PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
26165278-5	2015	Captured GOx catalyzed the reduction of Fe(CN)6(3-) to Fe(CN)6(4-), which was oxidized electrochemically to determine the captured albumin.	fe(cn)6	40-47	hydroxyacid oxidase 1	Homo sapiens	9-12
26165278-5	2015	Captured GOx catalyzed the reduction of Fe(CN)6(3-) to Fe(CN)6(4-), which was oxidized electrochemically to determine the captured albumin.	fe(cn)6	55-62	hydroxyacid oxidase 1	Homo sapiens	9-12
23911771-8	2013	Experimental conditions were optimised and a linear relationship was observed between the peak current of [Fe(CN)6](3-)/[Fe(CN)6](4-) and the concentration of TnT in buffer over the range 0.009-0.8 ng/mL, with a detection limit of 9 pg/mL.	fe(cn)6	107-114	troponin T1, slow skeletal type	Homo sapiens	159-162
24389061-4	2014	Accompanying the sandwiched immunocomplex, the conjugated GOx could catalyze the oxidation of glucose, simultaneously resulting in the conversion of [Fe(CN)6](3-) to [Fe(CN)6](4-).	fe(cn)6	150-157	hydroxyacid oxidase 1	Homo sapiens	58-61
24460092-11	2014	By monitoring Fe(CN)6(3-/4-) taking place at the TC-modified electrodes in pH 7 solutions, we observed that the adsorption of GOx imposed impedance on Fe(CN)6(3-/4-).	fe(cn)6	14-21	hydroxyacid oxidase 1	Homo sapiens	126-129
24460092-11	2014	By monitoring Fe(CN)6(3-/4-) taking place at the TC-modified electrodes in pH 7 solutions, we observed that the adsorption of GOx imposed impedance on Fe(CN)6(3-/4-).	fe(cn)6	151-158	hydroxyacid oxidase 1	Homo sapiens	126-129
23911771-8	2013	Experimental conditions were optimised and a linear relationship was observed between the peak current of [Fe(CN)6](3-)/[Fe(CN)6](4-) and the concentration of TnT in buffer over the range 0.009-0.8 ng/mL, with a detection limit of 9 pg/mL.	fe(cn)6	121-128	troponin T1, slow skeletal type	Homo sapiens	159-162
24162097-0	2013	Sensitive electrochemical immunoassay of metallothionein-3 based on K3[Fe(CN)6] as a redox-active signal and C-dots/Nafion film for antibody immobilization.	fe(cn)6	71-78	metallothionein 3	Homo sapiens	41-58
24245933-4	2013	The results demonstrate that Gd(3+)/[Fe(CN)6](3-) nanoparticles have r1p and r2p relaxivities about four times higher than the values observed in the same conditions for the commercial Contrast Agents (CAs) ProHance or Omniscan, regardless of the stabilizing agent used, while nanoparticles of Prussian blue and its analogues M(2+)/[Fe(CN)6](3-) (M = Ni, Cu, Fe) present relatively modest values.	fe(cn)6	37-44	CD1b molecule	Homo sapiens	69-72
24245933-4	2013	The results demonstrate that Gd(3+)/[Fe(CN)6](3-) nanoparticles have r1p and r2p relaxivities about four times higher than the values observed in the same conditions for the commercial Contrast Agents (CAs) ProHance or Omniscan, regardless of the stabilizing agent used, while nanoparticles of Prussian blue and its analogues M(2+)/[Fe(CN)6](3-) (M = Ni, Cu, Fe) present relatively modest values.	fe(cn)6	37-44	CD1e molecule	Homo sapiens	77-80
11893069-5	2001	Likewise, negatively charged aspartic acid peptides interacted with the positively charged sites of cytfand cyt c, and competitively inhibited electron transfer from reduced cytfor cyt c to oxidized PC and from [Fe(CN)6]4- to oxidized cyt c.	fe(cn)6	212-219	cytochrome c, somatic	Homo sapiens	108-113
23830440-4	2013	With this new selected aptamer, a novel electrochemical label-free codeine aptamer biosensor based on Au-mesoporous silica nanoparticles (Au-MSN) as immobilized substrate has been proposed using [Fe(CN)6](3-/4-) as electroactive redox probe.	fe(cn)6	196-203	moesin	Homo sapiens	141-144
19362182-5	2009	After electrode preparation, the detection of thrombin was investigated in the presence of the reversible [Fe(CN)6](3-/4-) redox couple using impedance technique.	fe(cn)6	107-114	coagulation factor II, thrombin	Homo sapiens	46-54
23811556-3	2013	In vitro, a variety of aconitase-inhibitors, such as fluorocitrate, cyanide ion, ferricyanide ([Fe(CN)6]), and various oxidants including superoxide anion, inhibited the activity of m-aconitase even in the presence of Fe(II), whereas a NO-donor, nitroprusside (SNP) ([Fe(CN)5NO]), was the only agent that significantly increased activity of that enzyme.	fe(cn)6	96-103	aconitase 2	Homo sapiens	182-193
20126733-0	2010	Microscale hexagonal rods of a charge-assisted second-sphere coordination compound [Co(DABP)3][Fe(CN)6].	fe(cn)6	95-102	D-box binding PAR bZIP transcription factor	Homo sapiens	87-91
18187315-1	2008	Electrochemical label free DNA hybridization discrimination of the brain tumor sequence CK20 has been made at the gold-thiol and thiol diluent binary and ternary mixed monolayer interfaces in presence of the [Fe(CN)6](3-) and double stranded DNA (dsDNA) specific cationic intercalators, proflavine (PF) and methylene blue (MB), respectively.	fe(cn)6	209-216	keratin 20	Homo sapiens	88-92
17378614-6	2007	Differences in the rho values in the Hammett plots for NaClO2 and K3[Fe(CN)6] asymmetric dihydroxylations indicate that in dihydroxylations with NaClO2 as the secondary oxidant, the reactive osmium(VI) mono(glycolate) is oxidized to osmium(VIII) mono(glycolate) prior to hydrolysis.	fe(cn)6	69-76	cytochrome c oxidase subunit 8A	Homo sapiens	240-244
16212053-3	2005	It was shown that the mechanism of the catalysis involves specific binding of [Fe(CN)6]4- to the protein at the His119(GH1) region, which is in agreement with a large positive electrostatic potential and the presence at this site of Mb of a cavity large enough to accommodate [Fe(CN)6]4- anion.	fe(cn)6	79-86	somatotropin	Physeter catodon	119-122
11893069-5	2001	Likewise, negatively charged aspartic acid peptides interacted with the positively charged sites of cytfand cyt c, and competitively inhibited electron transfer from reduced cytfor cyt c to oxidized PC and from [Fe(CN)6]4- to oxidized cyt c.	fe(cn)6	212-219	cytochrome c, somatic	Homo sapiens	181-186
11893069-5	2001	Likewise, negatively charged aspartic acid peptides interacted with the positively charged sites of cytfand cyt c, and competitively inhibited electron transfer from reduced cytfor cyt c to oxidized PC and from [Fe(CN)6]4- to oxidized cyt c.	fe(cn)6	212-219	cytochrome c, somatic	Homo sapiens	181-186
1390826-1	1992	Electron-transfer reactions of myoglobin, hemocyanin and hemerythrin with the inorganic complexes [Fe(CN)6]3- (oxidant) and [Co(sep)]2+ (reductant) are considered.	fe(cn)6	99-106	myoglobin	Equus caballus	31-40
34517645-6	2021	Under the optimal conditions of 30 mM K3(Fe(CN)6), OD600 = 1 cell concentration, and 50 mM phosphate-buffered solution (PBS), the half-maximal inhibitory concentration (IC50) values measured for Cd2+, Cu2+ and Ni2+ were 3.99 mg/L, 1.16 mg/L and 2.37 mg/L, respectively.	fe(cn)6	41-48	CD2 molecule	Homo sapiens	195-198
33862074-6	2021	Catalytic studies indicate that electron-rich or poor aromatic halides were smoothly cyanated with good reaction yields by Pd NPs/CS/Co3O4 catalyst by using K4[Fe(CN)6] as the cyanating agent.	fe(cn)6	160-167	citrate synthase	Homo sapiens	130-132
184452-1	1976	The reactions of horse heart cytochrome c with Fe(ethylenediaminetetraacetate)2-, Co(1,10-phenanthroline)3(3+), Ru(NH3)6(2+), and Fe(CN)6(3-) have been analyzed within the formalism of the Marcus theory of outer-sphere electron transfer, including compensation for electrostatic interactions.	fe(cn)6	130-137	cytochrome c, somatic	Equus caballus	29-41
35272213-3	2022	It is found that the Fe2+-based MOF (MOF-Fe2+) can act as the Fe2+ source to react with K3(Fe(CN)6), leading to the in-situ formation of prussian blue (PB) on MOF-Fe2+.	fe(cn)6	91-98	lysine acetyltransferase 8	Homo sapiens	32-35
35272213-3	2022	It is found that the Fe2+-based MOF (MOF-Fe2+) can act as the Fe2+ source to react with K3(Fe(CN)6), leading to the in-situ formation of prussian blue (PB) on MOF-Fe2+.	fe(cn)6	91-98	lysine acetyltransferase 8	Homo sapiens	37-45
35272213-3	2022	It is found that the Fe2+-based MOF (MOF-Fe2+) can act as the Fe2+ source to react with K3(Fe(CN)6), leading to the in-situ formation of prussian blue (PB) on MOF-Fe2+.	fe(cn)6	91-98	lysine acetyltransferase 8	Homo sapiens	159-162
6268746-1	1981	Use of rigorous equilibration kinetics to evaluate rate constants for the Fe(CN)6 4- reduction of horse-heart cytochrome c in the oxidized form, cyt c (III), has shown that limiting kinetics do not apply with concentrations of Fe(CN)6 4- (the reactant in excess) in the range 2-10 x 10(-4) M, I = 0.10 M (NaCl).	fe(cn)6	74-81	cytochrome c, somatic	Equus caballus	110-122
33111821-5	2020	Cyclic voltammetry (CV) for the Nanocomposite modified electrode revealed two well-defined redox couples at -0.073 ((E1/2)1) and 0.665 mV ((E1/2)2), attributed to the conversion of Cu2+ to Cu+ and CuFe2+ CuFe3+ pairs, respectively, which is similar to those in the CuO and Cu2[Fe(CN)6]components.	fe(cn)6	277-284	RNA, U105B small nucleolar	Homo sapiens	140-146
32836089-8	2020	On the other hand, the addition of the yellow K3[Fe(CN)6] into different amounts of the produced PB was able to result in different colors, which enabled the visual detection of cTnI.	fe(cn)6	49-56	troponin I3, cardiac type	Homo sapiens	178-182
31360429-6	2019	The formation and evolution of Au(CN)2 - depends on the ratio of Fe(iii) and Fe(ii) on the surface of the gold electrode, which was determined by the redox conversion between Fe(iii) and Fe(ii) as well as the electric field force-based attraction or repulsion between the gold electrode and [Fe(CN)6]3/4-.	fe(cn)6	292-299	carnosine dipeptidase 2	Homo sapiens	31-38
32724991-9	2020	The IC50 value of 0.89 mg L-1 for BQ was obtained using K3[Fe(CN)6] as the single mediator.	fe(cn)6	59-66	L1 cell adhesion molecule	Homo sapiens	26-29
32374492-3	2020	This pro-NTA, also called PBAM, is composed of an MIL-100 (Fe)-coated Prussian blue (PB) analogue (K2 Mn[Fe(CN)6 ]) with negligible absorption in the near-infrared region and spatial confinement of Mn2+ ions.	fe(cn)6	105-112	solute carrier family 10 member 2	Homo sapiens	26-30
29473308-3	2018	The mild postsynthetic ligand exchange reaction of the presynthesized ZIF-67 TPAs with K4 [Fe(CN)6 ] in an aqueous solution at room temperature is of critical importance in achieving the final hollow nanostructure, which results in the production of CoFe(II)-PBA HTPAs that not only determine the formation of the interior voids in the nanostructure, but also provide the doping of Fe atoms to the CoP lattice.	fe(cn)6	91-98	caspase recruitment domain family member 16	Homo sapiens	398-401
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.	fe(cn)6	300-307	transmembrane p24 trafficking protein 3	Homo sapiens	27-30
27542739-6	2016	Furthermore, isothermal titration calorimetry (ITC) experiments demonstrated that K3[Fe(CN)6]is able to bind to MMP-13 and endothelial cell tube formation tests provide further evidence for this interaction to exhibit anti-angiogenesis potential.	fe(cn)6	85-92	matrix metallopeptidase 13	Homo sapiens	112-118
26415134-3	2015	The saliva sample wicks into the reaction zone on the sensing chip so that the sAA reacts with the preloaded reagents, resulting in conversion of an electron mediator Fe(CN)6(3-) to Fe(CN)6(4-).	fe(cn)6	167-174	amylase alpha 1A	Homo sapiens	79-82
26745792-5	2016	On the other hand, the hybridization with GNS further enhances the electrocatalytic activity towards Fe(CN)6(3-/4-).	fe(cn)6	101-108	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	42-45
26838859-6	2016	Under optimal experimental parameters, differential pulse voltammetry (DPV) signal changes of the [Fe(CN)6](3-/4-) are used to detect hCG with two broad linear ranges: 0.001 to 0.2 and 0.2 to 60.7 ng mL(-1).	fe(cn)6	99-106	chorionic gonadotropin subunit beta 5	Homo sapiens	134-137
26523504-3	2016	Impedimetric measurements in the presence of the redox couple [Fe(CN)6](3-/4-) showed significant changes in charge transfer resistance upon binding of CRP.	fe(cn)6	63-70	C-reactive protein	Homo sapiens	152-155
26415134-3	2015	The saliva sample wicks into the reaction zone on the sensing chip so that the sAA reacts with the preloaded reagents, resulting in conversion of an electron mediator Fe(CN)6(3-) to Fe(CN)6(4-).	fe(cn)6	182-189	amylase alpha 1A	Homo sapiens	79-82