cyanide by extraction into a sodium hydroxide trap, followed by the addition of exogenous methemoglobin as a colormetric indicator.	Cyanides	55-62	hemoglobin subunit gamma 2	Homo sapiens	145-158
9356097-13	1997	We developed a new, rapid blood test for cyanide using methemoglobin as a colormetric indicator.	Cyanides	41-48	hemoglobin subunit gamma 2	Homo sapiens	55-68
11671969-5	1997	Isocyanides were also detected as intermediates in the P(4) phototransposition of a variety of other pyrazoles confirming the generality of this pathway in pyrazole photochemistry.	Cyanides	0-11	solute carrier family 10 member 4	Homo sapiens	55-59
9312549-4	1997	Molecular oxygen is required for enzymatic activity, and cyanide, divalent copper, as well as antibodies raised against cytochrome b5 are inhibitory, which suggests that this enzyme should be named dihydroceramide desaturase based on these similarities with the mechanism of delta9-desaturase (stearoyl-CoA desaturase).	Cyanides	57-64	stearoyl-CoA desaturase	Rattus norvegicus	294-317
9285046-2	1997	These methemoglobin-containing red cell granules were very effective for detecting and absorbing cyanide in water.	Cyanides	97-104	hemoglobin subunit gamma 2	Homo sapiens	6-19
9285046-4	1997	An instant detector for cyanide was also devised by applying and gelling methemoglobin-containing red cells onto a filter paper.	Cyanides	24-31	hemoglobin subunit gamma 2	Homo sapiens	73-86
9251819-5	1997	The distal Tyr29(B10) in the triple mutant provides a strong hydrogen bond to the bound cyanide comparable to that provided by His64(E7) in wild-type myoglobin.	Cyanides	88-95	myoglobin	Physeter catodon	150-159
9381482-4	1997	Peroxide generation by cyanide is decreased to about 50% by phospholipase A2 inhibitors indicating involvement of arachidonic acid in the oxidative process.	Cyanides	23-30	phospholipase A2 group IB	Rattus norvegicus	60-76
9369328-0	1997	Hydrogen cyanide generation by mu-opiate receptor activation: possible neuromodulatory role of endogenous cyanide.	Cyanides	9-16	opioid related nociceptin receptor 1	Rattus norvegicus	31-49
9369328-9	1997	These data show that cyanide generation is increased in neuronal tissue by a mu-opiate receptor agonist and it is proposed that endogenous cyanide may modulate the NMDA receptor response.	Cyanides	21-28	opioid related nociceptin receptor 1	Rattus norvegicus	77-95
9294867-3	1997	The structure of the cyanide adduct of the Met80Ala mutant of the yeast iso-1-cytochrome c has been used for successfully testing the calculations.	Cyanides	21-28	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	72-77
9207193-5	1997	The behaviour of this protoheme-enzyme is typical of the class of prokaryotic catalase-peroxidases, which is sensitive to cyanide (Ki = 27.2 microM) and insensitive to the eukaryotic catalase inhibitor 3-amino-1,2,4-triazole.	Cyanides	122-129	pfam00199	Synechococcus elongatus PCC 7942	78-86
9167939-7	1997	The sensitivity to catalase inhibitors, such as aminotriazole, azide, or cyanide varies among the isoforms.	Cyanides	73-80	catalase	Mus musculus	19-27
9202197-7	1997	Evidence suggesting this was that both diimine accumulation and the ensuing cytotoxicity were markedly increased by inactivating hepatocyte DT diaphorase but were prevented by a subtoxic concentration of the mitochondrial respiratory inhibitor cyanide.	Cyanides	244-251	NAD(P)H quinone dehydrogenase 1	Homo sapiens	140-153
9163728-5	1997	A functional assay using flow cytometry showed decreased accumulation of daunorubicin in these sublines as compared to that of AML-2, which was reversed by cyclosporin A or cyanide.	Cyanides	173-180	RUNX family transcription factor 3	Homo sapiens	127-132
9163514-4	1997	The ferrous myoglobin is capable of strong binding with pyridine, imidazole, cyanide, and azide, and reacts moderately with ammonia.	Cyanides	77-84	myoglobin	Homo sapiens	12-21
9065496-0	1997	Adenosine release mediates cyanide-induced suppression of CA1 neuronal activity.	Cyanides	27-34	carbonic anhydrase 1	Homo sapiens	58-61
9080376-18	1997	It is concluded that the inhibition of oxidative phosphorylation with cyanide results in dissociation of both the [Ca2+]i-force and MLC20 phosphorylation-force relationships in rat uterine smooth muscle.	Cyanides	70-77	myosin light chain 12B	Rattus norvegicus	132-137
9106445-9	1997	Specifically, we observe a metabolic response to kainic acid that was selective for CA3-derived tissue, and a response to cyanide that was selective for CA1-derived tissue.	Cyanides	122-129	carbonic anhydrase 1	Rattus norvegicus	153-156
9048335-7	1997	This abnormal cell-cell adhesion is ameliorated by the presence of an excess of RGD-containing peptide and is reversed if cyanide-treated cells are allowed to recover for 1 h. It was concluded that the beta 1 integrin becomes expressed on the apical surface of MPT cells after sublethal injury.	Cyanides	122-129	hemoglobin, beta adult major chain	Mus musculus	202-208
8981030-5	1997	The amount of NADH- or succinate-reducible cytochrome b in the presence of cyanide was strongly decreased, but could be recovered by the addition of antimycin.	Cyanides	75-82	mitochondrially encoded cytochrome b	Homo sapiens	43-55
8900071-5	1996	Cyanide titration analyses with the succinate-reduced membrane suggested that cytochrome b562 was upstream of both the "gy = 1.89" Rieske FeS cluster and the a-type cytochromes.	Cyanides	0-7	cytochrome bc complex cytochrome b subunit	Sulfurisphaera tokodaii str. 7	78-90
9228566-3	1997	The time dependent expression of p-selectin in lung tissue was investigated in five groups of cases with different causes of death: carbon-monoxide and cyanide intoxication (n = 11), drowning (n = 5), hanging (n = 9), pneumonia (n = 13) and polytrauma with blunt thorax trauma (n = 14).	Cyanides	152-159	selectin P	Homo sapiens	33-43
9098948-10	1997	The data indicate that PCN is readily distributed in the rat, it is metabolized to cyanide via the cytochrome P-450-dependent mixed-function oxidase system and that the direct interaction of PCN and/or its metabolites with duodenal tissues appears to be the first step in the expression of its overall toxicity.	Cyanides	83-90	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	99-115
8956097-0	1996	Effectiveness of intramuscularly administered cyanide antidotes on methemoglobin formation and survival.	Cyanides	46-53	hemoglobin subunit gamma 2	Homo sapiens	67-80
8956097-3	1996	Exceptionally rapid methemoglobin formers-hydroxylamine hydrochloride (HH) and dimethylaminophenol (DMAP)-are usually able to prevent the lethal effect of cyanide following intramuscular injections in doses sufficient to induce 20% methemoglobin (HH = 20 mg kg-1 and DMAP = 2 mg kg-1).	Cyanides	155-162	hemoglobin subunit gamma 2	Homo sapiens	20-33
8956097-3	1996	Exceptionally rapid methemoglobin formers-hydroxylamine hydrochloride (HH) and dimethylaminophenol (DMAP)-are usually able to prevent the lethal effect of cyanide following intramuscular injections in doses sufficient to induce 20% methemoglobin (HH = 20 mg kg-1 and DMAP = 2 mg kg-1).	Cyanides	155-162	hemoglobin subunit gamma 2	Homo sapiens	232-245
8956097-6	1996	If the bradycardia is prevented or reversed by atropine, the rate of absorption of sodium nitrite and the formation of methemoglobin is able to reverse the otherwise lethal effects of cyanide.	Cyanides	184-191	hemoglobin subunit gamma 2	Homo sapiens	119-132
22062129-6	1997	Using the sensitive test with cyanide and hydrogen peroxide, the acrylamide gel of the SOD showed this enzyme was of the Cu Zn  type.	Cyanides	30-37	superoxide dismutase 1	Homo sapiens	87-90
7595537-0	1995	Bcl-2 protects neural cells from cyanide/aglycemia-induced lipid oxidation, mitochondrial injury, and loss of viability.	Cyanides	33-40	BCL2 apoptosis regulator	Homo sapiens	0-5
8917673-3	1996	Parallel biochemical investigations showed that there was a dose-dependent increase in the peroxisomal cyanide-insensitive palmitoyl CoA oxidase and acetyl carnitine transferase activities in treated rats and mice.	Cyanides	103-110	acyl-CoA oxidase 1	Homo sapiens	123-144
8700549-1	1996	Bcl-2, Bcl-xL, CrmA and tetrapeptide ICE inhibitor reduce the extent of necrotic cell death induced by cyanide, which primarily damages mitochondria.	Cyanides	103-110	BCL2 apoptosis regulator	Homo sapiens	0-5
8700549-1	1996	Bcl-2, Bcl-xL, CrmA and tetrapeptide ICE inhibitor reduce the extent of necrotic cell death induced by cyanide, which primarily damages mitochondria.	Cyanides	103-110	BCL2 like 1	Homo sapiens	7-13
8700549-1	1996	Bcl-2, Bcl-xL, CrmA and tetrapeptide ICE inhibitor reduce the extent of necrotic cell death induced by cyanide, which primarily damages mitochondria.	Cyanides	103-110	carboxylesterase 2	Homo sapiens	37-40
8700549-2	1996	Although none of them affects the drastic decrease in ATP levels induced by cyanide, Bcl-2 and Bcl-xL but not CrmA or ICE inhibitor inhibit the cyanide-induced decrease in mitochondrial membrane potential.	Cyanides	144-151	BCL2 apoptosis regulator	Homo sapiens	85-90
8700549-2	1996	Although none of them affects the drastic decrease in ATP levels induced by cyanide, Bcl-2 and Bcl-xL but not CrmA or ICE inhibitor inhibit the cyanide-induced decrease in mitochondrial membrane potential.	Cyanides	144-151	BCL2 like 1	Homo sapiens	95-101
8662862-10	1996	When cyanide-bound caa3 is mixed with ascorbate plus TMPD, cytochrome c and cytochrome a are synchronously reduced; the value of the second order rate constant (k = 3 x 10(5) M-1 s-1 at 30 degrees C) suggests that cytochrome c is the electron entry site.	Cyanides	5-12	cytochrome c, somatic	Homo sapiens	59-71
8662862-10	1996	When cyanide-bound caa3 is mixed with ascorbate plus TMPD, cytochrome c and cytochrome a are synchronously reduced; the value of the second order rate constant (k = 3 x 10(5) M-1 s-1 at 30 degrees C) suggests that cytochrome c is the electron entry site.	Cyanides	5-12	cytochrome c, somatic	Homo sapiens	214-226
24301826-7	1996	Low concentrations of cyanide (in the muM range) prolonged the oxidation time while high concentrations suppressed the oxidation (I50=1.5 mM KCN).	Cyanides	22-29	latexin	Homo sapiens	38-41
8752110-8	1996	Addition of either ascorbate or catalase to the cultures partially attenuated the loss of cell viability induced by cyanide, and decreased the incidence of apoptotic cells after treatment, based on the in situ detection of DNA strand breaks.	Cyanides	116-123	catalase	Rattus norvegicus	32-40
8678898-1	1996	When incubated with catalase/glucose-glucose oxidase, 13C-labeled cyanamide gave rise not only to 13C-labeled cyanide, but also to 13C-labeled CO2.	Cyanides	110-117	catalase	Homo sapiens	20-28
8660602-1	1996	Cyanide toxicity can be reduced by the use of methemoglobin (MetHb) formers, and antidotal dosage is based on the extent of MetHb formation.	Cyanides	0-7	hemoglobin subunit gamma 2	Homo sapiens	46-59
8660602-1	1996	Cyanide toxicity can be reduced by the use of methemoglobin (MetHb) formers, and antidotal dosage is based on the extent of MetHb formation.	Cyanides	0-7	hemoglobin subunit gamma 2	Homo sapiens	61-66
8660602-4	1996	In the detoxication of cyanide with methemoglobin, an intermediate dicyanhemimethemoglobin was demonstrated to be the predominant species in the formation of tetracyanmethemoglobin.	Cyanides	23-30	hemoglobin subunit gamma 2	Homo sapiens	36-49
8679537-6	1996	The major determinants of the cyanide affinity are the ease of water displacement from the ferric iron atom in metmyoglobin, the acid dissociation constant of HCN inside the protein (K*a), and steric hindrance and electrostatic interactions at the sixth coordination position.	Cyanides	30-37	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	159-162
12226312-1	1996	Suspension cells of tobacco (Nicotiana tabacum L. cv Bright Yellow) were used to investigate signals regulating the expression of the nuclear gene Aox1 encoding the mitochondrial alternative oxidase (AOX) protein responsible for cyanide-resistant respiration in plants.	Cyanides	229-236	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	147-151
12226312-1	1996	Suspension cells of tobacco (Nicotiana tabacum L. cv Bright Yellow) were used to investigate signals regulating the expression of the nuclear gene Aox1 encoding the mitochondrial alternative oxidase (AOX) protein responsible for cyanide-resistant respiration in plants.	Cyanides	229-236	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	200-203
8627283-0	1996	Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a comparative study.	Cyanides	7-14	cytochrome c, somatic	Equus caballus	98-110
8613912-11	1996	However, significant protection from cyanide-induced cytotoxicity was observed when L-NAME was combined with SOD/catalase.	Cyanides	37-44	superoxide dismutase 1	Homo sapiens	109-112
8613912-11	1996	However, significant protection from cyanide-induced cytotoxicity was observed when L-NAME was combined with SOD/catalase.	Cyanides	37-44	catalase	Homo sapiens	113-121
8573077-7	1996	Apoenzyme preparation by treatment of DCT with cyanide or o-phenanthroline followed by reconstitution experiments of tautomerase activity in the presence of different ions confirmed that the metal cofactor for the DCT active site is zinc.	Cyanides	47-54	dopachrome tautomerase	Homo sapiens	38-41
8573077-7	1996	Apoenzyme preparation by treatment of DCT with cyanide or o-phenanthroline followed by reconstitution experiments of tautomerase activity in the presence of different ions confirmed that the metal cofactor for the DCT active site is zinc.	Cyanides	47-54	dopachrome tautomerase	Homo sapiens	214-217
8806051-1	1996	3-Mercaptopyruvate sulfurtransferase catalyzes the transfer of sulfur from 3-mercaptopyruvate to several possible acceptor molecules, one of which is cyanide.	Cyanides	150-157	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
8806051-2	1996	Because the transsulfuration of cyanide is the primary in vivo mechanism of detoxification, 3-mercaptopyruvate sulfurtransferase may function in the enzymatic detoxification of cyanide in vivo.	Cyanides	177-184	mercaptopyruvate sulfurtransferase	Homo sapiens	92-128
7488186-1	1995	Rhodanese (thiosulfate sulfurtransferase) is expressed at high levels in liver and is involved in the detoxification of cyanide.	Cyanides	120-127	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	0-9
7488186-1	1995	Rhodanese (thiosulfate sulfurtransferase) is expressed at high levels in liver and is involved in the detoxification of cyanide.	Cyanides	120-127	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	11-40
7488186-6	1995	When the mouse and rat cDNAs were expressed under the control of IPTG-inducible promoters in E. coli, the cell extracts exhibited cyanide-metabolizing activity, indicating that both genes encode functional rhodanese molecules.	Cyanides	130-137	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	206-215
7667073-3	1995	The application of cyanide produced an abolition of spontaneous contractions and a rapid initial fall in pHi.	Cyanides	19-26	glucose-6-phosphate isomerase	Rattus norvegicus	105-108
7632673-1	1995	The kinetics of cyanide binding to cytochrome c oxidase were systematically studied as a function of [HCN], [oxidase], pH, ionic strength, temperature, type and concentration of solubilizing detergent, and monomer-dimer content of oxidase.	Cyanides	16-23	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	102-105
7626092-1	1995	Reduction of nitric oxide (NO) to nitrous oxide (N2O) is catalyzed by bovine heart cytochrome c oxidase (CcO) in anaerobic solutions at pH 7.2 and 20 degrees C. Cyanide inhibits and forms Fea3(3+)CN.	Cyanides	161-168	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	83-103
7626092-1	1995	Reduction of nitric oxide (NO) to nitrous oxide (N2O) is catalyzed by bovine heart cytochrome c oxidase (CcO) in anaerobic solutions at pH 7.2 and 20 degrees C. Cyanide inhibits and forms Fea3(3+)CN.	Cyanides	161-168	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	105-108
7768907-6	1995	In addition, azaheme myoglobin forms stable complexes with imidazole, pyridine, or cyanide in ferrous state.	Cyanides	83-90	myoglobin	Homo sapiens	21-30
8654706-0	1995	Rapid-scan FTIR spectroscopic studies on the photolysis and recombination of the cyanide adduct of fully reduced bovine cytochrome c oxidase.	Cyanides	81-88	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	120-140
9383439-4	1995	Mutation of the heme axial ligand (Met80) to Ala in Saccharomyces cerevisiae iso-1-cytochrome c yields a protein (Ala80cyt c) capable of binding exogenous ligands such as dioxygen and cyanide.	Cyanides	184-191	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	77-82
7641845-1	1995	Tyrosinase in crude extracts from the adult rabbit choroid and retina/retinal pigment epithelium was found to be differently affected by the inhibitors sodium metabisulfite, cyanide, diethyldithiocarbamate and 2,2"-dipyridyl:the latter inhibited the activity in the retina/retinal pigment epithelium extract after 24 hr of incubation, but not that in the choroid.	Cyanides	174-181	tyrosinase	Oryctolagus cuniculus	0-10
7766663-3	1995	In the presence of cyanide (inhibitor of mitochondrial respiration) insulin did not activate GS.	Cyanides	19-26	insulin	Homo sapiens	68-75
7560734-2	1995	Benzocaine has structural similarities to methemoglobin (MHb)-forming drugs that are current candidates for cyanide prophylaxis, while LC has been reported to increase MHb in man.	Cyanides	108-115	hemoglobin subunit gamma 2	Homo sapiens	42-55
7560734-2	1995	Benzocaine has structural similarities to methemoglobin (MHb)-forming drugs that are current candidates for cyanide prophylaxis, while LC has been reported to increase MHb in man.	Cyanides	108-115	hemoglobin subunit gamma 2	Homo sapiens	57-60
7667073-9	1995	It is concluded that cyanide decreases pHi and force in the uterus, but that there is not a simple relationship between the two.	Cyanides	21-28	glucose-6-phosphate isomerase	Rattus norvegicus	39-42
7733330-5	1995	Intravenous angiotensin II caused a stimulation of chloride absorption from a high-chloride perfusate by 55 peq.mm-1.min-1 (632 +/- 17 to 687 +/- 14, P < 0.05), which was partially cyanide-sensitive (510 +/- 6 peq.mm-1.min-1).	Cyanides	184-191	angiotensinogen	Rattus norvegicus	12-26
7603631-0	1995	Seizures and selective CA-1 hippocampal lesions induced by an excitotoxic cyanide metabolite, 2-iminothiazolidine-4-carboxylic acid.	Cyanides	74-81	carbonic anhydrase 1	Rattus norvegicus	23-27
12232424-4	1994	Transgenic cells with increased AOX protein had an increased capacity for cyanide-resistant, salicylhydroxamic acid-sensitive respiration compared to wild-type cells, whereas transgenic cells with decreased AOX protein had a decreased capacity for such respiration.	Cyanides	74-81	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	32-35
7881866-0	1994	Protein kinase C modulation of rhodanese-catalyzed conversion of cyanide to thiocyanate.	Cyanides	65-72	thiosulfate sulfurtransferase	Bos taurus	31-40
7881866-1	1994	Detoxification of cyanide is catalyzed by a sulfurtransferase, rhodanese, a phosphoprotein regulated by unknown protein kinases.	Cyanides	18-25	thiosulfate sulfurtransferase	Bos taurus	63-72
7891846-0	1994	MK-801 prevents cyanide-induced changes of Fos levels in rat brain.	Cyanides	16-23	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	43-46
7891846-1	1994	The effect of acute cyanide intoxication on levels of transcriptional regulatory proteins Fos and c-Jun in rat cortex, hippocampus, cerebellum and brain stem was studied.	Cyanides	20-27	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	90-93
7891846-2	1994	Western blot analysis showed a differential effect of cyanide on Fos levels in the selected brain areas.	Cyanides	54-61	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	65-68
7891846-10	1994	Pretreatment with the NMDA receptor antagonist, MK-801, prevented the cyanide-induced changes of Fos.	Cyanides	70-77	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	97-100
7891846-11	1994	The differential effect of cyanide on Fos levels in different brain areas and the blockade of these changes by MK-801 suggest involvement of multiple neuronal pathways, including the excitatory amino acid (EAA) neurotransmitter system.	Cyanides	27-34	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	38-41
7891846-12	1994	It is concluded that cyanide alters levels of the transcriptional regulatory protein Fos through activation of the EAA neurotransmitter system and, thus, may affect gene expression in neuronal or glia cells.	Cyanides	21-28	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	85-88
7982101-3	1994	Using D-[2,3-3H]aspartic acid ([3H]D-Asp) as a tracer, we found that corticosterone (CORT, the physiological GC in rats) increased the accumulation of extracellular [3H]D-Asp by 25% in hippocampal cultures during cyanide-induced ischemia.	Cyanides	213-220	cortistatin	Rattus norvegicus	85-89
7982101-5	1994	Instead, analysis of [3H]D-Asp uptake kinetics indicates that CORT decreased the maximum uptake rate and the Michaelis constant by 44% and 50%, respectively, in cells treated with cyanide.	Cyanides	180-187	cortistatin	Rattus norvegicus	62-66
7982101-6	1994	It is concluded that, during cyanide-induced ischemia, CORT might enhance extracellular overflow of [3H]D-Asp by decreasing its uptake, thereby endangering neurons.	Cyanides	29-36	cortistatin	Rattus norvegicus	55-59
8031836-8	1994	Cyanide interaction with heme.hemopexin produces an additional low-spin adduct.	Cyanides	0-7	HEME	Bos taurus	25-29
8031836-8	1994	Cyanide interaction with heme.hemopexin produces an additional low-spin adduct.	Cyanides	0-7	hemopexin	Oryctolagus cuniculus	30-39
7958565-2	1994	Previous studies have indicated that resealed erythrocytes containing rhodanese (CRBC) and sodium thiosulfate can rapidly metabolize cyanide to the less toxic thiocyanate.	Cyanides	133-140	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	70-79
7958565-3	1994	This thiosulfate-rhodanese system was very efficacious as a new conceptual approach to antagonize cyanide intoxication both in vitro and in vivo.	Cyanides	98-105	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	17-26
7958565-7	1994	Moreover, the rhodanese reaction rate of any of these organic thiosulfonates is much faster than the rate observed with the classic cyanide antidote, sodium thiosulfate.	Cyanides	132-139	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	14-23
7516710-8	1994	Ca2+ uptake was achieved in the presence of 3 microM antimycin or 0.1 mM cyanide; this finding indicates that the alternative respiratory chain present in Euglena mitochondria can support this energy-dependent reaction.	Cyanides	73-80	carbonic anhydrase 2	Homo sapiens	0-3
8209387-1	1994	Toxicity of cyanide is related to its inhibitory action on cytochrome c oxidase (COx).	Cyanides	12-19	coproporphyrinogen oxidase	Rattus norvegicus	81-84
8209387-9	1994	The combination of both high oxygen concentration and the presence of either pyruvate or alpha-ketoglutarate was necessary to effectively protect COx against cyanide poisoning.	Cyanides	158-165	coproporphyrinogen oxidase	Rattus norvegicus	146-149
7910421-6	1994	Tyrosine hydroxylase (TH) immunohistochemical examination of brains from cyanide-treated animals showed a reduced number of TH-positive cells in substantia nigra, indicating a loss of dopaminergic neurons.	Cyanides	73-80	tyrosine hydroxylase	Mus musculus	0-20
8197590-3	1994	The heart also showed no increase, whereas kidney conjugated dienes slowly increased to a peak 1 h after cyanide.	Cyanides	105-112	pseudopodium-enriched atypical kinase 1	Mus musculus	90-96
8126749-0	1994	Antagonism of cyanide intoxication with murine carrier erythrocytes containing bovine rhodanese and sodium thiosulfate.	Cyanides	14-21	thiosulfate sulfurtransferase	Bos taurus	86-95
8126749-3	1994	The present studies demonstrate the ability of these carrier red blood cells containing rhodanese and thiosulfate to antagonize the lethal effects of cyanide either alone or in various combinations with sodium nitrite and/or sodium thiosulfate.	Cyanides	150-157	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	88-97
8126749-5	1994	These results indicate that the administration of carrier erythrocytes containing rhodanese and thiosulfate alone can provide significant protection against the lethal effects of cyanide.	Cyanides	179-186	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	82-91
8117318-0	1994	Effects of cyanide in vitro on the activity of monoamine oxidase in striatal tissue from rat and pig.	Cyanides	11-18	monoamine oxidase A	Rattus norvegicus	47-64
8117318-7	1994	The effect of cyanide on MAO was immediate.	Cyanides	14-21	monoamine oxidase A	Rattus norvegicus	25-28
8117318-8	1994	In rat, as well as pig, striatal tissue we found that cyanide produced a dose-dependent increase in the activity of MAO-A (as measured with 5-HT), but not MAO-B (as measured with PEA).	Cyanides	54-61	monoamine oxidase A	Sus scrofa	116-121
8087243-11	1994	Stabilization of the methemoglobin by cyanide, haptoglobin or capture of the heme by hemopexin abrogates this effect.	Cyanides	38-45	hemoglobin subunit gamma 2	Homo sapiens	21-34
8240571-0	1993	A spectrophotometric method for estimating methemoglobin concentration in the presence of cyanide.	Cyanides	90-97	hemoglobin subunit gamma 2	Homo sapiens	43-56
8399138-1	1993	Low-frequency resonance Raman spectra of the cyanide and carbon monoxide adducts of lactoperoxidase are obtained with Soret excitation.	Cyanides	45-52	lactoperoxidase	Homo sapiens	84-99
8399138-5	1993	On the basis of a previous normal-mode analysis of the cyanoferric adduct of myeloperoxidase, a bent Fe-C-N linkage is suggested for the cyanide adduct of lactoperoxidase.	Cyanides	137-144	myeloperoxidase	Homo sapiens	77-92
8399138-5	1993	On the basis of a previous normal-mode analysis of the cyanoferric adduct of myeloperoxidase, a bent Fe-C-N linkage is suggested for the cyanide adduct of lactoperoxidase.	Cyanides	137-144	lactoperoxidase	Homo sapiens	155-170
8399138-6	1993	The nu(Fe-CN) (374 cm-1) and delta(Fe-C-N) (480 cm-1) modes are observed for the cyanide adduct of reduced lactoperoxidase.	Cyanides	81-88	lactoperoxidase	Homo sapiens	107-122
8214084-7	1993	Pretreatment of EC with the iron chelator deferoxamine mesylate (1-10 mM) for 4 h attenuated the PMN-mediated decrease in ACE activity, as did the thiol reducing agent, 2-mercaptoethanol (0.1 mM), and the myeloperoxidase inhibitor, cyanide (5 mM), but not azide (1-50 mM).	Cyanides	232-239	angiotensin I converting enzyme	Bos taurus	122-125
8353957-0	1993	Rapid multicomponent analysis of hemoglobin derivatives for controlled antidotal use of methemoglobin-forming agents in cyanide poisoning.	Cyanides	120-127	hemoglobin subunit gamma 2	Homo sapiens	88-101
8353957-1	1993	When cyanide poisoning is treated with a methemoglobin-forming agent, oxidative metabolism is protected at the expense of the oxygen capacity of the blood.	Cyanides	5-12	hemoglobin subunit gamma 2	Homo sapiens	41-54
8353957-5	1993	All conditions appeared to be fulfilled for the construction of a practical multiwavelength photometer for reliably monitoring methemoglobin therapy in patients with cyanide poisoning, even in the presence of carboxyhemoglobin, as often occurs in fire victims.	Cyanides	166-173	hemoglobin subunit gamma 2	Homo sapiens	127-140
8392865-1	1993	Resonance Raman spectra are reported for the fully reduced unliganded and cyanide-bound mixed-valence forms of the cytochrome c oxidases from bovine heart and Paracoccus denitrificans in both detergent-solubilized forms and within their natural membrane environments.	Cyanides	74-81	LOC104968582	Bos taurus	115-127
8384444-5	1993	This cyanide- and antimycin-insensitive but hypoxia-sensitive cytochrome b would be an attractive candidate for controlled Epo production in response to pO2.	Cyanides	5-12	mitochondrially encoded cytochrome b	Homo sapiens	62-74
8384444-5	1993	This cyanide- and antimycin-insensitive but hypoxia-sensitive cytochrome b would be an attractive candidate for controlled Epo production in response to pO2.	Cyanides	5-12	erythropoietin	Homo sapiens	123-126
8382954-1	1993	Cyanide and formate induce spectral changes in E. coli cytochrome bo which are similar to those induced in bovine heart cytochrome-c oxidase (cytochrome aa3).	Cyanides	0-7	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	120-140
8441752-3	1993	We have determined the structure of human carbonic anhydrase II inhibited by cyanide and cyanate, respectively, by X-ray crystallography.	Cyanides	77-84	carbonic anhydrase 2	Homo sapiens	42-63
8427023-0	1993	Protective effect of calmodulin inhibitors against acute cyanide-induced lethality and convulsions in mice.	Cyanides	57-64	calmodulin 2	Mus musculus	21-31
8427023-1	1993	The ED50 value of cyanide as measured by induction of convulsions (tonic seizure) was significantly increased by 80% or 69% when trifluoperazine (TFP) or chlorpromazine (CHP), a specific calmodulin inhibitor was preinjected intracerebroventricularly (i.v.t.)	Cyanides	18-25	calmodulin 2	Mus musculus	187-197
20732163-0	1992	The effect of picrylsulphonic acid on In vitro conversion of cyanide to thiocyanate by 3-mercaptopyruvate sulphurtransferase and rhodanese.	Cyanides	61-68	mercaptopyruvate sulfurtransferase	Homo sapiens	87-124
20732163-2	1992	The time course and capacity of MPST to detoxify cyanide was equal to or exceeded that of rhodanese.	Cyanides	49-56	mercaptopyruvate sulfurtransferase	Homo sapiens	32-36
1325837-9	1992	Cyt b-558 showed an anisotropic signal at a g value of 3.2 +/- 0.05, which was cyanide-insensitive and reducible with reductants.	Cyanides	79-86	cytochrome b	Sus scrofa	0-5
1444430-1	1992	Products observed during anaerobic cyanide transformation are consistent with a hydrolytic pathway (HCN + H2O <--> HCONH2 + H2O <--> HCOOH + NH3).	Cyanides	35-42	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	100-103
1324720-4	1992	The characteristics of the cleaved enzymes were the same as for native lipoxygenase 1 in all aspects examined: insensitivity to cyanide, fluoride, and EDTA, regiochemical and stereochemical consequences of catalysis, and EPR spectroscopy upon oxidation by product.	Cyanides	128-135	seed linoleate 13S-lipoxygenase-1	Glycine max	71-85
1356586-6	1992	A 24 h pre-treatment with CORT did not influence normoxic ATP levels but potentiated the loss of ATP following both cyanide and hypoxia.	Cyanides	116-123	cortistatin	Rattus norvegicus	26-30
1356586-7	1992	CORT also exacerbated the loss of ATP seen after combined exposure to cyanide and glutamate, as well as that following cyanide + 0 mM glucose.	Cyanides	70-77	cortistatin	Rattus norvegicus	0-4
1356586-7	1992	CORT also exacerbated the loss of ATP seen after combined exposure to cyanide and glutamate, as well as that following cyanide + 0 mM glucose.	Cyanides	119-126	cortistatin	Rattus norvegicus	0-4
1314665-0	1992	Rates of cyanide binding to the catalytic intermediates of mammalian cytochrome c oxidase, and the effects of cytochrome c and poly(L-lysine).	Cyanides	9-16	cytochrome c, somatic	Homo sapiens	69-81
1314665-5	1992	Evidence is presented suggesting that mediation of electron transfer from one-electron-reduced, cyanide-liganded enzyme to free, ferric oxidase, rather than a global protein conformational change of the enzyme, is responsible for the greatly enhanced cyanide binding rates seen in the presence of cytochrome c or poly(L-lysine).	Cyanides	96-103	cytochrome c, somatic	Homo sapiens	297-309
1314665-5	1992	Evidence is presented suggesting that mediation of electron transfer from one-electron-reduced, cyanide-liganded enzyme to free, ferric oxidase, rather than a global protein conformational change of the enzyme, is responsible for the greatly enhanced cyanide binding rates seen in the presence of cytochrome c or poly(L-lysine).	Cyanides	251-258	cytochrome c, somatic	Homo sapiens	297-309
1522520-12	1992	After being exposed to cyanide for 5 min without stimulation, the tetanic tension was reduced to about 0.9 Po and pHi was alkaline by about 0.1 units.	Cyanides	23-30	glucose-6-phosphate isomerase 1	Mus musculus	114-117
1592227-7	1992	Cyanide (1 mM) when added during angiotensin II (5 nM) infusion blocked the pressor effect and completely inhibited all O2 uptake.	Cyanides	0-7	angiotensinogen	Rattus norvegicus	33-47
1385361-7	1992	The isolated Hb FX was unstable, had spectral changes characteristic for the M-hemoglobins, while its methemoglobin derivative reacted rapidly with cyanide.	Cyanides	148-155	hemoglobin subunit gamma 2	Homo sapiens	102-115
1747420-2	1991	The ATP/ADP-antiporter inhibitor carboxyatractylate slowed down the respiration rate, increased delta psi and decreased the ionic conductivity of the inner mitochondrial membrane as measured by the rate of the delta psi decline after addition of cyanide (in the presence of oligomycin and EGTA).	Cyanides	246-253	ATPase phospholipid transporting 8A2	Homo sapiens	4-22
1855626-4	1991	Prior studies indicated that erythrocytes containing encapsulated rhodanese and sodium thiosulfate metabolized cyanide to thiocyanate in vitro.	Cyanides	111-118	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	66-75
2006499-0	1991	The cyanide-metabolizing enzyme rhodanese in human nasal respiratory mucosa.	Cyanides	4-11	thiosulfate sulfurtransferase	Rattus norvegicus	32-41
2006499-1	1991	The cyanide-metabolizing enzyme rhodanese is present in rat nasal epithelium at high activity levels.	Cyanides	4-11	thiosulfate sulfurtransferase	Rattus norvegicus	32-41
2006499-4	1991	The high rhodanese activity in rat nasal epithelium may provide a mechanism for detoxicating inhaled hydrogen cyanide and may also play a role in olfaction by limiting the concentrations of cyanide in the nasal epithelium.	Cyanides	110-117	thiosulfate sulfurtransferase	Rattus norvegicus	9-18
2006499-6	1991	On a per milligram mitochondrial protein basis, the rhodanese in human nasal tissue exhibited both a lower affinity (higher Km) for cyanide and a lower maximum velocity (Vmax) for cyanide metabolism than did rhodanese from rat nasal tissue.	Cyanides	132-139	thiosulfate sulfurtransferase	Rattus norvegicus	52-61
2006499-6	1991	On a per milligram mitochondrial protein basis, the rhodanese in human nasal tissue exhibited both a lower affinity (higher Km) for cyanide and a lower maximum velocity (Vmax) for cyanide metabolism than did rhodanese from rat nasal tissue.	Cyanides	180-187	thiosulfate sulfurtransferase	Rattus norvegicus	52-61
2006499-9	1991	The Vmax/Km ratios for rhodanese from the nasal tissue of nonsmokers were consistently greater, thus suggesting the possibility of higher rates of cyanide metabolism in nonsmokers than in smokers.	Cyanides	147-154	thiosulfate sulfurtransferase	Rattus norvegicus	23-32
7796171-7	1995	Cyanide-induced PKC translocation persisted for at least 120 min.	Cyanides	0-7	protein kinase C, gamma	Rattus norvegicus	16-19
7870031-9	1995	Therefore, the differences in the size and/or the electronegativity of the isothiocyanate and isonitrile moieties appear to dramatically affect the abilities of the compounds to interact with P-glycoprotein.	Cyanides	94-104	ATP binding cassette subfamily B member 1	Homo sapiens	192-206
7744285-1	1995	The study of general toxicological mechanism of acetone cyanhydrin and cyanides provided the data for reconsideration of their MACs in the water which is recommended at the level of 0.035 mg/l (as CN for each substance alone and both together).	Cyanides	71-79	myristoylated alanine rich protein kinase C substrate	Homo sapiens	127-131
7881866-12	1994	It is suggested that addition of purified, exogenous PKC may accept phosphate from phosphorylated rhodanese or HI-6 may dephosphorylate rhodanese, both of which stimulate the conversion of cyanide anion to the less toxic SCN-.	Cyanides	189-202	thiosulfate sulfurtransferase	Bos taurus	98-107
7881866-12	1994	It is suggested that addition of purified, exogenous PKC may accept phosphate from phosphorylated rhodanese or HI-6 may dephosphorylate rhodanese, both of which stimulate the conversion of cyanide anion to the less toxic SCN-.	Cyanides	189-202	thiosulfate sulfurtransferase	Bos taurus	136-145
7881866-13	1994	These observations support the possibility that rhodanese may be regulated by protein phosphorylation and treatments that alter the phosphorylation state of rhodanese may affect cyanide detoxification via SCN- formation.	Cyanides	178-185	thiosulfate sulfurtransferase	Bos taurus	48-57
7881866-13	1994	These observations support the possibility that rhodanese may be regulated by protein phosphorylation and treatments that alter the phosphorylation state of rhodanese may affect cyanide detoxification via SCN- formation.	Cyanides	178-185	thiosulfate sulfurtransferase	Bos taurus	157-166
7800649-5	1994	These results suggest that in the chicken part of the ingested cyanide is detoxified in the digestive tract, mainly by the proventriculus, and part of the absorbed cyanide is metabolized by hepatic rhodanese.	Cyanides	164-171	thiosulfate sulfurtransferase	Gallus gallus	198-207
12232282-6	1994	Respiratory inhibitors were used to assess the activity of the cytochrome (cyanide-sensitive) and alternative (cyanide-resistant) pathways in GCP and MCP.	Cyanides	75-82	CD46 molecule	Homo sapiens	150-153
12232282-9	1994	The activity of the cyanide-resistant electron transport path constituted only one-third of total respiration in GCP but accounted for two-thirds of respiration in MCP.	Cyanides	20-27	CD46 molecule	Homo sapiens	164-167
8011669-13	1994	The presence of oxidized cytochrome c did enhance the reactivity towards cyanide and towards carbon monoxide in cytochrome c oxidase of all three preparations.	Cyanides	73-80	cytochrome c, somatic	Homo sapiens	25-37
8194601-4	1994	The ESEEM spectra of 15N SOD with cyanide as an inhibitor containing 14N and 15N are also discussed.	Cyanides	34-41	superoxide dismutase 1	Homo sapiens	25-28
8188662-8	1994	His64, Gln64, and distal pocket water molecules appear to facilitate deprotonation of HCN, which is the major kinetic barrier to cyanide binding at neutral pH.	Cyanides	129-136	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	86-89
8137504-5	1994	Compared with hypoxia, cyanide mediated small transient inductions of fos and jun transcripts that followed a different time course.	Cyanides	23-30	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	70-73
8122272-0	1994	Activation of a calcium- and pH-dependent phospholipase A2 by cyanide in PC12 cells.	Cyanides	62-69	phospholipase A2 group IB	Rattus norvegicus	42-58
8122272-9	1994	These data indicate that in PC12 cells KCN activates a Ca(2+)- and pH-dependent PLA2 which may contribute to cyanide-induced cell damage.	Cyanides	109-116	phospholipase A2 group IB	Rattus norvegicus	80-84
7549543-1	1994	We have measured the vibrational circular dichroism (VCD) spectra of the stretching vibrations of azide and cyanide ligated to the Fe3+ atoms of haemoglobin (Hb) and myoglobin (Mb).	Cyanides	108-115	myoglobin	Homo sapiens	166-175
8162104-1	1993	In experiments on different species of animals respiratory stimulating effects of naloxone, TRH and its analogue RGH 2202 during respiratory rhythmogenesis disturbances, evoked by hyperventilation of lungs, bleeding and intoxication with cyanides or opiates, were investigated.	Cyanides	238-246	thyrotropin releasing hormone	Homo sapiens	92-95
8415693-6	1993	These cellular methemoglobin effects were inhibited by the heme-scavenging protein hemopexin and by haptoglobin or cyanide, agents that strengthen the liganding between heme and globin.	Cyanides	115-122	hemoglobin subunit gamma 2	Homo sapiens	15-28
8265567-0	1993	Binding of cyanide, cyanate, and thiocyanate to human carbonic anhydrase II.	Cyanides	11-18	carbonic anhydrase 2	Homo sapiens	54-75
8265567-1	1993	Computer simulation techniques are used to address the question of how cyanide and related ions interact with human carbonic anhydrase II (HCAII).	Cyanides	71-78	carbonic anhydrase 2	Homo sapiens	116-137
8363114-0	1993	Cyanide and methemoglobin kinetics in smoke inhalation victims treated with the cyanide antidote kit.	Cyanides	80-87	hemoglobin subunit gamma 2	Homo sapiens	12-25
8314748-4	1993	Cell killing by cyanide was prevented when the phospholipase A2 inhibitor butacaine was added together with CyA.	Cyanides	16-23	phospholipase A2 group IB	Rattus norvegicus	47-63
8486618-3	1993	Treatment of cyanide-poisoned rat adipocytes with 1 mg/ml trypsin at 37 degrees C for 30 min produced an immunoreactive GLUT4 protein species in subsequently isolated plasma membranes that migrated with higher mobility (apparent M(r) = 35,000) than native GLUT4 (apparent M(r) = 46,000) on SDS-polyacrylamide gel electrophoresis.	Cyanides	13-20	solute carrier family 2 member 4	Rattus norvegicus	120-125
8486618-3	1993	Treatment of cyanide-poisoned rat adipocytes with 1 mg/ml trypsin at 37 degrees C for 30 min produced an immunoreactive GLUT4 protein species in subsequently isolated plasma membranes that migrated with higher mobility (apparent M(r) = 35,000) than native GLUT4 (apparent M(r) = 46,000) on SDS-polyacrylamide gel electrophoresis.	Cyanides	13-20	solute carrier family 2 member 4	Rattus norvegicus	256-261
8486618-5	1993	Insulin treatment of adipocytes for 20 min prior to sequential additions of cyanide and trypsin caused a 16-fold increase in the proteolytically cleaved GLUT4 species.	Cyanides	76-83	solute carrier family 2 member 4	Rattus norvegicus	153-158
8097233-5	1993	TGF-beta 3 was able to reduce the cyanide-induced neuronal damage at concentrations of 0.3 and 1 ng/ml, whereas TGF-beta 2 only showed neuroprotective activity at concentrations of 30 and 50 ng/ml.	Cyanides	34-41	transforming growth factor beta 3	Gallus gallus	0-10
8472668-5	1993	A dose-dependent inhibition of cyanide formation arising from allylnitrile in the liver and a dose-dependent attenuation of acute toxicity of allylnitrile were observed when CCl4 was given just prior to the nitrile administration in rats and mice.	Cyanides	31-38	C-C motif chemokine ligand 4	Rattus norvegicus	174-178
8440119-0	1993	Use of vitamin B12 in the treatment and prevention of nitroprusside-induced cyanide toxicity.	Cyanides	76-83	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	15-18
8380331-0	1993	Fourier-transform infrared study of cyanide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: implication of the redox-linked conformational change at the binuclear site.	Cyanides	36-43	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	99-119
8380331-1	1993	Cyanide binding to the Fea3-CuB binuclear center of cytochrome c oxidase purified from bovine heart mitochondria was examined by Fourier-transform infrared spectroscopy.	Cyanides	0-7	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	52-72
8380332-4	1993	Upon addition of cyanide to the preformed fully oxidized cytochrome c oxidase-azide complex, a new azide species exhibiting a sharp antisymmetric stretching band at 2032.5 cm-1 was formed.	Cyanides	17-24	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	57-77
8380332-6	1993	This cytochrome c oxidase-azide-cyanide ternary complex is relatively stable, and cyanide ion replaces the 2032.5-cm-1 azide species very slowly, resulting in the formation of the Fea3(3+)-C-N-CuB2+ bridging structure characterized by the 2152-cm-1 band.	Cyanides	32-39	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	5-25
8380332-6	1993	This cytochrome c oxidase-azide-cyanide ternary complex is relatively stable, and cyanide ion replaces the 2032.5-cm-1 azide species very slowly, resulting in the formation of the Fea3(3+)-C-N-CuB2+ bridging structure characterized by the 2152-cm-1 band.	Cyanides	82-89	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	5-25
8427023-4	1993	Since it is known that the inhibitory effect of TFP or CHP against calmodulin-dependent enzymes such as phosphodiesterase is 100-400-fold higher compared to PMZ, it is speculated that the inhibitory effect of TFP or CHP against cyanide-induced convulsions may be based on its strong inhibitory properties into calmodulin-dependent enzymes.	Cyanides	228-235	calmodulin 2	Mus musculus	67-77
1429633-6	1992	The ligand binding properties of these recombinant myoglobin proteins were studied by measurements of azide equilibrium and cyanide binding.	Cyanides	124-131	myoglobin	Homo sapiens	51-60
1554111-0	1992	Interspecies comparison of cellular localization of the cyanide metabolizing enzyme rhodanese within olfactory mucosa.	Cyanides	56-63	thiosulfate sulfurtransferase	Rattus norvegicus	84-93
1554111-3	1992	The enzyme rhodanese metabolizes cyanide, which is a commonly inhaled toxicant and an odorant and therefore of interest to both toxicologists and olfactory neurobiologists.	Cyanides	33-40	thiosulfate sulfurtransferase	Rattus norvegicus	11-20
1554111-9	1992	The differences in localization of rhodanese in these two species may have important implications for cell types at risk during inhalation of cyanide or organonitrile compounds metabolized to cyanide within the nasal mucosa.	Cyanides	142-149	thiosulfate sulfurtransferase	Rattus norvegicus	35-44
1554111-9	1992	The differences in localization of rhodanese in these two species may have important implications for cell types at risk during inhalation of cyanide or organonitrile compounds metabolized to cyanide within the nasal mucosa.	Cyanides	192-199	thiosulfate sulfurtransferase	Rattus norvegicus	35-44
1737776-17	1992	Cyanide formed a complex with SAHase that was analogous to ENADH.	Cyanides	0-7	adenosylhomocysteinase	Homo sapiens	30-36
1737776-18	1992	Adenine stabilized this complex sufficiently that addition of 65 microM adenine and 25 mM cyanide to SAHase caused total complex formation with loss of over 95% of the catalytic activity.	Cyanides	90-97	adenosylhomocysteinase	Homo sapiens	101-107
1316115-4	1992	Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol).	Cyanides	114-121	myeloperoxidase	Homo sapiens	38-53
1316115-4	1992	Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol).	Cyanides	114-121	myeloperoxidase	Homo sapiens	55-58
1316115-4	1992	Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol).	Cyanides	114-121	myeloperoxidase	Homo sapiens	98-101
1667623-1	1991	We have developed a sensitive method for the measurement of rhodanese activity in human serum which is based on the colorimetric method for the determination of thiocyanate produced from methanethiosulfonate and cyanide as substrates.	Cyanides	212-219	thiosulfate sulfurtransferase	Bos taurus	60-69
1667623-3	1991	The present method is about 70-fold more sensitive than the conventional method using cyanide and thiosulfate as substrates and correlates well (r = 0.997) with the conventional method in bovine liver rhodanese.	Cyanides	86-93	thiosulfate sulfurtransferase	Bos taurus	201-210
1891774-1	1991	Resealed erythrocytes containing sodium thiosulfate and rhodanese (CRBC) are being employed as a new approach in the antagonism of cyanide intoxication.	Cyanides	131-138	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	56-65
1891774-2	1991	In earlier in vitro studies, the behavior of red blood cells containing rhodanese and sodium thiosulfate was investigated with regard to their properties and their capability of metabolizing cyanide to thiocyanate.	Cyanides	191-198	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	72-81
1891774-11	1991	Red blood cells containing sodium thiosulfate and rhodanese apparently are effective in vivo in the biotransformation of cyanide.	Cyanides	121-128	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	50-59
1891774-12	1991	In animals pretreated with encapsulated rhodanese and sodium thiosulfate, blood cyanide concentrations are appreciably decreased with a concomitant increase in thiocyanate ion, a metabolite of cyanide.	Cyanides	80-87	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	40-49
1891774-12	1991	In animals pretreated with encapsulated rhodanese and sodium thiosulfate, blood cyanide concentrations are appreciably decreased with a concomitant increase in thiocyanate ion, a metabolite of cyanide.	Cyanides	193-200	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	40-49
1891774-14	1991	Furthermore, carrier erythrocytes containing rhodanese and sodium thiosulfate were found to increase the protection against the lethal effects of cyanide by approximately twofold.	Cyanides	146-153	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	45-54
2018478-1	1991	Rhodanese (EC 2.8.1.1), a mitochondrial thiosulphate sulphurtransferase, is involved in the formation of iron-sulphur complexes and cyanide detoxification.	Cyanides	132-139	thiosulfate sulfurtransferase	Rattus norvegicus	0-9
1648113-5	1991	The contribution of the two types of SOD to the F- relaxation rate in the homogenates was measured by addition of either diethyldithiocarbamate or cyanide, both of which selectively inhibit the CuSOD.	Cyanides	147-154	superoxide dismutase 2	Homo sapiens	37-40
1685401-9	1991	Mercaptopyruvate and rhodanese substrates also differed in their effects on blood cyanide concentration and on the excretion of isotope from radiolabelled cyanide.	Cyanides	82-89	thiosulfate sulfurtransferase	Gallus gallus	21-30
1685401-9	1991	Mercaptopyruvate and rhodanese substrates also differed in their effects on blood cyanide concentration and on the excretion of isotope from radiolabelled cyanide.	Cyanides	155-162	thiosulfate sulfurtransferase	Gallus gallus	21-30
1646752-2	1991	To assay MnSOD, Cu,ZnSOD can be inhibited selectively by millimolar concentrations of cyanide ion.	Cyanides	86-93	superoxide dismutase 2	Homo sapiens	9-14
1646752-3	1991	However, calculation of MnSOD activity from the differential cyanide inhibition assay is complex and small experimental errors can cause large errors in the calculated MnSOD activity.	Cyanides	61-68	superoxide dismutase 2	Homo sapiens	24-29
1646752-4	1991	We have assessed how interaction of cyanide and hydrogen peroxide with cytochrome c can lead to further errors in the xanthine oxidase-cytochrome c assay for SOD.	Cyanides	36-43	cytochrome c, somatic	Homo sapiens	71-83
1646752-4	1991	We have assessed how interaction of cyanide and hydrogen peroxide with cytochrome c can lead to further errors in the xanthine oxidase-cytochrome c assay for SOD.	Cyanides	36-43	cytochrome c, somatic	Homo sapiens	135-147
1646752-4	1991	We have assessed how interaction of cyanide and hydrogen peroxide with cytochrome c can lead to further errors in the xanthine oxidase-cytochrome c assay for SOD.	Cyanides	36-43	superoxide dismutase 2	Homo sapiens	158-161
2229052-0	1990	Transient spectroscopy of the reaction of cyanide with ferrous myoglobin.	Cyanides	42-49	myoglobin	Physeter catodon	63-72
1847831-0	1991	Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide.	Cyanides	32-39	myeloperoxidase	Homo sapiens	51-66
1847831-0	1991	Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide.	Cyanides	141-148	myeloperoxidase	Homo sapiens	51-66
1847831-0	1991	Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide.	Cyanides	141-148	myeloperoxidase	Homo sapiens	160-175
1647344-6	1991	Cyanide and thiosulphate inhibited ALA-D activity when both compounds were present in the incubation or the preincubation mixture.	Cyanides	0-7	aminolevulinate dehydratase	Homo sapiens	35-40
2229052-2	1990	The reaction of cyanide metmyoglobin with dithionite conforms to a two-step sequential mechanism with formation of an unstable intermediate, identified as cyanide bound ferrous myoglobin.	Cyanides	16-23	myoglobin	Physeter catodon	27-36
2229052-13	1990	A mechanism of control for the rate of dissociation of cyanide from ferrous myoglobin, involving protonation of the bound anion, is discussed.	Cyanides	55-62	myoglobin	Physeter catodon	76-85
2256111-0	1990	Cyanide-induced alteration of cytosolic pH: involvement of cellular hydrogen ion handling processes.	Cyanides	0-7	glucose-6-phosphate isomerase	Rattus norvegicus	40-42
2145276-14	1990	The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.	Cyanides	105-112	rhodopsin	Bos taurus	42-51
2165795-2	1990	The apparent intravascular decomposition of nitroprusside (SNP) has been attributed to photolysis and artefactual generation of cyanide (HCN) during assay, leading some workers to believe that large doses of SNP may be infused safely if light is excluded.	Cyanides	128-135	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	137-140
2376694-6	1990	Moreover, in dogs preloaded with HO-Cbl (20 micrograms/ml plasma), up to 10% of the cyanide administered as NaCN infusions was recovered in urine as CN-Cbl by 60 minutes, compared with less than 0.3% in dogs not treated with HO-Cbl.	Cyanides	84-91	Cbl proto-oncogene	Canis lupus familiaris	36-39
2158989-2	1990	The low-spin, cyanide-ligated ferric complex of the intact bovine granulocyte myeloperoxidase (MPO-CN) has been studied by proton nuclear magnetic resonance utilizing the nuclear Overhauser effect (NOE).	Cyanides	14-21	myeloperoxidase	Bos taurus	78-93
2337355-7	1990	Cyanide, which inhibited both catalase and peroxidase activities, bound the heme in a noncooperative manner.	Cyanides	0-7	catalase	Homo sapiens	30-38
2158989-2	1990	The low-spin, cyanide-ligated ferric complex of the intact bovine granulocyte myeloperoxidase (MPO-CN) has been studied by proton nuclear magnetic resonance utilizing the nuclear Overhauser effect (NOE).	Cyanides	14-21	myeloperoxidase	Bos taurus	95-98
2079230-5	1990	Example of interference were stimulation of xanthine oxidase activity, color formation without xanthine oxidase, color formation despite excess Cu-Zn SOD addition, and absorbance changes with cyanide inhibition of EC SOD that were above or below blank values.	Cyanides	192-199	superoxide dismutase 3	Rattus norvegicus	214-220
2317511-8	1990	Sulfane sulfurtransferase, like rhodanese, catalyzes the transfer of sulfur from thiosulfate to cyanide via a persulfide intermediate, and displays remarkably similar kinetics in this process (Aird, B.A., Heinrikson, R.L.	Cyanides	96-103	thiosulfate sulfurtransferase	Bos taurus	32-41
2154220-3	1990	The cytochrome P450 inhibitor cyanide abolished this activity.	Cyanides	30-37	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	4-19
34802936-1	2022	We have successfully synthesized NIRF as a near-infrared fluorescence probe for relay recognition of zinc and cyanide ions.	Cyanides	110-117	ubiquitin-like, containing PHD and RING finger domains 2	Mus musculus	33-37
2159465-0	1990	Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase.	Cyanides	21-28	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	78-98
2159465-2	1990	Cyanide binding to bovine heart cytochrome c oxidase at five redox levels has been investigated by use of infrared and visible-Soret spectra.	Cyanides	0-7	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	32-52
33810344-0	2021	ACTH(6-9)PGP Peptide Protects SH-SY5Y Cells from H2O2, tert-Butyl Hydroperoxide, and Cyanide Cytotoxicity via Stimulation of Proliferation and Induction of Prosurvival-Related Genes.	Cyanides	85-92	phosphoglycolate phosphatase	Homo sapiens	9-12
34619120-0	2022	Synthesis of gold nanoclusters-loaded lysozyme nanoparticles for ratiometric fluorescent detection of cyanide in tap water, cyanogenic glycoside-containing plants, and soils.	Cyanides	102-109	lysozyme	Homo sapiens	38-46
34619120-0	2022	Synthesis of gold nanoclusters-loaded lysozyme nanoparticles for ratiometric fluorescent detection of cyanide in tap water, cyanogenic glycoside-containing plants, and soils.	Cyanides	102-109	nuclear RNA export factor 1	Homo sapiens	113-116
34619120-2	2022	This study developed a straightforward strategy to prepare lysozyme nanoparticle-encapsulated gold nanoclusters (LysNP-AuNCs) as a dual-emission probe for the ratiometric sensing of cyanide through fluorescence resonance energy transfer (FRET) without the conjugation of additional fluorophores.	Cyanides	182-189	lysozyme	Homo sapiens	59-67
34619120-6	2022	The presence of cyanide triggered the etching of the AuNCs in the LysNP-AuNCs, leading to the suppression of FRET from lysozyme nanoparticle to AuNCs.	Cyanides	16-23	lysozyme	Homo sapiens	119-127
34619120-9	2022	The practicality of the proposed probe was evaluated by quantifying cyanide in tap water and soils and monitoring the liberation of hydrogen cyanide from cyanogenic glycoside-containing foods.	Cyanides	68-75	nuclear RNA export factor 1	Homo sapiens	79-82
34789405-5	2022	Furthermore, CTR displayed fluorescent and colorimetric response to cyanide.	Cyanides	68-75	calcitonin receptor	Homo sapiens	13-16
34904839-3	2022	To develop a lower cost and more widely available alternative to positron emission tomography (PET), two isocyanide-containing FAP inhibitors (CN-C5-FAPI and CN-PEG4-FAPI) were synthesized and radiolabeled with 99mTc to obtain (99mTc)(Tc-(CN-C5-FAPI)6)+ and (99mTc)(Tc-(CN-PEG4-FAPI)6)+ in high yields (>95%).	Cyanides	105-115	fibroblast activation protein alpha	Homo sapiens	127-130
34963029-1	2022	We herein report a cyanide-free continuous-flow process for cyanation of sp 2 and sp carbons to synthesize aryl, vinyl and acetylenic nitriles from (5-methyl-2-phenyloxazol-4-yl) boronic acid (OxBA) reagent as a sole source of carbon-bound masked -CN source.	Cyanides	19-26	Sp2 transcription factor	Homo sapiens	73-77
34963029-0	2022	Cyanide-Free Cyanation of sp2 and sp-Carbons by Oxazole based Masked CN Source Using Flow Microreactors.	Cyanides	0-7	Sp2 transcription factor	Homo sapiens	26-29
34741369-3	2021	Herein, we demonstrate that crystal morphology of a cyanide-bridged 2D-CP of type (Mn(salen)) 2 (ReN(CN) 4 ) ( 1 ) consisting of flexible undulating layers significantly impacts the layer configuration and assembly.	Cyanides	52-59	renin	Homo sapiens	97-100
34930834-6	2021	The SOD function of Cygb was inhibited by cyanide and CO that coordinate to Fe3+-Cygb and Fe2+-Cygb, respectively, suggesting that dismutation involves iron redox cycling, and this was confirmed by spectrophotometric titrations.	Cyanides	42-49	cytoglobin	Mus musculus	20-24
34930834-6	2021	The SOD function of Cygb was inhibited by cyanide and CO that coordinate to Fe3+-Cygb and Fe2+-Cygb, respectively, suggesting that dismutation involves iron redox cycling, and this was confirmed by spectrophotometric titrations.	Cyanides	42-49	cytoglobin	Mus musculus	81-85
34930834-6	2021	The SOD function of Cygb was inhibited by cyanide and CO that coordinate to Fe3+-Cygb and Fe2+-Cygb, respectively, suggesting that dismutation involves iron redox cycling, and this was confirmed by spectrophotometric titrations.	Cyanides	42-49	cytoglobin	Mus musculus	95-99
34580769-7	2021	Alternatively, cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO to yield a low-spin (S = 1/2) EPR signal that is distinct from that observed for cyanide/Cys-bound Fe(III)CDO, revealing differences in the active-site pockets between ADO and CDO.	Cyanides	15-22	2-aminoethanethiol (cysteamine) dioxygenase	Mus musculus	243-246
2153608-11	1990	These results support the belief that rhodanese plays a fundamental role in the detoxification process only when high levels of cyanide are administered.	Cyanides	128-135	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	38-47
34310360-4	2021	Sodium nitrite is used mostly in the food industry (as a preservative) and in medical field (as an antidote to cyanide poisoning), and if ingested in large enough amounts, it can be fatal.The ingestion of sodium nitrite can cause severe methemoglobinemia, which is a metabolic disorder characterized by an inability of hemoglobin (which gets oxidized into methemoglobin) to bind (and therefore carry) oxygen.	Cyanides	111-118	hemoglobin subunit gamma 2	Homo sapiens	356-369
34580769-7	2021	Alternatively, cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO to yield a low-spin (S = 1/2) EPR signal that is distinct from that observed for cyanide/Cys-bound Fe(III)CDO, revealing differences in the active-site pockets between ADO and CDO.	Cyanides	15-22	cysteine dioxygenase 1, cytosolic	Mus musculus	251-254
34580769-7	2021	Alternatively, cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO to yield a low-spin (S = 1/2) EPR signal that is distinct from that observed for cyanide/Cys-bound Fe(III)CDO, revealing differences in the active-site pockets between ADO and CDO.	Cyanides	156-163	general transcription factor IIE subunit 1	Homo sapiens	174-184
34580769-7	2021	Alternatively, cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO to yield a low-spin (S = 1/2) EPR signal that is distinct from that observed for cyanide/Cys-bound Fe(III)CDO, revealing differences in the active-site pockets between ADO and CDO.	Cyanides	156-163	cysteine dioxygenase 1, cytosolic	Mus musculus	251-254
34171736-5	2021	Under turnover conditions, the biosensor showed a linear response with the logarithm of cyanide concentration in the 5-76 muM (cyclic voltammetry) and 1-40 muM (square-wave voltammetry) ranges, with a sensitivity of 20-25% ln (cyanide muM)-1 and a detection limit of 0.86-4.4 muM.	Cyanides	88-95	PWWP domain containing 3A, DNA repair factor	Homo sapiens	235-241
34171736-5	2021	Under turnover conditions, the biosensor showed a linear response with the logarithm of cyanide concentration in the 5-76 muM (cyclic voltammetry) and 1-40 muM (square-wave voltammetry) ranges, with a sensitivity of 20-25% ln (cyanide muM)-1 and a detection limit of 0.86-4.4 muM.	Cyanides	227-234	PWWP domain containing 3A, DNA repair factor	Homo sapiens	235-241
34553913-2	2021	In this study, we report an unprecedented eta2 (side-on) coordination of U by a cyanide in a UCN cluster, which was stabilized inside a C82 fullerene cage.	Cyanides	80-87	DNA polymerase iota	Homo sapiens	42-46
34553913-2	2021	In this study, we report an unprecedented eta2 (side-on) coordination of U by a cyanide in a UCN cluster, which was stabilized inside a C82 fullerene cage.	Cyanides	80-87	urocortin	Homo sapiens	93-96
34390101-0	2021	Cyanides, Isocyanides, and Hydrides of Zn, Cd and Hg from Metal Atom and HCN Reactions: Matrix Infrared Spectra and Electronic Structure Calculations.	Cyanides	0-8	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	73-76
34519320-0	2021	Cu(OTf)2 catalyzed Ugi-type reaction of N,O-acetals with isocyanides for the synthesis of pyrrolidinyl and piperidinyl 2-carboxamides.	Cyanides	57-68	POU class 2 homeobox 2	Homo sapiens	0-8
34519320-1	2021	The Cu(OTf)2 catalyzed Ugi-type reactions of N,O-acetals with isocyanides have been described for the synthesis of pyrrolidinyl and piperidinyl 2-carboxamides.	Cyanides	62-73	POU class 2 homeobox 2	Homo sapiens	4-12
34390101-0	2021	Cyanides, Isocyanides, and Hydrides of Zn, Cd and Hg from Metal Atom and HCN Reactions: Matrix Infrared Spectra and Electronic Structure Calculations.	Cyanides	10-21	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	73-76
34360816-7	2021	Collectively, these data show that ME beta2-tanycytes exhibit early structural and chemical alterations due to HFD and reveal for the first-time hypothalamic cyanide presence following high dietary lipids consumption, which is a novel aspect with potential implications in the field of obesity.	Cyanides	158-165	G protein-coupled receptor 162	Mus musculus	38-43
34328332-3	2021	A less toxic cyanide reagent, Zn(CN)2, is utilized, and diverse functional groups and heterocycles are tolerated.	Cyanides	13-20	carnosine dipeptidase 2	Homo sapiens	30-37
34334797-2	2021	Cyano thioformaldehyde presents a series of prominent a- and b-type lines, which are the strongest previously unassigned features in our Q-band line survey of TMC-1.	Cyanides	0-5	transmembrane channel like 1	Homo sapiens	159-164
35482971-5	2022	Consequently, Pd/MIL-101-PPh3 exhibits excellent activity for the three-component reaction of 2-iodoaniline, CO2, and isocyanide, as well as Suzuki-Miyaura and Heck coupling reactions, far exceeding amino-functionalized Pd/MIL-101-NH2, naked Pd/MIL-101, and other commercial-supported Pd catalysts.	Cyanides	118-128	caveolin 1	Homo sapiens	25-29
34169954-0	2021	Spin and valence isomerism in cyanide-bridged {FeMII} (M = Fe and Co) clusters.	Cyanides	30-37	spindlin 1	Homo sapiens	0-4
34191493-3	2021	Therefore, we developed a new two-photon fluorescence imaging probe, PX-P, in which the triphenylamine and cyanide moieties can real-time sense peroxisomal polarity changes.	Cyanides	107-114	fibronectin type III domain containing 5	Mus musculus	69-73
35635289-2	2022	TPE-Lac acts as a sensitive sensor for the detection of cyanide ions (CN-) with an immediate turn-off response in the presence of many other interfering cations and anions.	Cyanides	56-63	lactase	Homo sapiens	4-7
35635289-4	2022	Cyanide detection in the solid phase was successfully demonstrated by drop-casting the solution of the TPE-Lac probe on TLC plates and measuring and analysing the fluorescence response by ImageJ analysis.	Cyanides	0-7	lactase	Homo sapiens	107-110
2558649-2	1989	The enzyme oxidized horse heart cytochrome C with a Vmax of 63 mumols/min/mg at 50 degrees C. The activity was sensitive to cyanide.	Cyanides	124-131	cytochrome c, somatic	Equus caballus	32-44
34927663-2	2022	Although eta2-imidoyl metal complexes, which are important intermediates in isocyanide chemistry, have been extensively explored, their boron species analogues have remained elusive.	Cyanides	76-86	DNA polymerase iota	Homo sapiens	9-13
35474139-4	2022	AtHNL catalyzes the reversible interconversion between cyanohydrins and derived carbonyl compounds with free cyanide.	Cyanides	109-116	methyl esterase 5	Arabidopsis thaliana	0-5
35377631-1	2022	The incorporation of two different cyanide building blocks of ((TpR)FeIII(CN)3)- and (AuI(CN)2)- into one molecule afforded a novel hexanuclear (FeIII2FeII2AuI2) complex (1 2Et2O), in which the cyanide-bridged (FeIII2FeII2) square was further grafted by two (AuI(CN)2)- fragments as long arms in syn orientations.	Cyanides	35-42	synemin	Homo sapiens	296-299
35377631-1	2022	The incorporation of two different cyanide building blocks of ((TpR)FeIII(CN)3)- and (AuI(CN)2)- into one molecule afforded a novel hexanuclear (FeIII2FeII2AuI2) complex (1 2Et2O), in which the cyanide-bridged (FeIII2FeII2) square was further grafted by two (AuI(CN)2)- fragments as long arms in syn orientations.	Cyanides	194-201	synemin	Homo sapiens	296-299
2519724-0	1989	Role of cytochrome P-450 IIE1 and catalase in the oxidation of acetonitrile to cyanide.	Cyanides	79-86	catalase	Rattus norvegicus	8-42
2539272-4	1989	Furthermore, cyanide was trapped in the erythrocytes and stabilized during the initial washing steps by conversion of hemoglobin to methemoglobin with inorganic nitrite.	Cyanides	13-20	hemoglobin subunit gamma 2	Homo sapiens	132-145
2539041-4	1989	The oxidized form of the modified cytochrome c-552 bound cyanide to the high-spin ferric heme with a rate constant of (2.1 +/- 0.1) X 10(3) M-1 s-1.	Cyanides	57-64	cytochrome c3 family protein	Pseudomonas stutzeri	34-46
2776771-3	1989	There was a marked compound dependence on induction of both cytochrome P-450-IVA1-dependent omega-hydroxylation of lauric acid and enzymes of the peroxisomal fatty acid beta-oxidation pathway (measured as cyanide-insensitive palmitoyl-CoA oxidation and enoyl-CoA hydratase).	Cyanides	205-212	cytochrome P450, family 4, subfamily a, polypeptide 1	Rattus norvegicus	60-81
2559376-2	1989	Cyanide concentrations between 10 and 200 microM rapidly depressed synaptic transmission between Schaffer collateral-commissural fibers and CA1 pyramidal cells.	Cyanides	0-7	carbonic anhydrase 1	Cavia porcellus	140-143
2559376-7	1989	In some experiments, postsynaptic responses in the gyrus dentatus (GD), evoked by perforant path stimulation, were recorded simultaneously with CA1 responses during cyanide application.	Cyanides	165-172	carbonic anhydrase 1	Cavia porcellus	144-147
2550034-0	1989	Cyanide binding to canine myeloperoxidase.	Cyanides	0-7	myeloperoxidase	Canis lupus familiaris	26-41
2550034-1	1989	Equilibria and kinetics of cyanide binding to canine myeloperoxidase were studied.	Cyanides	27-34	myeloperoxidase	Canis lupus familiaris	53-68
2919401-0	1989	The cyanide-metabolizing enzyme rhodanese in rat nasal respiratory and olfactory mucosa.	Cyanides	4-11	thiosulfate sulfurtransferase	Rattus norvegicus	32-41
2919401-3	1989	Experiments with rat nasal tissues showed that the cyanide-metabolizing enzyme, rhodanese, is present in high concentrations, particularly in the olfactory region.	Cyanides	51-58	thiosulfate sulfurtransferase	Rattus norvegicus	80-89
2922757-2	1989	The physiological function of rhodanese is controversial, but it and other sulfurtransferases can catalyze the conversion of cyanide to the much less toxic thiocyanate.	Cyanides	125-132	thiosulfate sulfurtransferase	Rattus norvegicus	30-39
2922757-9	1989	When thiosulfate was omitted, staining for rhodanese activity was still clearly identifiable in both liver and muscle sections with cyanide alone.	Cyanides	132-139	thiosulfate sulfurtransferase	Rattus norvegicus	43-52
2844603-1	1988	Cyanide binding with the oxidized resting Yonetani-type cytochrome c-oxidase followed spectrophotometrically reveals a relatively rapid initial phase the rate of which shows saturation behaviour with respect to [HCN] and secondary slower absorption changes to a first approximation independent of the ligand concentration.	Cyanides	0-7	cytochrome c, somatic	Homo sapiens	56-68
2972815-1	1988	Technetium-99m isonitrile myocardial perfusion imaging was employed in a patient undergoing thrombolytic therapy with recombinant tissue plasminogen activator for acute anteroseptal myocardial infarction.	Cyanides	15-25	chromosome 20 open reading frame 181	Homo sapiens	130-158
2461938-8	1988	All MABs recognized rhodanese that was oxidized with peroxide and allowed to undergo a secondary cyanide-dependent reaction which also resulted in a fluorescence shift and increased proteolytic susceptibility.	Cyanides	97-104	thiosulfate sulfurtransferase	Bos taurus	20-29
3170581-1	1988	The interaction of bovine liver rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) with the acceptor substrates, dithiothreitol or cyanide, was studied.	Cyanides	55-62	thiosulfate sulfurtransferase	Bos taurus	32-41
3170581-2	1988	When incubated in the presence of cyanide or dithiothreitol, rhodanese was inactivated in a time-dependent process.	Cyanides	34-41	thiosulfate sulfurtransferase	Bos taurus	61-70
3170581-6	1988	Substrate-potentiated inactivation of rhodanese (with cyanide) has been reported before, but the cause and nature of this interaction were unexplained.	Cyanides	54-61	thiosulfate sulfurtransferase	Bos taurus	38-47
2844603-1	1988	Cyanide binding with the oxidized resting Yonetani-type cytochrome c-oxidase followed spectrophotometrically reveals a relatively rapid initial phase the rate of which shows saturation behaviour with respect to [HCN] and secondary slower absorption changes to a first approximation independent of the ligand concentration.	Cyanides	0-7	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	212-215
2844603-2	1988	Oxidized cytochrome c greatly accelerates the initial phase of cyanide binding but does not affect significantly contribution or rate constant of the slow phase.	Cyanides	63-70	cytochrome c, somatic	Homo sapiens	9-21
2843226-0	1988	The possible role of the closed-open transition in proton pumping by cytochrome c oxidase: the pH dependence of cyanide inhibition.	Cyanides	112-119	cytochrome c, somatic	Homo sapiens	69-81
2843226-1	1988	The rate of oxidation of reduced cytochrome c catalyzed by cytochrome oxidase in the presence and absence of cyanide has been measured spectrophotometrically at pH 5.5, 6.4, 7.4 and 8.3.	Cyanides	109-116	cytochrome c, somatic	Homo sapiens	33-45
2835983-5	1988	Reaction of cyanide or azide ion with native thyroid peroxidase resulted in the loss of the axial EPR signal within several hours.	Cyanides	12-19	thyroid peroxidase	Homo sapiens	45-63
2457025-9	1988	Cytochrome c reduction was not inhibited by several mitochondrial respiratory chain inhibitors (azide, cyanide, and rotenone) but was sensitive to thiol-reactive agents (p-chloromercuribenzoate and monoiodo acetate).	Cyanides	103-110	cytochrome c, somatic	Homo sapiens	0-12
2842331-0	1988	Kinetics and activation parameters of the reaction of cyanide with free aquocobalamin and aquocobalamin bound to a haptocorrin from chicken serum.	Cyanides	54-61	transcobalamin 1	Homo sapiens	115-126
2842331-1	1988	The kinetics of the reaction of cyanide with free aquocobalamin (H2OCbl) and with aquocobalamin bound to a vitamin B12-binding protein (haptocorrin) from chicken serum (HC-H2OCbl) have been investigated as a function of temperature and pH.	Cyanides	32-39	transcobalamin 1	Homo sapiens	136-147
3225554-11	1988	This Na+-independent pHi recovery was not significantly affected by lowering [HEPES]o from 32 to 3 mM or by adding N"N"-dicyclohexylcarbodiimide (10(-4) M) to the lumen, but it was reduced approximately 57% by iodoacetate (0.5 mM) plus cyanide (1 mM).	Cyanides	236-243	glucose-6-phosphate isomerase	Oryctolagus cuniculus	21-24
3349028-9	1988	Salivary peroxidase is similar to bovine lactoperoxidase (LPO) in amino acid composition, in ultraviolet and visible spectrum, in reaction with cyanide, in susceptibility to 2-mercaptoethanol inactivation, and in thermal stability.	Cyanides	144-151	lactoperoxidase	Homo sapiens	0-19
2454843-1	1988	Imposition of a protonmotive force across the inner membrane of coupled cyanide-inhibited, beef heart mitochondria by addition of ATP causes reduction of cytochrome c and CuA with concomitant oxidation of haem aA.	Cyanides	72-79	cytochrome c, somatic	Homo sapiens	154-166
3170524-6	1988	Resonance Raman spectra of Mb coordinated with various sizes of isocyanides are interpreted in terms of vinyl orientational changes induced by ligation.	Cyanides	64-75	myoglobin	Homo sapiens	27-29
3355717-0	1988	Carbamylation of hemoglobin in vivo with chronic sublethal dietary cyanide: implications for hemoglobin S. Carbamylation of the hemoglobin in sickle cell anemia has been demonstrated to improve the status of this hemoglobinopathy.	Cyanides	67-74	HGB	Sus scrofa	17-27
3355717-2	1988	Throughout the study, the hematological status of all animals remained similar; however, the levels of carbamylated hemoglobin as measured by nanomoles of valine hydantoin varied proportionally to dietary sublethal cyanide intakes, indicating that these natural dietary levels could effect an important and presumably permanent modification of the hemoglobin"s beta chain.	Cyanides	215-222	HGB	Sus scrofa	116-126
2826445-6	1988	The glutamate-binding characteristics of these isolated protein fractions were very similar to those previously described for the 14-kDa GBP, including estimated dissociation constants for L-glutamate binding of 0.25 and 1 microM, inhibition of glutamate binding by azide and cyanide, and a selectivity of the ligand binding site for L-glutamate and L-aspartate.	Cyanides	276-283	transmembrane protein 132A	Rattus norvegicus	137-140
3349028-9	1988	Salivary peroxidase is similar to bovine lactoperoxidase (LPO) in amino acid composition, in ultraviolet and visible spectrum, in reaction with cyanide, in susceptibility to 2-mercaptoethanol inactivation, and in thermal stability.	Cyanides	144-151	lactoperoxidase	Bos taurus	41-56
3349028-9	1988	Salivary peroxidase is similar to bovine lactoperoxidase (LPO) in amino acid composition, in ultraviolet and visible spectrum, in reaction with cyanide, in susceptibility to 2-mercaptoethanol inactivation, and in thermal stability.	Cyanides	144-151	lactoperoxidase	Bos taurus	58-61
3426555-2	1987	The disubstituted ligands 2,6-dimethylphenylisonitrile and 2,6-diethylphenylisonitrile were found to bind to horse-heart myoglobin with affinities ranging from 500 to 5000 times greater than that of ethylisonitrile (4.6 x 10(-6) M) which has been the tightest binding isonitrile ligand for myoglobin thus far reported.	Cyanides	44-54	myoglobin	Equus caballus	121-130
2854389-4	1988	Cyanide binding to CuA-modified cytochrome c oxidase during turnover suggests that reduction of cytochrome a leads to exposure of the cytochrome a3-CuB binuclear center to incoming ligands.	Cyanides	0-7	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	32-52
3426555-2	1987	The disubstituted ligands 2,6-dimethylphenylisonitrile and 2,6-diethylphenylisonitrile were found to bind to horse-heart myoglobin with affinities ranging from 500 to 5000 times greater than that of ethylisonitrile (4.6 x 10(-6) M) which has been the tightest binding isonitrile ligand for myoglobin thus far reported.	Cyanides	44-54	myoglobin	Equus caballus	290-299
3660418-6	1987	These results suggest lipid peroxidation of neuronal membranes play a role in cyanide intoxication and this action is related to altered regulation of neuronal calcium homeostasis and activation of xanthine oxidase.	Cyanides	78-85	xanthine dehydrogenase	Mus musculus	198-214
2827630-4	1987	Comparison of steady-state measurements obtained by absorbance and fluorescence spectroscopy in the presence and in the absence of cyanide show that it is the reduction of cytochrome a and/or CuA that triggers a conformational change: this increases the zinc cytochrome c to acceptor (most probably cytochrome a itself) distance by some 0.5 nm.	Cyanides	131-138	cytochrome c, somatic	Homo sapiens	259-271
3663637-2	1987	Rp1 (percent) values were 53 (pH 5.5) and 52 (pH 7.0) for cyanide and 38 (pH 5.5) and 32 (pH 7.0) for azide, while Rp2 (percent) values were 98 (pH 5.5) and 96 (pH 7.0) for azide.	Cyanides	58-65	RP1 axonemal microtubule associated	Homo sapiens	0-3
3040708-0	1987	Proton hyperfine resonance assignments in cyanide-ligated cytochrome c peroxidase using the nuclear Overhauser effect.	Cyanides	42-49	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	58-81
3040708-1	1987	The development of the proton nuclear Overhauser effect (NOE) for hyperfine shifted resonances of cyanide-ligated cytochrome c peroxidase (Saccharomyces cerevisiae) has been studied.	Cyanides	98-105	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	114-137
2825485-4	1987	Human and rat PMN also show a similar depletion of endogenous LTB4; but unlike the guinea pig PMN, exogenous LTB4 is rapidly oxygenated to the omega hydroxy- and carboxy-LTB4 by mechanisms unaffected by cyanide.	Cyanides	203-210	prostaglandin reductase 1	Cavia porcellus	109-113
2825485-4	1987	Human and rat PMN also show a similar depletion of endogenous LTB4; but unlike the guinea pig PMN, exogenous LTB4 is rapidly oxygenated to the omega hydroxy- and carboxy-LTB4 by mechanisms unaffected by cyanide.	Cyanides	203-210	prostaglandin reductase 1	Cavia porcellus	109-113
2825485-6	1987	That the myeloperoxidase may be responsible for the depletion of LTB4 has not been eliminated and is suspected due to the cyanide inhibitable nature of this phenomenon.	Cyanides	122-129	myeloperoxidase	Cavia porcellus	9-24
2825485-6	1987	That the myeloperoxidase may be responsible for the depletion of LTB4 has not been eliminated and is suspected due to the cyanide inhibitable nature of this phenomenon.	Cyanides	122-129	prostaglandin reductase 1	Cavia porcellus	65-69
3606208-0	1987	Changes in plasma, liver, and ovary vitellogenin in landlocked Atlantic salmon following exposure to sublethal cyanide.	Cyanides	111-118	vitellogenin	Salmo salar	36-48
3663604-2	1987	The Raman spectra of ferric cytochrome P-450scc complexed with inhibitors such as cyanide, phenyl isocyanide, aminoglutethimide, and metyrapone were characteristic of low-spin state and were very similar.	Cyanides	82-89	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	28-47
3590232-1	1987	Cyanide was detected as a product of cyanamide oxidation by bovine liver catalase in vitro under conditions that also produced an active aldehyde dehydrogenase (AlDH) inhibitor.	Cyanides	0-7	catalase	Bos taurus	73-81
2853945-3	1987	Choline acetyltransferase activity was reduced significantly from control values at cyanide concentrations greater than 100 microM; there were similar reductions on a percentage basis in high-affinity uptake of beta-alanine and GABA and in clonazepam-displaceable benzodiazepine (BDZ) binding which reflected the neuronal BDZ receptor population.	Cyanides	84-91	choline acetyltransferase	Mus musculus	0-25
3590232-2	1987	Cyanide formation was directly related to both cyanamide and catalase concentrations and was also dependent on incubation time.	Cyanides	0-7	catalase	Bos taurus	61-69
3590232-0	1987	Cyanide is a product of the catalase-mediated oxidation of the alcohol deterrent agent, cyanamide.	Cyanides	0-7	catalase	Bos taurus	28-36
3590232-4	1987	Cyanide formation was blocked by ethanol, a known substrate for catalase Compound I.	Cyanides	0-7	catalase	Bos taurus	64-72
3576625-1	1987	Pyridoxal 5"-phosphate (PLP), the active form of vitamin B6, readily forms complexes with a wide variety of potentially toxic substances, including cyanide (KCN), spermine (SPM), gentamicin (GM), and dopamine (DOP).	Cyanides	148-155	pyridoxal phosphatase	Homo sapiens	24-27
3106087-0	1987	The generation of an organic free radical in substrate-reduced pig kidney diamine oxidase-cyanide.	Cyanides	90-97	amine oxidase copper containing 1	Sus scrofa	74-89
3106087-1	1987	When the cyanide complex of the copper protein, pig kidney diamine oxidase, is reduced anaerobically by cadaverine (1,5-diaminopentane), the broad, 480 nm, absorption band characteristic of the resting enzyme is bleached and a new absorption spectrum with features at 457, 429, 403 (shoulder), 360 (shoulder) and 332 nm appears.	Cyanides	9-16	amine oxidase copper containing 1	Sus scrofa	59-74
3106087-3	1987	The g values and hyperfine splittings are similar to those previously assigned to a free radical observed when the cyanide complex of lentil seedling diamine oxidase is reacted with the substrate p-dimethylaminomethylbenzylamine [(1984) FEBS Lett.	Cyanides	115-122	amine oxidase copper containing 1	Sus scrofa	150-165
3556837-6	1987	BSO reduced the cellular GSH content by greater than 80%, but did not appear to affect the metabolism of acetonitrile: the liberation of cyanide correlated with cytochrome P-450, and not GSH, concentrations.	Cyanides	137-144	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	161-177
3829379-1	1987	We studied the kinetics of the reaction of cyanide with methemoglobin (mHb), used the information to develop a fast kinetic method for quantifying methemoglobin, then used that method to quantify hemoglobin (Hb) in whole blood based on the reaction with ferricyanide to produce mHb.	Cyanides	43-50	hemoglobin subunit gamma 2	Homo sapiens	56-69
3038442-2	1987	Catalase, azide, cyanide and three aminoacids employed as quenchers of ClO, significantly inhibited this nonspecific cytotoxicity (NSC), suggesting an important role for the myeloperoxidase (MPO) system.	Cyanides	17-24	myeloperoxidase	Homo sapiens	174-189
3793732-14	1987	Significant kinetic heterogeneity was observed only for long-chain isonitrile binding to newly reconstituted myoglobin, and even in these cases, the rate constants for the abnormal and normal heme conformations differed by less than a factor of 4.	Cyanides	67-77	myoglobin	Physeter catodon	109-118
3426683-5	1987	Induction of the cytochrome P-450 enzymes by phenobarbital (PB) pretreatment doubled the yield of cyanide, while SKF-525A blocked this PB-induced increase.	Cyanides	98-105	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	17-33
3426683-7	1987	These results suggest that while catalase is responsible in major part for the oxidation of cyanamide to cyanide by uninduced microsomes, the participation of the hepatic cytochrome P-450 enzymes cannot be ruled out in PB-induced microsomes.	Cyanides	105-112	catalase	Rattus norvegicus	33-41
3023317-0	1986	Cyanide binding to bovine heart cytochrome c oxidase depleted of subunit III by treatment with lauryl maltoside.	Cyanides	0-7	LOC104968582	Bos taurus	32-44
3011897-3	1986	Detoxification required each component of the myeloperoxidase system and was prevented by the addition of agents that inhibit heme enzymes (azide, cyanide) or degrade H2O2 (catalase).	Cyanides	147-154	myeloperoxidase	Homo sapiens	46-61
3019258-0	1986	The effect of sublethal cyanide exposure on plasma vitellogenin levels in rainbow trout (Salmo gairdneri) during early vitellogenesis.	Cyanides	24-31	LOC100136735	Oncorhynchus mykiss	51-63
3530615-9	1986	Nitrites convert hemoglobin to methemoglobin, which reacts with cyanide to form cyanomethemoglobin.	Cyanides	64-71	hemoglobin subunit gamma 2	Homo sapiens	31-44
3730393-3	1986	The proton NMR spectrum of the cyanide derivative of the purified prosthetic group which decomposes upon extraction from the protein was found to be the same as that of the cyanide derivative of the prosthetic group extracted from myoglobin and a sample prepared from hemin-Cl.	Cyanides	31-38	myoglobin	Homo sapiens	231-240
3730393-3	1986	The proton NMR spectrum of the cyanide derivative of the purified prosthetic group which decomposes upon extraction from the protein was found to be the same as that of the cyanide derivative of the prosthetic group extracted from myoglobin and a sample prepared from hemin-Cl.	Cyanides	173-180	myoglobin	Homo sapiens	231-240
2941899-10	1986	The slow rate of cyanide release due to spontaneous hydrolysis interfered with the determinations of alcohol dehydrogenase activity, but it cannot account for the rapid action and high toxicity of the cyanohydrins in vivo, or for the efficacy of the treatment regimens which protected against death.	Cyanides	17-24	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	101-122
3741137-4	1986	14C-PCBD-NAC uptake was temperature dependent and reduced by the metabolic inhibitors cyanide and iodoacetate.	Cyanides	86-93	pterin-4 alpha-carbinolamine dehydratase 1	Rattus norvegicus	4-8
3514426-0	1986	Inhibition and adaptation of red cell glucose-6-phosphate dehydrogenase (G6PD) in vivo to chronic sublethal dietary cyanide in an animal model.	Cyanides	116-123	glucose-6-phosphate dehydrogenase	Homo sapiens	38-71
3705622-3	1986	For the hydrogen peroxide-cytochrome P-450-promoted oxidation, cyanide, but not carbon monoxide, was an effective inhibitor of all the reactions.	Cyanides	63-70	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	26-42
3514426-0	1986	Inhibition and adaptation of red cell glucose-6-phosphate dehydrogenase (G6PD) in vivo to chronic sublethal dietary cyanide in an animal model.	Cyanides	116-123	glucose-6-phosphate dehydrogenase	Homo sapiens	73-77
3004496-3	1986	The ability of Ru(NH3)6(2+) and phenazine methosulfate to support the generation of delta psi by cytochrome c-oxidase correlates with their effectiveness as electron donors to cytochrome a in the cyanide-inhibited membrane-bound enzyme.	Cyanides	196-203	cytochrome c, somatic	Homo sapiens	97-109
3571848-1	1986	Resting neutrophils possess cytosolic cyanide-sensitive (CNs) superoxide dismutase (SOD) and cyanide-insensitive (CNi) SOD, located in an undefined organelle of the 27,000 g sedimentable fraction of its homogenate.	Cyanides	38-45	superoxide dismutase 1	Homo sapiens	62-82
3029209-4	1986	Cyanide, an inhibitor of both catalase and superoxide dismutase, stimulated chemiluminescence in 50% at a concentration (0.15 mM) which is much closer from the Ki for superoxide dismutase (0.25 mM) than from the Ki for catalase (15 microM).	Cyanides	0-7	catalase	Homo sapiens	30-38
3029209-4	1986	Cyanide, an inhibitor of both catalase and superoxide dismutase, stimulated chemiluminescence in 50% at a concentration (0.15 mM) which is much closer from the Ki for superoxide dismutase (0.25 mM) than from the Ki for catalase (15 microM).	Cyanides	0-7	catalase	Homo sapiens	219-227
3571848-1	1986	Resting neutrophils possess cytosolic cyanide-sensitive (CNs) superoxide dismutase (SOD) and cyanide-insensitive (CNi) SOD, located in an undefined organelle of the 27,000 g sedimentable fraction of its homogenate.	Cyanides	38-45	superoxide dismutase 1	Homo sapiens	84-87
4084587-6	1985	This difference in behavior, as well as the slower overall association rate of n-butyl isocyanide to myoglobin, can be rationalized as arising from distortion of the protein structure by the larger isocyanide ligand along the binding pathway.	Cyanides	87-97	myoglobin	Homo sapiens	101-110
2995315-5	1985	Succinate-reduced cytochrome c was oxidized by oxygen via a cyanide-sensitive, membrane-associated system.	Cyanides	60-67	cytochrome c, somatic	Equus caballus	18-30
2995315-6	1985	NADPH-reduced cytochrome c was oxidized by a cyanide-insensitive system.	Cyanides	45-52	cytochrome c, somatic	Equus caballus	14-26
2995315-7	1985	Partially purified carbon monoxide-binding cytochrome c, isolated from the cytoplasm, could serve as electron acceptor for NADPH-cytochrome c oxidoreductase; the reduced cytochrome was oxidized by oxygen by a cyanide-insensitive system present in the cytoplasmic fraction.	Cyanides	209-216	cytochrome c, somatic	Equus caballus	43-55
2995315-7	1985	Partially purified carbon monoxide-binding cytochrome c, isolated from the cytoplasm, could serve as electron acceptor for NADPH-cytochrome c oxidoreductase; the reduced cytochrome was oxidized by oxygen by a cyanide-insensitive system present in the cytoplasmic fraction.	Cyanides	209-216	cytochrome c, somatic	Equus caballus	129-141
2995315-8	1985	Horse heart cytochrome c was also reducible by NADPH and by succinate; the reduced cytochrome was oxidized by a cyanide-sensitive system in the membrane fraction.	Cyanides	112-119	cytochrome c, somatic	Equus caballus	12-24
4059037-7	1985	10(-1) M cyanide, applied after superfusion of the brain cortex with oxygen saturated CSF resulted in comparable NAD reduction to that produced by "non flow anoxia".	Cyanides	9-16	colony stimulating factor 2	Homo sapiens	86-89
2992394-4	1985	In contrast, the broadening of the NMR signals for the heme and methionine-80 methyl groups and the conformational transition in the vicinity of the heme moiety on change from the native to the cyanide-bound or urea-denatured form of cytochrome c showed a similar binding-ratio dependence to the rate constants for the oxidation and reduction reactions.	Cyanides	194-201	cytochrome c, somatic	Homo sapiens	234-246
2996621-1	1985	Interaction between methemoglobin and cyanide was studied by low temperature inhibition method in combination with ESR.	Cyanides	38-45	hemoglobin subunit gamma 2	Homo sapiens	20-33
4032476-1	1985	A molecular model for the protein and ambient solvent of the complex of cyanide with methemoglobin V from the sea lamprey Petromyzon marinus yields an R-factor of 0.142 against X-ray diffraction data to 2.0 A resolution.	Cyanides	72-79	hemoglobin subunit gamma 2	Homo sapiens	85-98
4032476-9	1985	The environment of the heme in the cyanide complex of lamprey methemoglobin resembles the deoxy state of the mammalian tetramer.	Cyanides	35-42	hemoglobin subunit gamma 2	Homo sapiens	62-75
3997841-7	1985	Cyanide and iron-chelators strikingly inhibit the 5-desaturase activity, thus suggesting that 5-desaturase is a metalloenzyme as are other well-characterized cytochrome b5-dependent oxidases.	Cyanides	0-7	cytochrome b5 type A	Rattus norvegicus	158-171
2579678-9	1985	Moreover, uptake and degradation of alpha 2-macroglobulin X trypsin was much more sensitive than insulin to the action of metabolic inhibitors such as dinitrophenol and cyanide.	Cyanides	169-176	alpha-2-macroglobulin	Rattus norvegicus	36-57
4026577-5	1985	After receiving each nitrile, the mean survival time of mice pretreated with CCl4 was prolonged and their brain cyanide level decreased when compared with the corresponding control.	Cyanides	112-119	chemokine (C-C motif) ligand 4	Mus musculus	77-81
4026577-8	1985	Microsomal metabolism of nitriles to cyanide was greatly inhibited when microsomes were prepared from livers of mice pretreated with CCl4.	Cyanides	37-44	chemokine (C-C motif) ligand 4	Mus musculus	133-137
3922372-0	1985	Different effects of cyanide on the activities of 7-ethoxycoumarin O-deethylation catalyzed by two forms of cytochrome P-450 purified from 3-methylcholanthrene-treated rats.	Cyanides	21-28	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	108-124
3922372-1	1985	The effect of cyanide on 7-ethoxycoumarin O-deethylation by two cytochrome P-450 isozymes obtained from 3-methylcholanthrene treated rat liver microsomes was investigated.	Cyanides	14-21	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	64-80
3922372-2	1985	7-Ethoxycoumarin O-deethylation was stimulated by the addition of cyanide to a reconstituted monooxygenase system consisting of NADPH, dilauroyl 3-L-phosphatidylcholine, NADPH-cytochrome P-450 reductase and MC P-448(2) (low spin form of cytochrome).	Cyanides	66-73	cytochrome p450 oxidoreductase	Rattus norvegicus	170-202
3978792-4	1985	Cyanide added to whole blood was bound to a saturable component in erythrocytes, which we identified as methemoglobin.	Cyanides	0-7	hemoglobin subunit gamma 2	Homo sapiens	104-117
2981925-12	1985	The addition of cyanide at various times interrupted lysis at once, indicating a requirement for ongoing myeloperoxidase-dependent reactions.	Cyanides	16-23	myeloperoxidase	Homo sapiens	105-120
2986860-4	1985	However higher concentrations of azide and cyanide prevented binding without affecting the respiratory burst indicating that myeloperoxidase is a catalyst for the binding.	Cyanides	43-50	myeloperoxidase	Bos taurus	125-140
4018534-0	1985	The binding of isocyanides to cytochrome P-450 from mouse hepatic microsomes.	Cyanides	15-26	cytochrome P450, family 21, subfamily a, polypeptide 1	Mus musculus	30-46
2981586-3	1985	Recovery of B12 binding protein from neutrophils exposed to phorbol myristate acetate or opsonized zymosan was significantly enhanced on addition of heme enzyme inhibitors (azide, cyanide) or catalase or when halide-free medium was used.	Cyanides	180-187	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	12-15
4018534-1	1985	The spectral interactions of a number of isocyanides with cytochrome P-450 were investigated.	Cyanides	41-52	cytochrome P450, family 21, subfamily a, polypeptide 1	Mus musculus	58-74
4018535-0	1985	Spectral interactions of piperonyl butoxide and isocyanides with purified hepatic cytochrome P-450 from uninduced mice.	Cyanides	48-59	cytochrome P450, family 21, subfamily a, polypeptide 1	Mus musculus	82-98
4018535-1	1985	The binding of isocyanides and the metabolites of piperonyl butoxide (PBO) to reduced cytochrome P-450 in intact microsomes gives rise to the type III optical difference spectrum which is characterized by two pH dependent peaks in the Soret region.	Cyanides	15-26	cytochrome P450, family 21, subfamily a, polypeptide 1	Mus musculus	86-102
6099695-3	1984	The enzymatic mitochondrial CCl4 activation operates more efficiently under anaerobic conditions; it requires NADPH, is CO sensitive, is inducible by phenobarbital pretreatment and is only weakly inhibited by high concentrations of cyanide or azide.	Cyanides	232-239	C-C motif chemokine ligand 4	Rattus norvegicus	28-32
6094249-1	1984	The decay rate of the excited triplet state of Zn cytochrome c was enhanced by electron acceptors including methyl viologen and ferric complexes of cyanide, oxalate, EDTA and cytochrome c at room temperature.	Cyanides	148-155	cytochrome c, somatic	Homo sapiens	50-62
6095975-3	1984	The optical absorption of P. mirabilis PR catalase in the presence of various anionic species (cyanide, azide, formate) was examined.	Cyanides	95-102	catalase	Bos taurus	42-50
6096396-5	1984	Phagocytic SOD in PMNs and monocytes of leprotic patients was both host and bacillus derived, because the presence of cyanide, to which human-derived cuprozinc SOD is susceptible, did not completely abrogate SOD activity.	Cyanides	118-125	superoxide dismutase 1	Homo sapiens	11-14
6096396-5	1984	Phagocytic SOD in PMNs and monocytes of leprotic patients was both host and bacillus derived, because the presence of cyanide, to which human-derived cuprozinc SOD is susceptible, did not completely abrogate SOD activity.	Cyanides	118-125	superoxide dismutase 1	Homo sapiens	160-163
6096396-5	1984	Phagocytic SOD in PMNs and monocytes of leprotic patients was both host and bacillus derived, because the presence of cyanide, to which human-derived cuprozinc SOD is susceptible, did not completely abrogate SOD activity.	Cyanides	118-125	superoxide dismutase 1	Homo sapiens	160-163
6090506-3	1984	Inactivation of MPO with heat or with cyanide ion prevented light production.	Cyanides	38-45	myeloperoxidase	Homo sapiens	16-19
6092276-8	1984	The NADP formation associated with a dense granule fraction observed previously in our laboratory was probably due to a cyanide-stimulated oxidation of NADPH by myeloperoxidase.	Cyanides	120-127	myeloperoxidase	Homo sapiens	161-176
6593495-1	1984	In mammals the major portion of cyanide is converted to thiocyanate by the liver enzyme thiosulfate sulfur transferase (TST) (rhodanese).	Cyanides	32-39	thiosulfate sulfurtransferase	Homo sapiens	88-118
6593495-1	1984	In mammals the major portion of cyanide is converted to thiocyanate by the liver enzyme thiosulfate sulfur transferase (TST) (rhodanese).	Cyanides	32-39	thiosulfate sulfurtransferase	Homo sapiens	120-123
6331509-8	1984	The pH-dependence of the dissociation constant of the myeloperoxidase-chloride complex obtained from the spectral changes induced by chloride is the same as observed in the inhibition by chloride of the binding of cyanide.	Cyanides	214-221	myeloperoxidase	Homo sapiens	54-69
6331509-0	1984	A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide.	Cyanides	82-89	myeloperoxidase	Homo sapiens	46-61
6331509-6	1984	The binding of cyanide to myeloperoxidase (k1 = (1.30 +/- 0.05) X 10(6) M-1 X s-1) is also regulated by an acid/base group with a pKa of 4.00 +/- 0.05 as is the case with hydrogen peroxide; also, only the protonated uncharged form of cyanide reacts with the enzyme.	Cyanides	15-22	myeloperoxidase	Homo sapiens	26-41
6331509-6	1984	The binding of cyanide to myeloperoxidase (k1 = (1.30 +/- 0.05) X 10(6) M-1 X s-1) is also regulated by an acid/base group with a pKa of 4.00 +/- 0.05 as is the case with hydrogen peroxide; also, only the protonated uncharged form of cyanide reacts with the enzyme.	Cyanides	234-241	myeloperoxidase	Homo sapiens	26-41
6331511-1	1984	Complex formation between ferricytochrome c and cytochrome c peroxidase inhibits the rate of cyanide binding by ferricytochrome c nearly 90%.	Cyanides	93-100	cytochrome c, somatic	Homo sapiens	31-43
6331509-7	1984	From their effects on the binding of cyanide to the enzyme it is concluded that chloride and thiocyanate bind to myeloperoxidase only when the acid/base group is protonated.	Cyanides	37-44	myeloperoxidase	Homo sapiens	113-128
6319404-5	1984	Dopamine beta-hydroxylase was also inhibited under these reaction conditions but the amount of cyanide produced was insufficient to account for the extent of enzyme inhibition.	Cyanides	95-102	dopamine beta-hydroxylase	Homo sapiens	0-25
11539605-0	1984	Cyanide and isocyanide abundances in the cold, dark cloud TMC-1.	Cyanides	0-7	transmembrane channel like 1	Homo sapiens	58-63
11539605-0	1984	Cyanide and isocyanide abundances in the cold, dark cloud TMC-1.	Cyanides	12-22	transmembrane channel like 1	Homo sapiens	58-63
6327443-1	1984	The mechanism of action of nitrite-thiosulfate (Chen et al., 1933a ,b; Hug , 1933) in the antagonism of the lethal effects of cyanide is much more complex than proposed 50 years ago.	Cyanides	126-133	ciliogenesis and planar polarity effector complex subunit 1	Homo sapiens	71-74
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	198-205	dopamine beta-hydroxylase	Homo sapiens	13-38
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	198-205	dopamine beta-hydroxylase	Homo sapiens	158-183
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	198-205	dopamine beta-hydroxylase	Homo sapiens	158-183
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	198-205	dopamine beta-hydroxylase	Homo sapiens	158-183
6319404-10	1984	Tyramine stabilized [14C]cyanide binding to dopamine beta-hydroxylase, consistent with the lack of enzyme reactivation observed under certain conditions (Colombo, G., Giedroc, D. P., Rajashekhar, B., and Villafranca, J. J.	Cyanides	25-32	dopamine beta-hydroxylase	Homo sapiens	44-69
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	116-123	dopamine beta-hydroxylase	Homo sapiens	13-38
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	116-123	dopamine beta-hydroxylase	Homo sapiens	158-183
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	116-123	dopamine beta-hydroxylase	Homo sapiens	158-183
6319404-14	1984	EPR data for dopamine beta-hydroxylase-bound Cu2+ directly demonstrated that a quaternary complex with tyramine and cyanide was formed, since the spectrum of dopamine beta-hydroxylase-Cu2+-tyramine-cyanide is distinct from that of dopamine beta-hydroxylase-Cu2+-cyanide and dopamine beta-hydroxylase-Cu2+-tyramine.	Cyanides	116-123	dopamine beta-hydroxylase	Homo sapiens	158-183
6319070-3	1984	Palmitoylcarnitine and palmitoyl-CoA oxidation were measured spectrophotometrically by following the reduction of added cytochrome c in the presence of cyanide.	Cyanides	152-159	cytochrome c, somatic	Homo sapiens	120-132
6639949-8	1983	Hyperporphyrin (split Soret) cytochrome P-450 complexes with thiolates, phosphines and cyanide trans to cysteinate have complex CD spectra, reflecting the intrinsic non-degeneracy of the Soret pi pi transitions.	Cyanides	87-94	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	29-45
6693427-17	1984	These data suggest at least two inactivation mechanisms by benzyl cyanides: 1) formation of a tightly bound or covalent adduct between dopamine beta-hydroxylase and enzyme-bound mandelonitrile (or a rearranged form of this molecule), and 2) reversible inhibition resulting from cyanide binding to enzyme-Cu2+.	Cyanides	66-73	dopamine beta-hydroxylase	Homo sapiens	135-160
6717088-4	1984	Activity of total and cyanide-insensitive superoxide dismutase decreased during the last trimester of life.	Cyanides	22-29	superoxide dismutase	Musca domestica	42-62
6318832-8	1984	EPR spectroscopy of low-spin cyanide and azide derivatives of eosinophil peroxidase, lactoperoxidase, myeloperoxidase and catalase revealed that the haem-ligand structure of eosinophil peroxidase is closely related to lactoperoxidase, whereas that of myeloperoxidase shows great resemblance to catalase.	Cyanides	29-36	eosinophil peroxidase	Homo sapiens	62-83
6318832-8	1984	EPR spectroscopy of low-spin cyanide and azide derivatives of eosinophil peroxidase, lactoperoxidase, myeloperoxidase and catalase revealed that the haem-ligand structure of eosinophil peroxidase is closely related to lactoperoxidase, whereas that of myeloperoxidase shows great resemblance to catalase.	Cyanides	29-36	catalase	Homo sapiens	122-130
6318832-8	1984	EPR spectroscopy of low-spin cyanide and azide derivatives of eosinophil peroxidase, lactoperoxidase, myeloperoxidase and catalase revealed that the haem-ligand structure of eosinophil peroxidase is closely related to lactoperoxidase, whereas that of myeloperoxidase shows great resemblance to catalase.	Cyanides	29-36	eosinophil peroxidase	Homo sapiens	174-195
6386168-6	1984	In primary XTH cells but not in XTH-2 cells cyanide disintegrates most of the actin fibres during 3 h of treatment.	Cyanides	44-51	actin like 6A S homeolog	Xenopus laevis	78-83
6386168-7	1984	This effect is independent of the inhibition of respiration, since actin gels prepared from skeletal muscle also undergo destruction in the presence of cyanide.	Cyanides	152-159	actin like 6A S homeolog	Xenopus laevis	67-72
18963533-3	1984	Cyanide in industrial waste water and in sea-water is determined after distillation as HCN from the sample and collection in sodium hydroxide solution.	Cyanides	0-7	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	87-90
6311631-1	1983	Cyanide-promoted inactivation of the enzyme rhodanese [thiosulfate sulfurtransferase (EC 2.8.1.1)] in the presence of ketoaldehydes is caused by reduced forms of molecular oxygen generated during autoxidation of the reaction products.	Cyanides	0-7	thiosulfate sulfurtransferase	Homo sapiens	55-84
6318748-4	1983	The inhibitory activity of E-3 in the model system is blocked by 1 mM KCN while E-1 is only slightly cyanide sensitive.	Cyanides	101-108	transcription factor E1	Glycine max	80-83
6873225-4	1983	The enzyme was characterized as a copper- and zinc-containing, cyanide-sensitive, superoxide dismutase with a molecular weight of 36,000 (estimated by get filtration), consisting of two subunits of 17,000 Mr (estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis).	Cyanides	63-70	Tsp_12552	Trichinella spiralis	82-102
6626606-2	1983	In the cyanide-inhibited submitochondrial particles of bovine heart, HOQNO strongly stimulates cytochrome b reduction by ascorbate in the presence of redox mediators, e. g. N,N,N",N"-tetramethylparaphenylene diamine, 2,6-dichlorophenolindophenol, diaminodurol and phenazine methosulfate; this effect can be reversed by antimycin.	Cyanides	7-14	cytochrome b	Bos taurus	95-107
6357925-6	1983	Epidemiological evidence (differing sex ratios, excess of smokers) indicates that defective cyanide metabolism may contribute to the development of sub-acute combined degeneration of the cord in vitamin B12 deficiency.	Cyanides	92-99	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	203-206
6301583-4	1983	At subsaturating concentrations of 3H-FMLP (20 nM), 1 mM cyanide (KCN) increased the binding of 3H-FMLP to human neutrophils (PMN) by 51% +/- 12%.	Cyanides	57-64	formyl peptide receptor 1	Homo sapiens	38-42
6301583-4	1983	At subsaturating concentrations of 3H-FMLP (20 nM), 1 mM cyanide (KCN) increased the binding of 3H-FMLP to human neutrophils (PMN) by 51% +/- 12%.	Cyanides	57-64	formyl peptide receptor 1	Homo sapiens	99-103
6133865-9	1983	The patterns of altered tryptic susceptibility and cyanide cleavage suggested that multimer formation is mediated by both sulfhydryls of fibronectin.	Cyanides	51-58	fibronectin 1	Homo sapiens	137-148
6830827-3	1983	We can show that cyanide inhibits the rate of exhaustion of NADH, and therefore reoxidation of cytochrome b5 by microsomes, and that stearoyl CoA enhances the rate of reoxidation of the cytochrome.	Cyanides	17-24	cytochrome b5 type A	Rattus norvegicus	95-108
6404306-8	1983	The inhibition of human carbonic anhydrase B by several industrial batches of acetonitrile agrees completely with the spectrophotometrically determined cyanide content of these batches.	Cyanides	152-159	carbonic anhydrase 2	Homo sapiens	24-44
6300255-2	1983	Inhibition by anaerobiosis, azide, cyanide, halide-free conditions, catalase, histidine, and tryptophan suggested mediation of hyphal damage primarily through the myeloperoxidase system.	Cyanides	35-42	myeloperoxidase	Homo sapiens	163-178
6838894-10	1983	The MCD spectra of bovine liver catalase and its cyanide adduct have been recorded in the Soret, visible and near infrared regions.	Cyanides	49-56	catalase	Bos taurus	32-40
6296068-0	1983	Temperature and pH dependence of the proton magnetic hyperfine resonances of cytochrome c peroxidase-cyanide.	Cyanides	101-108	cytochrome c, somatic	Homo sapiens	77-89
6292103-9	1982	Damage to hyphae by the myeloperoxidase system was inhibited by azide, cyanide, catalase, histidine, and tryptophan, but not by superoxide dismutase, dimethyl sulfoxide, or mannitol.	Cyanides	71-78	myeloperoxidase	Homo sapiens	24-39
6301562-0	1983	[Acceleration by cytochrome c of cyanide binding to oxidized cytochrome c oxidase].	Cyanides	33-40	cytochrome c, somatic	Homo sapiens	17-29
6301562-0	1983	[Acceleration by cytochrome c of cyanide binding to oxidized cytochrome c oxidase].	Cyanides	33-40	cytochrome c, somatic	Homo sapiens	61-73
6862089-3	1983	An increase in the sensitivity of superoxide dismutase (SOD) to the action of diethyldithio-carbamate and cyanide was observed in red cell fractions of greater age.	Cyanides	106-113	superoxide dismutase 1	Homo sapiens	34-54
6862089-3	1983	An increase in the sensitivity of superoxide dismutase (SOD) to the action of diethyldithio-carbamate and cyanide was observed in red cell fractions of greater age.	Cyanides	106-113	superoxide dismutase 1	Homo sapiens	56-59
6676476-0	1983	Stroma-free methemoglobin solution as an antidote for cyanide poisoning: a preliminary study.	Cyanides	54-61	hemoglobin subunit gamma 2	Homo sapiens	12-25
6341732-3	1983	The proposed oxidation of tertiary amines to iminium ions by cytochrome P-450 may explain the isolation of various intramolecular and cyanide-trapped metabolites.	Cyanides	134-141	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	61-77
6288661-5	1982	Spectroscopic evidence with intact cells suggested that a form of cytochrome c, reducible with formate but not with lactate or ascorbate-N,N,N",N"-tetramethyl-p-phenylenediamine, can be reoxidized by a cyanide-insensitive system.	Cyanides	202-209	cytochrome c, somatic	Homo sapiens	66-78
6213639-13	1982	Injection of SOD and streptozotocin simultaneously was much less effective, and cyanide-inactivated SOD was ineffective.	Cyanides	80-87	superoxide dismutase 1	Homo sapiens	100-103
7107631-5	1982	At either Ca2+ concentration, PTH secretion was strongly dependent on cell metabolism; it was inhibited by 80-85% within 10 min when cells were suspended in glucose-free buffer containing either cyanide or oxidative phosphorylation uncoupler.	Cyanides	195-202	parathyroid hormone	Bos taurus	30-33
6127113-5	1982	The delta 12-desaturase also exhibited a higher tolerance to pH changes and to cyanide than did the delta 9-desaturase.	Cyanides	79-86	fatty acid desaturase 3	Homo sapiens	100-118
7049672-9	1982	The level of Mn-SOD was not affected by diabetes or insulin treatment, but the cyanide-sensitive [copper- and zinc containing SOD (Cu-Zn SOD] SOD was depressed in the small intestine and colon of diabetic rats.	Cyanides	79-86	superoxide dismutase 1	Rattus norvegicus	131-140
6982070-7	1982	The other species present in cyanide solutions, HCN, was shown to be the substrate (Km = 4.5 mM at Av2/Av1 = 8), and extrapolation of the data indicates that at high enough HCN concentration H2 evolution can be eliminated.	Cyanides	29-36	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	48-51
6982070-7	1982	The other species present in cyanide solutions, HCN, was shown to be the substrate (Km = 4.5 mM at Av2/Av1 = 8), and extrapolation of the data indicates that at high enough HCN concentration H2 evolution can be eliminated.	Cyanides	29-36	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	173-176
7104039-6	1982	The inhibition of methemoglobin reductase activity may be, in part, responsible for the therapeutic effectiveness of cobalt salts and chelates in cyanide poisoning.	Cyanides	146-153	hemoglobin subunit gamma 2	Homo sapiens	18-31
6288209-0	1982	Effect of citrate on the reactions of cytochrome c with reductants and cyanide.	Cyanides	71-78	cytochrome c, somatic	Homo sapiens	38-50
6288209-3	1982	The reaction between cyanide ion and cytochrome c is also affected by anions: increasing the ionic strength decreases the apparent association rate constant for cyanide binding.	Cyanides	21-28	cytochrome c, somatic	Homo sapiens	37-49
6288209-3	1982	The reaction between cyanide ion and cytochrome c is also affected by anions: increasing the ionic strength decreases the apparent association rate constant for cyanide binding.	Cyanides	161-168	cytochrome c, somatic	Homo sapiens	37-49
6288209-4	1982	Substitution of citrate for morpholinopropane sulphonate in isoionic buffer media increases the apparent dissociation constant for cyanide suggesting citrate stabilizes the cytochrome c heme crevice.	Cyanides	131-138	cytochrome c, somatic	Homo sapiens	173-185
6288209-5	1982	Binding of cytochrome c to cytochrome aa3 also affects the Kd for the cyanide - cytochrome c complex indicating that cytochrome c bound to cytochrome aa3 does not react with cyanide as readily as does free cytochrome c.	Cyanides	70-77	cytochrome c, somatic	Homo sapiens	11-23
6288209-5	1982	Binding of cytochrome c to cytochrome aa3 also affects the Kd for the cyanide - cytochrome c complex indicating that cytochrome c bound to cytochrome aa3 does not react with cyanide as readily as does free cytochrome c.	Cyanides	70-77	cytochrome c, somatic	Homo sapiens	80-92
6288209-5	1982	Binding of cytochrome c to cytochrome aa3 also affects the Kd for the cyanide - cytochrome c complex indicating that cytochrome c bound to cytochrome aa3 does not react with cyanide as readily as does free cytochrome c.	Cyanides	70-77	cytochrome c, somatic	Homo sapiens	80-92
6288209-5	1982	Binding of cytochrome c to cytochrome aa3 also affects the Kd for the cyanide - cytochrome c complex indicating that cytochrome c bound to cytochrome aa3 does not react with cyanide as readily as does free cytochrome c.	Cyanides	70-77	cytochrome c, somatic	Homo sapiens	80-92
6288202-7	1982	the initial events parallel some of the events in the interaction of the cytochrome c-cytochrome aa3 system with monothiols; the final inhibitory event resembles that with cyanide.	Cyanides	172-179	cytochrome c, somatic	Homo sapiens	73-85
7061389-9	1982	The purified formate dehydrogenase was strongly inhibited by cyanide (Ki = 6 microM), azide (Ki = 39 microM), alpha,alpha-dipyridyl, and 1,10-phenanthroline.	Cyanides	61-68	SagB/ThcOx family dehydrogenase	Methanobacterium formicicum	21-34
7118416-0	1982	Mechanistic implications of cyanide binding to carboxypeptidase B.	Cyanides	28-35	carboxypeptidase B1	Homo sapiens	47-65
7118416-2	1982	The absorption spectra of Co2+-carboxypeptidase B in the presence of cyanide pointed to a direct interaction of the ligands with the metal.	Cyanides	69-76	carboxypeptidase B1	Homo sapiens	31-49
7118416-7	1982	The dissociation constant evaluated from kinetic studies for the binding of cyanide to Co2+-carboxypeptidase B was in good agreement with that obtained from spectral measurements.	Cyanides	76-83	carboxypeptidase B1	Homo sapiens	92-110
7118417-4	1982	The luminescence spectra of Zn2+- and Co2+-carboxypeptidase B in the presence of the metal coordinating ligand cyanide, used to displace the water from the metal coordination sphere, is also described.	Cyanides	111-118	carboxypeptidase B1	Homo sapiens	43-61
6801056-6	1982	Since the inactive xanthine dehydrogenase and aldehyde oxidase proteins present in ma-l mutants are identical with the catalytically inactive desulfo forms obtained by cyanide treatment of active enzymes, these data constitute evidence for genetic control of the incorporation of the cyanolyzable sulfur of Mo hydroxylases.	Cyanides	168-175	maroon-like	Drosophila melanogaster	83-87
6276383-2	1982	Upon anaerobic incubation with 1 mM S2- and 1 mM dithionite, desulfo xanthine oxidase and chicken liver xanthine dehydrogenase prepared by cyanide treatment of active enzymes, are activated to the specific activity predicted by their molybdenum content.	Cyanides	139-146	xanthine dehydrogenase	Gallus gallus	104-126
6217856-3	1982	This azoreductase activity was inhibited by cyanide and cytochrome b5 antibody, but was resistant to carbon monoxide and SKF-525A (beta-diethylaminoethyl-diphenylpropylacetate).	Cyanides	44-51	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	5-17
6276383-4	1982	Cyanide-inactivated chicken liver xanthine dehydrogenase was reconstituted with 35S2- in the presence of dithionite.	Cyanides	0-7	xanthine dehydrogenase	Gallus gallus	34-56
7061348-3	1982	Approximately 74% of this SOD is cyanide-inhibitable, indicating that it is the Cu/Zn isoenzyme usually found in the cytoplasm.	Cyanides	33-40	superoxide dismutase 1	Homo sapiens	26-29
6790543-5	1981	Cyanide at 1 and 3 mM inhibits the activity of superoxide dismutase 92 and 100%, but 5 and 10 mM azide caused 15 and 30% inhibition.	Cyanides	0-7	Superoxide dismutase 1	Drosophila melanogaster	47-67
6271809-10	1981	This conclusion was based on the kinetics and dose-response relationships for the effects of azide and cyanide on H2O2 release and on the activities of catalase and myeloperoxidase.	Cyanides	103-110	catalase	Homo sapiens	152-160
6271809-10	1981	This conclusion was based on the kinetics and dose-response relationships for the effects of azide and cyanide on H2O2 release and on the activities of catalase and myeloperoxidase.	Cyanides	103-110	myeloperoxidase	Homo sapiens	165-180
6267057-5	1981	In a cell-free system, the fluorescence of 3,3"-dipropylthiodicarbocyanine, but not that of 3,3"-dipentyloxadicarbocyanine, was rapidly eliminated by myeloperoxidase in the presence of hydrogen peroxide and a halide; this loss of fluorescence was inhibited by azide, cyanide, or catalase.	Cyanides	267-274	myeloperoxidase	Homo sapiens	150-165
7284355-6	1981	(4) In the presence of antimycin and cyanide, cytochrome b-562 is, to some extent, preferentially reduced in the rapid phase and b-566 in the slow phase.	Cyanides	37-44	mitochondrially encoded cytochrome b	Homo sapiens	46-58
16661947-6	1981	Studies with nine additional crop species generally supported the interpretation that cyanide inhibition of germination has been underestimated in the past due to escape of volatile HCN from open systems.	Cyanides	86-93	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	182-185
7262080-3	1981	Spectroscopic measurements of the binding of the weak-acid ligands formate, azide and cyanide to catalase indicate interaction of a primary haem-binding site with the undissociated forms of the ligands between pH 5 and 8.	Cyanides	86-93	catalase	Homo sapiens	97-105
6455440-7	1981	The insulin-stimulated increase was insensitive to cycloheximide and cyanide during the first 30 minutes, and this early, rapid stimulation was also produced by brain FGF (fibroblast growth factor), pituitary FGF, epidermal growth factor, calf serum, and some but not all samples of follicular fluid.	Cyanides	69-76	insulin	Bos taurus	4-11
7262080-4	1981	A similar conclusion can be drawn from observations on the pH dependence of catalase activity in the presence of cyanide and formate.	Cyanides	113-120	catalase	Homo sapiens	76-84
7019262-3	1981	The natural forms of serum Cbl were converted to cyanocobalamin (CN Cbl) by this process of extraction which included cyanide (CN).	Cyanides	118-125	Cbl proto-oncogene	Homo sapiens	27-30
7019262-3	1981	The natural forms of serum Cbl were converted to cyanocobalamin (CN Cbl) by this process of extraction which included cyanide (CN).	Cyanides	118-125	Cbl proto-oncogene	Homo sapiens	68-71
7019262-3	1981	The natural forms of serum Cbl were converted to cyanocobalamin (CN Cbl) by this process of extraction which included cyanide (CN).	Cyanides	65-67	Cbl proto-oncogene	Homo sapiens	27-30
7019262-3	1981	The natural forms of serum Cbl were converted to cyanocobalamin (CN Cbl) by this process of extraction which included cyanide (CN).	Cyanides	65-67	Cbl proto-oncogene	Homo sapiens	68-71
18962947-2	1981	Cyanide masking and selective demasking of zinc can be used to deal with the interference of many metal ions, cadmium can be masked with semithiocarbazide, and thiosulphate can be used for masking Hg(II), Pd(II) and Os(VIII).	Cyanides	0-7	cytochrome c oxidase subunit 8A	Homo sapiens	219-223
7236705-0	1981	Resonance Raman studies of methemoglobin derivatives at room temperature and 77 K. Raman spectra in preresonance with the Soret absorption band are reported for the following methemoglobin derivatives: cyanide, cyanate, thiocyanate, hydroxy-, azide, and fluoride methemoglobin at 285 K and 77 K. For the mixed-spin derivatives, Raman intensity is observed to shift from the high-spin marker band (approx.	Cyanides	202-209	hemoglobin subunit gamma 2	Homo sapiens	27-40
6162845-3	1981	Inactivation was rapid (10 to 20 s); required active myeloperoxidase, micromolar concentrations of H2O2 (or glucose oxidase as a peroxide generator), and a halide cofactor (Cl- or I-); and was blocked by azide, cyanide, and catalase.	Cyanides	211-218	myeloperoxidase	Homo sapiens	53-68
7236705-0	1981	Resonance Raman studies of methemoglobin derivatives at room temperature and 77 K. Raman spectra in preresonance with the Soret absorption band are reported for the following methemoglobin derivatives: cyanide, cyanate, thiocyanate, hydroxy-, azide, and fluoride methemoglobin at 285 K and 77 K. For the mixed-spin derivatives, Raman intensity is observed to shift from the high-spin marker band (approx.	Cyanides	202-209	hemoglobin subunit gamma 2	Homo sapiens	175-188
7236705-0	1981	Resonance Raman studies of methemoglobin derivatives at room temperature and 77 K. Raman spectra in preresonance with the Soret absorption band are reported for the following methemoglobin derivatives: cyanide, cyanate, thiocyanate, hydroxy-, azide, and fluoride methemoglobin at 285 K and 77 K. For the mixed-spin derivatives, Raman intensity is observed to shift from the high-spin marker band (approx.	Cyanides	202-209	hemoglobin subunit gamma 2	Homo sapiens	175-188
16661720-8	1981	These data indicate that lipoxygenase oxygenation, the enzyme physically separable from the mitochondria, is responsible for the cyanide-insensitive component of O(2) uptake that was observed in subcellular fractions isolated from etiolated wheat seedlings.	Cyanides	129-136	LOC543232	Triticum aestivum	25-37
6264858-0	1981	Cyanide catalyzes the oxidation of alpha-hydroxyaldehydes and related compounds: monitored as the reduction of dioxygen, cytochrome c, and nitroblue tetrazolium.	Cyanides	0-7	cytochrome c, somatic	Homo sapiens	121-133
6790664-7	1980	Inclusion of haematin in the growth medium caused the bacterium to form a cyanide- and azide-sensitive catalase.	Cyanides	74-81	catalase	Bos taurus	103-111
7435608-4	1980	Peroxisomal activity was followed as cyanide-insensitive palmitoyl-CoA-dependent NAD+ reduction (palmitoyl-CoA oxidase) and as catalase.	Cyanides	37-44	acyl-CoA oxidase 1	Rattus norvegicus	97-118
6253528-10	1980	In the case of PMA-stimulated polymorphonuclear leukocytes or monocytes, extracellular myeloperoxidase may have also played a role in alpha(1)-Pi inactivation since serum EIC was partly protected by azide, cyanide, or the depletion of extracellular chloride.	Cyanides	206-213	myeloperoxidase	Homo sapiens	87-102
16661455-2	1980	In cauliflower, mitochondria malate oxidation via malate dehydrogenase is rotenone- and cyanide-sensitive.	Cyanides	88-95	NAD-dependent malic enzyme 62 kDa isoform, mitochondrial	Solanum tuberosum	50-70
6263242-9	1980	However, extensive sonication of spermatozoa released a small amount of a cyanide-insensitive enzyme, presumably a mangano superoxide dismutase, from the mitochondrial matrix.	Cyanides	74-81	superoxide dismutase 2	Homo sapiens	115-143
16661455-7	1980	Similarly, malate dehydrogenase and another specific pool of NAD(+)/NADH are connected to the cyanide- (and antimycin-) sensitive pathway by a rotenone-sensitive NADH dehydrogenase located on the inner face of the inner membrane.	Cyanides	94-101	NAD-dependent malic enzyme 62 kDa isoform, mitochondrial	Solanum tuberosum	11-31
6247350-0	1980	Cyanide binding to the cytochrome c ferric heme octapeptide.	Cyanides	0-7	cytochrome c, somatic	Homo sapiens	23-35
6258556-3	1980	The chemiluminescence of the present system was sensitive to cyanide and to the radical trap 2,5-di-t-butylquinol, indicating a catlytic activity of cytochrome c and the presence of free-radical species respectively.	Cyanides	61-68	cytochrome c, somatic	Homo sapiens	149-161
6247350-3	1980	The equilibrium constant for cyanide binding at 20 degrees C and pH 7.4 is 3.47 X 10(7), which is approximately 15-fold lower than that observed for cyanide binding to methemoglobin or metmyoglobin.	Cyanides	29-36	hemoglobin subunit gamma 2	Homo sapiens	168-181
6246992-6	1980	The myeloperoxidase inhibitor cyanide did not reduce red blood destruction, while azide consistently impaired cytolysis.	Cyanides	30-37	myeloperoxidase	Homo sapiens	4-19
6247350-3	1980	The equilibrium constant for cyanide binding at 20 degrees C and pH 7.4 is 3.47 X 10(7), which is approximately 15-fold lower than that observed for cyanide binding to methemoglobin or metmyoglobin.	Cyanides	149-156	hemoglobin subunit gamma 2	Homo sapiens	168-181
6268262-5	1980	Both processes are sensitive to cyanide, but azide inhibits only the authentic cytochrome c oxidase catalyzed process and BCS the ferricytochrome c stimulated reaction.	Cyanides	32-39	cytochrome c, somatic	Equus caballus	79-91
7390994-3	1980	The reconstituted activity was sensitive to carbon monoxide, metyrapone, phenyl isocyanide, and cyanide, indicating that the cytochrome P-450 used is cyanide-sensitive and is involved in the catalytic process.	Cyanides	83-90	cytochrome P-450	Oryctolagus cuniculus	125-141
7423537-0	1980	Acetylcholinesterase activity in rat brain: effect of acute cyanide intoxication.	Cyanides	60-67	acetylcholinesterase	Rattus norvegicus	0-20
7423537-2	1980	Compared with control, cyanide-treated animals showed significant increases in the AChE activity of the cerrebral cortex, hippocampus and midbrain.	Cyanides	23-30	acetylcholinesterase	Rattus norvegicus	83-87
7423537-3	1980	This finding suggests an involvement of brain AChE in acute cyanide toxicity.	Cyanides	60-67	acetylcholinesterase	Rattus norvegicus	46-50
7390994-3	1980	The reconstituted activity was sensitive to carbon monoxide, metyrapone, phenyl isocyanide, and cyanide, indicating that the cytochrome P-450 used is cyanide-sensitive and is involved in the catalytic process.	Cyanides	96-103	cytochrome P-450	Oryctolagus cuniculus	125-141
7402127-2	1980	The electron transport chain (ETC) of Pseudomonas thermophila K-2 was examined by the amperometric determination of O2 uptake by the preparations of membranes isolated by ultracentrifugation at 14,000 g. Amytal and cyanide were found to inhibit endogenous respiration of membranes from freshly grown cells.	Cyanides	215-222	RBPJ pseudogene 3	Homo sapiens	62-65
7389037-6	1980	However, cyanide was found to be stimulating in this system and this may be due to the inhibition of enzymes such as catalase and superoxide dismutase known to be present in S9.	Cyanides	9-16	catalase	Homo sapiens	117-125
6928374-0	1980	3-Mercaptopyruvate sulfurtransferase: rapid equilibrium-ordered mechanism with cyanide as the acceptor substrate.	Cyanides	79-86	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
6244290-1	1980	The reduced forms of xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase are inactivated by cyanide.	Cyanides	120-127	xanthine dehydrogenase	Homo sapiens	39-61
6244290-1	1980	The reduced forms of xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase are inactivated by cyanide.	Cyanides	120-127	aldehyde oxidase 1	Homo sapiens	63-79
6244290-1	1980	The reduced forms of xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase are inactivated by cyanide.	Cyanides	120-127	sulfite oxidase	Homo sapiens	85-100
6244304-3	1980	In 0.01 M MgCl2, the refoleded protein recovers the behavior towards cyanide of native cytochrome c.	Cyanides	69-76	cytochrome c, somatic	Equus caballus	87-99
6249264-0	1980	Role of adenosine deaminase, ecto-(5"-nucleotidase) and ecto-(non-specific phosphatase) in cyanide-induced adenosine monophosphate catabolism in rat polymorphonuclear leucocytes.	Cyanides	91-98	adenosine deaminase	Rattus norvegicus	8-27
6249264-0	1980	Role of adenosine deaminase, ecto-(5"-nucleotidase) and ecto-(non-specific phosphatase) in cyanide-induced adenosine monophosphate catabolism in rat polymorphonuclear leucocytes.	Cyanides	91-98	5' nucleotidase, ecto	Rattus norvegicus	29-50
6928374-1	1980	A steady-state kinetic analysis of 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) using cyanide as the sulfur-acceptor substrate was performed.	Cyanides	91-98	mercaptopyruvate sulfurtransferase	Homo sapiens	35-71
6987309-2	1980	The EPO-H2O2-halide bactericidal system had an acid pH optimum and was inhibited by the proteins albumin and gelatin and by the hemeprotein inhibitors azide, cyanide, and aminotriazole.	Cyanides	158-165	erythropoietin	Cavia porcellus	4-7
6101540-2	1980	In the livers of rats fed for one week on the high-fat diet containing 30% fat, the cyanide-insensitive palmitoyl-CoA oxidation was accelerated to eight times that of control and the enzymic activities of catalase, carnitine acetyltransferase and carnitine palmitoyltransferase were elevated by the factors of 1.3, 5 and 2, respectively.	Cyanides	84-91	catalase	Rattus norvegicus	205-213
6248741-3	1980	The oxidation of reduced TMPD and exogenous cytochrome c by the membrane preparations of the two bacteria is inhibited by formate and cyanide; Ki50% = 2.5 X 10(-2) and 10(-6) M, respectively.	Cyanides	134-141	MEXAM1_RS12150	Methylobacterium extorquens AM1	44-56
6101540-2	1980	In the livers of rats fed for one week on the high-fat diet containing 30% fat, the cyanide-insensitive palmitoyl-CoA oxidation was accelerated to eight times that of control and the enzymic activities of catalase, carnitine acetyltransferase and carnitine palmitoyltransferase were elevated by the factors of 1.3, 5 and 2, respectively.	Cyanides	84-91	carnitine O-acetyltransferase	Rattus norvegicus	215-242
6243963-6	1980	Reduced cytochrome bK in the presence of cyanide can be reoxidized by CoQ2.	Cyanides	41-48	coenzyme Q2, polyprenyltransferase	Homo sapiens	70-74
7355775-0	1980	Stability of vitamin B12 in the presence of ascorbic acid in food and serum: restoration by cyanide of apparent loss.	Cyanides	92-99	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	21-24
6244265-7	1980	When hydrazine was added to cyanide complex I of myeloperoxidase the complex was converted to the hydrazine-enzyme compound.	Cyanides	28-35	myeloperoxidase	Homo sapiens	49-64
6244265-8	1980	Myeloperoxidase reacted with bisulfite to form a compound with an absorption spectrum similar to that of cyanide complex I.	Cyanides	105-112	myeloperoxidase	Homo sapiens	0-15
6244265-9	1980	Borohydride-treated myeloperoxidase formed only one cyanide complex, while the native enzyme formed two different cyanide complexes, I (Kd = 0.3 muM) and II (approximate Kd = 0.1 mM).	Cyanides	52-59	myeloperoxidase	Homo sapiens	20-35
6244265-9	1980	Borohydride-treated myeloperoxidase formed only one cyanide complex, while the native enzyme formed two different cyanide complexes, I (Kd = 0.3 muM) and II (approximate Kd = 0.1 mM).	Cyanides	114-121	myeloperoxidase	Homo sapiens	20-35
6244265-10	1980	The EPR spectrum indicated that cyanide complex I of myeloperoxidase still contained high-spin heme.	Cyanides	32-39	myeloperoxidase	Homo sapiens	53-68
6244265-11	1980	The results suggested that cyanide complex I and the bisulfite compound of myeloperoxidase were adducts between the nucleophilic reagents and the formyl group of myeloperoxidase heme.	Cyanides	27-34	myeloperoxidase	Homo sapiens	75-90
490831-1	1979	Using extraction procedures in which the extracted vitamin B12 was protected by cyanide or metabisulfite, several investigators found no change in vitamin B12 when meals were incubated in the presence of ascorbic acid for 30 minutes at 37 degrees C. A previous report suggested degradation of vitamin B12 under these conditions, but this was apparently caused by incomplete protection of the extracted vitamin B12 in the assay procedure.	Cyanides	80-87	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	59-62
6244265-11	1980	The results suggested that cyanide complex I and the bisulfite compound of myeloperoxidase were adducts between the nucleophilic reagents and the formyl group of myeloperoxidase heme.	Cyanides	27-34	myeloperoxidase	Homo sapiens	162-177
7193485-6	1980	The results are interpreted as arising from a diminished steric hindrance to isocyanide binding with leghemoglobin, in conformity with the recently published X-ray structure which reports the existence of a large heme pocket on the distal side.	Cyanides	77-87	leghemoglobin A	Glycine max	101-114
6244567-7	1980	The myeloperoxidase inhibitor cyanide enhanced erythrocyte destruction, whereas azide reduced it modestly.	Cyanides	30-37	myeloperoxidase	Homo sapiens	4-19
229235-8	1979	A modification of the established procedure for using the cyanide electrode for cyanide analyses was used to follow the release of HCN from DAMN.	Cyanides	58-65	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	131-134
229235-8	1979	A modification of the established procedure for using the cyanide electrode for cyanide analyses was used to follow the release of HCN from DAMN.	Cyanides	80-87	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	131-134
479828-5	1979	Stimulation in 50 mM Ca seawater of an aequorin-phenol red-injected axon at 180 s-1 for 1 min produces a scarcely detectable change in Cai; the addition of 2 mM cyanide (CN) to the seawater produces an easily measureable increase in Cai, suggesting that mitochondrial buffering in the periphery is substantial.	Cyanides	161-168	carbonic anhydrase 1	Homo sapiens	233-236
231457-0	1979	Cyanide reactivity of cytochrome c derivatives.	Cyanides	0-7	cytochrome c, somatic	Equus caballus	22-34
479828-5	1979	Stimulation in 50 mM Ca seawater of an aequorin-phenol red-injected axon at 180 s-1 for 1 min produces a scarcely detectable change in Cai; the addition of 2 mM cyanide (CN) to the seawater produces an easily measureable increase in Cai, suggesting that mitochondrial buffering in the periphery is substantial.	Cyanides	161-168	carbonic anhydrase 1	Homo sapiens	135-138
231457-1	1979	The kinetic rates and equilibrium association constants for cyanide binding have been measured for a series of cytochrome c derivatives as a probe of heme accessibility.	Cyanides	60-67	cytochrome c, somatic	Equus caballus	111-123
479302-6	1979	Incorporation of cell-associated free iodine by endogenous myeloperoxidase during phagocytosis was inhibited by 1 mM cyanide, which had no effect on the rate of particle uptake.	Cyanides	117-124	myeloperoxidase	Oryctolagus cuniculus	59-74
36154-5	1979	Chloride competed with cyanide for binding at the active site of myeloperoxidase.	Cyanides	23-30	myeloperoxidase	Homo sapiens	65-80
752132-6	1978	The carbonium ions i-C3H7+ and t-C4H9+ condense also with HCN to yield protonated isocyanides.	Cyanides	82-93	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	58-61
229520-3	1979	These LPO-type enzymes, that are inhibited by cyanide and aminotriazole, appear to operate extracellularly as bactericidal agents in milk and in other biological fluids.	Cyanides	46-53	lactoperoxidase	Homo sapiens	6-9
711738-5	1978	Inactivation of free rhodanese by phenylglyoxal in the presence of cyanide was shown to be caused by a novel reaction in which disulfide bonds are formed between Cys-247 and either Cys-254 or Cys-263.	Cyanides	67-74	thiosulfate sulfurtransferase	Bos taurus	21-30
719868-5	1978	Rubber stoppers and expired air contaminated by HCN must be carefully avoided during cyanide analysis.	Cyanides	85-92	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	48-51
32876-1	1978	The binding of cyanide to both oxidized and ascorbate-reduced forms of Pseudomonas cytochrome c-551 oxidase was investigated.	Cyanides	15-22	cytochrome c, somatic	Homo sapiens	83-95
740000-8	1978	The low temperature reduction of azide and cyanide complexes of myoglobin led to formation of nonequilibrium low spin ferroforms whose spectra demonstrate the presence of N3- and CN- in heme iron"s coordination sphere.	Cyanides	43-50	myoglobin	Homo sapiens	64-73
16660377-1	1978	The 4S cytochrome c (Cyt c) reductase activity of several plant species was markedly stimulated by cyanide and ferrocyanide but those of the 8S nitrate reductase component and other particulate components of the maize (Zea mays L.) scutellum by comparison, were increased only slightly.	Cyanides	99-106	cytochrome c	Zea mays	7-19
16660540-5	1978	Soybean lipoxygenase exhibits similar characteristics of insensitivity to cyanide and sensitivity to salicylhydroxamate and to propyl gallate.	Cyanides	74-81	linoleate 9S-lipoxygenase-4	Glycine max	8-20
16660377-1	1978	The 4S cytochrome c (Cyt c) reductase activity of several plant species was markedly stimulated by cyanide and ferrocyanide but those of the 8S nitrate reductase component and other particulate components of the maize (Zea mays L.) scutellum by comparison, were increased only slightly.	Cyanides	99-106	cytochrome c	Zea mays	21-26
16660377-2	1978	The effect of cyanide and ferrocyanide was not due to elimination of cytochrome oxidase interference but resulted from the stimulation of NADH-dependent reduction of Cyt c.	Cyanides	14-21	cytochrome c	Zea mays	166-171
16660377-3	1978	A 4S Cyt c reductase component which could be isolated by ammonium sulfate fractionation and diethyl-aminoethyl-cellulose chromatography was found to be stimulated markedly by cyanide and ferrocyanide.	Cyanides	176-183	cytochrome c	Zea mays	5-10
22333-0	1977	The effect of methemoglobin on the inhibition of cytochrome c oxidase by cyanide, sulfide or azide.	Cyanides	73-80	hemoglobin subunit gamma 2	Homo sapiens	14-27
203651-4	1978	Further, inhibition of ethylene generation by azide and cyanide suggests that OH generation in granulocytes may be linked to myeloperoxidase.	Cyanides	56-63	myeloperoxidase	Homo sapiens	125-140
619988-4	1978	The intermediacy of methemoglobin can be demonstrated by direct spectral observation and by cyanide trapping.	Cyanides	92-99	hemoglobin subunit gamma 2	Homo sapiens	20-33
27984-1	1978	Using a fluorometric assay for the determination of oxidized pyridine nucleotides (NAD[P]+), total and cyanide-resistant NADPH-oxidative activities have been measured in subcellular fractions isolated from resting and phagocytosing human polymorphonuclears.	Cyanides	103-110	2,4-dienoyl-CoA reductase 1	Homo sapiens	121-126
410563-7	1977	Methemoglobin is added to combine with the cyanide formed and prevent its destruction.	Cyanides	43-50	hemoglobin subunit gamma 2	Homo sapiens	0-13
410563-8	1977	On acidification, the total amount of cyanide originally present as free cyanide or as nitroprusside is liberated as HCN, isolated by gas transfer into a sodium hydroxide trap, and quantified by spectrophotometry.	Cyanides	38-45	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	117-120
563483-3	1977	The binding reaction of aminopyrine with microsomal cytochrome P-450 was also modified by cyanide, and an abnormal aminopyrine-induced difference spectrum of microsomes by cyanide, and an abnormal aminopyrine-induced difference spectrum of microsomes appeared when cyanide was added to the reaction mixture.	Cyanides	172-179	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	52-68
22768-1	1977	Cyanide inhibited microsomal activities of aniline hydroxylation and aminopyrine, ethylmorphine and codeine demethylations and produced a modified type II difference spectrum of cytochrome P-450 to give two spectral dissociation constants, 0.21mM and 1.05 mM.	Cyanides	0-7	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	178-194
22768-2	1977	The binding of cyanide to cytochrome P-450 resulted in innhibition of NADPH-cytochrome P-450 reductase activity.	Cyanides	15-22	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	26-42
22768-2	1977	The binding of cyanide to cytochrome P-450 resulted in innhibition of NADPH-cytochrome P-450 reductase activity.	Cyanides	15-22	cytochrome p450 oxidoreductase	Rattus norvegicus	70-102
563483-1	1977	Cyanide, an inhibitor of many hemoproteins, was shown to affect a number of microsomal drug-metabolizing activities catalyzed by cytochrome P-450.	Cyanides	0-7	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	129-145
563483-3	1977	The binding reaction of aminopyrine with microsomal cytochrome P-450 was also modified by cyanide, and an abnormal aminopyrine-induced difference spectrum of microsomes by cyanide, and an abnormal aminopyrine-induced difference spectrum of microsomes appeared when cyanide was added to the reaction mixture.	Cyanides	90-97	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	52-68
563483-3	1977	The binding reaction of aminopyrine with microsomal cytochrome P-450 was also modified by cyanide, and an abnormal aminopyrine-induced difference spectrum of microsomes by cyanide, and an abnormal aminopyrine-induced difference spectrum of microsomes appeared when cyanide was added to the reaction mixture.	Cyanides	172-179	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	52-68
563483-6	1977	These results suggest that aminopyrine and cyanide reciprocally affect binding with cytochrome P-450 and modification by cyanide of aminopyrine binding reaction with the hemoprotein produces an inhibition of N-demethylase activity.	Cyanides	43-50	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	84-100
20335-1	1977	pH-Dependent features of heme-bound C15N-resonances in cyanide complexes of myoglobin and cytochrome c and some implications for their heme environmental structures.	Cyanides	55-62	myoglobin	Homo sapiens	76-85
20335-1	1977	pH-Dependent features of heme-bound C15N-resonances in cyanide complexes of myoglobin and cytochrome c and some implications for their heme environmental structures.	Cyanides	55-62	cytochrome c, somatic	Homo sapiens	90-102
16659973-4	1977	It contains glucan synthetase II activity, binding sites for N-naphthylphthalamic acid, NADH dehydrogenase activity which is both antimycin A- and cyanide-insensitive, and a b-type cytochrome.	Cyanides	147-154	Alternative NAD(P)H-ubiquinone oxidoreductase C1, chloroplastic/mitochondrial	Zea mays	88-106
907818-4	1977	Of the two SOD fractions of platelets, lymphocytes, and granulocytes rapidly migrating to the anode, by the capacity to be inhibited with cyanide or organic solvents the first SOD fraction was attributed to cytosol enzyme, while the second one -- to mitochondrial enzyme.	Cyanides	138-145	superoxide dismutase 1	Homo sapiens	11-14
907818-4	1977	Of the two SOD fractions of platelets, lymphocytes, and granulocytes rapidly migrating to the anode, by the capacity to be inhibited with cyanide or organic solvents the first SOD fraction was attributed to cytosol enzyme, while the second one -- to mitochondrial enzyme.	Cyanides	138-145	superoxide dismutase 1	Homo sapiens	176-179
192267-11	1977	Moreover, while cyanide binds to the native enzyme without reducing the Cu(II) atom, cyanide rapidly reduces the Cu(II) atom to Cu(I) in the NBS-oxidized enzyme.	Cyanides	16-23	nibrin	Homo sapiens	141-144
192267-11	1977	Moreover, while cyanide binds to the native enzyme without reducing the Cu(II) atom, cyanide rapidly reduces the Cu(II) atom to Cu(I) in the NBS-oxidized enzyme.	Cyanides	85-92	nibrin	Homo sapiens	141-144
845116-4	1977	The catalase was a nondialyzable, cyanide and azide-sensitive, heat-labile protein that coeluted with bovine erythrocyte catalase from Sepharose 6 B.	Cyanides	34-41	catalase	Bos taurus	4-12
856833-10	1977	When treated with cyanide, MFGM and mammary microsomes showed difference spectra of a reduced b-type cytochrome.	Cyanides	18-25	milk fat globule EGF and factor V/VIII domain containing	Homo sapiens	27-31
16659840-7	1977	The similar molecular weights and the cyanide sensitivities of these bands indicated that they are probably isozymes of a cupro-zinc superoxide dismutase.	Cyanides	38-45	superoxide dismutase	Zea mays	133-153
12504-2	1976	The volume changes associated with the binding of cyanide and azide ions to methemoglobin are pH-dependent.	Cyanides	50-57	hemoglobin subunit gamma 2	Homo sapiens	76-89
13072-14	1977	The spectrum of horse cytochrome c with added azide, cyanide, hydroxide, or imidazole as axial ligands has also been examined.	Cyanides	53-60	cytochrome c, somatic	Equus caballus	22-34
831781-17	1977	The increase in the reduction level of cytochrome b on addition of HQNO in the presence of succinate and oxygen, either in the presence or absence of cyanide, does not parallel the inhibition of overall electron transfer.	Cyanides	150-157	mitochondrially encoded cytochrome b	Homo sapiens	39-51
1022721-0	1976	Iodide, thiocyanate and cyanide ions as capturing reagents in one-step copper-thiocholine method for cytochemical localization of cholinesterase activity.	Cyanides	24-31	butyrylcholinesterase	Rattus norvegicus	130-144
184092-3	1976	The proximal ligand to the heme iron atom of ferric soybean leghemoglobin is identified as imidazole by comparison of the EPR of leghemoglobin hydroxide, azide, and cyanide with the corresponding derivatives of human hemoglobin.	Cyanides	165-172	leghemoglobin A	Glycine max	60-73
8450-2	1976	The reaction of sulfite, cyanide, and hydroxylamine with several deazaflavin-containing enzymes (glycolate oxidase, D-amino acid oxidase, glucose oxidase, N-methylglutamate synthetase) and free deazaFMN has been examined.	Cyanides	25-32	hydroxyacid oxidase 2	Homo sapiens	97-114
8450-2	1976	The reaction of sulfite, cyanide, and hydroxylamine with several deazaflavin-containing enzymes (glycolate oxidase, D-amino acid oxidase, glucose oxidase, N-methylglutamate synthetase) and free deazaFMN has been examined.	Cyanides	25-32	D-amino acid oxidase	Homo sapiens	116-136
8450-7	1976	The relative stability observed for the sulfite and cyanide complexes formed with various deazaflavin systems (glycolate oxidase greater than D-amino acid oxidase greater than free deazaFMN) follows the same trend observed for the stability of the sulfite complexes formed with the corresponding flavin system.	Cyanides	52-59	hydroxyacid oxidase 2	Homo sapiens	111-128
8450-7	1976	The relative stability observed for the sulfite and cyanide complexes formed with various deazaflavin systems (glycolate oxidase greater than D-amino acid oxidase greater than free deazaFMN) follows the same trend observed for the stability of the sulfite complexes formed with the corresponding flavin system.	Cyanides	52-59	D-amino acid oxidase	Homo sapiens	142-162
8450-10	1976	In the case of cyanide, a complex is formed only with native glycolate oxidase, which is the flavin-containing system most susceptible to attack by the more reactive sulfite.	Cyanides	15-22	hydroxyacid oxidase 2	Homo sapiens	61-78
956135-8	1976	The aniline and cyanide difference spectra of reduced cytochrome P-450 showed peaks at 423 nm and 429 nm, respectively, while that of azide had a peak at 445 nm and a trough at 404 nm.	Cyanides	16-23	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	54-70
1260002-5	1976	The ferric low spin derivatives such as myoglobin cyanide, myoglobin imidazole and myoglobin azide showed positive MCD spectra which are very similar to the electronic absorption spectra.	Cyanides	50-57	myoglobin	Homo sapiens	40-49
187902-3	1976	The "peroxidase" chain consists of pyridine nucleotides, cytochrome c, and cytochrome c peroxidase; it is inhibited by cyanide.	Cyanides	119-126	cytochrome c, somatic	Homo sapiens	57-69
187902-3	1976	The "peroxidase" chain consists of pyridine nucleotides, cytochrome c, and cytochrome c peroxidase; it is inhibited by cyanide.	Cyanides	119-126	cytochrome c, somatic	Homo sapiens	75-87
176720-4	1976	Since hexose monophosphate shunt activity was enhanced and azide and cyanide inhibited the intracellular killing of E. coli only moderately, the patient"s granulocytes may possess azide- and cyanide-resistant, MPO-independant microbicidal systems coupled to the oxidative metabolism.	Cyanides	191-198	myeloperoxidase	Homo sapiens	210-213
13869-3	1976	2) with or without cyanide in the incubation medium, LG omitted, Mn++ in the presence of NADPH induced superoxide anion (O- WITH 2) production, as evidenced by oxygen consumption and H2O2 production, which were abolished (in the absence of cyanide) by cytochrome C (a potent O- with 2 scavenger).	Cyanides	19-26	cytochrome c, somatic	Homo sapiens	252-264
401-10	1976	The complex reacted with cyanide and was reduced by ascorbate at about 32% and 40% respectively, of the rates of reaction with cytochrome c alone.	Cyanides	25-32	LOC104968582	Bos taurus	127-139
16659381-4	1975	Under red light, striking photoactivation of NAD kinase was obtained with ATP and subsequently CTP.In the presence of exogenous Mg(2+), which is required for NAD kinase activity, alpha-nitroso-beta-naphthol, cyanide, and dimethylglyoxime, strongly inhibited the activation by red light without affecting the level of NAD kinase in the dark.Of the divalent cations tested with the KCN-treated phytochrome preparation, only Co(2+) was effective for photoactivation of NAD kinase.	Cyanides	208-215	NAD kinase	Homo sapiens	45-55
1245233-9	1976	Chronic administration of nitroprusside results in the elevation of blood thiocyanate levels presumably because of continuous, endogenous cyanide metabolism via rhodanese (thiosulfate sulfurtransferase).	Cyanides	138-145	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	172-201
1220689-9	1975	Results of experiments on cyanide inhibition of respiration and cytochrome oxidation support the suggestion that the susceptibility of cytochrome b to oxidation by molecular oxygen (reflected in its ability to react with CO) is probably irrelevant to the normal physiology of Pseudomonas AM1.	Cyanides	26-33	MEXAM1_RS00595	Methylobacterium extorquens AM1	135-147
169897-4	1975	Refolding of cytochrome c after alkylation at low pH apparently gives a different configuration of modified methionine residues within the protein compared to that produced by alkylation at neutral pH in the presence of cyanide.	Cyanides	220-227	cytochrome c, somatic	Equus caballus	13-25
48-5	1975	Cyanide ion produced a much more effective inhibition of renal dipeptidase than the other monoanions, and it was shown that two cyanide ions were bound per enzyme molecule.	Cyanides	0-7	dipeptidase 1	Homo sapiens	57-74
48-5	1975	Cyanide ion produced a much more effective inhibition of renal dipeptidase than the other monoanions, and it was shown that two cyanide ions were bound per enzyme molecule.	Cyanides	128-135	dipeptidase 1	Homo sapiens	57-74
170968-7	1975	(3) Acceleration of glycogenolysis by inhibition of respiration with cyanide caused similar changes in phosphorylase activity but with the maximum effect observed only after 45 s. (4) Dibutyryl cyclic AMP had two effects; it partially activated phosphorylase and blocked further activation by thrombin, but not A23187.	Cyanides	69-76	coagulation factor II	Rattus norvegicus	293-301
1213990-3	1975	Kinetic studies revealed that Fraction I rat liver rhodanese catalyzes thiocyanate formation from thiosulfate and cyanide by a double displacement mechanism.	Cyanides	114-121	thiosulfate sulfurtransferase	Rattus norvegicus	51-60
169890-7	1975	In similar experiments with ferric myoglobin, the addition of cyanide caused a large decrease in the enhancement of the proton relaxation rate of both formate and water, indicating the displacement of water and formate from the heme and the vicinity of the heme, respectively.	Cyanides	62-69	myoglobin	Equus caballus	35-44
170101-6	1975	Chlorination in neutrophils is inhibited by the iodide and myeloperoxidase inhibitors azide and cyanide.	Cyanides	96-103	myeloperoxidase	Homo sapiens	59-74
168879-0	1975	Kinetic studies on the reaction between cytochrome c oxidase and ferrocytochrome c. In stopped-flow experiments in which oxidized cytochrome c oxidase was mixed with ferrocytochrome c in the presence of a range of oxygen concentrations and in the absence and presence of cyanide, a fast phase, reflecting a rapid approach to an equilibrium, was observed.	Cyanides	271-278	cytochrome c, somatic	Homo sapiens	40-52
1170853-0	1975	Glutathione S-transferase in the formation of cyanide from organic thiocyantes and as an organic nitrate reductase.	Cyanides	46-53	glutathione S-transferase kappa 1	Homo sapiens	0-25
168879-0	1975	Kinetic studies on the reaction between cytochrome c oxidase and ferrocytochrome c. In stopped-flow experiments in which oxidized cytochrome c oxidase was mixed with ferrocytochrome c in the presence of a range of oxygen concentrations and in the absence and presence of cyanide, a fast phase, reflecting a rapid approach to an equilibrium, was observed.	Cyanides	271-278	cytochrome c, somatic	Homo sapiens	70-82
235300-9	1975	A low level of cyanide (0.4 mu M) markedly enhanced the action of NAD(P)H on the maize enzyme; Cyanide at a higher level (6 mu M) did give inactivation of the Neurospora nitrate reductase in the presence of NADPH and FAD.	Cyanides	15-22	nitrate reductase [NADH] 1	Zea mays	170-187
234739-3	1975	The seven resonances observed in the histidine region of the proton magnetic resonance (pmr) spectrum of human carbonic anhydrase B and reported in the preceding paper are studied in the presence of sulfonamide, azide, cyanide, and chloride inhibitors and in metal-free, cadmium substituted, cobalt substituted, and carboxymethylated forms of the enzyme.	Cyanides	219-226	carbonic anhydrase 2	Homo sapiens	111-131
1115776-4	1975	Cyanide (0.2 mM) caused complete inhibition of the basal respiration, but only 15% inhibition of the thrombin-stimulated burst of oxygen consumption.	Cyanides	0-7	coagulation factor II, thrombin	Homo sapiens	101-109
235300-9	1975	A low level of cyanide (0.4 mu M) markedly enhanced the action of NAD(P)H on the maize enzyme; Cyanide at a higher level (6 mu M) did give inactivation of the Neurospora nitrate reductase in the presence of NADPH and FAD.	Cyanides	95-102	nitrate reductase [NADH] 1	Zea mays	170-187
235300-10	1975	The maize nitrate reductase, when partially inactivated by NADH and cyanide, was not altered as a substrate for the inactivating enzyme.	Cyanides	68-75	nitrate reductase [NADH] 1	Zea mays	10-27
4720713-3	1973	The magnitude of the inhibition of ethanol oxidation by cyanide was not paralleled by the formation of the catalase-cyanide complex and was altered greatly by varying either the ethanol concentration or the ratio of the rate of H(2)O(2) generation to catalase haem concentration.	Cyanides	56-63	catalase	Rattus norvegicus	251-259
4343916-0	1972	[Interaction of myoglobin with isocyanide spin label].	Cyanides	31-41	myoglobin	Homo sapiens	16-25
5116211-3	1971	Azide and cyanide increased glucose C-1 oxidation by normal leukocytes but had little or no effect on myeloperoxidase-deficient leukocytes suggesting that these agents normally stimulate glucose C-1 oxidation, in part, by inhibition of myeloperoxidase.	Cyanides	10-17	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	36-39
5116211-3	1971	Azide and cyanide increased glucose C-1 oxidation by normal leukocytes but had little or no effect on myeloperoxidase-deficient leukocytes suggesting that these agents normally stimulate glucose C-1 oxidation, in part, by inhibition of myeloperoxidase.	Cyanides	10-17	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	195-198
5116211-3	1971	Azide and cyanide increased glucose C-1 oxidation by normal leukocytes but had little or no effect on myeloperoxidase-deficient leukocytes suggesting that these agents normally stimulate glucose C-1 oxidation, in part, by inhibition of myeloperoxidase.	Cyanides	10-17	myeloperoxidase	Homo sapiens	236-251
4967774-6	1968	Cytochrome c oxidation by the Azotobacter electron transport system was markedly sensitive to cyanide, azide, and hydroxylamine, although carbon monoxide inhibition could not be demonstrated.	Cyanides	94-101	cytochrome c, somatic	Homo sapiens	0-12
5480860-14	1970	The binding of cyanide to the iron atom in methemoglobin is thought to be associated with increased planarity of the heme group and increased stability of the heme-globin complex.	Cyanides	15-22	hemoglobin subunit gamma 2	Homo sapiens	43-56
5480860-15	1970	The stabilizing effect of cyanide in the above experiments suggests that Heinz body formation, heat precipitation of hemoglobin, and the increased alkali denaturation of methemoglobin depend on changes of heme-globin binding.	Cyanides	26-33	hemoglobin subunit gamma 2	Homo sapiens	170-183
4988715-1	1970	Azide and, to a lesser extent, cyanide inhibit the microbicidal activity of myeloperoxidase and of intact normal leukocytes, but they have little or no effect on peroxidase-negative leukocytes.	Cyanides	31-38	myeloperoxidase	Homo sapiens	76-91
4385526-0	1968	The electron spin resonance and absorption spectra of microsomal cytochrome P-450 and its isocyanide complexes.	Cyanides	90-100	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	65-81
5657862-0	1968	Tryptophan and alpha-methyltryptophan facilitation in the interaction of cyanide with tryptophan oxygenase.	Cyanides	73-80	tryptophan 2,3-dioxygenase	Homo sapiens	86-106
6048304-0	1967	The properties of hemoglobin M. Reactivity of methemoglobin M to cyanide, azide and fluoride.	Cyanides	65-72	hemoglobin subunit gamma 2	Homo sapiens	46-59
5643798-0	1968	Binding of cyanide to methemoglobin.	Cyanides	11-18	hemoglobin subunit gamma 2	Homo sapiens	22-35
4293586-0	1967	Effect of cyanide and Antimycin A on the reduction of cytochrome b and ubiquinone in electron transport particles.	Cyanides	10-17	mitochondrially encoded cytochrome b	Homo sapiens	54-66
4176120-0	1966	[A method of determining methemoglobin in the blood on the basis of its cyanide (cyanomethemoglobin)].	Cyanides	72-79	hemoglobin subunit gamma 2	Homo sapiens	25-38
14247659-0	1964	THE REACTION OF CYANIDE WITH BOVINE SERUM ALBUMIN.	Cyanides	16-23	albumin	Homo sapiens	36-49
5866153-0	1965	Production of a "cytochrome c" with myoglobin-like properties by alkylating the cyanide complex with bromoacetate.	Cyanides	80-87	cytochrome c, somatic	Homo sapiens	17-29
16656017-0	1964	The Occurrence of and Effect of Cyanide on Respiratory Drift in the Developing Tung Nut.	Cyanides	32-39	NUT midline carcinoma family member 1	Homo sapiens	84-87
13913379-0	1961	[Changes in cholinesterase activity under the influence of cyanides and alcohol acting separately and in combination].	Cyanides	59-67	butyrylcholinesterase	Homo sapiens	12-26
14207394-0	1964	[CONTRIBUTION TO THE DETERMINATION OF METHEMOGLOBIN BY THE CYANIDE METHOD].	Cyanides	59-66	hemoglobin subunit gamma 2	Homo sapiens	38-51
13479119-0	1957	Cyanide inhibition of the catalase system.	Cyanides	0-7	catalase	Homo sapiens	26-34
13594104-0	1958	[Sigmoid coefficients of the cyanide equilibrium of methemoglobin and metmyoglobin].	Cyanides	29-36	hemoglobin subunit gamma 2	Homo sapiens	52-65
13260191-0	1955	Cyanide compounds of ferroperoxidase and myoglobin and their reversible photodissociation.	Cyanides	0-7	myoglobin	Homo sapiens	41-50
13050336-0	1953	ACTH treatment in a case of cyanide poisoning.	Cyanides	28-35	proopiomelanocortin	Homo sapiens	0-4
12978069-0	1952	[Catalysis by methemoglobin, by alloxan and the action of cyanide].	Cyanides	58-65	hemoglobin subunit gamma 2	Homo sapiens	14-27
13417109-0	1957	Preliminary observations in the treatment of cyanide poisoning with pangametin (vitamin B15).	Cyanides	45-52	NADH:ubiquinone oxidoreductase subunit B4	Homo sapiens	88-91
12986498-0	1952	[Action of methemoglobin on cytochrome oxidases inhibited by cyanides].	Cyanides	61-69	hemoglobin subunit gamma 2	Homo sapiens	11-24
14838882-0	1951	On the cyanide inactivation of succinic dehydrogenase and the relation of succinic dehydrogenase to cytochrome b.	Cyanides	7-14	mitochondrially encoded cytochrome b	Homo sapiens	100-112
14886317-0	1951	On the cyanide inactivation of succinic dehydrogenase and the relation of succinic dehydrogenase to cytochrome b.	Cyanides	7-14	mitochondrially encoded cytochrome b	Homo sapiens	100-112
18134592-0	1949	The reaction of catalase and cyanide.	Cyanides	29-36	catalase	Homo sapiens	16-24
20985634-0	1946	A spectrophotometric study of the competition of methemoglobin and cytochrome oxidase for cyanide in vitro.	Cyanides	90-97	hemoglobin subunit gamma 2	Homo sapiens	49-62
19872729-1	1933	The potentiometric method was applied to the study of the influence of cyanide and of hydroxyl ion on methemoglobin.	Cyanides	71-78	hemoglobin subunit gamma 2	Homo sapiens	102-115
19872729-3	1933	From the magnitude of the effect produced by cyanide and by variation in pH on the oxidation-reduction potential of the methemoglobin-hemoglobin system, it is concluded that cyanmethemoglobin and alkaline methemoglobin are undissociated ferric compounds, the first with cyanide and the second with hydroxyl.	Cyanides	45-52	hemoglobin subunit gamma 2	Homo sapiens	120-133
19872729-3	1933	From the magnitude of the effect produced by cyanide and by variation in pH on the oxidation-reduction potential of the methemoglobin-hemoglobin system, it is concluded that cyanmethemoglobin and alkaline methemoglobin are undissociated ferric compounds, the first with cyanide and the second with hydroxyl.	Cyanides	45-52	hemoglobin subunit gamma 2	Homo sapiens	178-191
33826216-3	2021	Exposed to soft Lewis donors, Si(OTf)4 leads to [L2Si(OTf)4] complexes (L = isocyanide, thioether and carbonyl compounds) with retention of all Si-OTf bonds.	Cyanides	76-86	POC1 centriolar protein A	Homo sapiens	11-15
33826216-3	2021	Exposed to soft Lewis donors, Si(OTf)4 leads to [L2Si(OTf)4] complexes (L = isocyanide, thioether and carbonyl compounds) with retention of all Si-OTf bonds.	Cyanides	76-86	POU class 5 homeobox 1	Homo sapiens	49-59
33826216-3	2021	Exposed to soft Lewis donors, Si(OTf)4 leads to [L2Si(OTf)4] complexes (L = isocyanide, thioether and carbonyl compounds) with retention of all Si-OTf bonds.	Cyanides	76-86	POU class 5 homeobox 1	Homo sapiens	30-38
33892380-5	2021	We solved the "Lys-off" X-ray structure of THB1, represented by the cyanide adduct of the Fe(III) protein, and hypothesized that interactions that differ between the known "Lys-on" structure and the Lys-off structure participate in the control of Lys53 affinity for the heme iron.	Cyanides	68-75	uncharacterized protein	Chlamydomonas reinhardtii	43-47
34010566-1	2021	Monometallic cyanide clusterfullerenes (CYCFs) represent a unique branch of endohedral clusterfullerenes with merely one metal atom encapsulated, offering a model system for elucidating structure-property correlation, while up to now only C82 and C76 cages have been isolated for the pristine CYCFs.	Cyanides	13-20	complement C8 beta chain	Homo sapiens	239-242
34003742-7	2021	This coupled Rip1/PdtaS/PdtaR circuit controls NO resistance and acute lung infection in mice by relieving PdtaS/R-mediated repression of isonitrile chalkophore biosynthesis.	Cyanides	138-148	receptor (TNFRSF)-interacting serine-threonine kinase 1	Mus musculus	13-17
34027151-0	2021	Quercetin upregulates CREM gene expression in cyanide-induced endocrine dysfunction.	Cyanides	46-53	cAMP responsive element modulator	Rattus norvegicus	22-26
34027151-13	2021	Significant down-regulation of CREM gene and reduction in serum level of follicle stimulating hormone (FSH), Luteinizing hormone (LH), testosterone, glutathione peroxidase (GPx) and zinc in cyanide-treated groups, whereas administration of quercetin concomitantly with cyanide exposure or post-treated significantly reversed the alterations.	Cyanides	190-197	cAMP responsive element modulator	Rattus norvegicus	31-35
34027151-13	2021	Significant down-regulation of CREM gene and reduction in serum level of follicle stimulating hormone (FSH), Luteinizing hormone (LH), testosterone, glutathione peroxidase (GPx) and zinc in cyanide-treated groups, whereas administration of quercetin concomitantly with cyanide exposure or post-treated significantly reversed the alterations.	Cyanides	269-276	cAMP responsive element modulator	Rattus norvegicus	31-35
33853327-1	2021	The excited-state energy was tuned successfully by guest molecules in a cyanide-bridged luminescent coordination polymer (CP).	Cyanides	72-79	ceruloplasmin	Homo sapiens	122-124
33853327-5	2021	Furthermore, time-resolved infrared spectroscopy indicated that cyanide bridging in the CP became more flexible in the excited states than that in the ground state, highlighting the sensitivity of the excited states to external stimuli, such as the guest vapor.	Cyanides	64-71	ceruloplasmin	Homo sapiens	88-90
33859176-4	2021	The electric dipole moments of cyanide ions in Cd(CN)2 assume the role of magnetic pseudospins, with the difference in energy scale reflecting the increased strength of electric vs magnetic dipolar interactions.	Cyanides	31-38	carnosine dipeptidase 2	Homo sapiens	47-54
33885298-6	2021	The cationic species and their synthetic precursors [(iPrPNHP)FeBr(CNtBu)2]X (X = BPh4, Br) can have different configurations for the isocyanide ligands (cis or trans) and the H-N-Fe-H(Br) unit (syn or anti).	Cyanides	134-144	synemin	Homo sapiens	31-34
33620620-4	2021	Furthermore, the cyanide bound receptor detects Cr3+ by the relay recognition method.	Cyanides	17-24	teratocarcinoma-derived growth factor 1 pseudogene 3	Homo sapiens	48-51
33280385-2	2021	Previous studies established that extending the pi-system of 2,6-diisopropylphenylisocyanide (CNDipp) by coupling aryl substituents para to the isocyanide functionality results in W(CNDippAr)6 oligoarylisocyanide complexes with greatly enhanced metal-to-ligand charge transfer (MLCT) excited-state properties relative to those of W(CNDipp)6.	Cyanides	82-92	nudix hydrolase 3	Homo sapiens	94-100
33331975-6	2021	However, established analytical methods for quantification of free cyanide only obtain limits of quantification (LOQs) in the range of 1 mug L-1.	Cyanides	67-74	TARBP2 subunit of RISC loading complex	Homo sapiens	113-117
3209423-6	1988	This compared to a non-linear reduction of NBT during the initial stages of the reactions (SDH and "nothing dehydrogenase") when using PMS and cyanide.	Cyanides	143-150	succinate dehydrogenase complex iron sulfur subunit B	Homo sapiens	91-94
33146011-1	2020	An efficient, safe, and environmentally friendly tertiary butyl hydrogen peroxide (TBHP)-mediated rearrangement of aryl/alkylidene malononitrile with anilines has been developed with in situ generation of HCN as the cyanide source for the synthesis of substituted alpha-aminonitriles and alpha-aminoamide.	Cyanides	216-223	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	205-208
33144263-5	2021	Herein, we attempt to clarify the effects of defined thiol oxidation states on small molecule binding of cytoglobin heme, using cyanide binding to probe the ferric state.	Cyanides	128-135	cytoglobin	Homo sapiens	105-115
33144263-6	2021	Cyanide binding kinetics to wild-type cytoglobin reveal at least two kinetically distinct subpopulations, depending on thiol oxidation states.	Cyanides	0-7	cytoglobin	Homo sapiens	38-48
32640058-2	2020	Three of the complexes ( 1 - 3 ) are of the general formula cis -Pt(CNR) 2 (C CPh) 2 , where CNR is a variably substituted isocyanide and C CPh is phenylacetylide.	Cyanides	123-133	cannabinoid receptor 2	Homo sapiens	65-84
33271974-0	2020	Isocyanide Multicomponent Reactions on Solid Phase: State of the Art and Future Application.	Cyanides	0-10	artemin	Homo sapiens	65-68
33256058-3	2020	In this study, a glutamate-urea-based PSMA-targeted ligand containing an isonitrile (CNGU) was synthesized and labeled with 99mTc to prepare [99mTc]Tc-CNGU with a high radiochemical purity (RCP).	Cyanides	73-83	folate hydrolase 1	Homo sapiens	38-42
33266406-2	2020	SPL-1cut is classified as hazardous waste in China because it contains large amounts of soluble sodium fluoride and a tiny amount of cyanide.	Cyanides	133-140	sphingosine-1-phosphate lyase 1	Homo sapiens	0-5
33179677-1	2020	The reaction of GaIIIClPc, SnIVCl2TPP and BIIIClSubPc containing phthalocyanine (Pc), tetraphenylporphyrin (TPP) and subphthalocyanine (SubPc) macrocycles with cyanide in the presence of cryptand[2.2.2] under anaerobic conditions yields crystalline salts in which cyano anions substitute chloride anions at GaIII, SnIV or BIII, as well as reducing the macrocycles or adding one or two CN- to them.	Cyanides	160-167	calcium voltage-gated channel subunit alpha1 B	Homo sapiens	42-46
33179677-1	2020	The reaction of GaIIIClPc, SnIVCl2TPP and BIIIClSubPc containing phthalocyanine (Pc), tetraphenylporphyrin (TPP) and subphthalocyanine (SubPc) macrocycles with cyanide in the presence of cryptand[2.2.2] under anaerobic conditions yields crystalline salts in which cyano anions substitute chloride anions at GaIII, SnIV or BIII, as well as reducing the macrocycles or adding one or two CN- to them.	Cyanides	264-269	calcium voltage-gated channel subunit alpha1 B	Homo sapiens	42-46
33146011-3	2020	This method features a broad substrate scope and good functional group tolerance, and the in situ-generated HCN bypasses the use of an external cyanide source.	Cyanides	144-151	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	108-111
33055309-3	2021	MPST activity is known to be involved in hydrogen sulfide (H2S) generation, tRNA thiolation, protein urmylation and cyanide detoxification.	Cyanides	116-123	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
32631055-4	2020	Here we cover from the initial applications of NIITP in the Nef isocyanide reaction to further derivations that render a variety of heterocyclic scaffolds.	Cyanides	64-74	S100 calcium binding protein B	Homo sapiens	60-63
32485159-4	2020	The strength of the coupling was evaluated by the determination of pH dependence of the midpoint potential of heme a (Em(a)) for the cyanide (the low-spin Fea33+) and the formate-ligated CcO (the high-spin Fea33+).	Cyanides	133-140	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	187-190
30372625-6	2020	In most studies conducted in rat liver, only the Cu,Zn or total SOD activities were assessed and sometimes the Cu,ZnSOD activity was calculated based on the inhibition by cyanide.	Cyanides	171-178	superoxide dismutase 1	Rattus norvegicus	111-119
32370496-8	2020	In addition, by using LC-MS/MS, GEF is metabolized in the rat heart microsomes into one cyanide- and two methoxylamine-adducts reactive metabolites, where their formation was entirely blocked by CYP1A1 inhibitor,  -naphthoflavone.	Cyanides	88-95	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	195-201
32401019-2	2020	Aqueous catalytic reaction conditions were explored where at the conditions employed the reaction proceeded to exhaustion in 1 h. The complex, syn-[Mo2O2(mu-S)2(S2)(DMF)3] 1, participates in a ligand exchange reaction of the dimethylformamide ligands and cyanide.	Cyanides	255-262	synemin	Homo sapiens	143-146
32170827-4	2020	As another example, oxidation of 10-10"-linked bis-pyridine-coordinated CoIII corrole dimer with DDQ produced a cobalt corrole radical dimer and a doubly-linked corrole dimer both as stable compounds bearing pyridine and cyanide axial ligands.	Cyanides	221-228	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	72-77
32170827-5	2020	Bis-pyridine-coordinated CoIII corrole monomer was also converted to the corresponding corrole radical upon treatment with cyanide anion.	Cyanides	123-136	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	25-30
32401019-0	2020	Reaction Chemistry of the syn-[Mo2O2(mu-S)2(S2)(DMF)3] Complex with Cyanide and Catalytic Thiocyanate Formation.	Cyanides	68-75	synemin	Homo sapiens	26-29
32401019-0	2020	Reaction Chemistry of the syn-[Mo2O2(mu-S)2(S2)(DMF)3] Complex with Cyanide and Catalytic Thiocyanate Formation.	Cyanides	68-75	adaptor related protein complex 1 subunit mu 2	Homo sapiens	37-43
32027458-4	2020	Both anions can be considered members of highly labile cyanide HCN-solvates of the type [CN(HCN) n ] - ( n = 1, 2, 3 ...) as well as formal polypseudohalide ions.	Cyanides	55-62	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	63-66
32027458-4	2020	Both anions can be considered members of highly labile cyanide HCN-solvates of the type [CN(HCN) n ] - ( n = 1, 2, 3 ...) as well as formal polypseudohalide ions.	Cyanides	55-62	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	92-95
32061776-2	2020	After its initial identification as a cyanide detoxification enzyme, it was found that its functions also include sulfur metabolism, modification of iron-sulfur clusters and the reduction of antioxidants glutathione and thioredoxin.	Cyanides	38-45	thioredoxin	Homo sapiens	220-231
32401019-2	2020	Aqueous catalytic reaction conditions were explored where at the conditions employed the reaction proceeded to exhaustion in 1 h. The complex, syn-[Mo2O2(mu-S)2(S2)(DMF)3] 1, participates in a ligand exchange reaction of the dimethylformamide ligands and cyanide.	Cyanides	255-262	adaptor related protein complex 1 subunit mu 2	Homo sapiens	154-160
32367820-6	2020	Thermogravimetric analysis indicates an initial loss of the base cation and one cyanide as HCN at temperatures in the range 130-250  C to form CuCN.	Cyanides	80-87	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	91-94
31951058-7	2020	The cyanide (CN)-resistant alternative respiration (Alt) mediated by AOX is significantly reduced in myb30-2 mutant due to loss-of-function of MYB30.	Cyanides	4-11	myb domain protein 30	Arabidopsis thaliana	143-148
31951058-7	2020	The cyanide (CN)-resistant alternative respiration (Alt) mediated by AOX is significantly reduced in myb30-2 mutant due to loss-of-function of MYB30.	Cyanides	13-15	myb domain protein 30	Arabidopsis thaliana	101-106
31951058-7	2020	The cyanide (CN)-resistant alternative respiration (Alt) mediated by AOX is significantly reduced in myb30-2 mutant due to loss-of-function of MYB30.	Cyanides	13-15	myb domain protein 30	Arabidopsis thaliana	143-148
32347262-1	2020	New trinuclear gold(i) N-arylimidazolate cluster complexes have been synthesized from cationic [Au(CNR)2]+ isocyanide complexes and their structure and photoluminescence behavior have been compared with those of their 1-methylimidazolate counterpart.	Cyanides	107-117	cannabinoid receptor 2	Homo sapiens	99-104
31951058-7	2020	The cyanide (CN)-resistant alternative respiration (Alt) mediated by AOX is significantly reduced in myb30-2 mutant due to loss-of-function of MYB30.	Cyanides	4-11	myb domain protein 30	Arabidopsis thaliana	101-106
32314761-1	2020	Three cyanide-bridged {Fe2Fe} complexes of formula {[(TpR)Fe(CN)3]2[Fe(bnbpen)]} S (TpR = Tp for 1 S, Tp3-Me for 2 S, and Tp* for 3 S, respectively; bnbpen = N,N"-bis-(2-naphthylmethyl)-N,N"-bis(2-picolyl)-ethylenediamine) have been prepared and characterized here.	Cyanides	6-13	translocated promoter region, nuclear basket protein	Homo sapiens	54-57
32314761-1	2020	Three cyanide-bridged {Fe2Fe} complexes of formula {[(TpR)Fe(CN)3]2[Fe(bnbpen)]} S (TpR = Tp for 1 S, Tp3-Me for 2 S, and Tp* for 3 S, respectively; bnbpen = N,N"-bis-(2-naphthylmethyl)-N,N"-bis(2-picolyl)-ethylenediamine) have been prepared and characterized here.	Cyanides	6-13	translocated promoter region, nuclear basket protein	Homo sapiens	84-87
32200199-0	2020	Structure-based discovery of novel 4-(2-fluorophenoxy)quinoline derivatives as c-Met inhibitors using isocyanide-involved multicomponent reactions.	Cyanides	102-112	steroid sulfatase	Homo sapiens	76-80
32260280-7	2020	Specific cyanide and benzene ring parts of RT"s structure were identified to be critical for its Mcl-1-targeting activity.	Cyanides	9-16	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	97-102
32146510-3	2020	Here, the kinetics of cyanide and carbon monoxide dissociation from ferrous-ligated Hp:Hb complexes are reported at pH 7.0 and 20.0  C. Cyanide dissociation from Hp1-1:Hb(II)-CN- and Hp2-2:Hb-CN- has been followed upon the dithionite-mediated conversion of ferric to ferrous-ligated Hp:Hb complexes.	Cyanides	22-29	chromobox 5	Homo sapiens	162-167
32146510-3	2020	Here, the kinetics of cyanide and carbon monoxide dissociation from ferrous-ligated Hp:Hb complexes are reported at pH 7.0 and 20.0  C. Cyanide dissociation from Hp1-1:Hb(II)-CN- and Hp2-2:Hb-CN- has been followed upon the dithionite-mediated conversion of ferric to ferrous-ligated Hp:Hb complexes.	Cyanides	22-29	ADP ribosylation factor like GTPase 6 interacting protein 5	Homo sapiens	183-188
32146510-3	2020	Here, the kinetics of cyanide and carbon monoxide dissociation from ferrous-ligated Hp:Hb complexes are reported at pH 7.0 and 20.0  C. Cyanide dissociation from Hp1-1:Hb(II)-CN- and Hp2-2:Hb-CN- has been followed upon the dithionite-mediated conversion of ferric to ferrous-ligated Hp:Hb complexes.	Cyanides	136-143	chromobox 5	Homo sapiens	162-167
32146510-3	2020	Here, the kinetics of cyanide and carbon monoxide dissociation from ferrous-ligated Hp:Hb complexes are reported at pH 7.0 and 20.0  C. Cyanide dissociation from Hp1-1:Hb(II)-CN- and Hp2-2:Hb-CN- has been followed upon the dithionite-mediated conversion of ferric to ferrous-ligated Hp:Hb complexes.	Cyanides	136-143	ADP ribosylation factor like GTPase 6 interacting protein 5	Homo sapiens	183-188
32146510-5	2020	Values of the first-order rate constant (i.e., h) for cyanide dissociation from Hp1-1:Hb(II)-CN- and Hp2-2:Hb(II)-CN- are (1.2 +- 0.2) x 10-1 s-1 and (1.3 +- 0.2) x 10-1 s-1, respectively.	Cyanides	54-61	chromobox 5	Homo sapiens	80-85
32146510-5	2020	Values of the first-order rate constant (i.e., h) for cyanide dissociation from Hp1-1:Hb(II)-CN- and Hp2-2:Hb(II)-CN- are (1.2 +- 0.2) x 10-1 s-1 and (1.3 +- 0.2) x 10-1 s-1, respectively.	Cyanides	54-61	ADP ribosylation factor like GTPase 6 interacting protein 5	Homo sapiens	101-106
32108847-2	2020	The imidoyl-palladium intermediate generated by tandem indole double bond/isocyanide insertion reactions could be trapped by intramolecular functional groups such as the C(sp2)-H bond and alkenes, affording diversified indoline derivatives bearing C3 imine-containing heterocycles.	Cyanides	74-84	Sp2 transcription factor	Homo sapiens	170-175
31858584-1	2020	beta-Cyanoalanine synthase (beta-CAS) is an enzyme involved in cyanide detoxification.	Cyanides	63-70	bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial	Nicotiana tabacum	0-26
31858584-1	2020	beta-Cyanoalanine synthase (beta-CAS) is an enzyme involved in cyanide detoxification.	Cyanides	63-70	bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial	Nicotiana tabacum	28-36
31858584-5	2020	These findings present novel insights into the synergistic effect between beta-CAS and AOX in protecting plants from salt stress, where beta-CAS plays a vital role in restraining cyanide accumulation, and AOX helps to alleviate the toxic effect of cyanide.	Cyanides	179-186	bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial	Nicotiana tabacum	74-82
31858584-5	2020	These findings present novel insights into the synergistic effect between beta-CAS and AOX in protecting plants from salt stress, where beta-CAS plays a vital role in restraining cyanide accumulation, and AOX helps to alleviate the toxic effect of cyanide.	Cyanides	179-186	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	87-90
31858584-5	2020	These findings present novel insights into the synergistic effect between beta-CAS and AOX in protecting plants from salt stress, where beta-CAS plays a vital role in restraining cyanide accumulation, and AOX helps to alleviate the toxic effect of cyanide.	Cyanides	179-186	bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial	Nicotiana tabacum	136-144
31858584-5	2020	These findings present novel insights into the synergistic effect between beta-CAS and AOX in protecting plants from salt stress, where beta-CAS plays a vital role in restraining cyanide accumulation, and AOX helps to alleviate the toxic effect of cyanide.	Cyanides	248-255	bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial	Nicotiana tabacum	74-82
31858584-5	2020	These findings present novel insights into the synergistic effect between beta-CAS and AOX in protecting plants from salt stress, where beta-CAS plays a vital role in restraining cyanide accumulation, and AOX helps to alleviate the toxic effect of cyanide.	Cyanides	248-255	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	87-90
31858584-5	2020	These findings present novel insights into the synergistic effect between beta-CAS and AOX in protecting plants from salt stress, where beta-CAS plays a vital role in restraining cyanide accumulation, and AOX helps to alleviate the toxic effect of cyanide.	Cyanides	248-255	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	205-208
31948575-1	2020	Cyanide (both HCN and CN- are represented by CN) has multiple industrial applications, is commonly found in some foods, and is a component of fire smoke.	Cyanides	0-7	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	14-17
31990092-2	2020	Herein, an unexpected reverse effect is observed for the first time in the S = 1/2 {Fe II LS - Co III LS - Fe III LS } (HS = high spin, LS = low spin) ground state of a novel V-shaped trinuclear cyanide-bridged {Fe 2 Co} complex.	Cyanides	195-202	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	95-101
32012740-1	2020	Mercaptopyruvate sulfurtransferase (Mpst) and its homolog thiosulfate sulfurtransferase (Tst = rhodanese) detoxify cyanide to thiocyanate.	Cyanides	115-122	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	58-87
32101433-7	2020	The isocyanide ligands in complex 10 undergo a reductive coupling reaction in toluene to give the titanium(IV) iminoacyl derivative [{Ti(eta5-C5Me5)Cl2}2(mu-eta2:eta2-tBuN C-C NtBu)] (11).	Cyanides	4-14	DNA polymerase iota	Homo sapiens	157-161
32101433-7	2020	The isocyanide ligands in complex 10 undergo a reductive coupling reaction in toluene to give the titanium(IV) iminoacyl derivative [{Ti(eta5-C5Me5)Cl2}2(mu-eta2:eta2-tBuN C-C NtBu)] (11).	Cyanides	4-14	DNA polymerase iota	Homo sapiens	162-166
32012740-1	2020	Mercaptopyruvate sulfurtransferase (Mpst) and its homolog thiosulfate sulfurtransferase (Tst = rhodanese) detoxify cyanide to thiocyanate.	Cyanides	115-122	mercaptopyruvate sulfurtransferase	Mus musculus	0-34
32012740-1	2020	Mercaptopyruvate sulfurtransferase (Mpst) and its homolog thiosulfate sulfurtransferase (Tst = rhodanese) detoxify cyanide to thiocyanate.	Cyanides	115-122	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	89-92
32012740-1	2020	Mercaptopyruvate sulfurtransferase (Mpst) and its homolog thiosulfate sulfurtransferase (Tst = rhodanese) detoxify cyanide to thiocyanate.	Cyanides	115-122	mercaptopyruvate sulfurtransferase	Mus musculus	36-40
31383327-2	2019	Conversion of plant derived thiocyanates into cyanide and isocyanic acid occurs by the activity of neutrophil-derived enzyme myeloperoxidase.	Cyanides	46-53	myeloperoxidase	Homo sapiens	125-140
31594612-6	2020	The limit of detection for cyanide ion was calculated as low as 0.45 muM.	Cyanides	27-34	latexin	Homo sapiens	69-72
32470868-1	2020	INTRODUCTION: 99mTc-labeled hexavalent probes can be readily synthesized by the coordination of six equivalent isocyanide ligands towards TcI, and alkyl isocyanide ligands have been extensively used for preparing such probes.	Cyanides	111-121	transcobalamin 1	Homo sapiens	138-141
31584578-0	2019	A colorimetric probe for the real-time naked eye detection of cyanide and hydroxide ions in tap water: experimental and theoretical studies.	Cyanides	62-69	nuclear RNA export factor 1	Homo sapiens	92-95
31584578-2	2019	The molar addition of anions, such as TBAF-, TBAOH-, TBACN- and TBAAcO-, induced a significant red shift in the charge transfer band (Deltalambda = 73 nm, from 337 nm to 410 nm), in agreement with visible "naked eye" detectable colorimetric activities; in addition, soaked-in-L paper strips were prepared, which could significantly discriminate cyanide (KCN) and hydroxide (NaOH) ions dissolved in tap water via the litmus test method.	Cyanides	345-352	nuclear RNA export factor 1	Homo sapiens	398-401
29609494-0	2019	Oxidative damage mediated iNOS and UCP-2 upregulation in rat brain after sub-acute cyanide exposure: dose and time-dependent effects.	Cyanides	83-90	nitric oxide synthase 2	Rattus norvegicus	26-30
29609494-0	2019	Oxidative damage mediated iNOS and UCP-2 upregulation in rat brain after sub-acute cyanide exposure: dose and time-dependent effects.	Cyanides	83-90	uncoupling protein 2	Rattus norvegicus	35-40
29609494-3	2019	The present study addresses the dose- and time-dependent effect of sub-acute cyanide exposure on various non-enzymatic and enzymatic oxidative stress markers and their correlation with inducible-nitric oxide synthase (iNOS) and uncoupling protein-2 (UCP-2) expression.	Cyanides	77-84	nitric oxide synthase 2	Rattus norvegicus	185-216
29609494-3	2019	The present study addresses the dose- and time-dependent effect of sub-acute cyanide exposure on various non-enzymatic and enzymatic oxidative stress markers and their correlation with inducible-nitric oxide synthase (iNOS) and uncoupling protein-2 (UCP-2) expression.	Cyanides	77-84	nitric oxide synthase 2	Rattus norvegicus	218-222
29609494-3	2019	The present study addresses the dose- and time-dependent effect of sub-acute cyanide exposure on various non-enzymatic and enzymatic oxidative stress markers and their correlation with inducible-nitric oxide synthase (iNOS) and uncoupling protein-2 (UCP-2) expression.	Cyanides	77-84	uncoupling protein 2	Rattus norvegicus	228-248
29609494-3	2019	The present study addresses the dose- and time-dependent effect of sub-acute cyanide exposure on various non-enzymatic and enzymatic oxidative stress markers and their correlation with inducible-nitric oxide synthase (iNOS) and uncoupling protein-2 (UCP-2) expression.	Cyanides	77-84	uncoupling protein 2	Rattus norvegicus	250-255
29609494-8	2019	It was concluded that long-term cyanide exposure caused oxidative stress, accompanied by upregulation of iNOS.	Cyanides	32-39	nitric oxide synthase 2	Rattus norvegicus	105-109
29609494-9	2019	The upregulation of UCP-2 further sensitized the cells to cyanide and accentuated the oxidative stress, which was independent of DNA damage.	Cyanides	58-65	uncoupling protein 2	Rattus norvegicus	20-25
31711010-5	2019	The amount of CN probably bound to the cytochrome c oxidase of the tissue cells (CCO-CN) was extrapolated from CN and hemoglobin contents in RHB and organs/tissues, MetHb saturation in RHB and binding capacity of MetHb for CN.	Cyanides	14-16	hemoglobin subunit gamma 2	Homo sapiens	165-170
31603399-6	2019	Application of physical, natural, biological, and chemical methods to detoxify cyanide to a permissible limit (50 mg L-1) can be achieved when the chemical compositions of cyanide (type of species) present in the tailings are known.	Cyanides	79-86	immunoglobulin kappa variable 1-16	Homo sapiens	117-120
31603399-6	2019	Application of physical, natural, biological, and chemical methods to detoxify cyanide to a permissible limit (50 mg L-1) can be achieved when the chemical compositions of cyanide (type of species) present in the tailings are known.	Cyanides	172-179	immunoglobulin kappa variable 1-16	Homo sapiens	117-120
31432680-1	2019	Using tetraaryllead compounds (PbAr4) as arylating reagents, isocyanides undergo selective diarylation in the presence of palladium catalysts such as Pd(OAc)2 or Pd(PPh3)4 to afford imines and/or alpha-diimines based on the isocyanide employed.	Cyanides	61-72	protein phosphatase 4 catalytic subunit	Homo sapiens	165-169
31432680-1	2019	Using tetraaryllead compounds (PbAr4) as arylating reagents, isocyanides undergo selective diarylation in the presence of palladium catalysts such as Pd(OAc)2 or Pd(PPh3)4 to afford imines and/or alpha-diimines based on the isocyanide employed.	Cyanides	61-71	protein phosphatase 4 catalytic subunit	Homo sapiens	165-169
31733428-4	2020	Cyanide and fluoride bind to Hb(III), Hp1-1:Hb(III), Hp2-2:Hb(III), alpha(III), and beta(III) with a simple behavior.	Cyanides	0-7	chromobox 5	Homo sapiens	38-41
31799552-0	2019	Correction: A colorimetric probe for the real-time naked eye detection of cyanide and hydroxide ions in tap water: experimental and theoretical studies.	Cyanides	74-81	nuclear RNA export factor 1	Homo sapiens	104-107
31799552-1	2019	Correction for "A colorimetric probe for the real-time naked eye detection of cyanide and hydroxide ions in tap water: experimental and theoretical studies" by Veikko Uahengo et al., Analyst, 2019, 144, 6422-6431.	Cyanides	78-85	nuclear RNA export factor 1	Homo sapiens	108-111
31299615-1	2019	Here in we report tris (3-aminopropyl) amine based tripodal receptors L, L1 and L2 which were functionalized with 4-nitrophenyl moieties having thio-urea, amide and sulfonamide as hydrogen bonding moieties respectively, shows a strong selectivity towards cyanide.	Cyanides	255-262	L1 cell adhesion molecule	Homo sapiens	73-82
31299615-3	2019	To the best of our knowledge, this is the first example of a naked-eye detection of cyanide via fluoride displacement assay by a tripodal receptor and such a displacement phenomenon is not observes in the cases of L1 and L2, instead the receptor L1 binds nitrate and cyanide; L2 binds dihydrogen phosphate and cyanide.	Cyanides	84-91	L1 cell adhesion molecule	Homo sapiens	214-223
31620758-3	2019	Starting with the end-on coordination of the isocyanide to the zirconium centre (2), elevated reaction temperatures and an excess of tert-butylisocyanide resulted after the elimination of the alkyne in the formation of zirconocene eta2-iminoacyl cyanide complexes 3a-d.	Cyanides	45-55	DNA polymerase iota	Homo sapiens	231-235
31711010-5	2019	The amount of CN probably bound to the cytochrome c oxidase of the tissue cells (CCO-CN) was extrapolated from CN and hemoglobin contents in RHB and organs/tissues, MetHb saturation in RHB and binding capacity of MetHb for CN.	Cyanides	14-16	hemoglobin subunit gamma 2	Homo sapiens	213-218
31711010-5	2019	The amount of CN probably bound to the cytochrome c oxidase of the tissue cells (CCO-CN) was extrapolated from CN and hemoglobin contents in RHB and organs/tissues, MetHb saturation in RHB and binding capacity of MetHb for CN.	Cyanides	85-87	hemoglobin subunit gamma 2	Homo sapiens	165-170
31711010-5	2019	The amount of CN probably bound to the cytochrome c oxidase of the tissue cells (CCO-CN) was extrapolated from CN and hemoglobin contents in RHB and organs/tissues, MetHb saturation in RHB and binding capacity of MetHb for CN.	Cyanides	85-87	hemoglobin subunit gamma 2	Homo sapiens	165-170
31711010-5	2019	The amount of CN probably bound to the cytochrome c oxidase of the tissue cells (CCO-CN) was extrapolated from CN and hemoglobin contents in RHB and organs/tissues, MetHb saturation in RHB and binding capacity of MetHb for CN.	Cyanides	85-87	hemoglobin subunit gamma 2	Homo sapiens	165-170
31322637-2	2019	In the presence of Na, 1 can promote linear- and cyclo-trimerization of isocyanides, affording products [Na][LAl{(tBuNC)3}AlL] (3 and 4) and [Na][LAl{(tBuNC)3}Al(C[triple bond, length as m-dash]N)L] (5), the latter of which features a unique aromatic tri(tert-butylimino)deltate dianion [C3N3(tBu)3]2-.	Cyanides	72-83	paired box 5	Homo sapiens	122-135
31117244-6	2019	The naked eye detection limit was 10 mug L-1 where the World Health Organization (WHO) have regulated the maximum level of cyanide in drinking water as 70 mug L-1.	Cyanides	123-130	immunoglobulin kappa variable 1-16	Homo sapiens	41-44
31343035-1	2019	The construction of fully decorated 1,2,3-triazole-fused 5-, 6- and 7-membered rings has been disclosed via a bimetallic relay-catalyzed cascade process combining azide-alkyne cycloaddition, C(sp2)-H functionalization of intermediary 1,2,3-triazoles and isocyanide insertion.	Cyanides	254-264	Sp2 transcription factor	Homo sapiens	191-196
31339323-1	2019	A highly enantioselective ring-opening desymmetrization of meso-aziridines with isocyanides was achieved in the presence of a chiral N,N"-dioxide/Mg(OTf)2 complex.	Cyanides	80-91	POU class 2 homeobox 2	Homo sapiens	149-154
30959343-0	2019	Tri-(2-picolyl)amine-modificated triarylborane: Synthesis, photophysical properties and distinguish for cyanide and fluoride anions in aqueous solution.	Cyanides	104-111	tRNA-Ile (anticodon AAT) 9-1	Homo sapiens	0-3
30920109-1	2019	A hydrogen-bonding donor-acceptor system, [Co2 Fe2 (bpy*)4 (CN)6 (tp*)2 ](PF6 )2  2ABA 4BN 2PE (1 solv ), was prepared by co-crystallization of an external stimuli-responsive cyanide-bridged tetranuclear [Co2 Fe2 ] complex and bifunctional hydrogen-bonding donors, p-aminobenzoic acid.	Cyanides	175-182	sperm associated antigen 17	Homo sapiens	74-77
31173149-0	2019	The central role of protein kinase C epsilon in cyanide cardiotoxicity and its treatment.	Cyanides	48-55	protein kinase C, epsilon	Mus musculus	20-44
31244408-6	2019	Cyanide induces oxidative stress by inhibiting metalloenzymes (catalase and superoxide dismutase) causing increase in lipid peroxidation (malondialdehyde) and decrease in reduced glutathione (GSH).	Cyanides	0-7	catalase	Rattus norvegicus	63-96
31117244-6	2019	The naked eye detection limit was 10 mug L-1 where the World Health Organization (WHO) have regulated the maximum level of cyanide in drinking water as 70 mug L-1.	Cyanides	123-130	immunoglobulin kappa variable 1-16	Homo sapiens	159-162
31117244-8	2019	Finally, our device has been successfully applied to determine cyanide ions in seawater, drinking water, tap water and wastewater providing satisfactory precision and accuracy.	Cyanides	63-70	nuclear RNA export factor 1	Homo sapiens	105-108
31050283-1	2019	A general method to construct the scaffolds of dibenzooxazepine and dibenzodiazepine, through Pd-catalyzed isocyanide insertion and intramolecular C(sp2)-H activation, has been developed.	Cyanides	107-117	Sp2 transcription factor	Homo sapiens	147-152
30893999-2	2019	The resulting eta2-benzenium complex reacts with a wide range of nucleophiles including protected enolates, cyanide, amines, methoxide, and aromatic nucleophiles to form 5-substituted 3,4-eta2-1,3-cyclohexadiene complexes in good yield (42-70%).	Cyanides	108-115	DNA polymerase iota	Homo sapiens	14-18
30893999-2	2019	The resulting eta2-benzenium complex reacts with a wide range of nucleophiles including protected enolates, cyanide, amines, methoxide, and aromatic nucleophiles to form 5-substituted 3,4-eta2-1,3-cyclohexadiene complexes in good yield (42-70%).	Cyanides	108-115	DNA polymerase iota	Homo sapiens	188-192
30935547-2	2019	However, due to metabolization of amygdalin to cyanide (HCN) following oral consumption, there could be a high risk of lactic acidosis caused by cyanide intoxication.	Cyanides	47-54	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	56-59
30662014-4	2019	Both catalysts showed almost the same catalytic reaction and the catalytic reaction was instantaneous at room temperature with a minimum concentration of cyanide ions of up to 1.0 muM.	Cyanides	154-161	latexin	Homo sapiens	180-183
30724077-1	2019	The direct analysis of cyanide (HCN or CN- inclusively symbolized as CN) to confirm exposure has major limitations due to cyanide"s volatility, reactivity, and short half-life in biological fluids.	Cyanides	23-30	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	32-35
30935547-2	2019	However, due to metabolization of amygdalin to cyanide (HCN) following oral consumption, there could be a high risk of lactic acidosis caused by cyanide intoxication.	Cyanides	145-152	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	56-59
30361767-8	2019	Then we confirmed that the cyanide binding kinetics were isomer dependent on wild-type Ngb and A90P and F106L variants.	Cyanides	27-34	neuroglobin	Homo sapiens	87-90
30776613-4	2019	The biological samples, which were obtained from women staying in a maternity ward, showed cyanide concentrations spanning 1.82-98.47 mug L-1.	Cyanides	91-98	immunoglobulin kappa variable 1-16	Homo sapiens	138-141
30822766-4	2019	The LOD of cyanide by R in water is 0.6 muM, which is much lower than the permissible limit of cyanide in drinking water according to the WHO.	Cyanides	11-18	latexin	Homo sapiens	40-43
30624005-3	2019	For BCl3 , the formation of the isocyanide adduct [(CN)BCl3 ]- and the corresponding Wheland complex was verified by mass spectrometry.	Cyanides	32-42	BCL3 transcription coactivator	Homo sapiens	4-8
30624005-3	2019	For BCl3 , the formation of the isocyanide adduct [(CN)BCl3 ]- and the corresponding Wheland complex was verified by mass spectrometry.	Cyanides	32-42	BCL3 transcription coactivator	Homo sapiens	55-59
30348419-7	2019	Quenching of the NIR emission upon interaction of the Ag2S quantum dots with cyanide ions was observed.	Cyanides	77-84	angiotensin II receptor type 1	Homo sapiens	54-58
30359465-0	2019	Asymmetric Carboxycyanation of Aldehydes by Cooperative AlF/Onium Salt Catalysts: from Cyanoformate to KCN as Cyanide Source.	Cyanides	110-117	afamin	Homo sapiens	56-59
30557002-7	2019	(NMe4)3MnII5(CN)13 possesses one low-spin octahedral and four high-spin pentacoordinate MnII sites and orders as an antiferromagnet at 11 K due to the layers being bridged and antiferromagnetically coupled by the nonmagnetic cyanides.	Cyanides	225-233	NME/NM23 nucleoside diphosphate kinase 4	Homo sapiens	1-5
30431281-1	2018	A nickel-catalyzed cyanation of unactivated secondary alkyl chlorides or bromides using less toxic Zn(CN)2 as the cyanide source has been developed.	Cyanides	114-121	carnosine dipeptidase 2	Homo sapiens	99-106
30152699-0	2018	Co(II)/Ag(I) Synergistically Catalyzed Monoinsertion Reaction of Isocyanide to Terminal Alkynes with H2O: Synthesis of Alkynamide Derivatives.	Cyanides	65-75	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	0-6
30318551-4	2018	By monitoring the surface-enhanced Raman signal change of isonitrile probes in the hot spot, it was revealed that gold and platinum nanoparticles show opposite directions of charge transfer over the same formaldehyde treatment.	Cyanides	58-68	alcohol dehydrogenase iron containing 1	Homo sapiens	83-86
29886332-0	2018	Degradation mechanism of cyanide in water using a UV-LED/H2O2/Cu2+ system.	Cyanides	25-32	small integral membrane protein 10 like 2A	Homo sapiens	53-56
29886332-1	2018	In this study, we developed a UV-LED/H2O2/Cu2+ system to remove cyanide, which is typically present in metal electroplating wastewater.	Cyanides	64-71	small integral membrane protein 10 like 2A	Homo sapiens	33-36
29886332-2	2018	The results showed the synergistic effects of UV-LED, H2O2, and Cu2+ ions on cyanide removal in comparison with UV-LED photolysis, H2O2 oxidation, UV-LED/H2O2, and H2O2/Cu2+ systems.	Cyanides	77-84	small integral membrane protein 10 like 2A	Homo sapiens	49-52
29886332-3	2018	Cyanide was removed completely in 30 min in the UV-LED/H2O2/Cu2+ system, and its loss followed pseudo-first order kinetics.	Cyanides	0-7	small integral membrane protein 10 like 2A	Homo sapiens	51-54
29886332-11	2018	In terms of removal efficiency and toxicity reduction, the UV-LED/H2O2/Cu2+ system may be an alternative method of cyanide removal from wastewaters.	Cyanides	115-122	small integral membrane protein 10 like 2A	Homo sapiens	62-65
30035828-1	2018	The newly discovered gold-catalysed reaction of isocyanides with hydrazoic acid generated in situ from trimethylsilyl azide and methanol (or, alternatively, from NaN3 /AcOH) produces either cyanamides or 1-substituted 1H-tetrazol-5-amines, depending on the amount of available HN3 .	Cyanides	48-59	MT-RNR2 like 3 (pseudogene)	Homo sapiens	277-280
30425157-0	2018	Setting and Diffusing the Cyanide Bomb in Plant Defense.	Cyanides	26-33	WW and C2 domain containing 2	Homo sapiens	34-38
30137112-0	2018	Relay tricyclic Pd(ii)/Ag(i) catalysis: design of a four-component reaction driven by nitrene-transfer on isocyanide yields inhibitors of EGFR.	Cyanides	106-116	epidermal growth factor receptor	Homo sapiens	138-142
30152699-1	2018	A Co(II)/Ag(I) synergistically catalyzed three-component reaction of isocyanide with terminal alkyne and water to afford alkynamide derivatives is reported.	Cyanides	69-79	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	2-8
30152699-3	2018	This synergistic process achieves the cleavage of a C-H bond and the construction of new C-C and C O bonds under mild conditions through the reaction of Co(II)-activated isocyanides and a Ag(I)-complex-activated terminal alkyne.	Cyanides	170-181	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	153-158
30083689-1	2018	An efficient three-step synthesis of a novel family of enantiomerically pure isocyanides derived from beta3-isocyanopropionic acids was elaborated.	Cyanides	77-88	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	102-107
30130097-5	2018	DFT calculations indicated an interesting correlation between the Wiberg bond indices (WBI) of Cu-H bonds and their natural atomic charge (NAC), where the isocyanide ligands had an appreciable influence on the Cu-H interactions.	Cyanides	155-165	synuclein alpha	Homo sapiens	139-142
30083689-4	2018	As a result a new family of isocyanides bearing a fragment of beta3-amino acids with different functional groups (amides, esters and short peptides) was obtained.	Cyanides	28-39	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	62-67
28621817-1	2018	Part 6: Cyanides and isocyanides.	Cyanides	8-16	tankyrase 2	Homo sapiens	0-6
29901852-3	2018	The cyanide electrolyte can be replenished with HCN, opening opportunities for salt-free industrial C-H cyanation.	Cyanides	4-11	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	48-51
30251719-0	2018	Isocyanide insertion into Au-H bonds: first gold iminoformyl complexes.	Cyanides	0-10	AU RNA binding methylglutaconyl-CoA hydratase	Homo sapiens	26-30
29949364-4	2018	In the following step, replacement of the aqua ligand of complex 2 by the monodentate isocyanide ligand leads to the formation of fac-[Re(CO)3(quin)(cisc)], 3.	Cyanides	86-96	FA complementation group C	Homo sapiens	130-133
28621817-1	2018	Part 6: Cyanides and isocyanides.	Cyanides	21-32	tankyrase 2	Homo sapiens	0-6
29398544-7	2018	Overall, this work describes an isocyanide based-multicomponent approach as a straightforward and versatile tool to rapidly access IDO1 inhibitors, providing a new direction for their future design and development.	Cyanides	32-42	indoleamine 2,3-dioxygenase 1	Homo sapiens	131-135
29570928-3	2018	Thus, the fluoride ligands are stereospecifically replaced by any heavier halide or by cyanide, the cyanide affording [PPh4 ][trans-(CF3 )2 Au(CN)2 ].	Cyanides	87-94	potassium two pore domain channel subfamily K member 3	Homo sapiens	119-123
29570928-3	2018	Thus, the fluoride ligands are stereospecifically replaced by any heavier halide or by cyanide, the cyanide affording [PPh4 ][trans-(CF3 )2 Au(CN)2 ].	Cyanides	100-107	potassium two pore domain channel subfamily K member 3	Homo sapiens	119-123
29630840-1	2018	The use of Pd(DPEPhos)Cl2 (P26) as a catalyst for the formation of benzonitriles and their heterocyclic analogues provides excellent complementarity to existing catalysts, allowing highly electron-deficient heterocyclic aryl halides to be efficiently converted to the corresponding nitriles using K4[Fe(CN)6]) as cyanide source.	Cyanides	313-320	transmembrane p24 trafficking protein 3	Homo sapiens	27-30
29496995-0	2018	Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: A potential carbamylation route involved in the formation of atherosclerotic plaques?	Cyanides	39-46	myeloperoxidase	Homo sapiens	0-15
29496995-3	2018	This work demonstrates that the heme protein myeloperoxidase (MPO), which is secreted at high concentrations at inflammatory sites from stimulated neutrophils and monocytes, is able to catalyze the two-electron oxidation of cyanide to cyanate and promote the carbamylation of taurine, lysine, and low-density lipoproteins.	Cyanides	224-231	myeloperoxidase	Homo sapiens	45-60
29496995-3	2018	This work demonstrates that the heme protein myeloperoxidase (MPO), which is secreted at high concentrations at inflammatory sites from stimulated neutrophils and monocytes, is able to catalyze the two-electron oxidation of cyanide to cyanate and promote the carbamylation of taurine, lysine, and low-density lipoproteins.	Cyanides	224-231	myeloperoxidase	Homo sapiens	62-65
29496995-5	2018	Moreover, we present two further pathways of carbamylation that involve reaction products of MPO, namely oxidation of cyanide by hypochlorous acid and reaction of thiocyanate with chloramines.	Cyanides	118-125	myeloperoxidase	Homo sapiens	93-96
29496995-6	2018	Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma.	Cyanides	138-145	myeloperoxidase	Homo sapiens	87-90
29496995-6	2018	Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma.	Cyanides	138-145	myeloperoxidase	Homo sapiens	192-195
29496995-6	2018	Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma.	Cyanides	316-323	myeloperoxidase	Homo sapiens	87-90
29496995-6	2018	Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma.	Cyanides	316-323	myeloperoxidase	Homo sapiens	192-195
29496995-7	2018	In summary, our findings indicate that cyanide is a substrate for MPO and suggest an additional pathway for in vivo cyanate formation and protein carbamylation that involves MPO either directly or via its reaction products hypochlorous acid or chloramines.	Cyanides	39-46	myeloperoxidase	Homo sapiens	66-69
29496995-7	2018	In summary, our findings indicate that cyanide is a substrate for MPO and suggest an additional pathway for in vivo cyanate formation and protein carbamylation that involves MPO either directly or via its reaction products hypochlorous acid or chloramines.	Cyanides	39-46	myeloperoxidase	Homo sapiens	174-177
29582997-0	2018	Co(III) Complexes with N2S3-Type Ligands as Structural/Functional Models for the Isocyanide Hydrolysis Reaction Catalyzed by Nitrile Hydratase.	Cyanides	81-91	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	0-7
29582997-2	2018	In order to investigate the unique isocyanide hydrolysis by NHase, we prepared three related Co(III) model complexes, PPh4[Co(L)] (1), PPh4[Co(L-O3)] (2), and PPh4[Co(L-O4)] (3), where L is bis( N-(2-mercapto-2-methylpropionyl)aminopropyl)sulfide.	Cyanides	35-45	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	93-100
29558397-7	2018	Cyanide treatment of both species, along with salt treatment of rice and drought treatment of barley led to enhanced expression of various AP components; there was a high level of co-expression of AOX1a and AOX1d, along with NDB3 during the stress treatments, reminiscent of the co-expression that has been well characterised in Arabidopsis for AtAOX1a and AtNDB2.	Cyanides	0-7	alternative oxidase 1A	Arabidopsis thaliana	197-202
29558397-7	2018	Cyanide treatment of both species, along with salt treatment of rice and drought treatment of barley led to enhanced expression of various AP components; there was a high level of co-expression of AOX1a and AOX1d, along with NDB3 during the stress treatments, reminiscent of the co-expression that has been well characterised in Arabidopsis for AtAOX1a and AtNDB2.	Cyanides	0-7	alternative oxidase 1A	Arabidopsis thaliana	345-352
29558397-7	2018	Cyanide treatment of both species, along with salt treatment of rice and drought treatment of barley led to enhanced expression of various AP components; there was a high level of co-expression of AOX1a and AOX1d, along with NDB3 during the stress treatments, reminiscent of the co-expression that has been well characterised in Arabidopsis for AtAOX1a and AtNDB2.	Cyanides	0-7	NAD(P)H dehydrogenase B2	Arabidopsis thaliana	357-363
29314448-0	2018	CoIII -Catalyzed Isonitrile Insertion/Acyl Group Migration Between C-H and N-H bonds of Arylamides.	Cyanides	17-27	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	0-5
30090308-0	2018	Large-bite diboranes for the mu(1,2) complexation of hydrazine and cyanide.	Cyanides	67-74	glutathione S-transferase mu 1	Homo sapiens	29-35
30090308-9	2018	In MeOH/CHCl3 (1/1 vol) both compounds selectively bind cyanide to form the corresponding mu(1,2) chelate complexes with a B-C[triple bond, length as m-dash]N-B bridge at their cores.	Cyanides	56-63	glutathione S-transferase mu 1	Homo sapiens	90-96
29537285-1	2018	A highly efficient synthesis of planar chiral pyrido[3,4- b] ferrocenes by a palladium-catalyzed enantioselective isocyanide insertion/desymmetric C(sp2)-H bond activation reaction was developed.	Cyanides	114-124	Sp2 transcription factor	Homo sapiens	147-152
29594654-3	2018	Through the strong interaction between cyanide ions (CN-) of AuHCF and AuNPs, gold nanoparticles are assembled on the modified SPE, and this allows for the covalent immobilization of thiolated aptamers against TNF-alpha (TNF-alpha-Apt).	Cyanides	39-46	tumor necrosis factor	Homo sapiens	210-219
29594654-3	2018	Through the strong interaction between cyanide ions (CN-) of AuHCF and AuNPs, gold nanoparticles are assembled on the modified SPE, and this allows for the covalent immobilization of thiolated aptamers against TNF-alpha (TNF-alpha-Apt).	Cyanides	39-46	tumor necrosis factor	Homo sapiens	221-230
29594654-3	2018	Through the strong interaction between cyanide ions (CN-) of AuHCF and AuNPs, gold nanoparticles are assembled on the modified SPE, and this allows for the covalent immobilization of thiolated aptamers against TNF-alpha (TNF-alpha-Apt).	Cyanides	39-46	LYPLA2 pseudogene 1	Homo sapiens	231-234
30357745-0	2018	Leptin in the Commissural Nucleus Tractus Solitarii Increases the Glucose Responses to Carotid Chemoreceptors Activation by Cyanide.	Cyanides	124-131	leptin	Rattus norvegicus	0-6
29116760-10	2017	Particularly in the case of cobinamide, these oxygen-dependent reactions could potentially lead to erroneous assessment of the ability of the cyanide scavenger to restore the activity of cyanide-inhibited cytochrome c oxidase.	Cyanides	142-149	cytochrome c, somatic	Homo sapiens	205-217
29261311-3	2018	Multiplets using mixed isotopic cyanogens reveal the stoichiometries of these products, and the band positions and quantum chemical calculations confirm the isocyanide bonding arrangements, which are 14 and 51 kJ/mol more stable than the cyanide isomers for UNC and U(NC)2, respectively, and 62 kJ/mol for U(NC)4 in the isolated gas phase at the CCSD(T)/CBS level.	Cyanides	157-167	cystathionine beta-synthase	Homo sapiens	354-357
29261311-3	2018	Multiplets using mixed isotopic cyanogens reveal the stoichiometries of these products, and the band positions and quantum chemical calculations confirm the isocyanide bonding arrangements, which are 14 and 51 kJ/mol more stable than the cyanide isomers for UNC and U(NC)2, respectively, and 62 kJ/mol for U(NC)4 in the isolated gas phase at the CCSD(T)/CBS level.	Cyanides	160-167	cystathionine beta-synthase	Homo sapiens	354-357
29116760-0	2017	Relative Propensities of Cytochrome c Oxidase and Cobalt Corrins for Reaction with Cyanide and Oxygen: Implications for Amelioration of Cyanide Toxicity.	Cyanides	83-90	cytochrome c, somatic	Homo sapiens	25-37
29116760-0	2017	Relative Propensities of Cytochrome c Oxidase and Cobalt Corrins for Reaction with Cyanide and Oxygen: Implications for Amelioration of Cyanide Toxicity.	Cyanides	136-143	cytochrome c, somatic	Homo sapiens	25-37
29116760-2	2017	In comparison, the cyanide binding constants for cobalamin and a fully oxidized form of cytochrome c oxidase, each binding a single cyanide anion, were found to be 7.9 (+-0.5) x 104 M-1 and 1.6 (+-0.2) x 107 M-1, respectively.	Cyanides	19-26	cytochrome c, somatic	Homo sapiens	88-100
29116760-2	2017	In comparison, the cyanide binding constants for cobalamin and a fully oxidized form of cytochrome c oxidase, each binding a single cyanide anion, were found to be 7.9 (+-0.5) x 104 M-1 and 1.6 (+-0.2) x 107 M-1, respectively.	Cyanides	132-145	cytochrome c, somatic	Homo sapiens	88-100
29144306-3	2017	The properties of Al-PAM were investigated in flocculating 10 wt% cyanide tailing suspensions.	Cyanides	66-73	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	21-24
28901154-4	2017	Additionally, the amount of cyanide in the reaction phase is minimized by taking advantage of the solubility of Zn(CN)2 in a two-solvent mixture.	Cyanides	28-35	carnosine dipeptidase 2	Homo sapiens	112-119
28951911-1	2017	A chemoselective Co(ii)-catalyzed effective synthesis of sulfonylamidyl amide and 3-imine indole derivatives by using isocyanides and sulfonyl azides has been developed.	Cyanides	118-129	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	17-22
28623432-0	2017	Identification and expression analysis of CYS-A1, CYS-C1, NIT4 genes in rice seedlings exposed to cyanide.	Cyanides	98-105	cysteine synthase C1	Arabidopsis thaliana	50-56
28751116-4	2017	The conversion of KW-2449 to the iminium (intermediate) by MAO-B was confirmed by the formation of its cyanide adduct.	Cyanides	103-110	monoamine oxidase B	Homo sapiens	59-64
28494173-1	2017	CONTEXT: Acetonitrile (ACN) is a solvent rapidly absorbed through lungs and intestinal tract, and is slowly metabolized to cyanide (CN) by enzymatic processes mediated by CYP2E1.	Cyanides	123-130	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	171-177
28623432-0	2017	Identification and expression analysis of CYS-A1, CYS-C1, NIT4 genes in rice seedlings exposed to cyanide.	Cyanides	98-105	nitrilase 4	Arabidopsis thaliana	58-62
28623432-1	2017	Involvement of genes (CYS-A1, CYS-C1 and NIT4) encoded with cysteine synthase, beta-cyanoalanine synthase, nitrilase and cyanide metabolisms are evident in Arabidopsis.	Cyanides	121-128	cysteine synthase C1	Arabidopsis thaliana	30-36
28623432-1	2017	Involvement of genes (CYS-A1, CYS-C1 and NIT4) encoded with cysteine synthase, beta-cyanoalanine synthase, nitrilase and cyanide metabolisms are evident in Arabidopsis.	Cyanides	121-128	nitrilase 4	Arabidopsis thaliana	41-45
27038311-1	2017	3-mercaptopyruvate sulfurtransferase (3-MST) was a novel hydrogen sulfide (H2S)-synthesizing enzyme that may be involved in cyanide degradation and in thiosulfate biosynthesis.	Cyanides	124-131	mercaptopyruvate sulfurtransferase	Mus musculus	0-36
28537620-1	2017	A new one-dimensional cyanide-bridged complex [MnIII(salphen)RuII(DMAP)4(CN)2](PF6) (1) and its oxidized derivative [MnIII(salphen)RuIII(DMAP)4(CN)2](PF6)2 (2) have been synthesized and fully characterized.	Cyanides	22-29	sperm associated antigen 17	Homo sapiens	79-82
28537620-1	2017	A new one-dimensional cyanide-bridged complex [MnIII(salphen)RuII(DMAP)4(CN)2](PF6) (1) and its oxidized derivative [MnIII(salphen)RuIII(DMAP)4(CN)2](PF6)2 (2) have been synthesized and fully characterized.	Cyanides	22-29	sperm associated antigen 17	Homo sapiens	150-153
28843240-3	2017	The research proposed that organic nitrites, nitro oxide, cyanides, and isocyanides of cigarette smoke interfere with vitamin B12 metabolism, and convert it to inactive forms.	Cyanides	58-66	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	126-129
28843240-3	2017	The research proposed that organic nitrites, nitro oxide, cyanides, and isocyanides of cigarette smoke interfere with vitamin B12 metabolism, and convert it to inactive forms.	Cyanides	72-83	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	126-129
28412453-5	2017	Here, we compared the specific activities of mercaptopyruvate sulfurtransferase (MST, required for sulfanegen"s activity), across common laboratory models of cyanide intoxication, and humans.	Cyanides	158-165	mercaptopyruvate sulfurtransferase	Homo sapiens	45-79
28685572-1	2017	A Co(II)-catalyzed isocyanide insertion reaction with sulfonyl azides in alcohols to form sulfonyl isoureas via nitrene intermediate has been developed.	Cyanides	19-29	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	2-8
28702034-12	2017	Alternative oxidase (AOX), the terminal oxidase of the cyanide (CN)-resistant alternative respiratory pathway, catalyze oxygen-dependent oxidation of ubiquinol in plants.	Cyanides	55-62	acyl-CoA oxidase 1	Homo sapiens	0-19
28702034-12	2017	Alternative oxidase (AOX), the terminal oxidase of the cyanide (CN)-resistant alternative respiratory pathway, catalyze oxygen-dependent oxidation of ubiquinol in plants.	Cyanides	55-62	acyl-CoA oxidase 1	Homo sapiens	21-24
28474046-6	2017	In contrast, CO repeatedly stimulates the human Slo1 BKCa channel opening, possibly by binding to an unknown iron site, because cyanide prohibits this heme-independent CO stimulation.	Cyanides	128-135	potassium calcium-activated channel subfamily M alpha 1	Homo sapiens	48-52
28485450-2	2017	This methodology uses an air and moisture stable nickel(ii) XantPhos precatalyst and Zn(CN)2 as the cyanide (CN-) source.	Cyanides	100-107	carnosine dipeptidase 2	Homo sapiens	85-92
28188514-2	2017	The chemosensor (E)-2-(4-mercaptostyryl)quinolin-8-ol L showed high selectivity for detection of cyanide over other anions such as F , Cl , Br , I , NO3 , SCN , N3 , ClO4 , H2PO4 , AcO , HCO3 , SO42  and HSO4 in aqueous solution.	Cyanides	97-104	NBL1, DAN family BMP antagonist	Homo sapiens	149-152
28188514-2	2017	The chemosensor (E)-2-(4-mercaptostyryl)quinolin-8-ol L showed high selectivity for detection of cyanide over other anions such as F , Cl , Br , I , NO3 , SCN , N3 , ClO4 , H2PO4 , AcO , HCO3 , SO42  and HSO4 in aqueous solution.	Cyanides	97-104	sorcin	Homo sapiens	155-158
28382204-0	2017	Nitrosopersulfide (SSNO-) decomposes in the presence of sulfide, cyanide or glutathione to give HSNO/SNO-: consequences for the assumed role in cell signalling.	Cyanides	65-72	strawberry notch homolog 1	Homo sapiens	20-23
28232079-7	2017	SNP also releases cyanide ions, which are converted in the liver to thiocyanate by the enzyme rhodanese and/or MPST and/or gamma-cystathionase - the activities of all the enzymes were elevated in reaction to SNP.	Cyanides	18-25	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	94-103
28232079-7	2017	SNP also releases cyanide ions, which are converted in the liver to thiocyanate by the enzyme rhodanese and/or MPST and/or gamma-cystathionase - the activities of all the enzymes were elevated in reaction to SNP.	Cyanides	18-25	mercaptopyruvate sulfurtransferase	Mus musculus	111-115
28232079-7	2017	SNP also releases cyanide ions, which are converted in the liver to thiocyanate by the enzyme rhodanese and/or MPST and/or gamma-cystathionase - the activities of all the enzymes were elevated in reaction to SNP.	Cyanides	18-25	cystathionase (cystathionine gamma-lyase)	Mus musculus	123-142
28121149-0	2017	Cobalt-Catalyzed Annulation of Amides with Isocyanides via C(sp2)-H Activation.	Cyanides	43-54	Sp2 transcription factor	Homo sapiens	59-64
28121149-1	2017	A cobalt-catalyzed [4 + 1] cycloaddition of easily accessible amides with isocyanides for the efficient synthesis of 3-iminoisoindolinone derivatives in high yield under mild conditions via intramolecular C(sp2)-H activation and isocyanide insertion is reported.	Cyanides	74-85	Sp2 transcription factor	Homo sapiens	205-210
28121149-1	2017	A cobalt-catalyzed [4 + 1] cycloaddition of easily accessible amides with isocyanides for the efficient synthesis of 3-iminoisoindolinone derivatives in high yield under mild conditions via intramolecular C(sp2)-H activation and isocyanide insertion is reported.	Cyanides	74-84	Sp2 transcription factor	Homo sapiens	205-210
28106395-4	2017	Our studies show that steric effects of N-substituents of the isocyanides play an important role in the stability of the three-membered metallacycles of the eta2-iminoketenyl complexes.	Cyanides	62-73	DNA polymerase iota	Homo sapiens	157-161
28106395-5	2017	Sterically bulky isocyanides, such as tert-butyl or 1-adamantyl isocyanides, inhibit bending at the isocyanide nitrogen atoms, a requirement for formation of eta2-iminoketenyl structures.	Cyanides	17-28	DNA polymerase iota	Homo sapiens	158-162
28106395-5	2017	Sterically bulky isocyanides, such as tert-butyl or 1-adamantyl isocyanides, inhibit bending at the isocyanide nitrogen atoms, a requirement for formation of eta2-iminoketenyl structures.	Cyanides	17-27	DNA polymerase iota	Homo sapiens	158-162
28580114-5	2017	The smart system was adjusted to be able to initiate the catalytic oxidation of cyanide at a threshold concentration of 20 muM (the World Health Organization"s suggested maximum allowable level for cyanide in wastewater) to the less harmful cyanate under ambient conditions.	Cyanides	80-87	latexin	Homo sapiens	123-126
28580114-5	2017	The smart system was adjusted to be able to initiate the catalytic oxidation of cyanide at a threshold concentration of 20 muM (the World Health Organization"s suggested maximum allowable level for cyanide in wastewater) to the less harmful cyanate under ambient conditions.	Cyanides	198-205	latexin	Homo sapiens	123-126
28193002-6	2017	The cyanide stretching vibration in MBN was highly sensitive and selective to Fe3+ and oxy-Hb with excellent binding affinity (Kd 0.4 pM and 0.1 nM, respectively).	Cyanides	4-11	proteinase 3	Homo sapiens	36-39
28106395-3	2017	Here we report direct formation of eta2-iminoketenyl complexes from reactions of metallapentalyne with isocyanides.	Cyanides	103-114	DNA polymerase iota	Homo sapiens	35-39
27038311-1	2017	3-mercaptopyruvate sulfurtransferase (3-MST) was a novel hydrogen sulfide (H2S)-synthesizing enzyme that may be involved in cyanide degradation and in thiosulfate biosynthesis.	Cyanides	124-131	mercaptopyruvate sulfurtransferase	Mus musculus	38-43
27713940-0	2016	Spin crossover and reversible single-crystal to single-crystal transformation behaviour in two cyanide-bridged mixed-valence {FeFe} clusters.	Cyanides	95-102	spindlin 1	Homo sapiens	0-4
28067338-1	2017	A pure aqueous phase recognition and corresponding detoxification of highly toxic cyanide ions has been achieved by a fluorescent metal-organic framework (MOF).	Cyanides	82-89	lysine acetyltransferase 8	Homo sapiens	130-159
28001417-3	2017	A triple isocyanide insertion to the hypothetic (sigma-allenyl)palladium(II) intermediate was involved in these ABC3-type multicomponent reactions.	Cyanides	9-19	ATP binding cassette subfamily A member 3	Homo sapiens	112-116
27878155-1	2016	For the first time, spin-labelled coumpounds have been obtained by isonitrile-based multi component reactions (IMCRs).	Cyanides	67-77	spindlin 1	Homo sapiens	20-24
27862731-2	2016	The insertion of the isocyanide into the pi-allyl Pd complex proceeded via an unusual eta1 -allyl Pd species.	Cyanides	21-31	secreted phosphoprotein 1	Homo sapiens	86-90
27934438-3	2016	The m-terphenyl isocyanide ligand CNArDipp2 improves the kinetic stability of the resulting mixed carbonyl/isocyanide systems, such that conversion among all three oxidation states is easily effected by chemical reagents.	Cyanides	16-26	nudix hydrolase 4	Homo sapiens	34-43
28067626-6	2017	AOX conferred robust resistance to inhibitors of the respiratory chain in organello; moreover, animals exposed to a systemically applied LD50 dose of cyanide did not succumb.	Cyanides	150-157	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	0-3
28004046-1	2017	A new 1D cyanide-bridged Co-Ru compound, {[trans-RuIII(dmap)4(CN)2Co(dipic)(MeOH)](PF6)}n (1a) (dmap = 4-dimethylaminopyridine, dipic = pyridine-2,6-dicarboxylate), and its reduced state, [trans-RuII(dmap)4(CN)2Co(dipic)]n (1b) have been synthesized.	Cyanides	9-16	sperm associated antigen 17	Homo sapiens	83-86
27925347-1	2017	Co-crystallization of a cyanide-bridged tetranuclear complex [Co2 Fe2 ] with 4-cyanophenol (CP) gave a hydrogen bonding donor-acceptor system, [Co2 Fe2 (bpy*)4 (CN)6 (tp*)2 ](PF6 )2  2 CP 8 BN (1).	Cyanides	24-31	sperm associated antigen 17	Homo sapiens	175-178
28735401-12	2017	Sulfite-generating ST activity is determined by colorimetric detection of SCN- formation at 460 nm as the red Fe(SCN)3 complex from cyanide and thiosulfate using acidic iron reagent.	Cyanides	132-139	HCLS1 associated protein X-1	Homo sapiens	113-118
27068154-10	2016	There is a strong influence of CO2 on increasing concentration other products as cyanide (HCN) and ammonia (NH3).	Cyanides	81-88	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	90-93
27474675-8	2016	Removal of cyanide from aqueous solution with PDC-Chit, PDC-Chit-Ni(II) and PDC-Chit-Fe(III) films was studied with batch equilibrium experiments.	Cyanides	11-18	chitinase 1	Homo sapiens	50-54
27474675-8	2016	Removal of cyanide from aqueous solution with PDC-Chit, PDC-Chit-Ni(II) and PDC-Chit-Fe(III) films was studied with batch equilibrium experiments.	Cyanides	11-18	chitinase 1	Homo sapiens	60-64
27474675-8	2016	Removal of cyanide from aqueous solution with PDC-Chit, PDC-Chit-Ni(II) and PDC-Chit-Fe(III) films was studied with batch equilibrium experiments.	Cyanides	11-18	chitinase 1	Homo sapiens	60-64
27606503-5	2016	Its behavior in solution has also been characterized, revealing an unexpected strong tendency to give cationic complexes, and notably [(ArC=NR)Pd(CNR)3 ]+ with excess isocyanide and [(ArC=NR)Pd(PP^ )(CNR)]+ with bidentate phosphines (PP^ ).	Cyanides	167-177	protocadherin alpha 14 pseudogene	Homo sapiens	146-151
27480670-3	2016	Treatment of CpCoI2(CNAr(Dipp2)) with KC8 produces the bridging isocyanide dimer, [CpCo(mu-CNAr(Dipp2))]2, thereby indicating that the steric combination of Cp and CNAr(Dipp2) ligands does not allow for the production of mononuclear complexes.	Cyanides	64-74	nudix hydrolase 4	Homo sapiens	25-30
27643514-1	2016	The facile redox-assisted assembly of a water-soluble, extremely robust, cyanide-bridged mixed-valence [{CoIII {(Me)2 (mu-ET)cyclen} }2 {(mu-NC)2 FeII (CN)4 }2 ]2- square is reported.	Cyanides	73-80	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	105-110
27480670-3	2016	Treatment of CpCoI2(CNAr(Dipp2)) with KC8 produces the bridging isocyanide dimer, [CpCo(mu-CNAr(Dipp2))]2, thereby indicating that the steric combination of Cp and CNAr(Dipp2) ligands does not allow for the production of mononuclear complexes.	Cyanides	64-74	nudix hydrolase 4	Homo sapiens	96-101
27480670-3	2016	Treatment of CpCoI2(CNAr(Dipp2)) with KC8 produces the bridging isocyanide dimer, [CpCo(mu-CNAr(Dipp2))]2, thereby indicating that the steric combination of Cp and CNAr(Dipp2) ligands does not allow for the production of mononuclear complexes.	Cyanides	64-74	nudix hydrolase 4	Homo sapiens	96-101
27816999-7	2016	Moreover, when expressed in yeast, Pacific oyster AOX is a functional quinol oxidase, conferring cyanide-resistant growth and myxothiazol-resistant oxygen consumption to yeast cells and isolated mitochondria.	Cyanides	97-104	alternative oxidase, mitochondrial-like	Crassostrea gigas	50-53
27503764-1	2016	Bismuth triflate (Bi(OTf)3) is identified as an efficient catalyst for the direct addition of isocyanides to 2H-chromene acetals.	Cyanides	94-105	POU class 5 homeobox 1	Homo sapiens	0-26
27607732-3	2016	[SiP(iPr) 3 ]Fe(CN) additionally serves as a useful entry point to rare examples of terminally-bound Fe(CNH) and Fe(CNH2 ) species that, in accord with preliminary mechanistic studies, are plausible intermediates of the cyanide reductive protonation to generate CH4 and NH3 .	Cyanides	220-227	tumor protein p53 inducible nuclear protein 1	Homo sapiens	1-11
27607732-4	2016	Comparative studies with a related [SiP(iPr) 3 ]Fe(CNMe2 ) complex suggests the possibility of multiple, competing mechanisms for cyanide activation and reduction.	Cyanides	130-137	tumor protein p53 inducible nuclear protein 1	Homo sapiens	36-46
27343172-3	2016	At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO.	Cyanides	146-153	myeloperoxidase	Homo sapiens	126-129
27492940-1	2016	The arsenic(III) and antimony(III) cyanides M(CN)3 (M=As, Sb) have been prepared in quantitative yields from the corresponding trifluorides through fluoride-cyanide exchange with Me3 SiCN in acetonitrile.	Cyanides	35-43	malic enzyme 3	Homo sapiens	179-182
27343172-3	2016	At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO.	Cyanides	146-153	myeloperoxidase	Homo sapiens	142-145
27343172-3	2016	At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO.	Cyanides	146-153	myeloperoxidase	Homo sapiens	142-145
27343172-4	2016	The reaction of ferric MPO with hypothiocyanite directly forms the MPO-cyanide complex, whereas a transient product derived from the reaction between hypothiocyanite and hydrogen peroxide is demonstrated to mediate the conversion of ferric MPO to Compound II.	Cyanides	71-78	myeloperoxidase	Homo sapiens	23-26
27343172-4	2016	The reaction of ferric MPO with hypothiocyanite directly forms the MPO-cyanide complex, whereas a transient product derived from the reaction between hypothiocyanite and hydrogen peroxide is demonstrated to mediate the conversion of ferric MPO to Compound II.	Cyanides	71-78	myeloperoxidase	Homo sapiens	67-70
27343172-4	2016	The reaction of ferric MPO with hypothiocyanite directly forms the MPO-cyanide complex, whereas a transient product derived from the reaction between hypothiocyanite and hydrogen peroxide is demonstrated to mediate the conversion of ferric MPO to Compound II.	Cyanides	71-78	myeloperoxidase	Homo sapiens	67-70
27348246-8	2016	Noteworthy, both Dd FDH-catalyzed formate oxidation and carbon dioxide reduction are completely inactivated by cyanide.	Cyanides	111-118	aldehyde dehydrogenase 1 family member L1	Homo sapiens	20-23
25614581-0	2016	In vitro activation of dibromoacetonitrile to cyanide by myeloperoxidase.	Cyanides	46-53	myeloperoxidase	Homo sapiens	57-72
25614581-2	2016	This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity.	Cyanides	90-97	myeloperoxidase	Homo sapiens	49-64
25614581-2	2016	This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity.	Cyanides	90-97	myeloperoxidase	Homo sapiens	66-69
25614581-2	2016	This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity.	Cyanides	99-102	myeloperoxidase	Homo sapiens	49-64
25614581-2	2016	This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity.	Cyanides	99-102	myeloperoxidase	Homo sapiens	66-69
30155124-0	2016	A N,N"-dioxide/Mg(OTf)2 complex catalyzed enantioselective alpha-addition of isocyanides to alkylidene malonates.	Cyanides	77-88	POU class 2 homeobox 2	Homo sapiens	18-23
27080474-1	2016	Cytochrome c (CYTc) is a soluble redox-active heme protein that transfers electrons from complex III to complex IV in the cyanide-sensitive mitochondrial respiratory pathway.	Cyanides	122-129	cytochrome c, somatic	Homo sapiens	0-12
27080474-1	2016	Cytochrome c (CYTc) is a soluble redox-active heme protein that transfers electrons from complex III to complex IV in the cyanide-sensitive mitochondrial respiratory pathway.	Cyanides	122-129	cytochrome c, somatic	Homo sapiens	14-18
26974051-5	2016	The reduction of (CN)Co(ii)/Co(i) was found to depend on cyanide-solvent exchange equilibrium with weakly coordinating solvents and bulky peripheral chains promoting intact (CN)Co(ii) species existence.	Cyanides	57-64	mitochondrially encoded cytochrome c oxidase I	Homo sapiens	28-33
27308865-6	2016	To meet this need, our laboratory is developing sulfanegen, a potential antidote for cyanide poisoning with a novel mechanism based on 3-mercaptopyruvate sulfurtransferase (3-MST) for the detoxification of cyanide.	Cyanides	206-213	mercaptopyruvate sulfurtransferase	Homo sapiens	135-171
27152023-5	2016	The ITC data also showed that although the copper ion alone hardly contributes to affinity, substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide, a mimic of O2 (-) Studies with CDH and its isolated heme b cytochrome domain unambiguously showed that the cytochrome domain of CDH interacts with the copper site of the LPMO and that substrate binding precludes interaction with CDH.	Cyanides	170-177	choline dehydrogenase	Homo sapiens	210-213
27152023-5	2016	The ITC data also showed that although the copper ion alone hardly contributes to affinity, substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide, a mimic of O2 (-) Studies with CDH and its isolated heme b cytochrome domain unambiguously showed that the cytochrome domain of CDH interacts with the copper site of the LPMO and that substrate binding precludes interaction with CDH.	Cyanides	170-177	choline dehydrogenase	Homo sapiens	307-310
27152023-5	2016	The ITC data also showed that although the copper ion alone hardly contributes to affinity, substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide, a mimic of O2 (-) Studies with CDH and its isolated heme b cytochrome domain unambiguously showed that the cytochrome domain of CDH interacts with the copper site of the LPMO and that substrate binding precludes interaction with CDH.	Cyanides	170-177	choline dehydrogenase	Homo sapiens	307-310
27081184-3	2016	In search of cyanide, a coproduct of ethylene and camalexin biosynthesis, we found that MPK3 and MPK6 also affect the accumulation of extracellular thiocyanate ion derived from the indole glucosinolate (IGS) pathway.	Cyanides	13-20	mitogen-activated protein kinase 3	Arabidopsis thaliana	88-92
27081184-3	2016	In search of cyanide, a coproduct of ethylene and camalexin biosynthesis, we found that MPK3 and MPK6 also affect the accumulation of extracellular thiocyanate ion derived from the indole glucosinolate (IGS) pathway.	Cyanides	13-20	MAP kinase 6	Arabidopsis thaliana	97-101
26584835-0	2016	A Post-Synthetically Modified MOF for Selective and Sensitive Aqueous-Phase Detection of Highly Toxic Cyanide Ions.	Cyanides	102-109	lysine acetyltransferase 8	Homo sapiens	30-33
26919691-4	2016	The iron component is fashioned by the proteins HypC, HypD, HypE, and HypF, which functionalize iron with cyanide and carbon monoxide.	Cyanides	106-113	pre-mRNA processing factor 40 homolog B	Homo sapiens	48-52
26919691-4	2016	The iron component is fashioned by the proteins HypC, HypD, HypE, and HypF, which functionalize iron with cyanide and carbon monoxide.	Cyanides	106-113	MAGE family member A3	Homo sapiens	54-58
26919691-4	2016	The iron component is fashioned by the proteins HypC, HypD, HypE, and HypF, which functionalize iron with cyanide and carbon monoxide.	Cyanides	106-113	FIC domain protein adenylyltransferase	Homo sapiens	60-64
26919691-4	2016	The iron component is fashioned by the proteins HypC, HypD, HypE, and HypF, which functionalize iron with cyanide and carbon monoxide.	Cyanides	106-113	fibroblast growth factor 23	Homo sapiens	70-74
26584835-1	2016	Selective and sensitive detection of toxic cyanide (CN(-) ) by a post-synthetically altered metal-organic framework (MOF) has been achieved.	Cyanides	43-50	lysine acetyltransferase 8	Homo sapiens	92-121
25386729-0	2016	A new PANI biosensor based on catalase for cyanide determination.	Cyanides	43-50	catalase	Homo sapiens	30-38
26704699-0	2016	Transition-Metal-Free Deacylative Cleavage of Unstrained C(sp(3))-C(sp(2)) Bonds: Cyanide-Free Access to Aryl and Aliphatic Nitriles from Ketones and Aldehydes.	Cyanides	82-89	regulator of calcineurin 2	Homo sapiens	66-73
26195431-6	2016	The experimental results indicate that hydroxyl radicals oxidize cyanide to OCN(-), NO2(-), NO3(-), HCO3(-), and CO3(2-), which have lower toxicity than cyanide.	Cyanides	65-72	bone gamma-carboxyglutamate protein	Homo sapiens	76-79
26195431-6	2016	The experimental results indicate that hydroxyl radicals oxidize cyanide to OCN(-), NO2(-), NO3(-), HCO3(-), and CO3(2-), which have lower toxicity than cyanide.	Cyanides	153-160	bone gamma-carboxyglutamate protein	Homo sapiens	76-79
26881185-1	2016	A water-soluble fluorescent probe (C-GGH) was used for the highly sensitive and selective detection of cyanide (CN(-)) in aqueous media based on the displacement strategy.	Cyanides	103-110	gamma-glutamyl hydrolase	Homo sapiens	37-40
26881185-1	2016	A water-soluble fluorescent probe (C-GGH) was used for the highly sensitive and selective detection of cyanide (CN(-)) in aqueous media based on the displacement strategy.	Cyanides	112-117	gamma-glutamyl hydrolase	Homo sapiens	37-40
32263129-6	2015	An apparent switch on the luminescence response, ultralow detection limit, low response time, cell membrane permeability and insignificant toxicity are key features of a probe molecule, which gives it a distinct edge over previously reported chemodosimetric reagents for the detection of cyanide species (CN- or HCN) in an aqueous environment.	Cyanides	288-295	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	312-315
25158995-2	2016	Previous studies indicated that during greening, chlorophyll accumulation was largely delayed in plants whose mitochondrial cyanide-resistant respiration was inhibited by knocking out nuclear encoded AOX gene.	Cyanides	124-131	alternative oxidase 2	Arabidopsis thaliana	200-203
28132465-1	2016	Investigations of plant cyanide resistant respiration lead to the discovery in mitochondrial respiratory chain of the second terminal oxidase, alternative oxidase (AOX).	Cyanides	24-31	acyl-CoA oxidase 1	Homo sapiens	143-162
28132465-1	2016	Investigations of plant cyanide resistant respiration lead to the discovery in mitochondrial respiratory chain of the second terminal oxidase, alternative oxidase (AOX).	Cyanides	24-31	acyl-CoA oxidase 1	Homo sapiens	164-167
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	75-82	CD1d1 molecule	Rattus norvegicus	53-57
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	75-82	Cd2 molecule	Rattus norvegicus	62-66
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	75-82	CD1d1 molecule	Rattus norvegicus	165-169
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	75-82	Cd2 molecule	Rattus norvegicus	170-174
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	136-143	CD1d1 molecule	Rattus norvegicus	53-57
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	136-143	Cd2 molecule	Rattus norvegicus	62-66
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	136-143	CD1d1 molecule	Rattus norvegicus	165-169
26403695-1	2015	Naphthimidazolium based monocationic chemodosimeters CD-1 and CD-2 undergo cyanide mediated catalytic transformation in the presence of cyanide ions (0.01% to 1% of CD-1/CD-2 concentrations) with a turnover number from 70 to 360.	Cyanides	136-143	Cd2 molecule	Rattus norvegicus	170-174
26403695-3	2015	The structures of CD-1 and its cyanide induced hydrolyzed product 4 have been confirmed by single crystal X-ray crystallography.	Cyanides	31-38	CD1d1 molecule	Rattus norvegicus	18-22
26403695-4	2015	CD-1 can also be used for the determination of 2 nM cyanide in the presence of blood serum.	Cyanides	52-59	CD1d1 molecule	Rattus norvegicus	0-4
26403695-5	2015	CD-1 and CD-2 also find applications in live cell imaging of 10 nM cyanide ions in rat brain C6 glioma cells.	Cyanides	67-74	CD1d1 molecule	Rattus norvegicus	0-4
26403695-5	2015	CD-1 and CD-2 also find applications in live cell imaging of 10 nM cyanide ions in rat brain C6 glioma cells.	Cyanides	67-74	Cd2 molecule	Rattus norvegicus	9-13
26331428-3	2015	Herein, we show that two sterically encumbering isocyanide ligands can destabilize the Mn Mn bond leading to the formation of the isolable, manganese(0) monoradical [Mn(CO)3 (CNAr(Dipp2) )2 ] (Ar(Dipp2) =2,6-(2,6-(iPr)2 C6 H3 )2 C6 H3 ).	Cyanides	48-58	nudix hydrolase 4	Homo sapiens	180-185
27239435-2	2016	The AOX1a transformant (pYES2AtAOX1a) showed cyanide resistant and salicylhydroxamic acid (SHAM)-sensitive respiration, indicating functional expression of AtAOX1a in S. cerevisiae.	Cyanides	45-52	alternative oxidase 1A	Arabidopsis thaliana	4-9
27239435-2	2016	The AOX1a transformant (pYES2AtAOX1a) showed cyanide resistant and salicylhydroxamic acid (SHAM)-sensitive respiration, indicating functional expression of AtAOX1a in S. cerevisiae.	Cyanides	45-52	alternative oxidase 1A	Arabidopsis thaliana	29-36
26331428-3	2015	Herein, we show that two sterically encumbering isocyanide ligands can destabilize the Mn Mn bond leading to the formation of the isolable, manganese(0) monoradical [Mn(CO)3 (CNAr(Dipp2) )2 ] (Ar(Dipp2) =2,6-(2,6-(iPr)2 C6 H3 )2 C6 H3 ).	Cyanides	48-58	nudix hydrolase 4	Homo sapiens	196-201
26269602-2	2015	Rhodanese catalyzes the transfer of sulfane sulfur from glutathione persulfide (GSSH) to sulfite generating thiosulfate and from thiosulfate to cyanide generating thiocyanate.	Cyanides	144-151	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	0-9
26401918-0	2015	Fully Synthetic Granulocyte Colony-Stimulating Factor Enabled by Isonitrile-Mediated Coupling of Large, Side-Chain-Unprotected Peptides.	Cyanides	65-75	colony stimulating factor 3	Homo sapiens	16-53
26269602-11	2015	Our studies show that polymorphic variations that are distant from the active site differentially modulate the sulfurtransferase activity of human rhodanese to cyanide versus sulfite and might be important in differences in susceptibility to diseases where rhodanese dysfunction has been implicated, e.g. inflammatory bowel diseases.	Cyanides	160-167	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	147-156
26269602-11	2015	Our studies show that polymorphic variations that are distant from the active site differentially modulate the sulfurtransferase activity of human rhodanese to cyanide versus sulfite and might be important in differences in susceptibility to diseases where rhodanese dysfunction has been implicated, e.g. inflammatory bowel diseases.	Cyanides	160-167	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	257-266
26398427-6	2015	The detection limit of the sensor 1 (1.1 muM) for cyanide is lower than the maximum permissible level of CN(-) (1.9 muM) in drinking water.	Cyanides	50-57	latexin	Homo sapiens	41-44
26398427-6	2015	The detection limit of the sensor 1 (1.1 muM) for cyanide is lower than the maximum permissible level of CN(-) (1.9 muM) in drinking water.	Cyanides	50-57	latexin	Homo sapiens	116-119
26198787-3	2015	The mechanism of the bimetallic complex for high-selectivity recognition and signaling toward cyanide ions was investigated through a series of binding kinetics of the complex with different analytes, including CN(-) , SO4 (2-) , HCO3 (-) , HPO4 (2-) , N3 (-) , CH3 COO(-) , NCS(-) , NO3 (-) , and Cl(-) ions.	Cyanides	94-101	NBL1, DAN family BMP antagonist	Homo sapiens	284-287
26148527-1	2015	We report a novel and environmentally friendly fluorescent probe for detecting the cyanide ion (CN(-)) using L-amino acid oxidase (LAAOx)-protected Au nanoclusters (LAAOx@AuNCs) with red emission.	Cyanides	83-90	interleukin 4 induced 1	Homo sapiens	109-129
26148527-1	2015	We report a novel and environmentally friendly fluorescent probe for detecting the cyanide ion (CN(-)) using L-amino acid oxidase (LAAOx)-protected Au nanoclusters (LAAOx@AuNCs) with red emission.	Cyanides	83-90	interleukin 4 induced 1	Homo sapiens	131-136
26148527-1	2015	We report a novel and environmentally friendly fluorescent probe for detecting the cyanide ion (CN(-)) using L-amino acid oxidase (LAAOx)-protected Au nanoclusters (LAAOx@AuNCs) with red emission.	Cyanides	83-90	interleukin 4 induced 1	Homo sapiens	165-170
26153651-2	2015	This cascade process proceeds through initial condensation of the allenic ketone with hydrazine followed by Pd-catalyzed isocyanide insertion into the C-Br bond and intramolecular C-N bond formation.	Cyanides	121-131	carbonyl reductase 1	Homo sapiens	151-155
26153651-3	2015	Interestingly, when acetohydrazide was used in place of hydrazine, a more sophisticated procedure involving condensation, isocyanide insertion into C-H and C-Br bonds, deacetylation, and formation of C-C, C-O, and C-N bonds occurred to afford pyrazolo[5,1-a]isoindole-3-carboxamides with good efficiency.	Cyanides	122-132	carbonyl reductase 1	Homo sapiens	156-160
26043946-3	2015	Here we show that a simple replacement of cyano for nitro at the 4 position to give compound 4b ("p-cyano-PABA/NO") has the dual effect of slowing the undesired side reactions while enhancing the proportion of NO release and arylating activity on catalysis by GSTP1.	Cyanides	42-47	glutathione S-transferase pi 1	Homo sapiens	260-265
26130923-9	2015	The neuron count increased ( NSE) after withdrawal of cyanide treatment and vascular occlusion and was accompanied by a corresponding decrease in endothelial and glia activation ( CD31/GFAP).	Cyanides	54-61	enolase 2	Rattus norvegicus	29-32
26130923-12	2015	CONCLUSION: We conclude that neuronal degeneration in cyanide toxicity or vascular occlusion is dependent on an increase in endothelial proliferation ( CD31), glia activation ( GFAP) and a decrease in monocyte expression ( CD45); representing a pro-inflammatory response.	Cyanides	54-61	platelet and endothelial cell adhesion molecule 1	Rattus norvegicus	152-156
26130923-12	2015	CONCLUSION: We conclude that neuronal degeneration in cyanide toxicity or vascular occlusion is dependent on an increase in endothelial proliferation ( CD31), glia activation ( GFAP) and a decrease in monocyte expression ( CD45); representing a pro-inflammatory response.	Cyanides	54-61	glial fibrillary acidic protein	Rattus norvegicus	177-181
26130923-12	2015	CONCLUSION: We conclude that neuronal degeneration in cyanide toxicity or vascular occlusion is dependent on an increase in endothelial proliferation ( CD31), glia activation ( GFAP) and a decrease in monocyte expression ( CD45); representing a pro-inflammatory response.	Cyanides	54-61	protein tyrosine phosphatase, receptor type, C	Rattus norvegicus	223-227
26130923-13	2015	Furthermore, cyanide toxicity induced more prominent degenerative changes when compared with the vascular occlusion due to a higher CD31/GFAP expression.	Cyanides	13-20	platelet and endothelial cell adhesion molecule 1	Rattus norvegicus	132-136
26130923-13	2015	Furthermore, cyanide toxicity induced more prominent degenerative changes when compared with the vascular occlusion due to a higher CD31/GFAP expression.	Cyanides	13-20	glial fibrillary acidic protein	Rattus norvegicus	137-141
25953104-4	2015	However, for CYP71A12, indole-3-carbaldehyde and cyanide were identified as major reaction products.	Cyanides	49-56	cytochrome P450 family 71 polypeptide	Arabidopsis thaliana	13-21
25862588-8	2015	injection of cyanide, reduced Fos expression in the caudal NTS, and increased Fos expression in the rostral VLM.	Cyanides	13-20	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	30-33
26057802-0	2015	X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state at 2.0 A resolution.	Cyanides	19-26	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	46-66
26057802-1	2015	The X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state was determined at 2.0 A resolution.	Cyanides	23-30	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	50-70
26246998-4	2015	The mechanism for detection is rationalized by the nucleophilic substitution of the phenolic oxygen atom at the indoline C-2 atom by the cyanide anion to form a stable indolylnitrile adduct and to generate the colored 4-nitrophenolate chromophore.	Cyanides	137-150	complement C2	Homo sapiens	121-124
25692407-0	2015	Protection from cyanide-induced brain injury by the Nrf2 transcriptional activator carnosic acid.	Cyanides	16-23	NFE2 like bZIP transcription factor 2	Homo sapiens	52-56
25692407-9	2015	Here, cyanide poisoning treated with the proelectrophillic compound carnosic acid, results in reduced neuronal cell death in both in vitro and in vivo models through activation of the Nrf2/ARE transcriptional pathway.	Cyanides	6-13	NFE2 like bZIP transcription factor 2	Homo sapiens	184-188
25866203-2	2015	The heteropolynuclear cyanide complexes exhibited higher catalytic activity than a polynuclear cyanide complex containing only Co(III) or Pt(IV) ions as C-bound metal ions.	Cyanides	22-29	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	127-134
25869356-1	2015	Mitochondria of all so far studied organisms, with the exception of Archaea, mammals, some yeasts, and protists, contain, along with the classical phosphorylating cytochrome pathway, a so-called cyanide-insensitive alternative oxidase (AOX) localized on the matrix side of the mitochondrial inner membrane, and electron transport through which is not coupled with ATP synthesis and energy accumulation.	Cyanides	195-202	acyl-CoA oxidase 1	Homo sapiens	236-239
25811407-7	2015	While the U-CN/NC coordination preference towards the U(III)/U(IV) pair is related to the subtle balance between steric, covalent and ionic factors, DFT computations and in particular the calculated total bonding energies between the metal and the cyanide ligand allowed the observed coordination mode to be predicted.	Cyanides	248-255	urocortin	Homo sapiens	10-14
25663081-0	2015	Pd-catalyzed Csp(2) -H functionalization of heteroarenes via isocyanide insertion: concise synthesis of di-(hetero)aryl ketones and di-(hetero)aryl alkylamines.	Cyanides	61-71	regulator of calcineurin 2	Homo sapiens	13-19
26038696-5	2015	Because metabolism was dramatically inhibited by cyanide, we assumed that sterol C4-methyl oxidase like gene product (SC4MOL) might contribute to the metabolism of ED-71.	Cyanides	49-56	methylsterol monooxygenase 1	Homo sapiens	118-124
25486065-1	2015	A novel derivatization method of free cyanide (HCN + CN(-)) including cyanogen chloride in chlorinated drinking water was developed with d-cysteine and hypochlorite.	Cyanides	38-45	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	47-50
26640525-1	2015	Cyanide poisoning from Inhaled HCN is all too common in victims of smoke inhalation in fires.	Cyanides	0-7	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	31-34
26640525-2	2015	While the toxic effects arise primarily from its inhibitory effects on cytochrome c oxidase, the majority of the cyanide binds to methemoglobin (metHb) in the blood.	Cyanides	113-120	hemoglobin subunit gamma 2	Homo sapiens	130-143
25770604-2	2015	The receptor M1 is highly sensitive and selective to cyanide anion due to the nucleophilic addition of cyanide anion with M1.	Cyanides	53-66	cholinergic receptor muscarinic 1	Homo sapiens	13-15
25770604-2	2015	The receptor M1 is highly sensitive and selective to cyanide anion due to the nucleophilic addition of cyanide anion with M1.	Cyanides	53-66	cholinergic receptor muscarinic 1	Homo sapiens	122-124
25770604-2	2015	The receptor M1 is highly sensitive and selective to cyanide anion due to the nucleophilic addition of cyanide anion with M1.	Cyanides	103-116	cholinergic receptor muscarinic 1	Homo sapiens	13-15
25770604-2	2015	The receptor M1 is highly sensitive and selective to cyanide anion due to the nucleophilic addition of cyanide anion with M1.	Cyanides	103-116	cholinergic receptor muscarinic 1	Homo sapiens	122-124
25770604-3	2015	Distinct changes on UV-vis and fluorescence spectra can be detected with the addition of cyanide anion to the DMSO solution of M1.	Cyanides	89-102	cholinergic receptor muscarinic 1	Homo sapiens	127-129
25826468-0	2015	Synthesis of carbodiimides by I2/CHP-mediated cross-coupling reaction of isocyanides with amines under metal-free conditions.	Cyanides	73-84	ras homolog family member V	Homo sapiens	33-36
25826468-1	2015	An I2/CHP-mediated cross-coupling reaction of isocyanides with readily accessible amines via C-N formation is described for carbodiimide synthesis in moderate to excellent yields.	Cyanides	46-57	ras homolog family member V	Homo sapiens	6-9
24830543-0	2015	(1)H, (15)N and (13)C backbone resonance assignments of murine met-neuroglobin, free and in complex with cyanide.	Cyanides	105-112	neuroglobin	Mus musculus	67-78
26146537-7	2015	This sensor set was able to identify two unknown anion samples from ten closely-responding anions and could also function quantitatively, determining unknown concentrations of anions such as cyanide (as low as 1 mM) and selenate (as low as 50 muM).	Cyanides	191-198	latexin	Homo sapiens	243-246
25341378-2	2015	This study tested the hypothesis that metabolic inhibition caused by cyanide-induced chemical anoxia plus glucose deprivation promotes both release of mitochondrial NAD(H) in response to opening of the permeability transition pore (PTP) and NAD(P)(H) degradation through activation of poly (ADP-ribose) polymerase (PARP).	Cyanides	69-76	poly (ADP-ribose) polymerase 1	Rattus norvegicus	285-313
25490042-5	2015	Application in 5 kinds of natural water source and accurate detection of cyanide in tap water solvent system also indicated the high practical significance of the probe.	Cyanides	73-80	nuclear RNA export factor 1	Homo sapiens	84-87
25485477-5	2015	The cyt c/H2O2-induced liposome leakage was abolished by cyanide presumably competing with H2O2 for coordination with the central iron atom of the heme in cyt c.	Cyanides	57-64	cytochrome c	Bos taurus	4-9
25485477-5	2015	The cyt c/H2O2-induced liposome leakage was abolished by cyanide presumably competing with H2O2 for coordination with the central iron atom of the heme in cyt c.	Cyanides	57-64	HEME	Bos taurus	147-151
25485477-5	2015	The cyt c/H2O2-induced liposome leakage was abolished by cyanide presumably competing with H2O2 for coordination with the central iron atom of the heme in cyt c.	Cyanides	57-64	cytochrome c	Bos taurus	155-160
25459631-2	2015	CS1 exhibited both colorimetric and fluorescence turn-off responses for cyanide (CN(-)) ion in aqueous solution.	Cyanides	72-79	chorionic somatomammotropin hormone 1	Homo sapiens	0-3
25539022-3	2015	Addition of the neutral monodentate donor L = 2,6-xylylisocyanide to [Ni(NS2)]2 affords the monomeric complex [LNi(NS2)] (3), which is characterized in the solid state by a square planar geometry with the isocyanide donor trans to the tertiary amine of NS2.	Cyanides	55-65	NS2	Homo sapiens	73-76
25539022-3	2015	Addition of the neutral monodentate donor L = 2,6-xylylisocyanide to [Ni(NS2)]2 affords the monomeric complex [LNi(NS2)] (3), which is characterized in the solid state by a square planar geometry with the isocyanide donor trans to the tertiary amine of NS2.	Cyanides	55-65	NS2	Homo sapiens	115-118
25539022-3	2015	Addition of the neutral monodentate donor L = 2,6-xylylisocyanide to [Ni(NS2)]2 affords the monomeric complex [LNi(NS2)] (3), which is characterized in the solid state by a square planar geometry with the isocyanide donor trans to the tertiary amine of NS2.	Cyanides	55-65	NS2	Homo sapiens	115-118
25559322-7	2015	Deprotonated adenine fragments by loss of hydrogen cyanide and/or isocyanide (HCN/HNC; 90%) and carbodiimide (HNCNH) and/or cyanamide (NH2CN; 10%).	Cyanides	66-76	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	78-81
25469708-2	2015	The reaction of phosphonium salt 3, arylglyoxals 4, amine 5 (or without), and isocyanide 6 produced the 2,3-dihydro-1H-2-benzazepin-1-ones 8 or 3H-2-benzoxepin-1-ones 10 in good yields via a sequential Ugi or Passerini condensation and intramolecular Wittig reaction in the presence of NEt3.	Cyanides	78-88	tetraspanin 2	Homo sapiens	286-290
25496238-2	2015	By using this mild and economical methodology, syntheses of beta-(2/4-nitroaryl)-indoles with sensitive functionalities such as bromo, iodo, cyano, and nitro were achieved chemo- and regioselectively.	Cyanides	141-146	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	60-67
25725525-1	2015	A cystine-catabolizing enzyme, 3-mercaptopyruvate sulfurtransferase catalyzes the trans-sulfuration reaction of mercaptopyruvate or thiosulfate to thiol-containing compounds or cyanide.	Cyanides	177-184	mercaptopyruvate sulfurtransferase	Homo sapiens	31-67
25441899-1	2014	In this study, we synthesized CTB and CB probes based on doubly activated Michael acceptors to selectively detect cyanide (CN(-)) anions through a one-step condensation reaction of coumarinyl acrylaldehyde with the corresponding derivatives of malonyl urea (thiourea).	Cyanides	114-121	chitobiase	Homo sapiens	30-33
25280224-3	2014	Theoretical calculations also predict that the cyanide-supported DNIC anion of [(NC)2Fe(NO)2](-) features C2v symmetry with a Fe-C-N bonding motif, and multireference theories suggest a minimal active space of CAS(9,9) to describe these {Fe(NO)2}(9) compounds, while larger CAS(13,13) calculations do not tend to significantly improve the geometries.	Cyanides	47-54	BCAR1 scaffold protein, Cas family member	Homo sapiens	210-213
25589927-3	2015	Detailed DMPK studies involving cyanide and GSH as trapping agents during microsomal incubations, in addition to deuterium-labeled compounds as mechanistic probes uncovered the molecular basis for the observed CYP3A4 TDI in the series.	Cyanides	32-39	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	210-216
25910742-2	2015	Branching from the traditional respiratory chain at the quinone pool, AOX is responsible for cyanide-resistant respiration in plants and fungi, heat generation in thermogenic plants, and survival of parasites, such as Trypanosoma brucei, in the human host.	Cyanides	93-100	acyl-CoA oxidase 1	Homo sapiens	70-73
24975519-6	2014	When it comes to thermal analysis, the complexes followed usual decomposition mechanism in which neutral ligands (hepH) are released first, and then cyanide ligands are decomposed.	Cyanides	149-156	hephaestin	Homo sapiens	114-118
25280224-3	2014	Theoretical calculations also predict that the cyanide-supported DNIC anion of [(NC)2Fe(NO)2](-) features C2v symmetry with a Fe-C-N bonding motif, and multireference theories suggest a minimal active space of CAS(9,9) to describe these {Fe(NO)2}(9) compounds, while larger CAS(13,13) calculations do not tend to significantly improve the geometries.	Cyanides	47-54	BCAR1 scaffold protein, Cas family member	Homo sapiens	274-277
24780244-5	2014	Heme ligand cyanide (CN(-)) decreased the yield and the rate of Cygb(Fe(3+)) reduction, but ligands CO and NO allowed the process of Cygb(Fe(3+)) reduction to continue to completion.	Cyanides	12-19	cytoglobin	Homo sapiens	64-68
25186256-1	2014	We have previously reported cyanide at concentrations of up to 150 muM in the sputum of cystic fibrosis patients infected with Pseudomonas aeruginosa and a negative correlation with lung function.	Cyanides	28-35	latexin	Homo sapiens	67-70
24780244-5	2014	Heme ligand cyanide (CN(-)) decreased the yield and the rate of Cygb(Fe(3+)) reduction, but ligands CO and NO allowed the process of Cygb(Fe(3+)) reduction to continue to completion.	Cyanides	21-26	cytoglobin	Homo sapiens	64-68
24623680-5	2014	Further, we showed that binding of substrate to CYP5A1 can induce conformational changes in the protein that block small-molecule ligand egress by measuring the kinetics of cyanide binding to CYP5A1 as a function of substrate concentration.	Cyanides	173-180	thromboxane A synthase 1	Homo sapiens	48-54
24632414-3	2014	In this study, we measured cyanide binding to the ferric state of the wild-type (WT) Cgb, and found that the binding consisted of multiple steps.	Cyanides	27-34	cytoglobin	Homo sapiens	85-88
24218104-8	2014	The distribution of glia cells (GFAP), Neuron specific Enolase (NSE) and Ki-67 increased with cyanide treatment, although the increases were more pronounced in the neurogenic cell area (PVZ) when compared to the cortex.	Cyanides	94-101	glial fibrillary acidic protein	Rattus norvegicus	32-36
24218104-8	2014	The distribution of glia cells (GFAP), Neuron specific Enolase (NSE) and Ki-67 increased with cyanide treatment, although the increases were more pronounced in the neurogenic cell area (PVZ) when compared to the cortex.	Cyanides	94-101	enolase 2	Rattus norvegicus	39-62
24218104-8	2014	The distribution of glia cells (GFAP), Neuron specific Enolase (NSE) and Ki-67 increased with cyanide treatment, although the increases were more pronounced in the neurogenic cell area (PVZ) when compared to the cortex.	Cyanides	94-101	enolase 2	Rattus norvegicus	64-67
24728709-7	2014	CYP71B6 was expressed in Saccharomyces cerevisiae and shown to efficiently convert indole-3-acetonitrile into ICHO and ICOOH, thereby releasing cyanide.	Cyanides	144-151	cytochrome p450 71b6	Arabidopsis thaliana	0-7
24786191-0	2014	Putting a terbium-monometallic cyanide cluster into the C82 fullerene cage: TbCN@C2(5)-C82.	Cyanides	31-38	complement C8 beta chain	Homo sapiens	56-59
24786191-0	2014	Putting a terbium-monometallic cyanide cluster into the C82 fullerene cage: TbCN@C2(5)-C82.	Cyanides	31-38	complement C8 beta chain	Homo sapiens	87-90
24786191-2	2014	The C2(5)-C82 isomeric cage represents a new cage capable of encapsulating a monometallic cyanide cluster.	Cyanides	90-97	complement C8 beta chain	Homo sapiens	10-13
24697240-2	2014	Most organic functional groups are tolerated by zinc organometallic reagents, and Csp(2)-centered magnesium organometallic reagents are compatible with important functional groups, such as the ester, aryl ketone, nitro, cyano, and amide functions.	Cyanides	220-225	regulator of calcineurin 2	Homo sapiens	82-87
24670138-0	2014	Time-dependent comparative evaluation of some important biomarkers of acute cyanide poisoning in rats: an aid in diagnosis.	Cyanides	76-83	activation-induced cytidine deaminase	Rattus norvegicus	106-109
24623680-5	2014	Further, we showed that binding of substrate to CYP5A1 can induce conformational changes in the protein that block small-molecule ligand egress by measuring the kinetics of cyanide binding to CYP5A1 as a function of substrate concentration.	Cyanides	173-180	thromboxane A synthase 1	Homo sapiens	192-198
24623680-6	2014	Notably, we observed that sensitivity to cyanide binding was different for two substrate analogues, U44069 and U46619, thus indicating that they bind differently to the active site of CYP5A1.	Cyanides	41-48	thromboxane A synthase 1	Homo sapiens	184-190
24575888-0	2014	Asymmetric synthesis of the HMG-CoA reductase inhibitor atorvastatin calcium: an organocatalytic anhydride desymmetrization and cyanide-free side chain elongation approach.	Cyanides	128-135	3-hydroxy-3-methylglutaryl-CoA reductase	Homo sapiens	28-45
24768788-0	2014	EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin.	Cyanides	16-23	neuroglobin	Homo sapiens	53-64
24768788-1	2014	Electron paramagnetic resonance (EPR) data reveal large differences between the ferric ((13)C-)cyanide complexes of wild-type human neuroglobin (NGB) and its H64Q and F28L point mutants and the cyanide complexes of mammalian myo- and haemoglobin.	Cyanides	95-102	neuroglobin	Homo sapiens	132-143
24768788-1	2014	Electron paramagnetic resonance (EPR) data reveal large differences between the ferric ((13)C-)cyanide complexes of wild-type human neuroglobin (NGB) and its H64Q and F28L point mutants and the cyanide complexes of mammalian myo- and haemoglobin.	Cyanides	95-102	neuroglobin	Homo sapiens	145-148
24768788-2	2014	The point mutations, which involve residues comprising the distal haem pocket in NGB, induce smaller, but still significant changes, related to changes in the stabilization of the cyanide ligand.	Cyanides	180-187	neuroglobin	Homo sapiens	81-84
24768788-5	2014	The same ENDOR procedure allowed also partial determination of the corresponding (13)C hyperfine tensor of cyanide-ligated NGB and H64QNGB.	Cyanides	107-114	neuroglobin	Homo sapiens	123-126
24389872-9	2014	Different stimuli considered as cell stresses (rotenone, cyanide, sorbitol, and complete absence of intracellular Ca(2+) by BAPTA-AM) also cause AMPK phosphorylation in spermatozoa.	Cyanides	57-64	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	145-149
24492802-1	2014	The self-assembly of [Mo(V)(CN)8](3-) and [Fe(II)(bik)2(S)2](2+) affords a cyanide-bridged {Mo(V)2Fe(II)2} rhombus molecule that shows photomagnetic effect under laser light irradiation at low temperature and exhibits thermo-induced spin crossover near ambient temperature.	Cyanides	75-82	BCL2 interacting killer	Homo sapiens	50-53
24573499-0	2014	A density functional theory study of paramagnetic cyclopentadienylcobalt(III) derivatives: fluoride versus cyanide.	Cyanides	107-114	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	73-76
24573499-1	2014	The cobalt(III) complexes Cp2Co2F4 and Cp2Co2(CN)4 have been studied by density functional theory methods as representatives of the experimentally known Cp2Co2X4 species with the weak-field fluoride ligand and the strong-field cyanide ligand.	Cyanides	227-234	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	11-14
24592975-4	2014	In the preparation of these Re(I) NHC complexes, it is found that the reactivity of the isocyanide ligands in the synthetic complex precursors is significantly affected by the electronic nature of the trans ligand.	Cyanides	88-98	high mobility group nucleosomal binding domain 4	Homo sapiens	34-37
24398435-3	2014	CYS-C1 knockout leads to an increased level of cyanide in the roots and leaves and a severe defect in root hair morphogenesis, suggesting that cyanide acts as a signaling factor in root development.	Cyanides	47-54	cysteine synthase C1	Arabidopsis thaliana	0-6
24062137-2	2014	Cyanogenesis is defined as the hydroxynitrile lyase catalysed release of a cyanide group in the form of HCN and the corresponding aldehyde or ketone.	Cyanides	75-82	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	104-107
24398435-2	2014	To maintain cyanide at non-toxic levels, Arabidopsis plants express the mitochondrial beta-cyanoalanine synthase CYS-C1.	Cyanides	12-19	cysteine synthase C1	Arabidopsis thaliana	113-119
24398435-3	2014	CYS-C1 knockout leads to an increased level of cyanide in the roots and leaves and a severe defect in root hair morphogenesis, suggesting that cyanide acts as a signaling factor in root development.	Cyanides	143-150	cysteine synthase C1	Arabidopsis thaliana	0-6
24398435-5	2014	Moreover, CYS-C1 mutation increases both plant tolerance to biotrophic pathogens and their susceptibility to necrotrophic fungi, indicating that cyanide could stimulate the salicylic acid-dependent signaling pathway of the plant immune system.	Cyanides	145-152	cysteine synthase C1	Arabidopsis thaliana	10-16
24398435-6	2014	We hypothesize that CYS-C1 is essential for maintaining non-toxic concentrations of cyanide in the mitochondria to facilitate cyanide"s role in signaling.	Cyanides	84-91	cysteine synthase C1	Arabidopsis thaliana	20-26
24398435-6	2014	We hypothesize that CYS-C1 is essential for maintaining non-toxic concentrations of cyanide in the mitochondria to facilitate cyanide"s role in signaling.	Cyanides	126-133	cysteine synthase C1	Arabidopsis thaliana	20-26
24279989-7	2013	Samples of the catalytically inactive substrate-bound Fe(III)-CDO species were treated with cyanide, resulting in a low-spin (S = 1/2) ternary complex.	Cyanides	92-99	cysteine dioxygenase 1, cytosolic	Mus musculus	62-65
24231741-0	2014	Lysozyme-stabilized gold nanoclusters as a novel fluorescence probe for cyanide recognition.	Cyanides	72-79	lysozyme	Homo sapiens	0-8
24231741-1	2014	Lysozyme-stabilized gold nanoclusters (Lys-AuNCs) have been synthesized and utilized as a fluorescent probe for selective detection of cyanide (CN(-)).	Cyanides	135-142	lysozyme	Homo sapiens	0-8
24231750-6	2014	The analytical utility of the method for the analysis of cyanide ions in electroplating wastewater (EPWW), human serum, tap and mineral water samples was demonstrated and the results were compared successfully with the conventional reference method.	Cyanides	57-64	nuclear RNA export factor 1	Homo sapiens	120-123
24304351-5	2013	The Fe-CN-Co electron transfer pathway is highlighted by a strongly XMCD dependent transition to a cyanide back bonding orbital, giving evidence for strong hybridization with Fe(III) t2g orbitals.	Cyanides	99-106	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	178-181
24100226-2	2013	Interestingly, the genome of the roundworm Caenorhabditis elegans contains three expressed genes predicted to encode OAS-TL orthologs (cysl-1-cysl-3), and a related pseudogene (cysl-4); these genes play different roles in resistance to hypoxia, hydrogen sulfide and cyanide.	Cyanides	266-273	Cysteine synthase	Caenorhabditis elegans	177-183
24100226-7	2013	Based on the available evidences we propose the following model: CYSL-1 interacts with EGL-9 and activates HIF-1 that upregulates expression of genes detoxifying sulfide and cyanide, the CYSL-2 acts as a cyanoalanine synthase in the cyanide detoxification pathway and simultaneously produces hydrogen sulfide, while the role of CYSL-3 remains unclear although it exhibits sulfhydrylase activity in vitro.	Cyanides	174-181	Cysteine synthase 1	Caenorhabditis elegans	65-71
24100226-7	2013	Based on the available evidences we propose the following model: CYSL-1 interacts with EGL-9 and activates HIF-1 that upregulates expression of genes detoxifying sulfide and cyanide, the CYSL-2 acts as a cyanoalanine synthase in the cyanide detoxification pathway and simultaneously produces hydrogen sulfide, while the role of CYSL-3 remains unclear although it exhibits sulfhydrylase activity in vitro.	Cyanides	174-181	Hypoxia-inducible factor prolyl hydroxylase	Caenorhabditis elegans	87-92
23929717-0	2013	Dose and time-dependent effects of cyanide on thiosulfate sulfurtransferase, 3-mercaptopyruvate sulfurtransferase, and cystathionine lambda-lyase activities.	Cyanides	35-42	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	46-75
23929717-0	2013	Dose and time-dependent effects of cyanide on thiosulfate sulfurtransferase, 3-mercaptopyruvate sulfurtransferase, and cystathionine lambda-lyase activities.	Cyanides	35-42	mercaptopyruvate sulfurtransferase	Mus musculus	77-113
23929717-5	2013	After 0.5 LD50 KCN, the elevated hepatic cyanide level was accompanied by increased TST, 3-MPST, and CST activities, and CCO inhibition.	Cyanides	41-48	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	84-87
23929717-5	2013	After 0.5 LD50 KCN, the elevated hepatic cyanide level was accompanied by increased TST, 3-MPST, and CST activities, and CCO inhibition.	Cyanides	41-48	mercaptopyruvate sulfurtransferase	Mus musculus	91-95
23929717-6	2013	Elevated renal cyanide level was only accompanied by increased 3-MPST activity.	Cyanides	15-22	mercaptopyruvate sulfurtransferase	Mus musculus	65-69
24195476-1	2013	By capitalizing on the different reactivity of nitrile N-oxides with isocyanides and amine, alpha-oximinoamidines, a so far elusive class of compounds, have been synthesized in a straightforward way by reacting isocyanides, syn-chlorooximes, and amines in a multicomponent fashion.	Cyanides	69-80	synemin	Homo sapiens	162-165
24195476-1	2013	By capitalizing on the different reactivity of nitrile N-oxides with isocyanides and amine, alpha-oximinoamidines, a so far elusive class of compounds, have been synthesized in a straightforward way by reacting isocyanides, syn-chlorooximes, and amines in a multicomponent fashion.	Cyanides	211-222	synemin	Homo sapiens	162-165
23805000-6	2013	We demonstrate that the cyanide resistance exhibited by egl-9 mutants is completely dependent on the HIF-1 hypoxia-inducible factor and is mediated by the cysl-2 cysteine synthase, which likely functions in metabolic pathways that inactivate cyanide.	Cyanides	24-31	Hypoxia-inducible factor prolyl hydroxylase	Caenorhabditis elegans	56-61
23955374-2	2013	This reaction affords the guanidinate complexes [Nb(NMe2)2{N(2,6-(i)Pr2C6H3)}{(N(i)Pr)2C(NH(i)Pr)}] or [Nb(NMe2)2{N(2,6-(i)Pr2C6H3)}{(N(i)Pr)2C(NH(n)Bu)}] and free isocyanide.	Cyanides	164-174	NME/NM23 nucleoside diphosphate kinase 2	Homo sapiens	52-56
23749193-2	2013	However, these nitriles can also be lethal due in large part to the microsomal metabolic release of cyanide, which is mostly dependent on the activity of the 2E1 isoform of the cytochrome P450 (CYP2E1).	Cyanides	100-107	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	194-200
23805000-6	2013	We demonstrate that the cyanide resistance exhibited by egl-9 mutants is completely dependent on the HIF-1 hypoxia-inducible factor and is mediated by the cysl-2 cysteine synthase, which likely functions in metabolic pathways that inactivate cyanide.	Cyanides	24-31	Bifunctional L-3-cyanoalanine synthase/cysteine synthase	Caenorhabditis elegans	155-161
23805000-6	2013	We demonstrate that the cyanide resistance exhibited by egl-9 mutants is completely dependent on the HIF-1 hypoxia-inducible factor and is mediated by the cysl-2 cysteine synthase, which likely functions in metabolic pathways that inactivate cyanide.	Cyanides	242-249	Hypoxia-inducible factor prolyl hydroxylase	Caenorhabditis elegans	56-61
23805000-6	2013	We demonstrate that the cyanide resistance exhibited by egl-9 mutants is completely dependent on the HIF-1 hypoxia-inducible factor and is mediated by the cysl-2 cysteine synthase, which likely functions in metabolic pathways that inactivate cyanide.	Cyanides	242-249	Bifunctional L-3-cyanoalanine synthase/cysteine synthase	Caenorhabditis elegans	155-161
23805000-7	2013	Further, the expression of cysl-2 correlates with the degree of cyanide resistance exhibited in each genetic background.	Cyanides	64-71	Bifunctional L-3-cyanoalanine synthase/cysteine synthase	Caenorhabditis elegans	27-33
23736999-1	2013	A systematic study of the 80-year-old simple and fundamental reaction of cobalt(II) salt with cyanide under one atmosphere CO was carried out and two novel Co(I) complexes were isolated in the absence of hydroxide.	Cyanides	94-101	mitochondrially encoded cytochrome c oxidase I	Homo sapiens	156-161
23598230-3	2013	The concentration of the cyanide anions that could be detected was as low as 1.0 muM.	Cyanides	25-32	latexin	Homo sapiens	81-84
23698001-4	2013	The kinetics of H2S production by MST from 3-MP was studied at pH 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glutathione, homocysteine, and thioredoxin, and in the presence of cyanide.	Cyanides	230-237	mercaptopyruvate sulfurtransferase	Homo sapiens	34-37
23827816-2	2013	Formate oxidoreductase activity was detected in blue native polyacrylamide gel electrophoresis (BN-PAGE) resolved membranes of E. coli, which were also capable of cyanide sensitive formate:oxygen oxidoreductase activity.	Cyanides	163-170	oxidoreductase	Escherichia coli	8-22
23827816-2	2013	Formate oxidoreductase activity was detected in blue native polyacrylamide gel electrophoresis (BN-PAGE) resolved membranes of E. coli, which were also capable of cyanide sensitive formate:oxygen oxidoreductase activity.	Cyanides	163-170	oxidoreductase	Escherichia coli	196-210
23784464-2	2013	Arabidopsis (Arabidopsis thaliana) detoxifies cyanide primarily through the enzyme beta-cyanoalanine synthase, mainly by the mitochondrial CYS-C1.	Cyanides	46-53	cysteine synthase C1	Arabidopsis thaliana	139-145
23784464-3	2013	CYS-C1 loss of function is not toxic for the plant and leads to an increased level of cyanide in cys-c1 mutants as well as a root hairless phenotype.	Cyanides	86-93	cysteine synthase C1	Arabidopsis thaliana	97-103
23784464-4	2013	The classification of genes differentially expressed in cys-c1 and wild-type plants reveals that the high endogenous cyanide content of the cys-c1 mutant is correlated with the biotic stress response.	Cyanides	117-124	cysteine synthase C1	Arabidopsis thaliana	56-62
23784464-4	2013	The classification of genes differentially expressed in cys-c1 and wild-type plants reveals that the high endogenous cyanide content of the cys-c1 mutant is correlated with the biotic stress response.	Cyanides	117-124	cysteine synthase C1	Arabidopsis thaliana	140-146
23784464-8	2013	We hypothesize that cyanide, which is transiently accumulated during avirulent bacterial infection and constitutively accumulated in the cys-c1 mutant, uncouples the respiratory electron chain dependent on the cytochrome c oxidase, and this uncoupling induces the alternative oxidase activity and the accumulation of reactive oxygen species, which act by stimulating the salicylic acid-dependent signaling pathway of the plant immune system.	Cyanides	20-27	cysteine synthase C1	Arabidopsis thaliana	137-143
23450248-0	2013	Syntheses, structures, and magnetic properties of cyano- and phenoxide-bridged Fe(III)-Mn(III) tetrameric assemblies formed by blocked fac-Fe tricyanide with aliphatic rings.	Cyanides	50-55	FA complementation group C	Homo sapiens	135-138
23348716-1	2013	Nanoaggregates of a supramolecular ensemble of triphenylene derivative 3 and Cu(2+) ions exhibit "turn-on" response towards CN(-) ions in an aqueous medium and can detect the trace amount of inorganic cyanide ions (NaCN) in tap water and blood serum milieu.	Cyanides	201-208	nuclear RNA export factor 1	Homo sapiens	224-227
23337638-0	2013	Urea-induced modification of cytochrome c flexibility as probed by cyanide binding.	Cyanides	67-74	cytochrome c, somatic	Homo sapiens	29-41
23337638-1	2013	Cyanide binding to cytochrome c was monitored by absorption spectroscopy from neutral to acidic pH in the presence of urea.	Cyanides	0-7	cytochrome c, somatic	Homo sapiens	19-31
23412550-0	2013	Interaction of dimeric horse cytochrome c with cyanide ion.	Cyanides	47-54	cytochrome c, somatic	Equus caballus	29-41
23440198-1	2013	A transketolase reaction was catalyzed by cyanide ion under prebiotic conditions instead of its modern catalyst, thiamine pyrophosphate (TPP).	Cyanides	42-49	transketolase	Homo sapiens	2-15
23022490-0	2013	Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants.	Cyanides	96-103	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	38-61
23165770-9	2013	Increased expression of ASIC3 in transgenic mice increased pH sensitivity while reducing cyanide sensitivity.	Cyanides	89-96	acid-sensing (proton-gated) ion channel 3	Mus musculus	24-29
23598025-0	2013	Cu2+-modulated cysteamine-capped CdS quantum dots as a turn-on fluorescence sensor for cyanide recognition.	Cyanides	87-94	CDP-diacylglycerol synthase 1	Homo sapiens	33-36
23598025-1	2013	A new fluorescence sensor for detection of cyanide ions (CN(-)) in aqueous media based on the recovered fluorescence of cysteamine capped CdS quantum dots [Cys-CdS QDs]-Cu(2+) system was proposed.	Cyanides	43-50	CDP-diacylglycerol synthase 1	Homo sapiens	138-141
23598025-1	2013	A new fluorescence sensor for detection of cyanide ions (CN(-)) in aqueous media based on the recovered fluorescence of cysteamine capped CdS quantum dots [Cys-CdS QDs]-Cu(2+) system was proposed.	Cyanides	43-50	CDP-diacylglycerol synthase 1	Homo sapiens	160-163
23262184-5	2013	The second objective was to examine how interruption of single genes (AtCysA1, AtCysC1 and AtNIT4) encoding enzymes of the pathway influenced the ability to metabolize cyanide and withstand water deficit.	Cyanides	168-175	cysteine synthase C1	Arabidopsis thaliana	79-86
23262184-5	2013	The second objective was to examine how interruption of single genes (AtCysA1, AtCysC1 and AtNIT4) encoding enzymes of the pathway influenced the ability to metabolize cyanide and withstand water deficit.	Cyanides	168-175	nitrilase 4	Arabidopsis thaliana	91-97
23022490-8	2013	The binding affinity for cyanide is reduced at least two orders of magnitude in the triple mutants compared to wild-type CcP and the rate of cyanide binding is reduced by four to five orders of magnitude.	Cyanides	25-32	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	121-124
23412550-2	2013	To gain insight into the effect of methionine dissociation in dimeric cytochrome c, we investigated its interaction with cyanide ion.	Cyanides	121-128	cytochrome c, somatic	Equus caballus	70-82
23412550-3	2013	We found that the Soret and Q bands of oxidized dimeric cytochrome c at 406.5 and 529 nm redshift to 413 and 536 nm, respectively, on addition of 1 mM cyanide ion.	Cyanides	151-158	cytochrome c, somatic	Equus caballus	56-68
23412550-4	2013	The binding constant of dimeric cytochrome c and cyanide ion was obtained as 2.5 x 10(4) M(-1).	Cyanides	49-56	cytochrome c, somatic	Equus caballus	32-44
23412550-7	2013	The low nu                 (Fe-CN) frequency suggests weaker binding of the cyanide ion to dimeric cytochrome c compared with other heme proteins possessing a distal heme cavity.	Cyanides	76-83	cytochrome c, somatic	Equus caballus	99-111
23135388-6	2013	In this work, we used (1)H NMR spectroscopy to probe the cyanide binding properties of different Ngb species in solution, including wild-type Ngb and the single (C120S) and triple (C46G/C55S/C120S) mutants.	Cyanides	57-64	neuroglobin	Homo sapiens	97-100
22711743-6	2012	To reduce cyanide-dependent ROS production in cassava root mitochondria, we generated transgenic plants expressing a codon-optimized Arabidopsis (Arabidopsis thaliana) mitochondrial alternative oxidase gene (AOX1A).	Cyanides	10-17	alternative oxidase 1A	Arabidopsis thaliana	208-213
22511607-2	2012	In mitochondria, cyanide is a potent inhibitor of the cytochrome c oxidase and is metabolized by the beta-cyanoalanine synthase CYS-C1, catalyzing the conversion of cysteine and cyanide to hydrogen sulfide and beta-cyanoalanine.	Cyanides	17-24	cysteine synthase C1	Arabidopsis thaliana	128-134
22511607-2	2012	In mitochondria, cyanide is a potent inhibitor of the cytochrome c oxidase and is metabolized by the beta-cyanoalanine synthase CYS-C1, catalyzing the conversion of cysteine and cyanide to hydrogen sulfide and beta-cyanoalanine.	Cyanides	178-185	cysteine synthase C1	Arabidopsis thaliana	128-134
22511607-6	2012	The mitochondria compromise their capacity to properly detoxify cyanide and the resulting sulfide because the latter cannot re-assimilate into cysteine in the oas-c null mutant.	Cyanides	64-71	O-acetylserine (thiol) lyase 	Arabidopsis thaliana	159-164
22511607-8	2012	Our results allow us to suggest that the significance of OAS-C is related to its role in the proper sulfide and cyanide detoxification in mitochondria.	Cyanides	112-119	O-acetylserine (thiol) lyase 	Arabidopsis thaliana	57-62
23300486-10	2013	Accordingly, AOX expression was able to support cyanide-resistant respiration by intact organs and to afford prolonged protection against a lethal concentration of gaseous cyanide in whole animals.	Cyanides	48-55	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	13-16
23300486-10	2013	Accordingly, AOX expression was able to support cyanide-resistant respiration by intact organs and to afford prolonged protection against a lethal concentration of gaseous cyanide in whole animals.	Cyanides	172-179	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	13-16
23123111-2	2012	The Fe(CN)(2)CO moiety of [NiFe] hydrogenases is assembled via unknown transient interactions among specific maturation proteins HypC (metallochaperone), HypD (redox protein), and HypE (cyanide synthesis/donor).	Cyanides	186-193	FIC domain protein adenylyltransferase	Homo sapiens	180-184
23123111-5	2012	The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer.	Cyanides	140-147	FIC domain protein adenylyltransferase	Homo sapiens	38-42
23123111-5	2012	The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer.	Cyanides	140-147	pre-mRNA processing factor 40 homolog B	Homo sapiens	51-55
23123111-5	2012	The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer.	Cyanides	140-147	MAGE family member A3	Homo sapiens	88-92
23123111-5	2012	The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer.	Cyanides	140-147	FIC domain protein adenylyltransferase	Homo sapiens	108-112
23068104-0	2012	Cyanide binding to human plasma heme-hemopexin: a comparative study.	Cyanides	0-7	hemopexin	Homo sapiens	37-46
22554042-5	2012	Importantly, the addition of the AOX inhibitor salicylhydroxamic acid (1 mm; SHAM) decreased plant resistance to environmental stress and even compromised the cyanide (CN)-enhanced stress tolerance.	Cyanides	159-166	ubiquinol oxidase 4, chloroplastic/chromoplastic	Cucumis sativus	33-36
22554042-5	2012	Importantly, the addition of the AOX inhibitor salicylhydroxamic acid (1 mm; SHAM) decreased plant resistance to environmental stress and even compromised the cyanide (CN)-enhanced stress tolerance.	Cyanides	168-170	ubiquinol oxidase 4, chloroplastic/chromoplastic	Cucumis sativus	33-36
22942274-5	2012	They also were comparable in the activation of AA oxygenation by cyanide-inhibited PGHS-2.	Cyanides	65-72	prostaglandin-endoperoxide synthase 2	Mus musculus	83-89
22937807-0	2012	Palladium-catalyzed C(sp2)-H cyanation using tertiary amine derived isocyanide as a cyano source.	Cyanides	68-78	Sp2 transcription factor	Homo sapiens	20-25
22610379-4	2012	Cyanide-induced artificial anoxia, as well as a direct AMPK activator (A-769662) also increase AMPK phosphorylation and Na(+),K(+)-ATPase activity.	Cyanides	0-7	protein kinase AMP-activated catalytic subunit alpha 2	Rattus norvegicus	95-99
22550634-1	2012	The self-assembly of [Fe(III)(Tp)(CN)(3)](-) and [Fe(II)(bik)(2)(S)(2)](2+) affords the cyanide-bridged mixed valence {Fe(III)(2)Fe(II)(2)}(2+) molecular square, which exhibits a photomagnetic effect under laser light irradiation at low temperature and also shows thermal spin-state conversion near ambient temperature.	Cyanides	88-95	BCL2 interacting killer	Homo sapiens	57-60
24061257-1	2012	The purpose of this study was to compare the composition of the biogas produced by the anaerobic degradation of glucose with or without the addition of cyanide (32.0 mg L-1) during the digestion process using the qualitative OxiTop method and the quantitative gas chromatography (GC).	Cyanides	152-159	immunoglobulin kappa variable 1-16	Homo sapiens	169-172
22378306-0	2012	Pd-catalyzed and CsF-promoted reaction of bromoalkynes with isocyanides: regioselective synthesis of substituted 5-iminopyrrolones.	Cyanides	60-71	colony stimulating factor 2	Homo sapiens	17-20
22378306-1	2012	The palladium-catalyzed and CsF-promoted annulation reaction of bromoalkynes and isocyanides regioselectively affords a diverse set of 5-iminopyrrolone derivatives.	Cyanides	81-92	colony stimulating factor 2	Homo sapiens	28-31
22378306-2	2012	This chemistry presumably proceeds through the bromoacrylamide intermediates, which can be readily prepared from the nucleophilic addition reaction of isocyanides to bromoalkynes in the presence of CsF.	Cyanides	151-162	colony stimulating factor 2	Homo sapiens	198-201
21854848-0	2012	Cyanide preconditioning protects brain endothelial and NT2 neuron-like cells against glucotoxicity: role of mitochondrial reactive oxygen species and HIF-1alpha.	Cyanides	0-7	hypoxia inducible factor 1 subunit alpha	Homo sapiens	150-160
22547189-12	2011	Biochemical analysis of liver enzymes showed that cyanide (group2) damaged the liver as there was significantly elevated presence (p<0.05) of Aspartate aminotransferase (AST) and Alanine aminotransferase (ALP) above those of the control group.	Cyanides	50-57	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	145-171
22547189-12	2011	Biochemical analysis of liver enzymes showed that cyanide (group2) damaged the liver as there was significantly elevated presence (p<0.05) of Aspartate aminotransferase (AST) and Alanine aminotransferase (ALP) above those of the control group.	Cyanides	50-57	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	173-176
22547189-12	2011	Biochemical analysis of liver enzymes showed that cyanide (group2) damaged the liver as there was significantly elevated presence (p<0.05) of Aspartate aminotransferase (AST) and Alanine aminotransferase (ALP) above those of the control group.	Cyanides	50-57	PDZ and LIM domain 3	Rattus norvegicus	208-211
21854848-9	2012	Altogether our results demonstrate that mitochondrial preconditioning induced by cyanide triggers a protective response mediated by mitochondrial ROS and HIF-1alpha activation and signaling, which render brain endothelial and neuronal cells resistant against glucotoxicity.	Cyanides	81-88	hypoxia inducible factor 1 subunit alpha	Homo sapiens	154-164
22050369-0	2011	Pentanuclear cyanide-bridged complexes based on highly anisotropic Co(II) seven-coordinate building blocks: synthesis, structure, and magnetic behavior.	Cyanides	13-20	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	67-73
22050369-5	2011	In 4, the central and terminal Co(II) ions are bound to cyanide groups cis to one another on the bridging {Cr(CN)(6)}, whereas in 5, the connections are via trans cyanide ligands, resulting in the zigzag and linear structures observed, respectively.	Cyanides	56-63	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	31-37
22050369-5	2011	In 4, the central and terminal Co(II) ions are bound to cyanide groups cis to one another on the bridging {Cr(CN)(6)}, whereas in 5, the connections are via trans cyanide ligands, resulting in the zigzag and linear structures observed, respectively.	Cyanides	163-170	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	31-37
21854848-2	2012	Rat brain endothelial cells (RBE4) treated with non-toxic concentrations of cyanide (<=1 muM; 1h) exhibited an increase in ROS levels, particularly hydrogen peroxide (H(2)O(2)).	Cyanides	76-83	latexin	Homo sapiens	92-95
21854848-4	2012	The stabilization and nuclear activation of HIF-1alpha in the presence of cyanide were also observed, which resulted in an increase in vascular endothelial growth factor (VEGF), endothelial nitric oxide synthase (eNOS) and erythropoietin (EPO) protein levels reflecting an adaptive response.	Cyanides	74-81	hypoxia inducible factor 1 subunit alpha	Homo sapiens	44-54
21854848-4	2012	The stabilization and nuclear activation of HIF-1alpha in the presence of cyanide were also observed, which resulted in an increase in vascular endothelial growth factor (VEGF), endothelial nitric oxide synthase (eNOS) and erythropoietin (EPO) protein levels reflecting an adaptive response.	Cyanides	74-81	vascular endothelial growth factor A	Homo sapiens	135-169
21854848-4	2012	The stabilization and nuclear activation of HIF-1alpha in the presence of cyanide were also observed, which resulted in an increase in vascular endothelial growth factor (VEGF), endothelial nitric oxide synthase (eNOS) and erythropoietin (EPO) protein levels reflecting an adaptive response.	Cyanides	74-81	vascular endothelial growth factor A	Homo sapiens	171-175
21854848-4	2012	The stabilization and nuclear activation of HIF-1alpha in the presence of cyanide were also observed, which resulted in an increase in vascular endothelial growth factor (VEGF), endothelial nitric oxide synthase (eNOS) and erythropoietin (EPO) protein levels reflecting an adaptive response.	Cyanides	74-81	nitric oxide synthase 3	Homo sapiens	178-211
21854848-4	2012	The stabilization and nuclear activation of HIF-1alpha in the presence of cyanide were also observed, which resulted in an increase in vascular endothelial growth factor (VEGF), endothelial nitric oxide synthase (eNOS) and erythropoietin (EPO) protein levels reflecting an adaptive response.	Cyanides	74-81	erythropoietin	Homo sapiens	223-237
21854848-4	2012	The stabilization and nuclear activation of HIF-1alpha in the presence of cyanide were also observed, which resulted in an increase in vascular endothelial growth factor (VEGF), endothelial nitric oxide synthase (eNOS) and erythropoietin (EPO) protein levels reflecting an adaptive response.	Cyanides	74-81	erythropoietin	Homo sapiens	239-242
21854848-6	2012	In mitochondrial DNA-depleted NT2 (NT2 rho0) cells, cyanide (0.1 muM) was unable to stimulate ROS production and, consequently, protect against glucotoxicity.	Cyanides	52-59	latexin	Homo sapiens	65-68
21854848-7	2012	Conversely, in NT2 cells, the parental cells with functional mitochondria, cyanide significantly increased ROS levels protecting against high glucose-induced neuronal cell loss and activation of caspase-3.	Cyanides	75-82	caspase 3	Homo sapiens	195-204
21854848-8	2012	The free radical scavenger N-acetyl-L-cysteine and the specific HIF-1alpha inhibitor 2-methoxyestradiol completely abolished the protective effects of cyanide preconditioning.	Cyanides	151-158	hypoxia inducible factor 1 subunit alpha	Homo sapiens	64-74
21519949-5	2011	After cyanide treatment, all caspases increased their activities in homozygous and highly expanded heterozygous cells, caspase 8 and 9 increased also in those cells carrying low-size mutations, remarking their key role as "caspase initiators" in HD.	Cyanides	6-13	caspase 2	Homo sapiens	29-37
21519949-5	2011	After cyanide treatment, all caspases increased their activities in homozygous and highly expanded heterozygous cells, caspase 8 and 9 increased also in those cells carrying low-size mutations, remarking their key role as "caspase initiators" in HD.	Cyanides	6-13	caspase 8	Homo sapiens	119-128
21519949-5	2011	After cyanide treatment, all caspases increased their activities in homozygous and highly expanded heterozygous cells, caspase 8 and 9 increased also in those cells carrying low-size mutations, remarking their key role as "caspase initiators" in HD.	Cyanides	6-13	caspase 2	Homo sapiens	29-36
21786773-0	2011	A density functional theory study of the Nef-isocyanide reaction: mechanism, influence of parameters and scope.	Cyanides	45-55	S100 calcium binding protein B	Homo sapiens	41-44
21819077-0	2011	Palladium-catalyzed intramolecular C(sp2)-H amidination by isonitrile insertion provides direct access to 4-aminoquinazolines from N-arylamidines.	Cyanides	59-69	Sp2 transcription factor	Homo sapiens	35-40
21786773-1	2011	The Nef reaction between isocyanides and acyl chlorides is studied at the M06-2X/6-311+G(d,p) level of theory in toluene.	Cyanides	25-36	S100 calcium binding protein B	Homo sapiens	4-7
22090917-1	2011	In the title complex, [Co(C(22)H(18)N(2)O(4))(CN)(H(2)O)] CH(3)CN, the Co(III) ion is six-coordinated in a distorted octa-hedral environment defined by two N atoms and two O atoms from a salen ligand in the equatorial plane and one O atom from a water mol-ecule and one C atom from a cyanide group at the axial positions.	Cyanides	284-291	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	71-78
21684191-2	2011	Among them 1 showed good sensitivity and selectivity for cyanide ion and also can distinguish it from other anions by different color changes.	Cyanides	57-64	acyl-CoA thioesterase 11	Homo sapiens	6-12
21684191-3	2011	Besides that, the receptor 1 has a sensitive detection limit (1.27 muM) for cyanide ion accordingly it can be used as a colorimetric sensor for the determination of cyanide ion.	Cyanides	76-83	latexin	Homo sapiens	67-70
21684191-3	2011	Besides that, the receptor 1 has a sensitive detection limit (1.27 muM) for cyanide ion accordingly it can be used as a colorimetric sensor for the determination of cyanide ion.	Cyanides	165-172	latexin	Homo sapiens	67-70
21735497-3	2011	Furthermore, several real water samples spiked with cyanide, including local groundwater, tap water, boiled water, and lake water, were analyzed, and the experimental results demonstrated that our sensing system worked well in the above water samples, with a good linear correlation.	Cyanides	52-59	nuclear RNA export factor 1	Homo sapiens	90-93
20135153-2	2011	The best characterized Str is bovine rhodanese (EC 2.8.1.1) which catalyses in vitro the transfer of a sulfane sulfur atom from thiosulfate to cyanide, leading to the formation of sulfite and thiocyanate.	Cyanides	143-150	thiosulfate sulfurtransferase	Bos taurus	37-46
21667987-0	2011	Stereospecific synthesis of syn-alpha-oximinoamides by a three-component reaction of isocyanides, syn-chlorooximes, and carboxylic acids.	Cyanides	85-96	synemin	Homo sapiens	15-18
21667987-0	2011	Stereospecific synthesis of syn-alpha-oximinoamides by a three-component reaction of isocyanides, syn-chlorooximes, and carboxylic acids.	Cyanides	85-96	synemin	Homo sapiens	28-31
21667987-1	2011	A stereospecific multicomponent reaction among isocyanides, syn-chlorooximes, and carboxylic acids provides an efficient synthesis of biologically relevant syn-alpha-oximinoamides.	Cyanides	47-58	synemin	Homo sapiens	121-124
21576503-7	2011	This is illustrated by the 5-fold increase in p50(mito) after partial cyanide inhibition of COX at doses that do not affect maximal mitochondrial electron flux through the ETS.	Cyanides	70-77	nuclear factor kappa B subunit 1	Homo sapiens	46-49
20734249-4	2011	After treatment with cyanide and cobalt, female cortical and mesencephalic astrocytes, respectively, revealed an up-regulation of COX IV-2 which was accompanied by increased ROS production and necrotic cell death.	Cyanides	21-28	cytochrome c oxidase subunit 4I2	Homo sapiens	130-138
21565312-3	2011	The detection limit of the new chromogenic probe was measured to be 1.29 muM which is much lower than most recently reported chromogenic probes for cyanide determination.	Cyanides	148-155	latexin	Homo sapiens	73-76
21246268-4	2011	Under the optimal condition, fluorescence intensity at 460 nm of m-NQB and p-NQB provided two sets of linear ranges, 0.5-15 muM and 20-40 muM and the limit of cyanide detection of 1.4 muM.	Cyanides	159-166	latexin	Homo sapiens	124-127
21550570-0	2011	Case report--death by subcutaneous injection of cyanide in Sri Lanka.	Cyanides	48-55	sorcin	Homo sapiens	59-62
21550570-6	2011	To our knowledge, this is the first reported case of cyanide poisoning by injection in Sri Lanka.	Cyanides	53-60	sorcin	Homo sapiens	87-90
21366342-0	2011	Unique cyanide adduct in human serum albumin: potential as a surrogate exposure marker.	Cyanides	7-14	albumin	Homo sapiens	31-44
21366342-1	2011	Cyanide (CN = HCN + CN(-)) is a renowned poison and neurotoxicant that is prevalent throughout the environment.	Cyanides	0-7	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	14-17
21413761-2	2011	During the electrochemical O(2) reduction process, the hydroperoxide anion (HO(2)(-)) is formed and then reacts to chemically oxidize cyanide (CN(-)) to form cyanate (OCN(-)).	Cyanides	134-141	bone gamma-carboxyglutamate protein	Homo sapiens	167-170
21968615-1	2011	To study the functional role of NADPH during mammalian catalase inhibition, the X-ray crystal structures of NADPH-depleted bovine liver catalase and its inhibitor complexes, cyanide and azide, determined at 2.8A resolution.	Cyanides	174-181	2,4-dienoyl-CoA reductase 1	Homo sapiens	108-113
20813591-0	2011	Impedance spectroscopy and conductometric biosensing for probing catalase reaction with cyanide as ligand and inhibitor.	Cyanides	88-95	catalase	Bos taurus	65-73
20813591-2	2011	This biosensor was used to study the kinetics of catalase-H(2)0(2) reaction and its inhibition by cyanide.	Cyanides	98-105	catalase	Bos taurus	49-57
20813591-6	2011	In parallel, electrochemical characteristics of the catalase/PVA biomembrane and its interaction with cyanide were studied by cyclic voltammetry and impedance spectroscopy.	Cyanides	102-109	catalase	Bos taurus	52-60
21166441-8	2011	Mid-UV/visible spectral changes upon redox transitions in native cytochrome c and its cyanide derivative, as well as dissociation of the ferrous cytochrome c-CN complex, are reported.	Cyanides	86-93	cytochrome c, somatic	Homo sapiens	65-77
21271699-0	2011	Spin crossover in tetranuclear cyanide-bridged iron(II) square complexes: a theoretical study.	Cyanides	31-38	spindlin 1	Homo sapiens	0-4
21271699-1	2011	Spin crossover in a series of six cyanide-bridged iron(II) tetranuclear square complexes was analyzed using density functional theory (DFT) methods.	Cyanides	34-41	spindlin 1	Homo sapiens	0-4
21968615-1	2011	To study the functional role of NADPH during mammalian catalase inhibition, the X-ray crystal structures of NADPH-depleted bovine liver catalase and its inhibitor complexes, cyanide and azide, determined at 2.8A resolution.	Cyanides	174-181	catalase	Bos taurus	136-144
21968615-3	2011	Comparing mammalian- and fungal- catalases, we speculate that NADPH-depleted mammalian catalases may function as a domain-swapped dimer of dimers, especially during inactivation by inhibitors like cyanide and azide.	Cyanides	197-204	2,4-dienoyl-CoA reductase 1	Homo sapiens	62-67
21280568-1	2010	Chill treatment of potato tubers for 8 days induced mitochondrial O2 consumption by cyanide-insensitive alternative oxidase (AOX).	Cyanides	84-91	ubiquinol oxidase 1, mitochondrial-like	Solanum tuberosum	125-128
20716069-1	2010	Mitochondrial alternative oxidase (AOX), the unique respiratory terminal oxidase in plants, catalyzes the energy wasteful cyanide (CN)-resistant respiration and plays a role in optimizing photosynthesis.	Cyanides	122-129	alternative oxidase 2	Arabidopsis thaliana	14-33
20716069-1	2010	Mitochondrial alternative oxidase (AOX), the unique respiratory terminal oxidase in plants, catalyzes the energy wasteful cyanide (CN)-resistant respiration and plays a role in optimizing photosynthesis.	Cyanides	122-129	alternative oxidase 2	Arabidopsis thaliana	35-38
20732392-4	2010	Intracellular recordings revealed that Mecp2(-/y) neurons show only reduced or no hyperpolarizations early during cyanide-induced anoxia, suggesting potassium channel (K(+) channel) dysfunction.	Cyanides	114-121	methyl CpG binding protein 2	Mus musculus	39-44
20882966-0	2010	Spin-crossover and liquid crystal properties in 2D cyanide-bridged Fe(II)-M(I/II) metalorganic frameworks.	Cyanides	51-58	spindlin 1	Homo sapiens	0-4
21270540-1	2011	Mitochondrial alternative oxidase (AOX), the unique respiratory terminal oxidase in plants, catalyzes the energy wasteful cyanide (CN)-resistant respiration and plays a role in optimizing photosynthesis.	Cyanides	122-129	acyl-CoA oxidase 1	Homo sapiens	14-33
21270540-1	2011	Mitochondrial alternative oxidase (AOX), the unique respiratory terminal oxidase in plants, catalyzes the energy wasteful cyanide (CN)-resistant respiration and plays a role in optimizing photosynthesis.	Cyanides	122-129	acyl-CoA oxidase 1	Homo sapiens	35-38
21062066-4	2010	Complex 1 reacts with cyanide to give Et(4)N[Fe(SPh)(Ph(2)PC(6)H(4)CO)(CN)(CO)(2)] (Et(4)N[2]).	Cyanides	22-29	surfactant associated 3	Homo sapiens	48-51
20705081-4	2010	Non-rhodanese mediated sulfur transferase pathways, including 3-mercaptopyruvate sulfurtransferase (3-MPST) catalyze the transfer of sulfur from 3-MP to cyanide, forming pyruvate and less toxic thiocyanate.	Cyanides	153-160	3-mercaptopyruvate sulfurtransferase	Oryctolagus cuniculus	102-106
20619250-11	2010	Since PTZ give rise to cation radicals chemically by the action of peroxidases and cyanide inhibited the PTZ-induced swelling, we propose that PTZ bury in the inner mitochondrial membrane and the chemically generated PTZ cation radicals modify specific thiol groups that in the presence of Ca(2+) result in MPT associated to cytochrome c release.	Cyanides	83-90	cytochrome c, somatic	Homo sapiens	325-337
20700628-5	2010	The cox3-RNAi mutant had only 40% of the wild-type rate of dark respiration which was cyanide-insensitive.	Cyanides	86-93	uncharacterized protein	Chlamydomonas reinhardtii	4-8
20630867-1	2010	Isocyanide (formerly isonitrile) hydratase (EC 4.2.1.103) is an enzyme of the DJ-1 superfamily that hydrates isocyanides to yield the corresponding N-formamide.	Cyanides	0-10	Parkinsonism associated deglycase	Homo sapiens	78-82
20935247-2	2010	The molecular and phenotypical analysis of T-DNA insertion mutants of the mitochondrial beta-cyanoalanine synthase CYS-C1 suggests that discrete accumulation of cyanide is not toxic for the plant and does not alter mitochondrial respiration rates but does act as a strong inhibitor of root hair development.	Cyanides	161-168	cysteine synthase C1	Arabidopsis thaliana	115-121
20935247-3	2010	The cys-c1 null allele is defective in root hair formation and accumulates cyanide in root tissues.	Cyanides	75-82	cysteine synthase C1	Arabidopsis thaliana	4-10
20935247-4	2010	The root hair defect is phenocopied in wild-type plants by the exogenous addition of cyanide to the growth medium and is reversed by the addition of hydroxocobalamin or by genetic complementation with the CYS-C1 gene.	Cyanides	85-92	cysteine synthase C1	Arabidopsis thaliana	205-211
20935247-6	2010	Transcriptional profiling of the cys-c1 mutant reveals that cyanide accumulation acts as a repressive signal for several genes encoding enzymes involved in cell wall rebuilding and the formation of the root hair tip as well as genes involved in ethylene signaling and metabolism.	Cyanides	60-67	cysteine synthase C1	Arabidopsis thaliana	33-39
20630867-1	2010	Isocyanide (formerly isonitrile) hydratase (EC 4.2.1.103) is an enzyme of the DJ-1 superfamily that hydrates isocyanides to yield the corresponding N-formamide.	Cyanides	109-120	Parkinsonism associated deglycase	Homo sapiens	78-82
20630178-0	2010	Amperometric sensor for cyanide utilizing cyanidase and formate dehydrogenase.	Cyanides	24-31	aldehyde dehydrogenase 1 family member L1	Homo sapiens	56-77
20887565-1	2010	We have previously reported that benzohydroxamic acid (BHAM), a potent inhibitor of cyanide (CN)-resistant respiration mediated by alternative oxidase (AOX), induces formation of unique cell masses (i.e., stalk-like cells with a large vacuole and thick cell wall) in starved Dictyostelium cells.	Cyanides	84-91	acyl-CoA oxidase 1	Homo sapiens	131-150
20887565-1	2010	We have previously reported that benzohydroxamic acid (BHAM), a potent inhibitor of cyanide (CN)-resistant respiration mediated by alternative oxidase (AOX), induces formation of unique cell masses (i.e., stalk-like cells with a large vacuole and thick cell wall) in starved Dictyostelium cells.	Cyanides	84-91	acyl-CoA oxidase 1	Homo sapiens	152-155
20887565-1	2010	We have previously reported that benzohydroxamic acid (BHAM), a potent inhibitor of cyanide (CN)-resistant respiration mediated by alternative oxidase (AOX), induces formation of unique cell masses (i.e., stalk-like cells with a large vacuole and thick cell wall) in starved Dictyostelium cells.	Cyanides	93-95	acyl-CoA oxidase 1	Homo sapiens	131-150
20887565-1	2010	We have previously reported that benzohydroxamic acid (BHAM), a potent inhibitor of cyanide (CN)-resistant respiration mediated by alternative oxidase (AOX), induces formation of unique cell masses (i.e., stalk-like cells with a large vacuole and thick cell wall) in starved Dictyostelium cells.	Cyanides	93-95	acyl-CoA oxidase 1	Homo sapiens	152-155
20630178-2	2010	The specificity of the sensor for cyanide is achieved by a reaction cascade involving two enzymes, cyanidase (EC 3.5.5.1) and formate dehydrogenase (FDH, EC 1.2.1.2).	Cyanides	34-41	aldehyde dehydrogenase 1 family member L1	Homo sapiens	126-147
20630178-2	2010	The specificity of the sensor for cyanide is achieved by a reaction cascade involving two enzymes, cyanidase (EC 3.5.5.1) and formate dehydrogenase (FDH, EC 1.2.1.2).	Cyanides	34-41	aldehyde dehydrogenase 1 family member L1	Homo sapiens	149-152
20476772-4	2010	With cyanide as a structural probe, we have investigated the thermodynamic and kinetic parameters associated with ligand and substrate binding to hIDO.	Cyanides	5-12	indoleamine 2,3-dioxygenase 1	Homo sapiens	146-150
20486105-0	2010	Cyanide-bridged [Co(II)2M(II)] and [Co(II)2M(II)2] complexes based on the [Co(II)(triphos)(CN)2] building block: syntheses, structures, magnetic properties, and density functional theoretical studies.	Cyanides	0-7	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	17-23
20539874-2	2010	SN-2 shows sensitive responses to fluoride anion and cyanide through both naked-eye detectable colour changes and ratiometric fluorescence changes.	Cyanides	53-60	solute carrier family 38 member 5	Homo sapiens	0-4
20127315-6	2010	The levels of cyanide (CN(-)), a terminal metabolite of AN, were significantly increased in the brains and livers of the AN-treated rats with increased CYP2E1 activity, compared with the levels in rats treated with AN alone, DCE + AN or acetone + DCE + AN.	Cyanides	14-21	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	152-158
20795898-0	2010	Nano-intercalated rhodanese in cyanide antagonism.	Cyanides	31-38	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	18-27
20795898-1	2010	Present studies have focused on nano-intercalated rhodanese in combination with sulfur donors to prevent cyanide lethality in a prophylactic mice model for future development of an effective cyanide antidotal system.	Cyanides	105-112	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	50-59
20795898-1	2010	Present studies have focused on nano-intercalated rhodanese in combination with sulfur donors to prevent cyanide lethality in a prophylactic mice model for future development of an effective cyanide antidotal system.	Cyanides	191-198	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	50-59
20795898-2	2010	Our approach is based on the idea of converting cyanide to the less toxic thiocyanate before it reaches the target organs by utilizing sulfurtransferases (e.g., rhodanese) and sulfur donors in a close proximity by injecting them directly into the blood stream.	Cyanides	48-55	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	161-170
20356861-6	2010	Cyanide caused marked decrease in the levels of cellular antioxidants like superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GR).	Cyanides	0-7	catalase	Rattus norvegicus	103-111
20356861-6	2010	Cyanide caused marked decrease in the levels of cellular antioxidants like superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GR).	Cyanides	0-7	catalase	Rattus norvegicus	113-116
20356861-6	2010	Cyanide caused marked decrease in the levels of cellular antioxidants like superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GR).	Cyanides	0-7	glutathione-disulfide reductase	Rattus norvegicus	153-174
20356861-6	2010	Cyanide caused marked decrease in the levels of cellular antioxidants like superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GR).	Cyanides	0-7	glutathione-disulfide reductase	Rattus norvegicus	176-178
20356861-8	2010	Cyanide-treated cells showed notable increase in caspase-3 activity and induction of apoptotic type of cell death after 24 hours.	Cyanides	0-7	caspase 3	Rattus norvegicus	49-58
20356861-9	2010	A-KG and NAC alone were very effective in restoring the levels of GSH and TAS, but together they significantly resolved the effects of cyanide on antioxidant enzymes, MDA levels, and caspase-3 activity.	Cyanides	135-142	caspase 3	Rattus norvegicus	183-192
20116365-0	2010	Reductive nitrosylation of ferric cyanide horse heart myoglobin is limited by cyanide dissociation.	Cyanides	34-41	myoglobin	Equus caballus	54-63
20447290-3	2010	In contrast with animal mitochondria, plant mitochondria possess a unique respiratory pathway, the cyanide-insensitive alternative pathway, which is catalysed by the alternative oxidase (AOX).	Cyanides	99-106	acyl-CoA oxidase 1	Homo sapiens	166-185
20447290-3	2010	In contrast with animal mitochondria, plant mitochondria possess a unique respiratory pathway, the cyanide-insensitive alternative pathway, which is catalysed by the alternative oxidase (AOX).	Cyanides	99-106	acyl-CoA oxidase 1	Homo sapiens	187-190
20404537-1	2010	The alternative oxidase (AOX) is the terminal oxidase that comprises the cyanide-resistant respiratory pathway in plant mitochondria.	Cyanides	73-80	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	4-23
20404537-1	2010	The alternative oxidase (AOX) is the terminal oxidase that comprises the cyanide-resistant respiratory pathway in plant mitochondria.	Cyanides	73-80	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	25-28
20358069-3	2010	1,4-PDI is bonded to Au by forming one Au-CN bond, with another isocyanide group being pendent with respect to the Au surface.	Cyanides	64-74	peptidyl arginine deiminase 1	Homo sapiens	4-7
20358069-5	2010	Upon attaching new Au nanoparticles onto the pendent isocyanide groups of 1,4-PDI, a Raman signal is distinctly observed.	Cyanides	53-63	peptidyl arginine deiminase 1	Homo sapiens	78-81
20116365-3	2010	The k(off) value for cyanide dissociation from ferric cyanide horse heart myoglobin (Mb(III)-cyanide) was determined at pH 9.2 and 20.0 degrees C. Mixing Mb(III)-cyanide and NO solutions brings about absorption spectral changes reflecting the disappearance of Mb(III)-cyanide with the concomitant formation of ferrous nitrosylated Mb.	Cyanides	21-28	myoglobin	Equus caballus	74-83
19921330-5	2010	Some proteins related with regulation of nitrogen assimilation pathways (glutamine synthetase), oxidative stress repairing (catalase), and protection (neutral trehalase and glycosyltransferase) could improve the effectiveness of cyanide biodegradation.	Cyanides	229-236	glutamate--ammonia ligase	Klebsiella oxytoca	73-93
20000485-0	2010	Cyanide lability and linkage isomerism of hexacyanochromate(III) induced by the Co(II) ion.	Cyanides	0-7	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	80-86
20092265-1	2010	A Co(II)-salen based fluorescent sensor (1.Co) that can selectively recognize cyanide anions in 1:2 binding stoichiometry over other anions has been developed.	Cyanides	78-85	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	2-8
20000485-6	2010	Results obtained by a combination of X-ray crystallography, infrared spectroscopy, and magnetometry provide unequivocal evidence that the presence of certain Lewis acids (e.g., Co(II) in this work and Fe(II) ions and BPh(3) in previously reported studies) promote the process of cyanide linkage isomerism, which, in the case of Co(II) species, leads to facile labilization of cyanide ligands from the [Cr(CN)(6)](3-) anion.	Cyanides	279-286	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	177-183
20000485-6	2010	Results obtained by a combination of X-ray crystallography, infrared spectroscopy, and magnetometry provide unequivocal evidence that the presence of certain Lewis acids (e.g., Co(II) in this work and Fe(II) ions and BPh(3) in previously reported studies) promote the process of cyanide linkage isomerism, which, in the case of Co(II) species, leads to facile labilization of cyanide ligands from the [Cr(CN)(6)](3-) anion.	Cyanides	376-383	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	177-183
19643077-4	2010	Namely, AcoAOX1a, an abundantly expressed transcript in vivo, shows an apparent cyanide-insensitive and n-propyl gallate-sensitive respiration during ectopic expression of the protein in HeLa cells, whereas AcoAOX1b exhibits a lower transcript expression, and appears to be totally inactive as AOX at the protein level.	Cyanides	80-87	acyl-CoA oxidase 1	Homo sapiens	11-14
19367471-1	2010	(1R,2R,3S,4R)-2-Amino-6,6-dimethylbicyclo[3.1.1]heptane-3-carboxylic acid 1 was reacted with three aldehydes and two isocyanides in methanol, in water, and under solvent-free conditions to prepare enantiomeric beta-lactams via U-4C-3CRs.	Cyanides	117-128	mediator complex subunit 25	Homo sapiens	69-75
19841471-0	2010	Cyanide-induced apoptosis of dopaminergic cells is promoted by BNIP3 and Bax modulation of endoplasmic reticulum-mitochondrial Ca2+ levels.	Cyanides	0-7	BCL2/adenovirus E1B interacting protein 3	Mus musculus	63-68
19958137-5	2010	Salicylhydroxamic acid (SHAM, an AOX inhibitor) pretreatment reduced the DEA/NO-induced cyanide-resistant respiration and partially compromised induced resistance to TMV.	Cyanides	88-95	acyl-CoA oxidase 1	Homo sapiens	33-36
20161157-0	2009	Thio-mediated synthesis of derivatized N-linked glycopeptides using isonitrile chemistry.	Cyanides	68-78	acetyl-CoA acyltransferase 1	Homo sapiens	0-4
19841471-0	2010	Cyanide-induced apoptosis of dopaminergic cells is promoted by BNIP3 and Bax modulation of endoplasmic reticulum-mitochondrial Ca2+ levels.	Cyanides	0-7	BCL2-associated X protein	Mus musculus	73-76
19841471-2	2010	In this study involvement of Bcl-2/adenovirus E1B 19-kDa interacting protein 3 (BNIP3), a BH3-only Bcl-2 protein, in cyanide-induced death of dopaminergic cells was determined in mice and Mes 23.5 cells.	Cyanides	117-124	B cell leukemia/lymphoma 2	Mus musculus	29-78
19841471-2	2010	In this study involvement of Bcl-2/adenovirus E1B 19-kDa interacting protein 3 (BNIP3), a BH3-only Bcl-2 protein, in cyanide-induced death of dopaminergic cells was determined in mice and Mes 23.5 cells.	Cyanides	117-124	BCL2/adenovirus E1B interacting protein 3	Mus musculus	80-85
19841471-2	2010	In this study involvement of Bcl-2/adenovirus E1B 19-kDa interacting protein 3 (BNIP3), a BH3-only Bcl-2 protein, in cyanide-induced death of dopaminergic cells was determined in mice and Mes 23.5 cells.	Cyanides	117-124	B cell leukemia/lymphoma 2	Mus musculus	29-34
19841471-3	2010	Treatment of mice with cyanide up-regulated BNIP3 and Bax expression in tyrosine hydroxylase (TH)-positive cells of the substantia nigra, and progressive loss of TH-positive neurons was observed over a 9-day period.	Cyanides	23-30	BCL2/adenovirus E1B interacting protein 3	Mus musculus	44-49
19841471-3	2010	Treatment of mice with cyanide up-regulated BNIP3 and Bax expression in tyrosine hydroxylase (TH)-positive cells of the substantia nigra, and progressive loss of TH-positive neurons was observed over a 9-day period.	Cyanides	23-30	BCL2-associated X protein	Mus musculus	54-57
19841471-4	2010	In Mes 23.5 dopaminergic cells, cyanide stimulated translocalization of BNIP3 to both endoplasmic reticulum (ER) and mitochondria.	Cyanides	32-39	BCL2/adenovirus E1B interacting protein 3	Mus musculus	72-77
19841471-6	2010	Cyanide also activated Bax to colocalize with BNIP3 in ER and mitochondria.	Cyanides	0-7	BCL2-associated X protein	Mus musculus	23-26
19841471-6	2010	Cyanide also activated Bax to colocalize with BNIP3 in ER and mitochondria.	Cyanides	0-7	BCL2/adenovirus E1B interacting protein 3	Mus musculus	46-51
19841471-8	2010	Knockdown of Bax expression by small interfering RNA blocked the BNIP3-mediated changes in ER and mitochondrial Ca(2+) to block cyanide-induced mitochondrial dysfunction and cell death.	Cyanides	128-135	BCL2-associated X protein	Mus musculus	13-16
19841471-8	2010	Knockdown of Bax expression by small interfering RNA blocked the BNIP3-mediated changes in ER and mitochondrial Ca(2+) to block cyanide-induced mitochondrial dysfunction and cell death.	Cyanides	128-135	BCL2/adenovirus E1B interacting protein 3	Mus musculus	65-70
19841471-9	2010	These findings show that BNIP3-mediates cyanide-induced dopaminergic cell death through a Bax downstream signal that mobilizes ER Ca(2+) stores, followed by mitochondrial Ca(2+) overload.	Cyanides	40-47	BCL2/adenovirus E1B interacting protein 3	Mus musculus	25-30
19841471-9	2010	These findings show that BNIP3-mediates cyanide-induced dopaminergic cell death through a Bax downstream signal that mobilizes ER Ca(2+) stores, followed by mitochondrial Ca(2+) overload.	Cyanides	40-47	BCL2-associated X protein	Mus musculus	90-93
19825401-0	2009	Lactoperoxidase catalyzes in vitro activation of acrylonitrile to cyanide.	Cyanides	66-73	lactoperoxidase	Homo sapiens	0-15
19825401-3	2009	The present study aimed at investigating the ability of LPO enzyme system to oxidize ACN to cyanide (CN(-)) in vitro.	Cyanides	92-99	lactoperoxidase	Homo sapiens	56-59
19493305-4	2009	We previously expressed the C. intestinalis AOX in human embryonic kidney (HEK 293-T-derived) cells conferring cyanide-resistance to cell respiration without any detectable detrimental effect (Hakkaart et al.	Cyanides	111-118	acyl-CoA oxidase 1	Homo sapiens	44-47
19719482-1	2009	In addition to the conventional cytochrome c oxidase, mitochondria of all plants studied to date contain a second cyanide-resistant terminal oxidase or alternative oxidase (AOX).	Cyanides	114-121	acyl-CoA oxidase 1	Homo sapiens	152-171
19719482-1	2009	In addition to the conventional cytochrome c oxidase, mitochondria of all plants studied to date contain a second cyanide-resistant terminal oxidase or alternative oxidase (AOX).	Cyanides	114-121	acyl-CoA oxidase 1	Homo sapiens	173-176
19859612-7	2009	This fact is in good agreement with the much larger Cr(III)-Fe(II) (t(2g)-t(2g)) coupling through cyanide bridging ligands expected for these complexes.	Cyanides	98-105	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	55-58
19694439-4	2009	In this study, we have examined the equilibrium binding of three isocyanides, isopropyl, n-butyl, and benzyl, to the two major human HO isoforms (hHO-1 and hHO-2), Candida albicans HO (CaHmx1), and human cytochrome P450 CYP3A4 using electronic absorption spectroscopy.	Cyanides	65-76	heme oxygenase 1	Homo sapiens	146-151
19694439-4	2009	In this study, we have examined the equilibrium binding of three isocyanides, isopropyl, n-butyl, and benzyl, to the two major human HO isoforms (hHO-1 and hHO-2), Candida albicans HO (CaHmx1), and human cytochrome P450 CYP3A4 using electronic absorption spectroscopy.	Cyanides	65-76	heme oxygenase 2	Homo sapiens	156-161
19694439-7	2009	Because the dissociation constants (KD) of the ligands for ferrous heme-hHO-1 were below the limit of accuracy for equilibrium titrations, stopped-flow kinetic experiments were used to measure the binding parameters of the isocyanides to ferrous hHO-1.	Cyanides	223-234	heme oxygenase 1	Homo sapiens	72-77
19694439-7	2009	Because the dissociation constants (KD) of the ligands for ferrous heme-hHO-1 were below the limit of accuracy for equilibrium titrations, stopped-flow kinetic experiments were used to measure the binding parameters of the isocyanides to ferrous hHO-1.	Cyanides	223-234	heme oxygenase 1	Homo sapiens	246-251
19653646-5	2009	As demonstrated by both (1)H NMR and FTIR spectroscopic studies, addition of a third equivalent of CNAr(Dipp2) to [(THF)(2)Cu(CNAr(Dipp2))(2)]OTf in C(6)D(6) solution results in slow isocyanide exchange.	Cyanides	183-193	nudix hydrolase 4	Homo sapiens	104-109
19653646-6	2009	However, rapid isocyanide exchange is observed when an additional equivalent of CNAr(Dipp2) is added to (TfO)Ag(CNAr(Dipp2))(2).	Cyanides	15-25	nudix hydrolase 4	Homo sapiens	85-90
19653646-6	2009	However, rapid isocyanide exchange is observed when an additional equivalent of CNAr(Dipp2) is added to (TfO)Ag(CNAr(Dipp2))(2).	Cyanides	15-25	nudix hydrolase 4	Homo sapiens	117-122
19545938-0	2009	Kinetics of cyanide binding as a probe of local stability/flexibility of cytochrome c.	Cyanides	12-19	cytochrome c, somatic	Equus caballus	73-85
19705807-1	2009	The chief sources of cyanide (CN(-)) in humans are tobacco and occupationally derived smoke, inflammation [vis-a-vis myeloperoxidase (MPO)-induced chlorination of glycine], and microbial cyanogenesis (including Pseudomonas aeruginosa infection of the cystic fibrosis lung).	Cyanides	21-28	myeloperoxidase	Homo sapiens	134-137
19625201-0	2009	A partial exploration of the potential energy surfaces of SCN and HSCN: implications for the enzyme-mediated detoxification of cyanide.	Cyanides	127-134	sorcin	Homo sapiens	58-61
19625201-4	2009	The potential energy surface for the conversion of cyanide anion to thiocyanate shows that the formation of thiocyanate (SCN) is vastly preferred to formation of its isomer SNC.	Cyanides	51-64	sorcin	Homo sapiens	121-124
19125696-1	2009	Mitochondrial AOX (alternative oxidase) is the terminal oxidase of the CN (cyanide)-resistant alternative respiratory pathway in plants.	Cyanides	75-82	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	14-17
19630396-2	2009	Variable temperature (1)H NMR and FTIR studies on Pd(CNAr(Dipp2))(2) in the presence of added CNAr(Dipp2) revealed that free and coordinated isocyanide undergo rapid exchange, but the components do not form a stable tris-isocyanide complex.	Cyanides	141-151	nudix hydrolase 4	Homo sapiens	58-63
19630396-2	2009	Variable temperature (1)H NMR and FTIR studies on Pd(CNAr(Dipp2))(2) in the presence of added CNAr(Dipp2) revealed that free and coordinated isocyanide undergo rapid exchange, but the components do not form a stable tris-isocyanide complex.	Cyanides	141-151	nudix hydrolase 4	Homo sapiens	99-104
19648408-1	2009	Alternative oxidase (AOX), a ubiquinol oxidase, introduces a branch point into the respiratory electron transport chain, bypassing complexes III and IV and resulting in cyanide-resistant respiration.	Cyanides	169-176	acyl-CoA oxidase 1	Homo sapiens	0-19
19648408-1	2009	Alternative oxidase (AOX), a ubiquinol oxidase, introduces a branch point into the respiratory electron transport chain, bypassing complexes III and IV and resulting in cyanide-resistant respiration.	Cyanides	169-176	acyl-CoA oxidase 1	Homo sapiens	21-24
19125696-1	2009	Mitochondrial AOX (alternative oxidase) is the terminal oxidase of the CN (cyanide)-resistant alternative respiratory pathway in plants.	Cyanides	75-82	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	19-38
19375411-1	2009	Oxygen consumption by alternative oxidase (AOX), present in mitochondria of many angiosperms, is known to be cyanide-resistant in contrast to cytochrome oxidase.	Cyanides	109-116	ubiquinol oxidase 1, mitochondrial-like	Solanum tuberosum	22-41
19549895-7	2009	In complementary studies, suppression of ABCB6 expression sensitized cells to stress induced by peroxide and cyanide, whereas overexpression of ABCB6 protected against both stressors.	Cyanides	109-116	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	41-46
19361538-0	2009	Cyanide-induced death of dopaminergic cells is mediated by uncoupling protein-2 up-regulation and reduced Bcl-2 expression.	Cyanides	0-7	uncoupling protein 2	Rattus norvegicus	59-79
19361538-0	2009	Cyanide-induced death of dopaminergic cells is mediated by uncoupling protein-2 up-regulation and reduced Bcl-2 expression.	Cyanides	0-7	BCL2, apoptosis regulator	Rattus norvegicus	106-111
19361538-2	2009	Cyanide toxicity is enhanced when mitochondrial uncoupling is stimulated following up-regulation of uncoupling protein-2 (UCP-2).	Cyanides	0-7	uncoupling protein 2	Rattus norvegicus	100-120
19361538-2	2009	Cyanide toxicity is enhanced when mitochondrial uncoupling is stimulated following up-regulation of uncoupling protein-2 (UCP-2).	Cyanides	0-7	uncoupling protein 2	Rattus norvegicus	122-127
19361538-3	2009	In this study, the role of a pro-survival protein, Bcl-2, in cyanide-mediated cell death was determined in a rat dopaminergic immortalized mesencephalic cell line (N27 cells).	Cyanides	61-68	BCL2, apoptosis regulator	Rattus norvegicus	51-56
19361538-4	2009	Following pharmacological up-regulation of UCP-2 by treatment with Wy14,643, cyanide reduced cellular Bcl-2 expression by increasing proteasomal degradation of the protein.	Cyanides	77-84	uncoupling protein 2	Rattus norvegicus	43-48
19361538-4	2009	Following pharmacological up-regulation of UCP-2 by treatment with Wy14,643, cyanide reduced cellular Bcl-2 expression by increasing proteasomal degradation of the protein.	Cyanides	77-84	BCL2, apoptosis regulator	Rattus norvegicus	102-107
19361538-7	2009	Repletion of mtGSH by loading cells with glutathione ethyl ester reduced H2O2 generation and in turn blocked the cyanide-induced decrease of Bcl-2.	Cyanides	113-120	BCL2, apoptosis regulator	Rattus norvegicus	141-146
19361538-9	2009	The RNAi decreased cyanide-induced depletion of mtGSH, reduced H2O2 accumulation, and inhibited down-regulation of Bcl-2, thus blocking cell death.	Cyanides	19-26	BCL2, apoptosis regulator	Rattus norvegicus	115-120
19361538-10	2009	To confirm the role of Bcl-2 down-regulation in the cell death, it was shown that over-expression of Bcl-2 by cDNA transfection attenuated the enhancement of cyanide toxicity after UCP-2 up-regulation.	Cyanides	158-165	BCL2, apoptosis regulator	Rattus norvegicus	101-106
19361538-10	2009	To confirm the role of Bcl-2 down-regulation in the cell death, it was shown that over-expression of Bcl-2 by cDNA transfection attenuated the enhancement of cyanide toxicity after UCP-2 up-regulation.	Cyanides	158-165	uncoupling protein 2	Rattus norvegicus	181-186
19361538-11	2009	It was concluded that UCP-2 up-regulation sensitizes cells to cyanide by increasing cellular oxidative stress, leading to an increase of Bcl-2 degradation.	Cyanides	62-69	uncoupling protein 2	Rattus norvegicus	22-27
19361538-11	2009	It was concluded that UCP-2 up-regulation sensitizes cells to cyanide by increasing cellular oxidative stress, leading to an increase of Bcl-2 degradation.	Cyanides	62-69	BCL2, apoptosis regulator	Rattus norvegicus	137-142
19361538-12	2009	Then the reduced Bcl-2 levels sensitize the cells to cyanide-mediated cell death.	Cyanides	53-60	BCL2, apoptosis regulator	Rattus norvegicus	17-22
19375411-1	2009	Oxygen consumption by alternative oxidase (AOX), present in mitochondria of many angiosperms, is known to be cyanide-resistant in contrast to cytochrome oxidase.	Cyanides	109-116	ubiquinol oxidase 1, mitochondrial-like	Solanum tuberosum	43-46
18980314-3	2009	It was proposed that double insertion of isocyanide into the Zr-C bond of 1-zirconacyclopent-3-ynes takes place via the isocyanide adduct of the eta2-pi-complex as an intermediate.	Cyanides	120-130	DNA polymerase iota	Homo sapiens	145-149
19416715-5	2009	However, mitochondrial suspensions from AOX-expressing flies exhibited a significant cyanide-resistant substrate oxidation, and the flies were partially resistant to both cyanide and antimycin.	Cyanides	85-92	Aldox89A	Drosophila melanogaster	40-43
19416715-5	2009	However, mitochondrial suspensions from AOX-expressing flies exhibited a significant cyanide-resistant substrate oxidation, and the flies were partially resistant to both cyanide and antimycin.	Cyanides	171-178	Aldox89A	Drosophila melanogaster	40-43
19320480-1	2009	The addition of isocyanides to acyl chlorides (Isocyanide-Nef reaction) leads to imidoyl chlorides which can later be treated with trialkylphosphites to afford new keteneimines in a Perkow-type reaction.	Cyanides	16-27	S100 calcium binding protein B	Homo sapiens	58-61
19320480-1	2009	The addition of isocyanides to acyl chlorides (Isocyanide-Nef reaction) leads to imidoyl chlorides which can later be treated with trialkylphosphites to afford new keteneimines in a Perkow-type reaction.	Cyanides	47-57	S100 calcium binding protein B	Homo sapiens	58-61
19249870-1	2009	Four cyanide-linked Fe(III)-Mn(III) complexes were prepared by reacting Mn Schiff bases with a new molecular precursor (PPh(4))[Fe(qcq)(CN)(3)] [1; qcq = 8-(2-quinolinecarboxamido)quinoline anion].	Cyanides	5-12	potassium two pore domain channel subfamily K member 3	Homo sapiens	120-126
20049701-4	2009	Here, we have tested whether the expression of a mitochondrially targeted, cyanide-resistant, alternative oxidase (AOX) from Ciona intestinalis could alleviate the metabolic abnormalities of COX-deficient human cells either from a patient harbouring a COX15 pathological mutation or rendered deficient by silencing the COX10 gene using shRNA.	Cyanides	75-82	acyl-CoA oxidase 1	Homo sapiens	94-113
20049701-4	2009	Here, we have tested whether the expression of a mitochondrially targeted, cyanide-resistant, alternative oxidase (AOX) from Ciona intestinalis could alleviate the metabolic abnormalities of COX-deficient human cells either from a patient harbouring a COX15 pathological mutation or rendered deficient by silencing the COX10 gene using shRNA.	Cyanides	75-82	acyl-CoA oxidase 1	Homo sapiens	115-118
20049701-4	2009	Here, we have tested whether the expression of a mitochondrially targeted, cyanide-resistant, alternative oxidase (AOX) from Ciona intestinalis could alleviate the metabolic abnormalities of COX-deficient human cells either from a patient harbouring a COX15 pathological mutation or rendered deficient by silencing the COX10 gene using shRNA.	Cyanides	75-82	cytochrome c oxidase subunit 8A	Homo sapiens	191-194
20049701-4	2009	Here, we have tested whether the expression of a mitochondrially targeted, cyanide-resistant, alternative oxidase (AOX) from Ciona intestinalis could alleviate the metabolic abnormalities of COX-deficient human cells either from a patient harbouring a COX15 pathological mutation or rendered deficient by silencing the COX10 gene using shRNA.	Cyanides	75-82	cytochrome c oxidase assembly homolog COX15	Homo sapiens	252-257
20049701-4	2009	Here, we have tested whether the expression of a mitochondrially targeted, cyanide-resistant, alternative oxidase (AOX) from Ciona intestinalis could alleviate the metabolic abnormalities of COX-deficient human cells either from a patient harbouring a COX15 pathological mutation or rendered deficient by silencing the COX10 gene using shRNA.	Cyanides	75-82	cytochrome c oxidase assembly factor heme A:farnesyltransferase COX10	Homo sapiens	319-324
19567706-8	2009	Surprisingly, yeast-expressed CYP71B15 also catalyzed thiazoline ring closure, DHCA formation, and cyanide release with Cys(IAN) as substrate.	Cyanides	99-106	Cytochrome P450 superfamily protein	Arabidopsis thaliana	30-38
19161297-1	2009	Substitution of Co(III)-bound water by cyanide allows the rapid colorimetric detection of micromolar amounts of cyanide with cobalt corrinoids.	Cyanides	112-119	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	16-22
19128966-3	2009	Many simple inorganic anions (thiocyanate, cyanide, azide, bicarbonate, hydrogen sulfide, bisulfite and sulfate) showed low micromolar inhibition constants against mCA XV (K(I)s of 8.2-10.1 microM), whereas they acted as much weaker (usually millimolar) inhibitors of other isoforms.	Cyanides	43-50	carbonic anhydrase 15	Mus musculus	164-170
18990727-12	2009	We conclude that CYP2E1-mediated metabolism of allylnitrile leads to cyanide release and acute mortality, probably through alpha-carbon hydroxylation, and hypothesize that epoxidation of the beta-gamma double bond by CYP2A5 mediates vestibular toxicity.	Cyanides	69-76	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	17-23
19173523-11	2009	The quadrupole constant for the (67)Zn nucleus in H(67)ZnCN is unusually large relative to that in (67)ZnF (-104.578 versus -60 MHz), evidence that the bonding in the cyanide has more covalent character than in the fluoride.	Cyanides	167-174	zinc finger protein 763	Homo sapiens	103-106
19108635-0	2009	EPR evidence of cyanide binding to the Mn(Mg) center of cytochrome c oxidase: support for Cu(A)-Mg involvement in proton pumping.	Cyanides	16-23	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	56-76
19108635-10	2009	Cyanide addition affected the Mn(II) CW-EPR spectrum of reduced cytochrome c oxidase by increasing Mn(II) zero field splitting and broadening the spectral line shapes but had no effect on oxidized enzyme.	Cyanides	0-7	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	64-84
19108635-11	2009	ESEEM measurements support a differential ability of Mn(II) to bind cyanide in the reduced state of cytochrome c oxidase.	Cyanides	68-75	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	100-120
19059403-1	2009	Alternative oxidase (AOX) plays a pivotal role in cyanide-resistance respiration in the mitochondria of plants, fungi and some protists.	Cyanides	50-57	acyl-CoA oxidase 1	Homo sapiens	0-19
19059403-1	2009	Alternative oxidase (AOX) plays a pivotal role in cyanide-resistance respiration in the mitochondria of plants, fungi and some protists.	Cyanides	50-57	acyl-CoA oxidase 1	Homo sapiens	21-24
19059403-2	2009	Here we show that AOX from thermogenic skunk cabbage successfully conferred cyanide resistance to human cells.	Cyanides	76-83	acyl-CoA oxidase 1	Homo sapiens	18-21
19538024-4	2009	Cyanide significantly reduced the activity of glutathione peroxidase (GPx), glutathione reductase (GR), superoxide dismutase (SOD), and catalase (CA) in all the organs after 7 days, while the activity of GPx in brain, liver, and kidney, GR in liver, and CA in brain remained diminished up to 14 days.	Cyanides	0-7	glutathione-disulfide reductase	Rattus norvegicus	76-97
19538024-4	2009	Cyanide significantly reduced the activity of glutathione peroxidase (GPx), glutathione reductase (GR), superoxide dismutase (SOD), and catalase (CA) in all the organs after 7 days, while the activity of GPx in brain, liver, and kidney, GR in liver, and CA in brain remained diminished up to 14 days.	Cyanides	0-7	glutathione-disulfide reductase	Rattus norvegicus	99-101
19538024-4	2009	Cyanide significantly reduced the activity of glutathione peroxidase (GPx), glutathione reductase (GR), superoxide dismutase (SOD), and catalase (CA) in all the organs after 7 days, while the activity of GPx in brain, liver, and kidney, GR in liver, and CA in brain remained diminished up to 14 days.	Cyanides	0-7	catalase	Rattus norvegicus	136-144
19538024-4	2009	Cyanide significantly reduced the activity of glutathione peroxidase (GPx), glutathione reductase (GR), superoxide dismutase (SOD), and catalase (CA) in all the organs after 7 days, while the activity of GPx in brain, liver, and kidney, GR in liver, and CA in brain remained diminished up to 14 days.	Cyanides	0-7	catalase	Rattus norvegicus	146-148
19538024-7	2009	Cyanide also increased the expression of HSP-70 activity in brain after 7 days alone.	Cyanides	0-7	heat shock protein family A (Hsp70) member 1B	Rattus norvegicus	41-47
18062945-2	2008	Exo-1,2-O-cyanoalkylidene derivatives formed by neighboring group participation and attack of cyanide underwent, after Lewis-acid mediated isomerization to the endo-isomer, intramolecular azide-cyanide cycloaddition leading to the formation of tetrazoles embedded in bridged tetracyclic ring systems.	Cyanides	94-101	exonuclease 1	Homo sapiens	0-5
19650716-7	2009	The potential for serious toxicity limits or prevents the use of the Cyanide Antidote Kit, dicobalt edetate, and 4-dimethylaminophenol in prehospital empiric treatment of suspected cyanide poisoning.	Cyanides	69-76	KIT proto-oncogene, receptor tyrosine kinase	Homo sapiens	86-89
19650716-7	2009	The potential for serious toxicity limits or prevents the use of the Cyanide Antidote Kit, dicobalt edetate, and 4-dimethylaminophenol in prehospital empiric treatment of suspected cyanide poisoning.	Cyanides	181-188	KIT proto-oncogene, receptor tyrosine kinase	Homo sapiens	86-89
21305121-6	2009	The EPR data of the cyanide-ligated ferric DmHb1* indicates a close similarity with cyanide-ligated ferric myoglobin.	Cyanides	20-27	globin 1	Drosophila melanogaster	43-48
21305121-6	2009	The EPR data of the cyanide-ligated ferric DmHb1* indicates a close similarity with cyanide-ligated ferric myoglobin.	Cyanides	84-91	globin 1	Drosophila melanogaster	43-48
18786181-4	2009	We reveal that pinA is a NIT4-type nitrilase that catalyses the hydrolysis of beta-cyano-L-alanine, a nitrile common in the plant environment and an intermediate in the cyanide detoxification pathway in plants.	Cyanides	169-176	nitrilase 4	Arabidopsis thaliana	25-29
18786181-5	2009	In plants cyanide is converted to beta-cyano-L-alanine, which is subsequently detoxified to aspartic acid and ammonia by NIT4.	Cyanides	10-17	nitrilase 4	Arabidopsis thaliana	121-125
18775958-3	2008	Coordination of cyanide to the met heme formed low-spin complexes.	Cyanides	16-23	spindlin 1	Homo sapiens	51-55
18985259-1	2008	The low temperature (approximately 5 K) X-band ESR spectra are reported of the cyanide-bridged mixed-valence complexes [(OC)5Cr(mu-CN)M(NH3)5]X2 (M = Ru, Os; X = PF6(-)) in frozen matrices formed from nitromethane, acetonitrile and dimethylformamide with toluene.	Cyanides	79-86	sperm associated antigen 17	Homo sapiens	162-165
18800354-1	2008	The activities of glycogen phosphorylase and synthase during infusions of glucagon, isoproterenol, or cyanide in isolated liver of fed rats submitted to short-term insulin-induced hypoglycemia (IIH) was investigated.	Cyanides	102-109	glycogen phosphorylase L	Rattus norvegicus	18-40
18980314-3	2009	It was proposed that double insertion of isocyanide into the Zr-C bond of 1-zirconacyclopent-3-ynes takes place via the isocyanide adduct of the eta2-pi-complex as an intermediate.	Cyanides	41-51	DNA polymerase iota	Homo sapiens	145-149
18950152-6	2008	For 5, only the fluorescence and phosphorescence bands of the PCP-NC ligand are observed [since the A-frame XPd(mu-dppm)2(mu-L)PdX (L ) isocyanide, X ) halide) is not luminescent], stressing that the NtC bridge exhibits modest electronic communication properties.	Cyanides	136-146	ERCC excision repair 2, TFIIH core complex helicase subunit	Homo sapiens	108-111
18779575-1	2008	The mystery of how the cyanide group in vitamin B(12) or cyanocobalamin, discovered 60 years ago, is removed, has been solved by the demonstration that the trafficking chaperone, MMACHC, catalyzes a reductive decyanation reaction.	Cyanides	23-30	metabolism of cobalamin associated C	Homo sapiens	179-185
18779575-4	2008	Defects in MMACHC represent the most common cause of inborn errors of B(12) metabolism, and our results explain the observation that fibroblasts from these patients are poorly responsive to vitamin B(12) but show some metabolic correction with aquocobalamin, a cofactor form lacking the cyanide ligand, which is mirrored by patients showing poorer clinical responsiveness to cyano- versus aquocobalamin.	Cyanides	287-294	metabolism of cobalamin associated C	Homo sapiens	11-17
18590329-1	2008	Spin-crossover coordination nanoparticles of the cyanide-bridged three-dimensional network Fe(pyrazine){Pt(CN) 4} were prepared at three different sizes using a microemulsion.	Cyanides	49-56	spindlin 1	Homo sapiens	0-4
18538917-0	2008	Solution 1H NMR study of the active site structure for the double mutant H64Q/V68F cyanide complex from mouse neuroglobin.	Cyanides	83-90	neuroglobin	Mus musculus	110-121
18507803-1	2008	Alternative oxidase (AOX) catalyses the ATP-uncoupling cyanide (CN)-resistant pathway.	Cyanides	55-62	alternative oxidase 2	Arabidopsis thaliana	21-24
18507803-1	2008	Alternative oxidase (AOX) catalyses the ATP-uncoupling cyanide (CN)-resistant pathway.	Cyanides	64-66	alternative oxidase 2	Arabidopsis thaliana	0-19
18507803-1	2008	Alternative oxidase (AOX) catalyses the ATP-uncoupling cyanide (CN)-resistant pathway.	Cyanides	64-66	alternative oxidase 2	Arabidopsis thaliana	21-24
18605554-7	2008	The formation of surface cyanide complexes with Ag and Au ions could be responsible for the fast removal of HCN from the gas phase and its further photooxidation in the case of using TiO2 with deposited Au and Ag.	Cyanides	25-32	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	108-111
18507803-1	2008	Alternative oxidase (AOX) catalyses the ATP-uncoupling cyanide (CN)-resistant pathway.	Cyanides	55-62	alternative oxidase 2	Arabidopsis thaliana	0-19
20201261-3	2008	The Pgp glycoprotein overexpression in the case of the MDR positive tumoral cells will determine both the chemotherapic drug and the isonitrile radiotracer quickly efflux from the cell.	Cyanides	133-143	phosphoglycolate phosphatase	Homo sapiens	4-7
18584368-1	2008	INTRODUCTION: Cyanide-poisoned patients often require pulse oximetry and co-oximetry to measure oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and methemoglobin.	Cyanides	14-21	hemoglobin subunit gamma 2	Homo sapiens	151-164
18419719-11	2008	Cyanide induced increases in dialysate myoglobin levels.	Cyanides	0-7	LOW QUALITY PROTEIN: myoglobin	Oryctolagus cuniculus	39-48
18469476-3	2008	In a single-line FIA system, the cyanide was allowed to react with AgX SPR, which in turn changed Ag ions in AgX to silver cyanide complexes in a sodium hydroxide carrier stream.	Cyanides	33-40	UDP-N-acetylglucosamine pyrophosphorylase 1	Homo sapiens	67-70
18469476-3	2008	In a single-line FIA system, the cyanide was allowed to react with AgX SPR, which in turn changed Ag ions in AgX to silver cyanide complexes in a sodium hydroxide carrier stream.	Cyanides	33-40	UDP-N-acetylglucosamine pyrophosphorylase 1	Homo sapiens	109-112
17551834-3	2008	In the presence of cyanide, rhodanese shifted the major mucosal metabolite of sulfide from thiosulfate to thiocyanate.	Cyanides	19-26	thiosulfate sulfurtransferase	Rattus norvegicus	28-37
18491921-4	2008	We demonstrate that the C-terminal domain of Uba4, like MOCS3, has rhodanese activity and is able to transfer the sulfur from thiosulfate to cyanide in vitro.	Cyanides	141-148	molybdenum cofactor synthesis 3	Homo sapiens	45-49
18491921-4	2008	We demonstrate that the C-terminal domain of Uba4, like MOCS3, has rhodanese activity and is able to transfer the sulfur from thiosulfate to cyanide in vitro.	Cyanides	141-148	molybdenum cofactor synthesis 3	Homo sapiens	56-61
18258600-7	2008	Furthermore, cyanide-treated ABA3 C terminus was shown to release thiocyanate, indicating that the molybdenum cofactor bound to the C-terminal domain is present in the sulfurated form.	Cyanides	13-20	molybdenum cofactor sulfurase (LOS5) (ABA3)	Arabidopsis thaliana	29-33
18296449-1	2008	Mitochondrial alternative oxidase (AOX), the unique respiratory terminal oxidase in plants, catalyzes the energy-wasteful cyanide (CN)-resistant respiration.	Cyanides	122-129	alternative oxidase 2	Arabidopsis thaliana	14-33
18296449-1	2008	Mitochondrial alternative oxidase (AOX), the unique respiratory terminal oxidase in plants, catalyzes the energy-wasteful cyanide (CN)-resistant respiration.	Cyanides	122-129	alternative oxidase 2	Arabidopsis thaliana	35-38
18237121-1	2008	Isocyanide [AuX(CNPy-2)] (X = Cl, C6F5, fluoromesityl, 1/2 octafluorobiphenyl) and carbene [AuX{C(NR1R2)(NHPy-2)}] (R1R2NH = primary or secondary amines or 1/2 primary diamine) gold(I) complexes have been synthesized and characterized.	Cyanides	0-10	canopy FGF signaling regulator 2	Homo sapiens	16-22
18060564-2	2008	These Pt(II) precursors coordinated directly to the Co(III)-bound cyanide, giving the conjugates [(Co)-CN-(trans-PtCl(NH3)2)]+ (5), [(Co)-CN-(trans-PtCl2(NH3))] (6), [(Co)-CN-(cis-PtCl2(NH3))] (7) and [(Co)-CN-(PtCl3)](-) (8) in good yields.	Cyanides	66-73	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	52-59
18163630-5	2008	Similar close C-N interactions are observed in the crystal structure of the more sterically demanding isocyanide adduct, [Ni(CNCy)(PCy2NBz2)2]2(BF4)2, 4.	Cyanides	102-112	forkhead box G1	Homo sapiens	144-152
18688420-2	2008	In the "4 + 1" approach the technetium(iii) is stabilized by a monodentate isocyanide bearing a quinazoline fragment (L1,L2 ) and by the tetradentate tripodal ligand tris(2-mercaptoethyl)-amine (NS3).	Cyanides	75-85	L1 cell adhesion molecule	Homo sapiens	118-123
18183618-0	2008	1Alpha,25-dihydroxyvitamin D3 attenuates cyanide-induced neurotoxicity by inhibiting uncoupling protein-2 up-regulation.	Cyanides	41-48	uncoupling protein 2	Homo sapiens	85-105
18183618-2	2008	The mechanism of the neuroprotection was studied in rat primary cortical cells in which Wy14,643, an agonist of peroxisome proliferator activated receptor-alpha (PPARalpha), enhances cyanide (KCN) neurotoxicity.	Cyanides	183-190	peroxisome proliferator activated receptor alpha	Rattus norvegicus	162-171
18345627-3	2008	In solution, the structure of metacyclophane 3 is mobile but can be locked in a rectangular gauche- anti- gauche- anti conformation by coordination of the isocyanide substituents to the [W(CO) 5] units to give [M] 4(mu 4-eta (1):eta (1):eta (1):eta (1)- 3) ( 5).	Cyanides	155-165	secreted phosphoprotein 1	Homo sapiens	245-255
18336024-3	2008	Each key step of the catalytic loop (Scheme 1) can be disrupted by excess cyanide, including ArX oxidative addition, X/CN exchange, and ArCN reductive elimination.	Cyanides	74-81	aristaless related homeobox	Homo sapiens	93-96
17997247-1	2008	Rhodanese (thiosulfate sulfurtransferase) is a ubiquitous enzyme that accelerates the transformation of cyanide into the very less toxic thiocyante.	Cyanides	104-111	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	0-9
17997247-1	2008	Rhodanese (thiosulfate sulfurtransferase) is a ubiquitous enzyme that accelerates the transformation of cyanide into the very less toxic thiocyante.	Cyanides	104-111	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	11-40
17997247-2	2008	Influence of cerebral rhodanese level on cyanide toxicity has already been shown in mice.	Cyanides	41-48	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	22-31
17997247-18	2008	The main findings of this study indicated that the increased sensitivity to cyanide, generally reported in old mice, may be due in part to a decrease in the activity of brain rhodanese.	Cyanides	76-83	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	175-184
17728063-3	2008	In the Brazilian Mint, bleed streams are treated with sodium hypochlorite, to destroy cyanide and precipitate copper hydroxide, a solid hazardous waste that has to be disposed properly in a landfill or treated for metal recovery.	Cyanides	86-93	spen family transcriptional repressor	Homo sapiens	17-21
18221936-3	2008	Cytotoxicity was preceded by ROS formation which was markedly increased by inactivating DT-diaphorase or catalase but were prevented by a subtoxic concentration of the mitochondrial respiratory inhibitor cyanide.	Cyanides	204-211	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	88-101
18221936-3	2008	Cytotoxicity was preceded by ROS formation which was markedly increased by inactivating DT-diaphorase or catalase but were prevented by a subtoxic concentration of the mitochondrial respiratory inhibitor cyanide.	Cyanides	204-211	catalase	Rattus norvegicus	105-113
17997575-2	2007	The synthesis combines a one-pot Horner-Wadsworth-Emmons/cyclocondensation sequence leading to isonitrile-functionalized DHP-2-ones with an isonitrile-based Passerini multicomponent reaction (MCR).	Cyanides	95-105	deoxyribonuclease 1 like 3	Homo sapiens	121-126
17878057-11	2007	We conclude that cis-crotononitrile is a CYP2E1 substrate as hypothesized, but that CYP2E1-mediated metabolism of this nitrile is not necessary for vestibular toxicity; rather, this metabolism constitutes a major pathway for cyanide release and subsequent lethality.	Cyanides	225-232	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	84-90
17986629-7	2008	Addition of a low concentration of cyanide, a specific COX inhibitor, restored the efficiency of mitochondria from MCDD rats back to the control level.	Cyanides	35-42	coproporphyrinogen oxidase	Rattus norvegicus	55-58
17725886-8	2007	Moreover, this method was applied to the analysis of SCN- plasma in deceased subjects, within the context of fire, and could be of interest in forensic science as a useful additional measurement tool for cyanide determination in blood.	Cyanides	204-211	sorcin	Homo sapiens	53-56
17980495-0	2007	Upregulation of BNIP3 and translocation to mitochondria mediates cyanide-induced apoptosis in cortical cells.	Cyanides	65-72	BCL2 interacting protein 3	Rattus norvegicus	16-21
17980495-5	2007	In BNIP3+ cells, cyanide-induced apoptotic death was markedly enhanced and preceded by reduction of mitochondrial membrane potential (delta psim), release of cytochrome c from mitochondria and elevated caspase 3 and 7 activity.	Cyanides	17-24	BCL2 interacting protein 3	Rattus norvegicus	3-8
17980495-8	2007	Immunohistochemical imaging showed that cyanide stimulated translocation of BNIP3 from cytosol to mitochondria and displacement studies with BNIP3 delta TM showed that integration of BNIP3 into the mitochondrial outer membrane was necessary for the cell death.	Cyanides	40-47	BCL2 interacting protein 3	Rattus norvegicus	76-81
17980495-9	2007	In BNIP3+ cells, cyclosporin-A, an inhibitor of mitochondrial pore transition, blocked the cyanide-induced reduction of delta psim and decreased the apoptotic death.	Cyanides	91-98	BCL2 interacting protein 3	Rattus norvegicus	3-8
17980495-10	2007	These results demonstrate in cortical cells that cyanide induces a rapid upregulation of BNIP3 expression, followed by translocation to the mitochondrial outer membrane to reduce delta psim.	Cyanides	49-56	BCL2 interacting protein 3	Rattus norvegicus	89-94
17761422-5	2007	The best hCA VB inhibitors were cyanate, thiocyanate, cyanide and hydrogensulfide (K(I)s of 80-76 microM) whereas the least effective ones were the halides (K(I)s of 11-72 mM), with the best inhibitor being fluoride and the least effective ones bromide and iodide.	Cyanides	54-61	carbonic anhydrase 5B	Homo sapiens	9-15
17650504-6	2007	In contrast, the slow phase in the kinetics of cyanide binding to the ferric CYP3A4 correlated with a shift of the heme iron spin state, which is only caused by the association of a second molecule of testosterone.	Cyanides	47-54	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	77-83
18062223-7	2007	The enzyme exhibited activity over a broad pH range from pH 5.0 to pH 11.0 and temperature range from 20 degrees C to 60 degrees C. The catalase activity was inhibited by 3-amino-1,2,4-triazole, cyanide, azide, and hydroxylamine.	Cyanides	195-202	Rru_A1356	Rhodospirillum rubrum ATCC 11170	136-144
17611046-3	2007	Here we show that expression of hmp is greatly enhanced by NO but not by other haem ligands (azide, cyanide and carbon monoxide).	Cyanides	100-107	inner membrane mitochondrial protein	Homo sapiens	32-35
17573087-0	2007	Uncoupling protein-2 up-regulation and enhanced cyanide toxicity are mediated by PPARalpha activation and oxidative stress.	Cyanides	48-55	peroxisome proliferator activated receptor alpha	Homo sapiens	81-90
17573087-5	2007	Wy14,643 produced a concentration- and time-dependent up-regulation of UCP-2 that was linked to enhanced cyanide-induced cell death.	Cyanides	105-112	uncoupling protein 2	Homo sapiens	71-76
17573087-10	2007	Co-treatment with PPARalpha-RNAi and GSH-EE blocked both the up-regulation of UCP-2 by Wy14,643 and the cyanide-induced cell death.	Cyanides	104-111	peroxisome proliferator activated receptor alpha	Homo sapiens	18-27
17573087-11	2007	It was concluded that a PPARalpha-mediated pathway and an oxidative stress pathway independent of PPARalpha mediate the up-regulation of UCP-2 and subsequent increased vulnerability to cyanide-induced cytotoxicity.	Cyanides	185-192	peroxisome proliferator activated receptor alpha	Homo sapiens	24-33
17573087-11	2007	It was concluded that a PPARalpha-mediated pathway and an oxidative stress pathway independent of PPARalpha mediate the up-regulation of UCP-2 and subsequent increased vulnerability to cyanide-induced cytotoxicity.	Cyanides	185-192	uncoupling protein 2	Homo sapiens	137-142
17333023-0	2007	Expression of MdCAS1 and MdCAS2, encoding apple beta-cyanoalanine synthase homologs, is concomitantly induced during ripening and implicates MdCASs in the possible role of the cyanide detoxification in Fuji apple (Malus domestica Borkh.)	Cyanides	176-183	L-3-cyanoalanine synthase 1, mitochondrial	Malus domestica	14-20
17333023-0	2007	Expression of MdCAS1 and MdCAS2, encoding apple beta-cyanoalanine synthase homologs, is concomitantly induced during ripening and implicates MdCASs in the possible role of the cyanide detoxification in Fuji apple (Malus domestica Borkh.)	Cyanides	176-183	L-3-cyanoalanine synthase 2, mitochondrial	Malus domestica	25-31
17561100-0	2007	HIF-1alpha activation by a redox-sensitive pathway mediates cyanide-induced BNIP3 upregulation and mitochondrial-dependent cell death.	Cyanides	60-67	hypoxia inducible factor 1 subunit alpha	Homo sapiens	0-10
17561100-0	2007	HIF-1alpha activation by a redox-sensitive pathway mediates cyanide-induced BNIP3 upregulation and mitochondrial-dependent cell death.	Cyanides	60-67	BCL2 interacting protein 3	Homo sapiens	76-81
17561100-5	2007	Cyanide induced a rapid surge of intracellular reactive oxygen species (ROS) generation, followed by p38 mitogen-activated protein kinase (MAPK) activation and nuclear accumulation of hypoxia-inducible factor-1alpha (HIF-1alpha).	Cyanides	0-7	mitogen-activated protein kinase 14	Homo sapiens	101-137
17561100-5	2007	Cyanide induced a rapid surge of intracellular reactive oxygen species (ROS) generation, followed by p38 mitogen-activated protein kinase (MAPK) activation and nuclear accumulation of hypoxia-inducible factor-1alpha (HIF-1alpha).	Cyanides	0-7	hypoxia inducible factor 1 subunit alpha	Homo sapiens	184-215
17561100-5	2007	Cyanide induced a rapid surge of intracellular reactive oxygen species (ROS) generation, followed by p38 mitogen-activated protein kinase (MAPK) activation and nuclear accumulation of hypoxia-inducible factor-1alpha (HIF-1alpha).	Cyanides	0-7	hypoxia inducible factor 1 subunit alpha	Homo sapiens	217-227
17561100-10	2007	Overexpression of BNIP3 produced mitochondrial dysfunction (reduced membrane potential), caspase-independent apoptosis, and sensitization of the cells to cyanide-induced toxicity.	Cyanides	154-161	BCL2 interacting protein 3	Homo sapiens	18-23
17561100-11	2007	Expression of a dominant-negative mutant or RNAi knockdown of BNIP3 protected the cells from cyanide.	Cyanides	93-100	BCL2 interacting protein 3	Homo sapiens	62-67
17561100-12	2007	It was concluded that cyanide activated the HIF-1alpha-mediated pathway of BNIP3 induction through a redox-sensitive process.	Cyanides	22-29	hypoxia inducible factor 1 subunit alpha	Homo sapiens	44-54
17561100-12	2007	It was concluded that cyanide activated the HIF-1alpha-mediated pathway of BNIP3 induction through a redox-sensitive process.	Cyanides	22-29	BCL2 interacting protein 3	Homo sapiens	75-80
17488037-2	2007	The synthesis of the polyketide template utilized a diastereoselective syn-aldol, ortho-ester Claisen rearrangement followed by efficient conversion to a cyanide.	Cyanides	154-161	synemin	Homo sapiens	4-7
17660693-1	2007	Mitochondrial alternative oxidase (AOX) is the terminal oxidase responsible for cyanide-insensitive and salicylhydroxamic acid-sensitive respiration in plants.	Cyanides	80-87	ubiquinol oxidase 1a, mitochondrial	Triticum aestivum	14-33
17660693-1	2007	Mitochondrial alternative oxidase (AOX) is the terminal oxidase responsible for cyanide-insensitive and salicylhydroxamic acid-sensitive respiration in plants.	Cyanides	80-87	ubiquinol oxidase 1a, mitochondrial	Triticum aestivum	35-38
17359937-5	2007	Compared with wild-type recombinant MPO the cyanide association rate with ferric Met243Val was significantly enhanced as were also the calculated apparent bimolecular compound I reduction rates by iodide (>10(8) M(-1)s(-1)) and thiocyanate (>10(8) M(-1)s(-1)).	Cyanides	44-51	myeloperoxidase	Homo sapiens	36-39
17436348-1	2007	The vibrational dynamics of the cyanide anion and the heme group in MbCN (CN complexed to Myoglobin) are investigated using molecular dynamics simulations.	Cyanides	32-45	myoglobin	Homo sapiens	90-99
17339232-1	2007	Alternative oxidase (AOX), the unique terminal oxidase in plant mitochondria, catalyzes the energy-wasteful cyanide (CN)-resistant respiration.	Cyanides	108-115	alternative oxidase 2	Arabidopsis thaliana	0-19
17339232-1	2007	Alternative oxidase (AOX), the unique terminal oxidase in plant mitochondria, catalyzes the energy-wasteful cyanide (CN)-resistant respiration.	Cyanides	108-115	alternative oxidase 2	Arabidopsis thaliana	21-24
17257840-6	2007	The best hCA XII inhibitors were cyanide (K(I) of 1 microM) and azide (K(I) of 80 microM).	Cyanides	33-40	carbonic anhydrase 12	Homo sapiens	9-16
17127063-7	2007	The best hCA VI inhibitors were cyanide, azide, sulfamide, and sulfamate, with inhibition constants in the range of 70-90microM.	Cyanides	32-39	carbonic anhydrase 6	Homo sapiens	9-15
17264905-1	2007	Reaction of UO2(OTf)2 with 5 molar equivalents of NEt4CN in acetonitrile led to the formation of the pentacyano uranyl complex [NEt4]3[UO2(CN)5] which is monomeric in the solid state with the five C-coordinated cyanide ions lying in the equatorial plane perpendicular to the linear {UO2} axis.	Cyanides	211-218	POU class 2 homeobox 2	Homo sapiens	12-21
17264905-1	2007	Reaction of UO2(OTf)2 with 5 molar equivalents of NEt4CN in acetonitrile led to the formation of the pentacyano uranyl complex [NEt4]3[UO2(CN)5] which is monomeric in the solid state with the five C-coordinated cyanide ions lying in the equatorial plane perpendicular to the linear {UO2} axis.	Cyanides	211-218	tetraspanin 5	Homo sapiens	50-54
17264905-1	2007	Reaction of UO2(OTf)2 with 5 molar equivalents of NEt4CN in acetonitrile led to the formation of the pentacyano uranyl complex [NEt4]3[UO2(CN)5] which is monomeric in the solid state with the five C-coordinated cyanide ions lying in the equatorial plane perpendicular to the linear {UO2} axis.	Cyanides	211-218	tetraspanin 5	Homo sapiens	128-132
17257035-0	2007	Cyanide-promoted demetalation of TrpyNiNCO: a route to sensitive metallotripyrrins of CoII, FeII, and MnII.	Cyanides	0-7	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	86-90
17322330-0	2007	Characterization of the regulatory and expression context of an alternative oxidase gene provides insights into cyanide-insensitive respiration during growth and development.	Cyanides	112-119	ubiquinol oxidase 1, mitochondrial	Glycine max	64-83
16847457-6	2007	ATF3 could also be induced by desferrioxamine but not by the mitochondrial poison cyanide or the nonspecific 2-oxoglutarate dioxygenase inhibitor dimethyloxalylglycine.	Cyanides	82-89	activating transcription factor 3	Homo sapiens	0-4
17098912-6	2007	We previously observed that RhdA overproduction protects Escherichia coli against cyanide toxicity, and here we show that physiological RhdA levels contribute to P. aeruginosa survival under cyanogenic conditions.	Cyanides	82-89	thiosulfate:cyanide sulfurtransferase	Pseudomonas aeruginosa PAO1	28-32
17098912-9	2007	Hence, RhdA could be regarded as an effector of P. aeruginosa intrinsic resistance to cyanide, insofar as it provides the bacterium with a defense mechanism against endogenous cyanide toxicity, in addition to cyanide-resistant respiration.	Cyanides	86-93	thiosulfate:cyanide sulfurtransferase	Pseudomonas aeruginosa PAO1	7-11
17098912-9	2007	Hence, RhdA could be regarded as an effector of P. aeruginosa intrinsic resistance to cyanide, insofar as it provides the bacterium with a defense mechanism against endogenous cyanide toxicity, in addition to cyanide-resistant respiration.	Cyanides	176-183	thiosulfate:cyanide sulfurtransferase	Pseudomonas aeruginosa PAO1	7-11
17098912-9	2007	Hence, RhdA could be regarded as an effector of P. aeruginosa intrinsic resistance to cyanide, insofar as it provides the bacterium with a defense mechanism against endogenous cyanide toxicity, in addition to cyanide-resistant respiration.	Cyanides	176-183	thiosulfate:cyanide sulfurtransferase	Pseudomonas aeruginosa PAO1	7-11
17157046-3	2007	The cyanide-sensitive 240 kDa SOD-like factor showed a significant homology to mammalian extracellular SOD (EC-SOD) reported, although the molecular mass of EC-SOD was 135 kDa.	Cyanides	4-11	superoxide dismutase 3	Homo sapiens	89-106
17157046-3	2007	The cyanide-sensitive 240 kDa SOD-like factor showed a significant homology to mammalian extracellular SOD (EC-SOD) reported, although the molecular mass of EC-SOD was 135 kDa.	Cyanides	4-11	superoxide dismutase 3	Homo sapiens	108-114
17157046-3	2007	The cyanide-sensitive 240 kDa SOD-like factor showed a significant homology to mammalian extracellular SOD (EC-SOD) reported, although the molecular mass of EC-SOD was 135 kDa.	Cyanides	4-11	superoxide dismutase 3	Homo sapiens	157-163
18182427-6	2007	A dual role for ZmNIT2 in auxin biosynthesis and in cyanide detoxification as a heteromer with ZmNIT1 is therefore proposed.	Cyanides	52-59	nitrilase 1	Zea mays	95-101
17088324-6	2006	The enzymatically active cysteine-containing domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases, and stress proteins such as senescence specific protein 1 in plants, PspE and GlpE in bacteria, and cyanide and arsenate resistance proteins.	Cyanides	220-227	Rhodanese/Cell cycle control phosphatase superfamily protein	Arabidopsis thaliana	67-72
17098912-2	2007	Here we report on the presence of multiple sulfurtransferases in the cyanogenic bacterium Pseudomonas aeruginosa PAO1 and investigate in detail RhdA, a thiosulfate:cyanide sulfurtransferase (rhodanese) which converts cyanide to less toxic thiocyanate.	Cyanides	164-171	thiosulfate:cyanide sulfurtransferase	Pseudomonas aeruginosa PAO1	144-148
17109651-10	2006	However, supplementing cyanide to CFC diet (without methionine) curtailed SOD and GSH-Px activities in diabetic rats.	Cyanides	23-30	glutathione peroxidase 1	Rattus norvegicus	82-88
17054353-8	2006	Complexes 3 and 4 show significant metamagnetic behavior, where the cyanides mediate the intrachain ferromagnetic coupling between Fe(III) and Co(II) or Ni(II) ions and the interchain pi-pi stacking interactions lead to antiferromagnetic couplings.	Cyanides	68-76	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	143-149
16996734-0	2006	Adamantane 11-beta-HSD-1 inhibitors: Application of an isocyanide multicomponent reaction.	Cyanides	55-65	hydroxysteroid 11-beta dehydrogenase 1	Mus musculus	11-24
17112248-1	2006	Two cyanide-bridged WV-M [M = Mn(II) (1), Co(II) (2)] bimetallic clusters were prepared by self-assembling a new molecular precursor [W(CN)6(bpy)]- and the corresponding metal complexes.	Cyanides	4-11	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	42-48
16950829-9	2006	Identification of the enzymes as tyrosinases was confirmed by the ability of lichen thalli or leachates derived by shaking lichens in distilled water to metabolize substrates such as L-dihydroxyphenylalanine (DOPA), tyrosine and epinephrine readily in the absence of hydrogen peroxide, the sensitivity of the enzymes to the inhibitors cyanide, azide and hexylresorcinol, activation by SDS and having typical tyrosinase molecular masses of approx.	Cyanides	335-342	tyrosinase	Homo sapiens	33-43
17042493-3	2006	The E(o)" values for free and cyanide-bound MPO (5 and -37 mV, respectively, at 25 degrees C and pH 7.0) are significantly higher than those of other heme peroxidases.	Cyanides	30-37	myeloperoxidase	Homo sapiens	44-47
17042493-6	2006	This peculiar behavior is discussed with respect to the MPO-typical covalent heme to protein linkages as well as to the published structures of ferric MPO and its cyanide complex and the recently published structure of lactoperoxidase as well as the physiological role of MPO in bacterial killing.	Cyanides	163-170	myeloperoxidase	Homo sapiens	151-154
17042493-6	2006	This peculiar behavior is discussed with respect to the MPO-typical covalent heme to protein linkages as well as to the published structures of ferric MPO and its cyanide complex and the recently published structure of lactoperoxidase as well as the physiological role of MPO in bacterial killing.	Cyanides	163-170	myeloperoxidase	Homo sapiens	151-154
16933320-0	2006	Inducible nitric oxide synthase up-regulation and mitochondrial glutathione depletion mediate cyanide-induced necrosis in mesencephalic cells.	Cyanides	94-101	nitric oxide synthase 2	Rattus norvegicus	0-31
17159296-2	2006	Mitochondrial alternative oxidase (AOX) is the terminal oxidase responsible for the cyanide-insensitive and salicylhydroxamic acid-sensitive respiration.	Cyanides	84-91	alternative oxidase 2	Arabidopsis thaliana	14-33
17159296-2	2006	Mitochondrial alternative oxidase (AOX) is the terminal oxidase responsible for the cyanide-insensitive and salicylhydroxamic acid-sensitive respiration.	Cyanides	84-91	alternative oxidase 2	Arabidopsis thaliana	35-38
16933320-9	2006	It was concluded that, in cyanide-mediated neurotoxicity, mtGSH is a vital component of the cellular antioxidant defense, and its depletion can lead to oxidative stress-mediated iNOS up-regulation, thus enhancing RNS generation and necrosis.	Cyanides	26-33	nitric oxide synthase 2	Rattus norvegicus	178-182
16782780-0	2006	PPARalpha-mediated upregulation of uncoupling protein-2 switches cyanide-induced apoptosis to necrosis in primary cortical cells.	Cyanides	65-72	peroxisome proliferator activated receptor alpha	Homo sapiens	0-9
16782780-0	2006	PPARalpha-mediated upregulation of uncoupling protein-2 switches cyanide-induced apoptosis to necrosis in primary cortical cells.	Cyanides	65-72	uncoupling protein 2	Homo sapiens	35-55
16782780-2	2006	Based on the report that Wy14,643, a PPARalpha agonist, can upregulate uncoupling protein-2 (UCP-2), this study was conducted in primary cortical cells to determine if PPARalpha activation enhances cyanide-induced neurotoxicity through changes in the level of UCP-2.	Cyanides	198-205	peroxisome proliferator activated receptor alpha	Homo sapiens	168-177
16782780-5	2006	The effect of UCP-2 upregulation on the cytotoxic response to cyanide was quantitated by terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (apoptosis) and propidium iodide staining (necrosis).	Cyanides	62-69	uncoupling protein 2	Homo sapiens	14-19
16782780-8	2006	Knock down of UCP-2 expression by RNA interference blocked the Wy14,643-mediated enhancement of cyanide-induced mitochondrial dysfunction and the switch of the cell death mode, thus confirming that the response was mediated by upregulation of UCP-2.	Cyanides	96-103	uncoupling protein 2	Homo sapiens	14-19
16782780-8	2006	Knock down of UCP-2 expression by RNA interference blocked the Wy14,643-mediated enhancement of cyanide-induced mitochondrial dysfunction and the switch of the cell death mode, thus confirming that the response was mediated by upregulation of UCP-2.	Cyanides	96-103	uncoupling protein 2	Homo sapiens	243-248
16782780-9	2006	This study shows that PPARalpha activation can upregulate UCP-2 expression, which in turn enhances cyanide-induced necrotic cell death through an increase of mitochondrial dysfunction.	Cyanides	99-106	peroxisome proliferator activated receptor alpha	Homo sapiens	22-31
16782780-9	2006	This study shows that PPARalpha activation can upregulate UCP-2 expression, which in turn enhances cyanide-induced necrotic cell death through an increase of mitochondrial dysfunction.	Cyanides	99-106	uncoupling protein 2	Homo sapiens	58-63
16906763-0	2006	Cyanide binding and heme cavity conformational transitions in Drosophila melanogaster hexacoordinate hemoglobin.	Cyanides	0-7	globin 1	Drosophila melanogaster	101-111
16545926-1	2006	Mercaptopyruvate sulfurtransferase (MPST) plays a central role in both cysteine degradation and cyanide detoxification.	Cyanides	96-103	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
16545926-1	2006	Mercaptopyruvate sulfurtransferase (MPST) plays a central role in both cysteine degradation and cyanide detoxification.	Cyanides	96-103	mercaptopyruvate sulfurtransferase	Homo sapiens	36-40
16895429-2	2006	Detailed infrared reflection absorption spectroscopic (IRRAS) and kinetic studies show that the reaction occurs by initial eta1-adsorption of the isocyanide on the Au surface, which activates the isocyanide to attack by the amine.	Cyanides	146-156	secreted phosphoprotein 1	Homo sapiens	123-127
16895429-2	2006	Detailed infrared reflection absorption spectroscopic (IRRAS) and kinetic studies show that the reaction occurs by initial eta1-adsorption of the isocyanide on the Au surface, which activates the isocyanide to attack by the amine.	Cyanides	196-206	secreted phosphoprotein 1	Homo sapiens	123-127
16906763-4	2006	Here we present kinetic data characterizing the exogenous cyanide ligand binding process, and the three-dimensional structure (at 1.4 A resolution) of the ensuing cyano-met D. melanogaster hemoglobin.	Cyanides	58-65	globin 1	Drosophila melanogaster	189-199
16802829-3	2006	Reactions of 2 and 3 with isocyanide at room temperature produced complexes 8-(CNBu(t))-8,8,8-(CO)(3)-9-Ph-nido-8,7,9,10-MC(3)B(7)H(9) [M = Mn (4), Re (5)], having the cage eta(4)-coordinated to the metal.	Cyanides	26-36	endothelin receptor type A	Homo sapiens	173-176
16790311-0	2006	Evidence for a functional genetic polymorphism of the human thiosulfate sulfurtransferase (Rhodanese), a cyanide and H2S detoxification enzyme.	Cyanides	105-112	thiosulfate sulfurtransferase	Homo sapiens	60-89
16790311-1	2006	Rhodanese or thiosulfate sulfurtransferase (TST) is a mitochondrial matrix enzyme that plays roles in cyanide detoxification, the formation of iron-sulfur proteins and the modification of sulfur-containing enzymes.	Cyanides	102-109	thiosulfate sulfurtransferase	Homo sapiens	13-42
16790311-1	2006	Rhodanese or thiosulfate sulfurtransferase (TST) is a mitochondrial matrix enzyme that plays roles in cyanide detoxification, the formation of iron-sulfur proteins and the modification of sulfur-containing enzymes.	Cyanides	102-109	thiosulfate sulfurtransferase	Homo sapiens	44-47
16621537-2	2006	Cyanate, cyanide, and hydrogensulfite were weak hCA VII inhibitors (K(I)s in the range of 7.3-15.2 mM).	Cyanides	9-16	carbonic anhydrase 7	Homo sapiens	48-55
16719481-4	2006	Analysis of the temperature dependence of the average structures suggests that the differences in the thermal expansion are due principally to the different strengths of the metal-cyanide binding interaction and, accordingly, the different energies of transverse vibration of the cyanide bridge, with enhanced NTE behavior for more flexible lattices.	Cyanides	180-187	patatin like phospholipase domain containing 6	Homo sapiens	310-313
16749845-7	2006	The cyanide was in situ formed via C-C bond cleavage of acetonitrile during the preparation of 6, which adopts a rare mu4-kC,kC:kN,kN mode to bridge four Ag(I) ions.	Cyanides	4-11	adaptor related protein complex 4 subunit mu 1	Homo sapiens	118-121
16611641-7	2006	CDO was also rendered inactive upon complexation with the metal-binding inhibitors azide and cyanide.	Cyanides	93-100	cysteine dioxygenase type 1	Rattus norvegicus	0-3
16322757-2	2006	Here we show that expression of the cyanide-insensitive alternative oxidase (AOX), recently identified in the ascidian Ciona intestinalis, is well tolerated by cultured human cells and confers spectacular cyanide resistance to mitochondrial substrate oxidation.	Cyanides	36-43	acyl-CoA oxidase 1	Homo sapiens	77-80
16322757-2	2006	Here we show that expression of the cyanide-insensitive alternative oxidase (AOX), recently identified in the ascidian Ciona intestinalis, is well tolerated by cultured human cells and confers spectacular cyanide resistance to mitochondrial substrate oxidation.	Cyanides	205-212	acyl-CoA oxidase 1	Homo sapiens	77-80
16511360-5	2006	Cyanide inhibited the reaction catalyzed by CuZnSOD but accelerated that by Cu(2+) and Fe(3+).	Cyanides	0-7	superoxide dismutase 1	Homo sapiens	44-51
16477023-2	2006	Here we report on the x-ray crystal structure of human IDO, complexed with the ligand inhibitor 4-phenylimidazole and cyanide.	Cyanides	118-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	55-58
16786295-0	2006	Cyanide metabolism in higher plants: cyanoalanine hydratase is a NIT4 homolog.	Cyanides	0-7	nitrilase 4	Arabidopsis thaliana	65-69
16789843-7	2006	In the presence of formate and cyanide ions, which bind at the binuclear heme a(3)/copper center in CcO, irradiation at 355 nm caused selective reduction of only the low-spin heme a and Cu(A).	Cyanides	31-38	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	100-103
16719481-4	2006	Analysis of the temperature dependence of the average structures suggests that the differences in the thermal expansion are due principally to the different strengths of the metal-cyanide binding interaction and, accordingly, the different energies of transverse vibration of the cyanide bridge, with enhanced NTE behavior for more flexible lattices.	Cyanides	280-287	patatin like phospholipase domain containing 6	Homo sapiens	310-313
16434742-0	2006	The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c.	Cyanides	37-44	cytochrome c, somatic	Equus caballus	24-36
16452535-10	2006	These data suggest, that in an era and area of decreased cyanide pollution, SCN- may remain a cofactor in the multifactorial aetiology of goiter.	Cyanides	57-64	sorcin	Homo sapiens	76-80
16289252-4	2006	Cells homozygous for expanded mutation showed greater amount of mutated fragments than heterozygotes and controls, caspase 3, 8 and 9 activities greater in mutated than control cell lines, after cyanide treatment, the caspase 3 and 8 particularly increased in homozygotes.	Cyanides	195-202	caspase 3	Homo sapiens	115-133
16434742-0	2006	The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c.	Cyanides	37-44	cytochrome c, somatic	Equus caballus	179-191
16434742-2	2006	In order to quantify this observation, the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple was determined for the first time by cyclic voltammetry.	Cyanides	94-101	cytochrome c, somatic	Equus caballus	81-93
16040185-4	2006	Nitration of cyt c resulted in disruption of the heme-methionine bond and rapid binding to cyanide.	Cyanides	91-98	cytochrome c, somatic	Homo sapiens	13-18
16288970-4	2006	Based on the published crystal structures of free MPO and its complexes with cyanide, bromide and thiocyanate as well as on sequence analysis and modeling, we critically discuss structure-function relationships.	Cyanides	77-84	myeloperoxidase	Homo sapiens	50-53
16337271-1	2006	Solution proton NMR has been used here to show that, as either the high-spin ferric, protohemin (PH) substrate complex at neutral pH, or the low-spin ferric, cyanide-inhibited PH substrate complex, the active site electronic and molecular structure of the 233- and 265-residue recombinant constructs of human heme oxygenase-1, hHO, are essentially indistinguishable.	Cyanides	158-165	heme oxygenase 1	Homo sapiens	309-325
16753941-1	2006	Thiosulfate sulfurtransferase (TST) is an important "enzyme of protection," that accelerates the detoxification of cyanide, converting it into thiocyanate.	Cyanides	115-122	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	0-29
16753941-1	2006	Thiosulfate sulfurtransferase (TST) is an important "enzyme of protection," that accelerates the detoxification of cyanide, converting it into thiocyanate.	Cyanides	115-122	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	31-34
16719781-7	2006	3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction.	Cyanides	53-60	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-7	2006	3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction.	Cyanides	180-187	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-9	2006	These facts suggest that 3-mercaptopyruvate sulfurtransferase has physiologic roles as an antioxidant and a cyanide antidote; is essential for neural function, and participates in cysteine degradation.	Cyanides	108-115	mercaptopyruvate sulfurtransferase	Homo sapiens	25-61
15937145-0	2005	Up-regulation of uncoupling protein 2 by cyanide is linked with cytotoxicity in mesencephalic cells.	Cyanides	41-48	uncoupling protein 2	Homo sapiens	17-37
16270978-3	2005	Compound 3 contains one-dimensional zigzag chains in which the Co(II) ion is coordinated by two chelating 2,2"-bipy ligands and two cyanides from two different [Ni(CN)4]2- units cis to each other.	Cyanides	132-140	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	63-69
16023819-3	2005	When I was incubated (45 microM) in the presence of NADPH-fortified human liver microsomes for 2h, 7.5 microM of cyanide was detected using the spectrophotometric assay and 8.9 microM was measured using the HPLC methodology.	Cyanides	113-120	2,4-dienoyl-CoA reductase 1	Homo sapiens	52-57
16209622-2	2005	The resulting aziridine underwent regioselective nucleophilic ring opening at C-5 at room temperature with cyanide, fluoride, and acetate.	Cyanides	107-114	complement C5	Homo sapiens	78-81
16133205-1	2005	The enthalpic and entropic changes accompanying the reduction reaction of the six-coordinate cyanide adducts of cytochrome c, microperoxidase-11 and a few plant peroxidases were measured electrochemically.	Cyanides	93-100	cytochrome c, somatic	Homo sapiens	112-124
16133205-4	2005	Comparison of the reduction thermodynamics for the cyanide adducts of cytochrome c and plant peroxidases with those for microperoxidase-11 and myoglobin, respectively, yielded an estimate of the consequences of protein encapsulation and of the anionic character of the proximal histidine on the reduction potential of the heme-cyanide group.	Cyanides	51-58	cytochrome c, somatic	Homo sapiens	70-82
15937145-3	2005	In the current study, we show UCP-2-mediated reduction in mitochondrial function contributes to the mitochondrial dysfunction and the necrotic death of primary cultured mesencephalic cells (MCs) after exposure to cyanide, a complex IV inhibitor.	Cyanides	213-220	uncoupling protein 2	Homo sapiens	30-35
15937145-5	2005	Treatment with cyanide for 6 h or longer upregulated UCP-2 expression.	Cyanides	15-22	uncoupling protein 2	Homo sapiens	53-58
15937145-7	2005	Knockdown with RNAi or transfection with a UCP-2 dominant-negative interfering mutant reduced the cyanide-induced mitochondrial dysfunction and cell death, showing that constitutive expression of UCP-2 plays a role in the response to cyanide.	Cyanides	98-105	uncoupling protein 2	Homo sapiens	43-48
15937145-7	2005	Knockdown with RNAi or transfection with a UCP-2 dominant-negative interfering mutant reduced the cyanide-induced mitochondrial dysfunction and cell death, showing that constitutive expression of UCP-2 plays a role in the response to cyanide.	Cyanides	98-105	uncoupling protein 2	Homo sapiens	196-201
15937145-7	2005	Knockdown with RNAi or transfection with a UCP-2 dominant-negative interfering mutant reduced the cyanide-induced mitochondrial dysfunction and cell death, showing that constitutive expression of UCP-2 plays a role in the response to cyanide.	Cyanides	234-241	uncoupling protein 2	Homo sapiens	43-48
15937145-7	2005	Knockdown with RNAi or transfection with a UCP-2 dominant-negative interfering mutant reduced the cyanide-induced mitochondrial dysfunction and cell death, showing that constitutive expression of UCP-2 plays a role in the response to cyanide.	Cyanides	234-241	uncoupling protein 2	Homo sapiens	196-201
15937145-8	2005	Overexpression of UCP-2 by transfection with human full-length cDNA potentiated the cyanide toxicity.	Cyanides	84-91	uncoupling protein 2	Homo sapiens	18-23
15937145-9	2005	These findings indicate that UCP-2 can serve as a regulator of mitochondria-mediated necrotic cell death, in which enhanced expression can increase the vulnerability of primary MCs to injury due to complex IV-mediated inhibition by cyanide.	Cyanides	232-239	uncoupling protein 2	Homo sapiens	29-34
15958286-8	2005	Horse cytochrome c increased 2-3 times the rate of electron flow across the cyanide-sensitive pathway and the contribution of the cyanide-resistant route became negligible.	Cyanides	76-83	cytochrome c, somatic	Equus caballus	6-18
16013451-4	2005	The oscillations plus the resistance to inhibition by cyanide identify the bulk of the oxygen consumption as due to ECTO-NOX proteins.	Cyanides	54-61	tripartite motif containing 33	Homo sapiens	116-120
15952810-4	2005	Cyanide decomposition and heating treatment studies suggest that (Oct)4N+-O3SS-protected nanoparticles have much higher overall stability compared to (Oct)4N+-Br-protected gold nanoparticles.	Cyanides	0-7	plexin A2	Homo sapiens	66-69
15910006-3	2005	Recent studies have shown that the MOCS3 rhodanese-like domain (MOCS3-RLD) catalyzes the transfer of sulfur from thiosulfate to cyanide and is also able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z.	Cyanides	128-135	molybdenum cofactor synthesis 3	Homo sapiens	35-40
15910006-3	2005	Recent studies have shown that the MOCS3 rhodanese-like domain (MOCS3-RLD) catalyzes the transfer of sulfur from thiosulfate to cyanide and is also able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z.	Cyanides	128-135	molybdenum cofactor synthesis 3	Homo sapiens	64-69
16018892-1	2005	Upon exposure to ultraviolet (UV) radiation, non-toxic hexacyanoferrate (II) (Fe(CN)6(-4)) undergoes direct photolysis, resulting in the liberation of toxic free cyanide (HCN,CN-).	Cyanides	162-169	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	171-174
15800031-0	2005	Enhancement of cyanide-induced mitochondrial dysfunction and cortical cell necrosis by uncoupling protein-2.	Cyanides	15-22	uncoupling protein 2	Homo sapiens	87-107
15800031-12	2005	It is concluded that UCP-2 levels influence cellular responses to cyanide-induced mitochondrial dysfunction.	Cyanides	66-73	uncoupling protein 2	Homo sapiens	21-26
15893539-2	2005	We have recently shown that CYP2E1 is essential for AN epoxidation and subsequent cyanide liberation.	Cyanides	82-89	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	28-34
15893539-7	2005	Further, while significant reduction in blood cyanide levels occurred in MAN-treated CYP2E1-null vs. WT mice, AN metabolism to cyanide was largely abolished in CYP2E1-null mice.	Cyanides	46-53	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	85-91
15893539-9	2005	Blood cyanide levels in mEH-null mice treated with aliphatic nitriles are generally lower than levels in similarly treated WT mice.	Cyanides	6-13	epoxide hydrolase 1, microsomal	Mus musculus	24-27
15893539-13	2005	In conclusion, these data showed that (1) at equimolar doses, higher blood cyanide levels were detected in mice treated with MAN vs. AN; (2) while CYP2E1 is the only enzyme responsible for AN metabolism to cyanide, other CYPs also contribute to MAN metabolism; and (3) significantly higher levels of cyanide were measured in the blood of male vs. female treated with either nitrile.	Cyanides	75-82	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	147-153
15893539-13	2005	In conclusion, these data showed that (1) at equimolar doses, higher blood cyanide levels were detected in mice treated with MAN vs. AN; (2) while CYP2E1 is the only enzyme responsible for AN metabolism to cyanide, other CYPs also contribute to MAN metabolism; and (3) significantly higher levels of cyanide were measured in the blood of male vs. female treated with either nitrile.	Cyanides	206-213	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	147-153
15893539-13	2005	In conclusion, these data showed that (1) at equimolar doses, higher blood cyanide levels were detected in mice treated with MAN vs. AN; (2) while CYP2E1 is the only enzyme responsible for AN metabolism to cyanide, other CYPs also contribute to MAN metabolism; and (3) significantly higher levels of cyanide were measured in the blood of male vs. female treated with either nitrile.	Cyanides	206-213	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	147-153
15844996-5	2005	The key nitrile anion 5-exo-tet cyclization concomitantly formed the pyrrolidine ring with clean inversion of the C-4 center to afford 1,3,4-trisubstituted chiral pyrrolidine in >95% yield and 94-99% ee.	Cyanides	8-21	complement C4A (Rodgers blood group)	Homo sapiens	114-117
15501671-4	2005	Inhibition of the esterase activity by metal chelating agents such as ethylenediamine tetraacetate, azide and cyanide has also supported the requirement of a metal ion for the activity.	Cyanides	110-117	alpha/beta fold hydrolase	Anoxybacillus gonensis	18-26
15780631-6	2005	The best hCA I inhibitors were cyanide, dicyanocuprate and dicyanoaurate (K(I)s in the range of 0.5-7.7 microM), whereas the least effective were fluoride and hexafluoroarsenate.	Cyanides	31-38	carbonic anhydrase 1	Homo sapiens	9-14
15780631-7	2005	The best hCA II inhibitors were cyanide, hexafluoroferrate and tetrachloroplatinate (K(I)s in the range of 0.02-0.51 mM), whereas the most ineffective ones were fluoride, hexafluoroaluminate and chloride.	Cyanides	32-39	carbonic anhydrase 2	Homo sapiens	9-15
15780631-9	2005	The most effective hCA V inhibitors were cyanide, heptafluoroniobate and dicyanocuprate (K(I)s in the range of 0.015-0.79 mM), whereas the most ineffective ones were fluoride, chloride and tetrafluoroborate (K(I)s in the range of 143-241 mM).	Cyanides	41-48	HCA1	Homo sapiens	19-22
15780631-10	2005	The best hCA IX inhibitors were on the other hand cyanide, heptafluoroniobate and dicyanoargentate (K(I)s in the range of 4 microM-0.33 mM), whereas the worst ones were hexacyanoferrate(III) and hexacyanoferrate(II).	Cyanides	50-57	carbonic anhydrase 9	Homo sapiens	9-15
15632145-6	2005	However, a stronger inhibition of root growth in KO-AtPrxII F seedlings as compared with wild type is observed under stress conditions induced by CdCl2 as well as after administration of salicylhydroxamic acid, an inhibitor of cyanide-insensitive respiration.	Cyanides	227-234	peroxiredoxin IIF	Arabidopsis thaliana	52-61
15667214-2	2005	In the cyanide-bridged, spin-coupled heme-copper center in an engineered myoglobin, the presence of Zn(II) in the Cu(B) center raises the heme reduction potential from -85 to 49 mV vs NHE.	Cyanides	7-14	solute carrier family 9 member C1	Homo sapiens	184-187
15886420-6	2005	Slight but significant cyanide-induced rise in MpST activity was observed only in the liver, which indicates a possibility of enhancement of its detoxification in reaction with mercapropyruvate in this organ.	Cyanides	23-30	mercaptopyruvate sulfurtransferase	Homo sapiens	47-51
15702190-1	2005	Ligand substitution reactions of the vitamin B12 analog cyanoimidazolylcobamide, CN(Im)Cbl, with cyanide were studied.	Cyanides	97-104	Cbl proto-oncogene	Homo sapiens	87-90
15607903-7	2005	Both mechanisms for generating immuno-spin trapping-detectable SOD1-centered radicals were susceptible to inhibition by cyanide and enhanced at high pH values.	Cyanides	120-127	superoxide dismutase 1	Homo sapiens	63-67
15763667-6	2005	The results showed that Ca(2+) presented an inhibitory effect on AOX pathway in potato mitochondria energized with NADH or succinate, which was only now observed when the cytochrome pathway was inhibited by cyanide.	Cyanides	207-214	ubiquinol oxidase 1, mitochondrial-like	Solanum tuberosum	65-68
15454240-2	2004	The inhibition of the newly discovered cytosolic carbonic anhydrase (CA, EC 4.2.1.1) isozyme XIII of murine origin (mCA XIII) has been investigated with a series of anions, such as the physiological ones (bicarbonate, chloride), or the metal complexing anions (cyanate, cyanide, azide, hydrogen sulfide, etc), nitrate, nitrite, sulfate, sulfamate, sulfamide as well as with phenylboronic and phenylarsonic acids.	Cyanides	270-277	carbonic anhydrase 13	Mus musculus	116-124
16459807-1	2005	Wastewater discharge from coal refining plants contains a number of biologically toxic compounds; 2000-2500 mg/l of COD of which 40% is composed of phenol, 100-400 mg/l of thiocyanate, 10-40 mg/l of cyanide, 100-250 mg/l of NH4+-N and 150-300 mg/l of total nitrogen.	Cyanides	199-206	small nuclear ribonucleoprotein polypeptides B and B1	Homo sapiens	116-119
15659779-2	2004	In assaying prooxidant or antioxidant activities, cyanide has been commonly used as an inhibitor of mitochondrial oxidases, peroxidases, or Cu,Zn-superoxide dismutase, which have an influence on intracellular levels of reactive oxygen species.	Cyanides	50-57	superoxide dismutase 1	Homo sapiens	140-166
15557251-1	2004	The alternative oxidase (AOX) is the terminal oxidase of the cyanide-resistant alternative respiratory pathway in plants and has been implicated in resistance to viruses.	Cyanides	61-68	acyl-CoA oxidase 1	Homo sapiens	4-23
15557251-1	2004	The alternative oxidase (AOX) is the terminal oxidase of the cyanide-resistant alternative respiratory pathway in plants and has been implicated in resistance to viruses.	Cyanides	61-68	acyl-CoA oxidase 1	Homo sapiens	25-28
15454240-3	2004	The best mCA XIII inhibitors were cyanate, thiocyanate, cyanide and sulfamide, with K(I)-s in the range of 0.25microM-0.74 mM, whereas fluoride, iodide, azide, carbonate and hydrogen sulfide were less effective (K(I)-s in the range of 3.0-5.5mM).	Cyanides	56-63	carbonic anhydrase 13	Mus musculus	9-17
15485138-4	2004	The effect of chemical hypoxia induced by cyanide (0.5 mM, 10 min perfusion) was studied with patch-clamp technique in visualized intact CA1 pyramidal neurons in rat brain slices.	Cyanides	42-49	carbonic anhydrase 1	Rattus norvegicus	137-140
15304319-3	2004	Purified recombinant proteins of these hemoglobins displayed hydrogen peroxide-dependent oxidation of several peroxidase substrates that was sensitive to cyanide, revealing intrinsic peroxidase-like activity.	Cyanides	154-161	peroxidase	Arabidopsis thaliana	110-120
15310197-7	2004	In the formation of [(CN)(5)Pt-Tl(CN)](-), Tl(CN)(2)(+) is the source of the cyanide ligand, while HCN is the cyanide donating agent in the formation of the trinuclear species.	Cyanides	110-117	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	99-102
15261109-3	2004	Chemical anoxia induced by cyanide, rotenone or p-trifluoromethoxy-phenylhydrazone (FCCP) decreased pH(i) by >0.4 pH units.	Cyanides	27-34	glucose-6-phosphate isomerase	Rattus norvegicus	100-105
15203186-10	2004	MPO-mediated lipid oxidation was inhibited by heme poisons (azide, cyanide) and catalase.	Cyanides	67-74	myeloperoxidase	Homo sapiens	0-3
15100225-5	2004	Cyanide bound relatively weakly in the ferric PADOX-1 heme vicinity (K(d) approximately 10 mm) but did not shift the heme to the low spin state.	Cyanides	0-7	Peroxidase superfamily protein	Arabidopsis thaliana	46-53
15100225-10	2004	PADOX-1 is unusual in that it has a high affinity, inhibitory cyanide-binding site distinct from the distal heme face and the fatty acid site.	Cyanides	62-69	Peroxidase superfamily protein	Arabidopsis thaliana	0-7
15230614-3	2004	When alk-2-yn-1-ols 9 were allowed to react with selenium and isocyanides under similar conditions, new selenium-containing heterocycles 10, 2-imino-4-alkylidene-1,3-oxaselenolanes, were obtained via cycloaddition of oxyimidoylselenoates 13 generated in situ by intramolecular addition of selenolates to carbon-carbon triple bonds.	Cyanides	62-73	activin A receptor type 1	Homo sapiens	5-10
15183197-5	2004	Dicumarol blocked the appearance of DQH2 when DQ was added to the cell medium, and cyanide blocked the appearance of DQ when DQH2 was added to the cell medium, suggesting that the two electron reductase NQO1 dominates DQ reduction and mitochondrial electron transport complex III is the predominant route of DQH2 oxidation.	Cyanides	83-90	NAD(P)H quinone dehydrogenase 1	Homo sapiens	203-207
15304319-3	2004	Purified recombinant proteins of these hemoglobins displayed hydrogen peroxide-dependent oxidation of several peroxidase substrates that was sensitive to cyanide, revealing intrinsic peroxidase-like activity.	Cyanides	154-161	peroxidase	Arabidopsis thaliana	183-193
15073332-4	2004	The MOCS3 rhodanese-like domain (MOCS3-RLD) was purified after heterologous expression in E. coli and was shown to catalyze the transfer of sulfur from thiosulfate to cyanide.	Cyanides	167-174	molybdenum cofactor synthesis 3	Homo sapiens	4-9
15073332-4	2004	The MOCS3 rhodanese-like domain (MOCS3-RLD) was purified after heterologous expression in E. coli and was shown to catalyze the transfer of sulfur from thiosulfate to cyanide.	Cyanides	167-174	molybdenum cofactor synthesis 3	Homo sapiens	33-38
15075239-7	2004	Hypoxia-induced RBM3 or CIRP transcription was inhibited by the respiratory chain inhibitors NaN(3) and cyanide in a dose-dependent fashion.	Cyanides	104-111	RNA binding motif (RNP1, RRM) protein 3	Mus musculus	16-20
15075239-7	2004	Hypoxia-induced RBM3 or CIRP transcription was inhibited by the respiratory chain inhibitors NaN(3) and cyanide in a dose-dependent fashion.	Cyanides	104-111	cold inducible RNA binding protein	Mus musculus	24-28
14998685-0	2004	Caspase inhibition switches the mode of cell death induced by cyanide by enhancing reactive oxygen species generation and PARP-1 activation.	Cyanides	62-69	poly(ADP-ribose) polymerase 1	Homo sapiens	122-128
15198024-4	2004	The kinetic constants, determined at pH 7.0, were as follows: oxidation by the enzyme of reduced TMPD at pH 7.0 was characterized by KM = 0.86 mM and Vmax = 1.1 mumol O2/(min mg protein), and oxidation of reduced cytochrome c from horse heart was characterized by KM = 0.09 mM and Vmax = 0.9 mumol O2/(min mg protein) Cyanide inhibited ascorbate/TMPD oxidase activity (Ki = 4.5-5.0 microM).	Cyanides	318-325	cytochrome c, somatic	Equus caballus	213-225
15252534-0	2004	Bi- and poly-metallic cyanide-bridged complexes of the redox-active cyanomanganese nitrosyl unit [Mn(CN)(PR3)(NO)(eta-C5H4Me)].	Cyanides	22-29	proteinase 3	Homo sapiens	105-108
15252534-0	2004	Bi- and poly-metallic cyanide-bridged complexes of the redox-active cyanomanganese nitrosyl unit [Mn(CN)(PR3)(NO)(eta-C5H4Me)].	Cyanides	22-29	endothelin receptor type A	Homo sapiens	14-17
15252534-1	2004	Cationic nitrile complexes and neutral halide and cyanide complexes, with the general formula [MnL1L2(NO)(eta-C5H4Me)]z, undergo one-electron oxidation at a Pt electrode in CH2Cl2.	Cyanides	50-57	endothelin receptor type A	Homo sapiens	106-109
14697048-0	2004	Subnanomolar cyanide detection at polyphenol oxidase/clay biosensors.	Cyanides	13-20	protoporphyrinogen oxidase	Homo sapiens	34-52
14687762-0	2004	Myeloperoxidase-catalyzed oxidation of chloroacetonitrile to cyanide.	Cyanides	61-68	myeloperoxidase	Homo sapiens	0-15
14687762-3	2004	The present work provides an evidence for CAN activation to cyanide (CN-) by myeloperoxidase (MPO)/hydrogen peroxide (H2O2)/chloride (Cl-) system in vitro.	Cyanides	60-67	myeloperoxidase	Homo sapiens	77-92
14687762-3	2004	The present work provides an evidence for CAN activation to cyanide (CN-) by myeloperoxidase (MPO)/hydrogen peroxide (H2O2)/chloride (Cl-) system in vitro.	Cyanides	60-67	myeloperoxidase	Homo sapiens	94-97
14577772-5	2003	Its eight cyanide groups are coordinated to Co(II) ions which have two coordinated water molecules in trans position.	Cyanides	10-17	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	44-50
14577772-8	2003	Only six of its eight cyanide groups are coordinated to Co(II) ions while the other two are terminal.	Cyanides	22-29	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	56-62
15338690-5	2004	The most substantial free cyanide (HCN.	Cyanides	26-33	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	35-38
14730575-1	2004	A capillary electrophoresis microchip is used to selectively and sensitively monitor cyanide levels in both vapor (HCN((g))) and aqueous (NaCN in drinking water) phases.	Cyanides	85-92	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	115-118
20021099-1	2004	The activity of rhodanese, 3-mercaptopyruvate sulfurtransferase (MPST) and cystathionase in mouse liver, kidney, and four brain regions: tele-, meso-, di- and rhombencephalon was studied 30 min and 2 h following a sublethal dose of cyanide (4 mg/ kg body weight) intraperitoneal injection.	Cyanides	232-239	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	16-25
20021099-3	2004	In the liver this dose of cyanide seemed to impair the process of cyanide detoxification by MPST, as well as rhodanese inhibition.	Cyanides	26-33	mercaptopyruvate sulfurtransferase	Mus musculus	92-96
20021099-3	2004	In the liver this dose of cyanide seemed to impair the process of cyanide detoxification by MPST, as well as rhodanese inhibition.	Cyanides	26-33	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	109-118
20021099-3	2004	In the liver this dose of cyanide seemed to impair the process of cyanide detoxification by MPST, as well as rhodanese inhibition.	Cyanides	66-73	mercaptopyruvate sulfurtransferase	Mus musculus	92-96
20021099-5	2004	In the kidney, a significant increase in the rhodanese activity was observed as early as 30 min following cyanide intoxication, and an elevated cystathionase activity after 2 h was detected.	Cyanides	106-113	thiosulfate sulfurtransferase, mitochondrial	Mus musculus	45-54
14644629-0	2003	Differential metabolism of acrylonitrile to cyanide is responsible for the greater sensitivity of male vs female mice: role of CYP2E1 and epoxide hydrolases.	Cyanides	44-51	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	127-133
14644629-2	2003	AN epoxidation to cyanoethylene oxide (CEO) via CYP2E1 and its subsequent metabolism via epoxide hydrolases (EH) to yield cyanide is thought to be responsible for the acute toxicity and mortality of AN.	Cyanides	122-129	epoxide hydrolase 1, microsomal	Mus musculus	109-111
14644629-13	2003	Further, higher expression of CYP2E1 and EH in male mice may contribute to greater formation of CEO and its subsequent metabolism to yield cyanide, respectively.	Cyanides	139-146	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	30-36
14644629-13	2003	Further, higher expression of CYP2E1 and EH in male mice may contribute to greater formation of CEO and its subsequent metabolism to yield cyanide, respectively.	Cyanides	139-146	epoxide hydrolase 1, microsomal	Mus musculus	41-43
14697048-1	2004	A novel, inexpensive, and simple amperometric biosensor based on immobilization of polyphenol oxidase (PPO) into Zn-Al layered double hydroxides, also called anionic clays, is applied for determination of cyanide.	Cyanides	205-212	protoporphyrinogen oxidase	Homo sapiens	83-101
14697048-1	2004	A novel, inexpensive, and simple amperometric biosensor based on immobilization of polyphenol oxidase (PPO) into Zn-Al layered double hydroxides, also called anionic clays, is applied for determination of cyanide.	Cyanides	205-212	protoporphyrinogen oxidase	Homo sapiens	103-106
14697048-2	2004	The detection of cyanide was performed via its inhibiting action on the PPO electrode.	Cyanides	17-24	protoporphyrinogen oxidase	Homo sapiens	72-75
14514298-0	2003	Cyanide adducts on the diruthenium core of [Ru2(L)4](+) (L = ap, CH3ap, Fap, or F3ap).	Cyanides	0-7	fibroblast activation protein alpha	Homo sapiens	72-75
16220934-1	2003	We developed a simple contrasting procedure to improve the AFM visualization of single positively charged polymer chains deposited on substrates of a relatively high roughness via the decoration of the molecules with hexacyanoferrate anions or negatively charged clusters of cyanide-bridged complexes.	Cyanides	275-282	afamin	Homo sapiens	59-62
12871026-0	2003	Do antidotes for acute cyanide poisoning act on mercaptopyruvate sulfurtransferase to facilitate detoxification?	Cyanides	23-30	mercaptopyruvate sulfurtransferase	Homo sapiens	48-82
14504927-3	2003	However, another metabolic inhibitor, antimycin A, which like cyanide inhibits electron transfer in the respiratory chain, totally interrupted cell-to-cell communication between Cx43-HeLa cells, even in whole-cell conditions, when ATP (5 mM) was present.	Cyanides	62-69	gap junction protein, alpha 1	Rattus norvegicus	178-182
12871026-2	2003	Sodium nitrite oxidizes oxy-hemoglobin, resulting in methemoglobin, which has a high affinity for cyanide.	Cyanides	98-105	hemoglobin subunit gamma 2	Homo sapiens	53-66
12935566-4	2003	Total (free and combined with cyanide) methemoglobin (MetHb) content was used to estimate the maximum capacity of MetHb for combining cyanide.	Cyanides	134-141	hemoglobin subunit gamma 2	Homo sapiens	39-52
12916121-0	2003	Spectroelectrochemical studies on mixed-valence states in a cyanide-bridged molecular square, [Ru(II)(2)Fe(II)(2)(mu-CN)(4)(bpy)(8)](PF6)(4).CHCl(3).H(2)O.	Cyanides	60-67	sperm associated antigen 17	Homo sapiens	133-136
12824013-1	2003	A novel isonitrile derivative was synthesized and used in an Ugi four component coupling reaction to explore aryl group substitution effects on inhibition of the coagulation cascade serine protease factor Xa.	Cyanides	8-18	coagulation factor X	Homo sapiens	198-207
12730222-6	2003	Using purified catalases from a variety of species, the ROS generating activity was found to be temperature- and O2-dependent, stimulated by inhibitors of the catalatic activity of catalase, including 3-aminotriazole and azide, and inhibited by cyanide.	Cyanides	245-252	catalase	Homo sapiens	15-23
12706538-0	2003	Cyanide binding study of neuronal nitric oxide synthase: effects of inhibitors and mutations at the substrate binding site.	Cyanides	0-7	nitric oxide synthase 1	Homo sapiens	25-55
12706538-1	2003	In order to understand the heme distal structure of neuronal nitric oxide synthase (nNOS), we studied cyanide binding to the ferric wild-type and substrate binding site mutants, Glu592Ala and Tyr588His, of the isolated oxygenase domain in the absence and presence of substrates and inhibitors.	Cyanides	102-109	nitric oxide synthase 1	Homo sapiens	84-88
12681909-1	2003	Replacement of the anomeric acetate by a cyanide group in the dimer of di-O-acetyl-L-fucal by the action of mild Lewis acid [Hg(CN)(2)-HgBr(2)-Me(3)SiCN], resulted not only in the desired transformation but also in the introduction of an additional double bond between C-2A and C-3A.	Cyanides	41-48	complement C3	Homo sapiens	278-282
12615119-5	2003	There were significant decreases (P < 0.05) in activities of superoxide dismutase (SOD), catalase and alkaline phosphatase (AP) in the liver, lung and kidney of the two groups given cyanide, but the decreases were significantly lower (P < 0.05) in the group fed antioxidant vitamins.	Cyanides	185-192	catalase	Oryctolagus cuniculus	92-100
12419774-1	2003	Cyanide (CN)-induced chemical anoxia of cultured mouse proximal tubular (MPT) cells increased the kinase activity of c-Src by approximately threefold.	Cyanides	0-7	Rous sarcoma oncogene	Mus musculus	119-122
12419774-1	2003	Cyanide (CN)-induced chemical anoxia of cultured mouse proximal tubular (MPT) cells increased the kinase activity of c-Src by approximately threefold.	Cyanides	9-11	Rous sarcoma oncogene	Mus musculus	119-122
12805646-0	2003	p38 Mitogen-activated protein kinase regulates Bax translocation in cyanide-induced apoptosis.	Cyanides	68-75	mitogen-activated protein kinase 14	Homo sapiens	0-3
12805646-0	2003	p38 Mitogen-activated protein kinase regulates Bax translocation in cyanide-induced apoptosis.	Cyanides	68-75	BCL2 associated X, apoptosis regulator	Homo sapiens	47-50
12805646-1	2003	Execution of cyanide-induced apoptosis is mediated by release of cytochrome c from mitochondria.	Cyanides	13-20	cytochrome c, somatic	Homo sapiens	65-77
12805646-2	2003	To determine how cyanide initiates cytochrome c release, Bax translocation was investigated in primary cultures of cortical neurons.	Cyanides	17-24	cytochrome c, somatic	Homo sapiens	35-47
12805646-4	2003	After 300-microM cyanide treatment for 1 h, Bax translocated to the mitochondria, as shown by immunocytochemical staining and subcellular fractionation; Western blot analysis confirmed "cytosol-to-mitochondria" translocation of Bax.	Cyanides	17-24	BCL2 associated X, apoptosis regulator	Homo sapiens	44-47
12805646-4	2003	After 300-microM cyanide treatment for 1 h, Bax translocated to the mitochondria, as shown by immunocytochemical staining and subcellular fractionation; Western blot analysis confirmed "cytosol-to-mitochondria" translocation of Bax.	Cyanides	17-24	BCL2 associated X, apoptosis regulator	Homo sapiens	228-231
12805646-5	2003	Temporal analysis showed that Bax translocation preceded cytochrome c release from the mitochondria, which was initiated 3 h after cyanide treatment.	Cyanides	131-138	BCL2 associated X, apoptosis regulator	Homo sapiens	30-33
12805646-5	2003	Temporal analysis showed that Bax translocation preceded cytochrome c release from the mitochondria, which was initiated 3 h after cyanide treatment.	Cyanides	131-138	cytochrome c, somatic	Homo sapiens	57-69
12805646-8	2003	The p38 MAP kinase was activated 30 min after cyanide, and its phosphorylation level of activity began to decrease 3 h later.	Cyanides	46-53	mitogen-activated protein kinase 14	Homo sapiens	4-18
12805646-11	2003	These results demonstrated that Bax translocation is critical for cyanide-induced cytochrome c release and that p38 MAP kinase regulates Bax translocation from cytosol to mitochondria.	Cyanides	66-73	BCL2 associated X, apoptosis regulator	Homo sapiens	32-35
12805646-11	2003	These results demonstrated that Bax translocation is critical for cyanide-induced cytochrome c release and that p38 MAP kinase regulates Bax translocation from cytosol to mitochondria.	Cyanides	66-73	cytochrome c, somatic	Homo sapiens	82-94
12854870-16	2003	Sodium thiosulfate, methemoglobin forming agents and cobalt compounds act efficiently by complexing or transforming cyanide into non-toxic stable derivatives.	Cyanides	116-123	hemoglobin subunit gamma 2	Homo sapiens	20-33
12637007-5	2003	The rate constant for cyanide binding to the heme iron of cytochrome c of cytochrome c-polyglutamate complex also decreases by approximately 42.5% with n>or approximately equal 8.	Cyanides	22-29	cytochrome c, somatic	Equus caballus	58-70
12637007-5	2003	The rate constant for cyanide binding to the heme iron of cytochrome c of cytochrome c-polyglutamate complex also decreases by approximately 42.5% with n>or approximately equal 8.	Cyanides	22-29	cytochrome c, somatic	Equus caballus	74-86
12935566-4	2003	Total (free and combined with cyanide) methemoglobin (MetHb) content was used to estimate the maximum capacity of MetHb for combining cyanide.	Cyanides	134-141	hemoglobin subunit gamma 2	Homo sapiens	54-59
12935566-4	2003	Total (free and combined with cyanide) methemoglobin (MetHb) content was used to estimate the maximum capacity of MetHb for combining cyanide.	Cyanides	134-141	hemoglobin subunit gamma 2	Homo sapiens	114-119
12935566-7	2003	MetHb at these levels is capable of scavenging up to 8.6-11.4 mg/l of blood cyanide.	Cyanides	76-83	hemoglobin subunit gamma 2	Homo sapiens	0-5
12935566-11	2003	Our results indicate that MetHb contents and CO-Hb saturation should be determined to evaluate the toxic effects of cyanide in fire victims.	Cyanides	116-123	hemoglobin subunit gamma 2	Homo sapiens	26-31
12480929-0	2003	Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.	Cyanides	105-112	biliverdin-producing heme oxygenase	Corynebacterium diphtheriae	141-155
12537503-5	2003	However, in the related compound, [(CH(3)NC)(2)Au(I)](PF(6)), each cation is surrounded by six hexafluorophosphate ions and there is no close Au...Au contact despite the fact that the isocyanide ligand has less steric bulk.	Cyanides	184-194	sperm associated antigen 17	Homo sapiens	54-59
14757960-6	2003	SCN- is also generated from cigarette smoking as a detoxifying product of cyanide.	Cyanides	74-81	sorcin	Homo sapiens	0-3
12553836-7	2003	At low pH and total NP concentration (pH < 3, [NP]/[Cbl(II)] approximately 1), the cyano-bridged successor complex [Cbl(III)-(mu-NC)-Fe(I)(CN)(3)(NO(+))](-) (1(s)()) is the final reaction product formed in an inner-sphere electron transfer reaction that is coupled to the release of cyanide from coordinated nitroprusside.	Cyanides	286-293	Cbl proto-oncogene	Homo sapiens	119-122
12553836-8	2003	At higher pH, subsequent reactions were observed which involve the attack of cyanide released in the electron transfer step on the initially formed cyano-bridged species, and lead to the formation of Cbl(III)CN and [Fe(I)(CN)(4)(NO(+))](2)(-).	Cyanides	77-84	Cbl proto-oncogene	Homo sapiens	200-203
12524477-1	2003	Methemoglobin (MHb) formation is effective in treating cyanide (CN) poisoning.	Cyanides	55-62	hemoglobin subunit gamma 2	Homo sapiens	0-13
12524477-1	2003	Methemoglobin (MHb) formation is effective in treating cyanide (CN) poisoning.	Cyanides	55-62	hemoglobin subunit gamma 2	Homo sapiens	15-18
12204582-8	2002	Inactivation of GAPDH by AN would be expected to impair glycolytic ATP production and when coupled with the inhibition of mitochondrial ATP synthesis by the AN metabolite cyanide would result in metabolic arrest.	Cyanides	171-178	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	16-21
12460737-0	2002	Oxidative stress and cyclooxygenase-2 induction mediate cyanide-induced apoptosis of cortical cells.	Cyanides	56-63	prostaglandin-endoperoxide synthase 2	Homo sapiens	21-37
12460737-1	2002	Cyanide (KCN)-induced generation of reactive oxygen species (ROS) involves cyclooxygenase-2 (COX-2)-mediated reactions in some neurons.	Cyanides	0-7	prostaglandin-endoperoxide synthase 2	Homo sapiens	75-91
12460737-1	2002	Cyanide (KCN)-induced generation of reactive oxygen species (ROS) involves cyclooxygenase-2 (COX-2)-mediated reactions in some neurons.	Cyanides	0-7	prostaglandin-endoperoxide synthase 2	Homo sapiens	93-98
12460737-12	2002	Increased nitric oxide levels caused by cyanide may directly activate the COX-2 enzyme.	Cyanides	40-47	prostaglandin-endoperoxide synthase 2	Homo sapiens	74-79
12460737-13	2002	These data show that cyanide treatment of cortical cells involves increased COX-2 expression, PGE(2) accumulation, and ROS generation, resulting in apoptotic cell death.	Cyanides	21-28	prostaglandin-endoperoxide synthase 2	Homo sapiens	76-81
12489125-10	2003	The activation mechanism of PsADH2 also, in this respect, has similarities to the mammalian HIF-1 system, which is inducible by Co(2+) but not by cyanide.	Cyanides	146-153	hypoxia inducible factor 1 subunit alpha	Homo sapiens	92-97
12124309-0	2002	Cytochrome P450 2E1 (CYP2E1) is essential for acrylonitrile metabolism to cyanide: comparative studies using CYP2E1-null and wild-type mice.	Cyanides	74-81	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	0-19
12124309-0	2002	Cytochrome P450 2E1 (CYP2E1) is essential for acrylonitrile metabolism to cyanide: comparative studies using CYP2E1-null and wild-type mice.	Cyanides	74-81	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	21-27
12124309-10	2002	In conclusion, under the current experimental conditions using CYP2E1-null mice, current work demonstrated for the first time that CYP2E1-mediated oxidation is a prerequisite for AN metabolism to cyanide.	Cyanides	196-203	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	63-69
12124309-10	2002	In conclusion, under the current experimental conditions using CYP2E1-null mice, current work demonstrated for the first time that CYP2E1-mediated oxidation is a prerequisite for AN metabolism to cyanide.	Cyanides	196-203	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	131-137
12124309-11	2002	Since earlier studies showed that CYP2E1 is the only enzyme responsible for AN epoxidation, it is concluded that AN metabolism to CEO is a prerequisite for cyanide formation, and this pathway is exclusively catalyzed by CYP2E1.	Cyanides	156-163	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	34-40
12151639-8	2002	The induction of oxidative stress by cyanide involved an early and temporal inhibition of antioxidant enzymes (catalase and superoxide dismutase) as well as an increased production of reactive oxygen species (1.5- to 2.0-fold over control).	Cyanides	37-44	catalase	Mesocricetus auratus	111-144
12135496-1	2002	We previously reported that GTS1 is involved in regulating ultradian oscillations of the glycolytic pathway induced by cyanide in cell suspensions as well as oscillations of energy metabolism in aerobic continuous cultures.	Cyanides	119-126	Gts1p	Saccharomyces cerevisiae S288C	28-32
11803471-2	2002	We demonstrate that manipulation of redox in air, achieved by inhibiting cytochrome oxidase with cyanide, induces HIF-1 mediated transcription in wild-type CHO and HT1080 human tumour cells but not in CHO cells deficient in the oxygen responsive, HIF-1alpha sub-unit of HIF-1.	Cyanides	97-104	hypoxia inducible factor 1 subunit alpha	Homo sapiens	114-119
12065643-9	2002	NMDA receptor activation and reactive oxygen species (ROS) generation are upstream events of NF-kappaB activation, as blockade of these two events by MK801, l-NAME or PBN inhibited cyanide-induced up-regulation of Bcl-X(S) and Bax.	Cyanides	181-188	nuclear factor kappa B subunit 1	Homo sapiens	93-102
12065643-9	2002	NMDA receptor activation and reactive oxygen species (ROS) generation are upstream events of NF-kappaB activation, as blockade of these two events by MK801, l-NAME or PBN inhibited cyanide-induced up-regulation of Bcl-X(S) and Bax.	Cyanides	181-188	BCL2 like 1	Homo sapiens	214-219
12065643-9	2002	NMDA receptor activation and reactive oxygen species (ROS) generation are upstream events of NF-kappaB activation, as blockade of these two events by MK801, l-NAME or PBN inhibited cyanide-induced up-regulation of Bcl-X(S) and Bax.	Cyanides	181-188	BCL2 associated X, apoptosis regulator	Homo sapiens	227-230
12065643-10	2002	Up-regulation of pro-apoptotic Bcl-X(S) and Bax contributed to cyanide-induced cytochrome c release, because SN50 and a specific Bax antisense oligodeoxynucleotide significantly reduced release of cytochrome c from mitochondria as shown by western blot analysis.	Cyanides	63-70	BCL2 like 1	Homo sapiens	31-36
12065643-10	2002	Up-regulation of pro-apoptotic Bcl-X(S) and Bax contributed to cyanide-induced cytochrome c release, because SN50 and a specific Bax antisense oligodeoxynucleotide significantly reduced release of cytochrome c from mitochondria as shown by western blot analysis.	Cyanides	63-70	BCL2 associated X, apoptosis regulator	Homo sapiens	44-47
12065643-10	2002	Up-regulation of pro-apoptotic Bcl-X(S) and Bax contributed to cyanide-induced cytochrome c release, because SN50 and a specific Bax antisense oligodeoxynucleotide significantly reduced release of cytochrome c from mitochondria as shown by western blot analysis.	Cyanides	63-70	cytochrome c, somatic	Homo sapiens	79-91
12065643-10	2002	Up-regulation of pro-apoptotic Bcl-X(S) and Bax contributed to cyanide-induced cytochrome c release, because SN50 and a specific Bax antisense oligodeoxynucleotide significantly reduced release of cytochrome c from mitochondria as shown by western blot analysis.	Cyanides	63-70	BCL2 associated X, apoptosis regulator	Homo sapiens	129-132
12065643-10	2002	Up-regulation of pro-apoptotic Bcl-X(S) and Bax contributed to cyanide-induced cytochrome c release, because SN50 and a specific Bax antisense oligodeoxynucleotide significantly reduced release of cytochrome c from mitochondria as shown by western blot analysis.	Cyanides	63-70	cytochrome c, somatic	Homo sapiens	197-209
12065643-11	2002	It was concluded that NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax is involved in regulating cytochrome c release in cyanide-induced apoptosis.	Cyanides	125-132	nuclear factor kappa B subunit 1	Homo sapiens	22-31
12065643-11	2002	It was concluded that NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax is involved in regulating cytochrome c release in cyanide-induced apoptosis.	Cyanides	125-132	BCL2 like 1	Homo sapiens	58-63
12065643-11	2002	It was concluded that NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax is involved in regulating cytochrome c release in cyanide-induced apoptosis.	Cyanides	125-132	BCL2 associated X, apoptosis regulator	Homo sapiens	71-74
12065643-11	2002	It was concluded that NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax is involved in regulating cytochrome c release in cyanide-induced apoptosis.	Cyanides	125-132	cytochrome c, somatic	Homo sapiens	101-113
12065643-0	2002	NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax contributes to cytochrome c release in cyanide-induced apoptosis.	Cyanides	92-99	nuclear factor kappa B subunit 1	Homo sapiens	0-9
12065643-0	2002	NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax contributes to cytochrome c release in cyanide-induced apoptosis.	Cyanides	92-99	BCL2 like 1	Homo sapiens	36-41
12065643-0	2002	NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax contributes to cytochrome c release in cyanide-induced apoptosis.	Cyanides	92-99	BCL2 associated X, apoptosis regulator	Homo sapiens	49-52
12065643-0	2002	NF-kappaB-mediated up-regulation of Bcl-X(S) and Bax contributes to cytochrome c release in cyanide-induced apoptosis.	Cyanides	92-99	cytochrome c, somatic	Homo sapiens	68-80
12065643-1	2002	Cyanide induces apoptosis through cytochrome c activated caspase cascade in primary cultured cortical neurons.	Cyanides	0-7	cytochrome c, somatic	Homo sapiens	34-46
12065643-2	2002	The underlying mechanism for cytochrome c release from mitochondria after cyanide treatment is still unclear.	Cyanides	74-81	cytochrome c, somatic	Homo sapiens	29-41
12065643-3	2002	In this study, the roles of endogenous Bcl-2 proteins in cyanide-induced apoptosis were investigated.	Cyanides	57-64	BCL2 apoptosis regulator	Homo sapiens	39-44
12065643-4	2002	After cyanide (100-500 microm) treatment for 24 h, two pro-apoptotic Bcl-2 proteins, Bcl-X(S) and Bax were up-regulated as shown by western blot and RT-PCR analysis.	Cyanides	6-13	BCL2 apoptosis regulator	Homo sapiens	69-74
12065643-4	2002	After cyanide (100-500 microm) treatment for 24 h, two pro-apoptotic Bcl-2 proteins, Bcl-X(S) and Bax were up-regulated as shown by western blot and RT-PCR analysis.	Cyanides	6-13	BCL2 like 1	Homo sapiens	85-90
12065643-4	2002	After cyanide (100-500 microm) treatment for 24 h, two pro-apoptotic Bcl-2 proteins, Bcl-X(S) and Bax were up-regulated as shown by western blot and RT-PCR analysis.	Cyanides	6-13	BCL2 associated X, apoptosis regulator	Homo sapiens	98-101
12065643-5	2002	The expression levels of two antiapoptotic Bcl-2 proteins, Bcl-2 and Bcl-X(L), remained unchanged after cyanide treatment, whereas the mRNA levels of Bcl-X(S) and Bax began to increase within 2 h and their protein levels increased 6 h after treatment.	Cyanides	104-111	BCL2 apoptosis regulator	Homo sapiens	43-48
12065643-6	2002	NF-kappaB, a redox-sensitive transcription factor activated after cyanide treatment, is responsible for the up-regulation of Bcl-X(S) and Bax.	Cyanides	66-73	nuclear factor kappa B subunit 1	Homo sapiens	0-9
12065643-6	2002	NF-kappaB, a redox-sensitive transcription factor activated after cyanide treatment, is responsible for the up-regulation of Bcl-X(S) and Bax.	Cyanides	66-73	BCL2 like 1	Homo sapiens	125-130
12065643-6	2002	NF-kappaB, a redox-sensitive transcription factor activated after cyanide treatment, is responsible for the up-regulation of Bcl-X(S) and Bax.	Cyanides	66-73	BCL2 associated X, apoptosis regulator	Homo sapiens	138-141
11925162-6	2002	The rate law of the cyanide exchange on the protonated complex is also purely second order, with (k(2)(PdH,CN))(298) = (4.5 +/- 1.3) x 10(3) s(-1) mol(-1) kg.	Cyanides	20-27	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	103-106
12087190-6	2002	The steady-state level of Waox1a and Waox1c transcripts increased under cold stress, while only that of Waox1a was increased by cyanide treatment.	Cyanides	128-135	ubiquinol oxidase 1a, mitochondrial	Triticum aestivum	104-110
11841242-4	2002	Cyanide and carbon monoxide trapping studies reveal that hydroxyurea oxidizes deoxyhemoglobin to methemoglobin and reduces methemoglobin to deoxyhemoglobin.	Cyanides	0-7	hemoglobin subunit gamma 2	Homo sapiens	123-136
11792862-3	2002	When carotid bodies isolated from wild-type mice were exposed to either cyanide or hypoxia, a marked increase in sinus nerve activity was recorded, whereas carotid bodies from Hif1a(+/-) mice responded to cyanide but not to hypoxia.	Cyanides	205-212	hypoxia inducible factor 1, alpha subunit	Mus musculus	176-181
11803471-3	2002	Hypoglycaemia attenuates cyanide-mediated transcription in non-transformed HIF-1 wild-type CHO cells but not the human tumour derived cell line.	Cyanides	25-32	hypoxia inducible factor 1 subunit alpha	Homo sapiens	75-80
12455380-3	2002	Activity of peroxidase in extracellular solution after a 1 h incubation and removal of roots was shown to be stimulated by the range of organic acids, detergents, metals, and to be inhibited by cyanide.	Cyanides	194-201	peroxidase-like	Triticum aestivum	12-22
11790120-3	2002	The ATR-FTIR method has been used to record redox difference spectra of cytochrome c oxidase in the unligated and cyanide-ligated states.	Cyanides	114-121	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	72-92
11700991-0	2001	Assay of superoxide dismutase: cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide.	Cyanides	107-114	superoxide dismutase 1	Homo sapiens	9-29
11705390-0	2001	Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.	Cyanides	38-45	myeloperoxidase	Homo sapiens	6-21
11705390-1	2001	The 1.9 A X-ray crystal structure of human myeloperoxidase complexed with cyanide (R = 0.175, R(free) = 0.215) indicates that cyanide binds to the heme iron with a bent Fe-C-N angle of approximately 157 degrees, and binding is accompanied by movement of the iron atom by 0.2 A into the porphyrin plane.	Cyanides	74-81	myeloperoxidase	Homo sapiens	43-58
11705390-1	2001	The 1.9 A X-ray crystal structure of human myeloperoxidase complexed with cyanide (R = 0.175, R(free) = 0.215) indicates that cyanide binds to the heme iron with a bent Fe-C-N angle of approximately 157 degrees, and binding is accompanied by movement of the iron atom by 0.2 A into the porphyrin plane.	Cyanides	126-133	myeloperoxidase	Homo sapiens	43-58
11705390-5	2001	The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding.	Cyanides	139-146	myeloperoxidase	Homo sapiens	158-173
11705390-5	2001	The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding.	Cyanides	205-212	myeloperoxidase	Homo sapiens	158-173
11700991-5	2001	Cyanide reacted with cytochrome c, but not XTT, in a concentration- and time-dependent manner and thus diminished its reducibility by superoxide.	Cyanides	0-7	cytochrome c, somatic	Homo sapiens	21-33
11714168-4	2001	The detection and quantification of cyanide and methemoglobin in biological samples from the case indicated that the lethal effect was due to both metabolic products (cyanide and methemoglobin).	Cyanides	36-43	hemoglobin subunit gamma 2	Homo sapiens	179-192
11714168-4	2001	The detection and quantification of cyanide and methemoglobin in biological samples from the case indicated that the lethal effect was due to both metabolic products (cyanide and methemoglobin).	Cyanides	167-174	hemoglobin subunit gamma 2	Homo sapiens	48-61
11575729-1	2001	Beta-cyanoalanine synthase (CAS, L-3-cyanoalanine synthase; EC 4.4.1.9) is the most important enzyme in cyanide metabolism.	Cyanides	104-111	bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial	Solanum tuberosum	0-26
11578192-1	2001	Ligand substitution equilibria of different alkylcobalamins (RCbl, R = Me, CH(2)Br, CH(2)CF(3), CHF(2), CF(3)) with cyanide have been studied.	Cyanides	116-123	hes related family bHLH transcription factor with YRPW motif 1	Homo sapiens	96-101
11578192-3	2001	The formation constants K(CN) for the 1:1 cyanide adducts (R(CN)Cbl) were found to be 0.38 +/- 0.03, 0.43 +/- 0.03, and 123 +/- 9 M(-1) for R = Me, CH(2)Br, and CF(3), respectively.	Cyanides	42-49	Cbl proto-oncogene	Homo sapiens	64-67
11513966-1	2001	Using spectroscopic techniques we studied the effect of the nucleophilic reagents cyanide, cyanate and thiocyanate on three flavo-oxidases namely alcohol oxidase (AO), glucose oxidase (GOX) and D-amino acid oxidase (DAOX).	Cyanides	82-89	hydroxyacid oxidase 1	Homo sapiens	168-183
11575729-1	2001	Beta-cyanoalanine synthase (CAS, L-3-cyanoalanine synthase; EC 4.4.1.9) is the most important enzyme in cyanide metabolism.	Cyanides	104-111	bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial	Solanum tuberosum	28-31
11060302-10	2001	NIT4 may play a role in cyanide detoxification during ethylene biosynthesis because extracts from senescent leaves of A. thaliana showed higher Ala(CN) hydratase/nitrilase activities than extracts from nonsenescent tissue.	Cyanides	24-31	nitrilase 4	Arabidopsis thaliana	0-4
11410286-4	2001	The distal residue hinders the access to the iron(III) center of hemin-HSA to small anionic ligands like azide and cyanide and destabilizes the binding of neutral diatomics like dioxygen and carbon monoxide to the iron(II) form.	Cyanides	115-122	albumin	Homo sapiens	71-74
11371207-0	2001	FTIR studies of the CO and cyanide adducts of fully reduced bovine cytochrome c oxidase.	Cyanides	27-34	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	67-87
11371207-1	2001	Photolysis spectra of the CO and cyanide adducts of reduced bovine cytochrome c oxidase have been studied by FTIR difference spectroscopy.	Cyanides	33-40	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	67-87
11377697-5	2001	Reaction of trans-[Au(CN)(2)X(2)](-) (X(-)=Cl(-) and Br(-)) or [AuCl(4)](-) with HCN in aqueous solution at pH 7.4 leads directly to [Au(CN)(4)](-) without detection of the anticipated [Au(CN)(x)X(4-x)](-)intermediates, which is attributed to the cis- and trans-accelerating effects of the cyanides.	Cyanides	290-298	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	81-84
11258981-6	2001	The myeloperoxidase-catalyzed reaction with 0.3 mM NO(2)(-) was completely inhibited by 1 mM cyanide, and not effected by 100 mM chloride with or without 1 mM taurine.	Cyanides	93-100	myeloperoxidase	Homo sapiens	4-19
11311573-0	2001	Diagnosis of cyanide intoxication by measurement of cytochrome c oxidase activity.	Cyanides	13-20	cytochrome c, somatic	Homo sapiens	52-64
11311573-1	2001	Cytochrome c oxidase (CCO), a mitochondrial enzyme, is inactivated by cyanide or carbon monoxide (CO) intoxication.	Cyanides	70-77	cytochrome c, somatic	Homo sapiens	0-12
11564419-1	2001	The aim of the present study was to analyze the effect of chemical hypoxia (cyanide) on the membrane potential of hippocampal CA1 neurons and to elucidate the reason for previously found differences in the reaction to hypoxia in these cells.	Cyanides	76-83	carbonic anhydrase 1	Rattus norvegicus	126-129
11564419-8	2001	In conclusion, chemical hypoxia with cyanide changes the membrane potential in CA1 cells in size and direction depending on the original resting potential of the cells.	Cyanides	37-44	carbonic anhydrase 1	Rattus norvegicus	79-82
11216837-4	2001	The maize NADH-dependent O2*--synthase activity could clearly be differentiated from peroxidase-mediated O2*--synthesizing activity by its insensitivity to cyanide and azide, as well as by its much higher affinity to O2.	Cyanides	156-163	peroxidase 1	Zea mays	85-95
11254178-1	2001	Cyanide detoxification is catalysed by two enzymes: rhodanese [thiosulphate: cyanide sulphurtransferase, E.C.	Cyanides	0-7	thiosulfate sulfurtransferase	Bos taurus	52-61
10900173-9	2000	A variety of inhibitors which act at different levels of the mitochondrial electron transport chain (rotenone, theonyltrifluoroacetone, antimycin A, cyanide) also inhibited activation of the ERK MAPKs by hydrogen peroxide but not TPA or hyperosmotic shock.	Cyanides	149-156	mitogen-activated protein kinase 1	Homo sapiens	191-194
11154562-2	2000	Under these conditions rate-determining Co-C heterolytic cleavage is preceded by rapid addition of cyanide to AdoCbl to form an intermediate, (beta-5"-deoxyadenosyl)(alpha-cyano)cobalamin ((beta-Ado)(alpha-CN)Cbl-), identified by 1H NMR spectroscopy.	Cyanides	99-106	Cbl proto-oncogene	Homo sapiens	113-116
11154562-7	2000	A mechanism in 92% DMF/8% D2O is proposed which involves rapid reversible formation of (beta-Ado)(alpha-CN)Cbl- from base-off AdoCbl plus cyanide, followed by rate-determining solvent-assisted cleavage of the Co-C bond of the intermediate and subsequent rapid addition of a second cyanide to give the products.	Cyanides	138-145	Cbl proto-oncogene	Homo sapiens	107-110
11154562-7	2000	A mechanism in 92% DMF/8% D2O is proposed which involves rapid reversible formation of (beta-Ado)(alpha-CN)Cbl- from base-off AdoCbl plus cyanide, followed by rate-determining solvent-assisted cleavage of the Co-C bond of the intermediate and subsequent rapid addition of a second cyanide to give the products.	Cyanides	281-288	Cbl proto-oncogene	Homo sapiens	107-110
10956427-3	2000	Because myeloperoxidase catalyses cyanide production in leukocytes, a selective myeloperoxidase inhibitor (aminobenzoic acid hydrazide) was tested and found to inhibit opiate agonist-induced cyanide production in pheochromocytoma cells and also in rat brain.	Cyanides	34-41	myeloperoxidase	Rattus norvegicus	8-23
10956427-3	2000	Because myeloperoxidase catalyses cyanide production in leukocytes, a selective myeloperoxidase inhibitor (aminobenzoic acid hydrazide) was tested and found to inhibit opiate agonist-induced cyanide production in pheochromocytoma cells and also in rat brain.	Cyanides	34-41	myeloperoxidase	Rattus norvegicus	80-95
10956427-3	2000	Because myeloperoxidase catalyses cyanide production in leukocytes, a selective myeloperoxidase inhibitor (aminobenzoic acid hydrazide) was tested and found to inhibit opiate agonist-induced cyanide production in pheochromocytoma cells and also in rat brain.	Cyanides	191-198	myeloperoxidase	Rattus norvegicus	8-23
10956427-3	2000	Because myeloperoxidase catalyses cyanide production in leukocytes, a selective myeloperoxidase inhibitor (aminobenzoic acid hydrazide) was tested and found to inhibit opiate agonist-induced cyanide production in pheochromocytoma cells and also in rat brain.	Cyanides	191-198	myeloperoxidase	Rattus norvegicus	80-95
11035248-4	2000	To obtain direct evidence on this question, in particular, as concerns the in vivo control of respiration by cytochrome c oxidase (COX), we have developed an approach for measuring COX activity in intact cells, by means of cyanide titration, either as an isolated step or as a respiratory chain-integrated step.	Cyanides	223-230	cytochrome c oxidase subunit 8A	Homo sapiens	131-134
11035248-4	2000	To obtain direct evidence on this question, in particular, as concerns the in vivo control of respiration by cytochrome c oxidase (COX), we have developed an approach for measuring COX activity in intact cells, by means of cyanide titration, either as an isolated step or as a respiratory chain-integrated step.	Cyanides	223-230	cytochrome c oxidase subunit 8A	Homo sapiens	181-184
11091434-0	2000	Novel Group-Transfer Three-Component Coupling of Silyltellurides, Carbonyl Compounds, and Isocyanides This work was partly supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture, Japan.	Cyanides	90-101	activation induced cytidine deaminase	Homo sapiens	147-150
10869507-8	2000	Increased exposure to GCs worsened the decline in metabolism in dentate gyrus explants induced by hypoglycemia, and in CA1 explants induced by cyanide (after eliminating the effects of glial release of lactate for the support of neuronal metabolism).	Cyanides	143-150	carbonic anhydrase 1	Rattus norvegicus	119-122
10920253-6	2000	On the other hand, cyanide induced a change in the spectrum of ferric P450(SPalpha) to one characteristic of cyanide-bound form of ferric P450.	Cyanides	19-26	CD5 molecule like	Homo sapiens	70-82
10920253-6	2000	On the other hand, cyanide induced a change in the spectrum of ferric P450(SPalpha) to one characteristic of cyanide-bound form of ferric P450.	Cyanides	109-116	CD5 molecule like	Homo sapiens	70-82
11360649-3	1999	Cytochrome C oxidase activity was measured by the rate of cyanide-sensitive oxidation of reduced cytochrome C using luminosity photographer.	Cyanides	58-65	cytochrome c, somatic	Homo sapiens	0-12
10851038-6	2000	The reaction is not sensitive to high concentrations of cyanide, which allows the separate determination of Cu,Zn- and Mn-SOD in mixtures.	Cyanides	56-63	superoxide dismutase 2	Homo sapiens	119-125
10766803-6	2000	The backward transition from the closed to the open conformation was the reason for the identical rate-limiting steps during substitution of H(2)O in TC.Cbl.OH(2) for cyanide or azide according to the reaction TC(Cbl) --> TC.Cbl.OH(2) + CN(-)/N(3)(-).	Cyanides	167-174	Cbl proto-oncogene	Homo sapiens	153-156
10766803-6	2000	The backward transition from the closed to the open conformation was the reason for the identical rate-limiting steps during substitution of H(2)O in TC.Cbl.OH(2) for cyanide or azide according to the reaction TC(Cbl) --> TC.Cbl.OH(2) + CN(-)/N(3)(-).	Cyanides	167-174	Cbl proto-oncogene	Homo sapiens	213-216
10766803-6	2000	The backward transition from the closed to the open conformation was the reason for the identical rate-limiting steps during substitution of H(2)O in TC.Cbl.OH(2) for cyanide or azide according to the reaction TC(Cbl) --> TC.Cbl.OH(2) + CN(-)/N(3)(-).	Cyanides	167-174	Cbl proto-oncogene	Homo sapiens	213-216
10764633-0	2000	Cyanide-induced apoptosis involves oxidative-stress-activated NF-kappaB in cortical neurons.	Cyanides	0-7	nuclear factor kappa B subunit 1	Homo sapiens	62-71
10764633-7	2000	Nuclear factor kappaB (NF-kappaB), a redox-sensitive transcription factor, was activated dose dependently after cyanide treatment.	Cyanides	112-119	nuclear factor kappa B subunit 1	Homo sapiens	23-32
10764633-9	2000	SN50, a synthetic peptide which inhibits the nuclear translocation of NF-kappaB, blocked cyanide-induced apoptotic cell death.	Cyanides	89-96	nuclear factor kappa B subunit 1	Homo sapiens	70-79
10764633-10	2000	These results indicate that NF-kappaB plays an important role in cyanide-induced apoptosis in cortical neurons, and the caspases may contribute in part to the activation of NF-kappaB after cyanide treatment by inducing the late phase of ROS generation.	Cyanides	65-72	nuclear factor kappa B subunit 1	Homo sapiens	28-37
10764633-10	2000	These results indicate that NF-kappaB plays an important role in cyanide-induced apoptosis in cortical neurons, and the caspases may contribute in part to the activation of NF-kappaB after cyanide treatment by inducing the late phase of ROS generation.	Cyanides	189-196	nuclear factor kappa B subunit 1	Homo sapiens	28-37
10764633-10	2000	These results indicate that NF-kappaB plays an important role in cyanide-induced apoptosis in cortical neurons, and the caspases may contribute in part to the activation of NF-kappaB after cyanide treatment by inducing the late phase of ROS generation.	Cyanides	189-196	nuclear factor kappa B subunit 1	Homo sapiens	173-182
10719376-6	2000	Linoleic acid, an abundant free fatty acid in plants which activates UCP, strongly inhibits cyanide-resistant respiration mediated by AOX.	Cyanides	92-99	putative uncoupling protein	Solanum lycopersicum	69-72
10723097-6	2000	When cyanide and ATP were added together, the expression of c-fos and zif268 expression was inhibited, and the effect was mimicked by simulating chemical hypoxia with sodium azide.	Cyanides	5-12	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	60-65
10723097-6	2000	When cyanide and ATP were added together, the expression of c-fos and zif268 expression was inhibited, and the effect was mimicked by simulating chemical hypoxia with sodium azide.	Cyanides	5-12	early growth response 1	Rattus norvegicus	70-76
10656833-7	2000	Structures of the non-specific cyanide and specific 3-amino-1,2, 4-triazole inhibitor complexes of human catalase identify their modes of inhibition and help reveal the catalytic mechanism of catalase.	Cyanides	31-38	catalase	Homo sapiens	105-113
10656833-7	2000	Structures of the non-specific cyanide and specific 3-amino-1,2, 4-triazole inhibitor complexes of human catalase identify their modes of inhibition and help reveal the catalytic mechanism of catalase.	Cyanides	31-38	catalase	Homo sapiens	192-200
18967859-3	2000	Flux of cyanide complexes and corresponding free cyanide are determined using five commercial anion exchanger membranes (AMV, ACS, RAI 5035, ADP and ADS).	Cyanides	8-15	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	126-129
18967859-5	2000	It is observed that the species number in the feed solution influences the transfer selectivity of metal ion complex against free cyanide Thus, gold which forms only one stable species with cyanides is transferred faster through an ACS membrane than copper which forms three species.	Cyanides	130-137	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	232-235
18967859-5	2000	It is observed that the species number in the feed solution influences the transfer selectivity of metal ion complex against free cyanide Thus, gold which forms only one stable species with cyanides is transferred faster through an ACS membrane than copper which forms three species.	Cyanides	190-198	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	232-235
10722152-2	2000	Their potency ranged from 1.1 to > 100 microM; the best ones compare very favorably with that of the novel cyano-containing 5,6-seco-cholesteryl acid 1 (IC50=2.2microM) reported by us recently (Peng, H.; Zalkow, L. H.; Abraham, R. T.; Powis, G. J. Med.	Cyanides	110-115	mediator complex subunit 25	Homo sapiens	148-154
10849697-12	2000	The responses to cyanide were augmented in NOS-1; whereas they were blunted in NOS-3 mutant mice.	Cyanides	17-24	nitric oxide synthase 1, neuronal	Mus musculus	43-48
10849697-12	2000	The responses to cyanide were augmented in NOS-1; whereas they were blunted in NOS-3 mutant mice.	Cyanides	17-24	nitric oxide synthase 3, endothelial cell	Mus musculus	79-84
10506943-0	1999	Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: molecular properties and mode of detoxification.	Cyanides	56-63	mercaptopyruvate sulfurtransferase	Rattus norvegicus	0-34
10506943-10	1999	MST then detoxifies cyanide again in cooperation with rhodanese in mitochondria.	Cyanides	20-27	mercaptopyruvate sulfurtransferase	Rattus norvegicus	0-3
10506943-10	1999	MST then detoxifies cyanide again in cooperation with rhodanese in mitochondria.	Cyanides	20-27	thiosulfate sulfurtransferase	Rattus norvegicus	54-63
10506943-11	1999	Tissues other than the liver and kidney are more susceptible to cyanide toxicity because they contain less MST and rhodanese.	Cyanides	64-71	mercaptopyruvate sulfurtransferase	Rattus norvegicus	107-110
10506943-11	1999	Tissues other than the liver and kidney are more susceptible to cyanide toxicity because they contain less MST and rhodanese.	Cyanides	64-71	thiosulfate sulfurtransferase	Rattus norvegicus	115-124
10502679-9	1999	The EPR results for cytochrome b(558) activated with arachidonic acid showed that the transient high-spin ferric heme can bind cyanide.	Cyanides	127-134	cytochrome b	Sus scrofa	20-32
10502679-11	1999	)(-) production of cytochrome b(558) in cell-free assays in the presence of cyanide.	Cyanides	76-83	cytochrome b	Sus scrofa	19-31
10540878-8	1999	6) By ligation of sciatic nerves, B12 bound to nerves was released from nerve tissues and cyanide ions were later released, though its mechanisms remains unknown.	Cyanides	90-97	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	34-37
10462537-9	1999	)radicals</compound-id> is completely blocked by myeloperoxidase inhibitors, cyanide and azide.	Cyanides	77-84	myeloperoxidase	Homo sapiens	49-64
10441390-1	1999	We have previously shown that exposure of Clone 9 cells to hypoxia, cyanide, or azide results in an acute stimulation of glucose transport that is largely mediated by "activation" of glucose transporter (Glut1) sites preexisting in the plasma membrane.	Cyanides	68-75	solute carrier family 2 member 1	Rattus norvegicus	204-209
10444490-6	1999	Immunofluorescence studies demonstrated translocation of GLUT-4 to the myocyte sarcolemma in response to stimulation with AICAR, cyanide, or insulin.	Cyanides	129-136	solute carrier family 2 member 4	Rattus norvegicus	57-63
10423453-0	1999	Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study.	Cyanides	0-7	myoglobin	Physeter catodon	68-77
10423453-5	1999	On the other hand, the crystal structure of the L. pectinata HbI:cyanide derivative at 100 K shows that the diatomic ligand is coordinated to the iron atom in an orientation almost perpendicular to the heme (the Fe-C distance being 1.95 A), adopting a coordination geometry strictly reminescent of that observed in sperm whale Mb, at room temperature.	Cyanides	65-72	myoglobin	Physeter catodon	327-329
10601869-2	2000	Assignment of three heme methyl resonances of the isocyanide adduct of cytochrome P450 in the ferric low-spin state was recently performed using electron exchange in the presence of putidaredoxin [Mouro, C., Bondon, A., Jung, C., Hui Bon Hoa, G., De Certaines, J.D., Spencer, R.G.S.	Cyanides	50-60	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	71-86
11360649-3	1999	Cytochrome C oxidase activity was measured by the rate of cyanide-sensitive oxidation of reduced cytochrome C using luminosity photographer.	Cyanides	58-65	cytochrome c, somatic	Homo sapiens	97-109
12840896-2	1999	Cytochrome c oxidase activity was determined by measuring the rate of cyanide-sensitive oxidation of reduced cytochrome c using luminosity photographer.	Cyanides	70-77	cytochrome c, somatic	Homo sapiens	0-12
10052944-7	1999	Binding of both CO and cyanide to ferrous cystathionine beta-synthase occurs in two distinct isotherms and indicates that the hemes are nonequivalent.	Cyanides	23-30	cystathionine beta-synthase	Homo sapiens	42-69
10512537-9	1999	Formation of the NO and cyanide complexes of ferrous CCP gives derivatives with MCD spectra similar to the analogous forms of HRP and Mb in both feature position and shape.	Cyanides	24-31	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	53-56
12840896-2	1999	Cytochrome c oxidase activity was determined by measuring the rate of cyanide-sensitive oxidation of reduced cytochrome c using luminosity photographer.	Cyanides	70-77	cytochrome c, somatic	Homo sapiens	109-121
10591050-4	1999	A comparison of the behaviour of rat and ox MAO revealed considerable differences in their sensitivities to pheniprazine and the potentiating effects of cyanide.	Cyanides	153-160	monoamine oxidase A	Rattus norvegicus	44-47
18924840-1	1999	This study presents a flow injection system for the sequential determination of free (CN(-)) and total (CN(-)+ HCN) cyanide using a potentiometric method which employs two different processes for the determination of these two chemical species.	Cyanides	116-123	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	111-114
10591050-3	1999	Whereas the maximum effects on pheniprazine inhibition of rat liver MAO-B occurred at about 5 microM cyanide, concentrations of 5 mM were necessary for maximum stimulation of MAO-A inhibition.	Cyanides	101-108	monoamine oxidase B	Rattus norvegicus	68-73
9819532-8	1998	This article illustrates the use of drug-induced methemoglobin as a surrogate marker for protection against cyanide intoxication.	Cyanides	108-115	hemoglobin subunit gamma 2	Homo sapiens	49-62
29711314-0	1998	Novel Cyanide Coordination Models in Layer-Type Hydrated Double Salts of AgCN and AgF.	Cyanides	6-13	angiopoietin like 6	Homo sapiens	82-85