PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 12235152-0 2002 Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Azides 72-77 heme oxygenase 1 Rattus norvegicus 25-41 12003789-8 2002 During normoxia, increases in mitochondrial ROS elicited by azide (1-2 mM) or by the mitochondrial inhibitor antimycin A caused increased phosphorylation of p38. Azides 60-65 mitogen-activated protein kinase 14 Homo sapiens 157-160 11996572-2 2002 Our approach was that of partitioning the E degrees " changes resulting from binding of imidazole, 2-methyl-imidazole, ammonia, and azide to both cytochrome c and microperoxidase-11 (MP11), into the enthalpic and entropic contributions. Azides 132-137 cytochrome c, somatic Homo sapiens 146-158 11796734-1 2002 Chronic treatment of cultured cells with very low levels of azide (I(50)<10 microm) leads to slow (t(12) = 6 h), irreversible loss of cytochrome c oxidase (COX) activity. Azides 60-65 cytochrome c oxidase subunit 8A Homo sapiens 159-162 11796734-2 2002 Azide-mediated COX losses were not accompanied by inhibition of other mitochondrial enzymes and were not dependent upon electron flux through oxidative phosphorylation. Azides 0-5 cytochrome c oxidase subunit 8A Homo sapiens 15-18 11796734-3 2002 Although azide treatment also reduced activity (but not content) of both CuZn superoxide dismutase and catalase, a spectrum of pro-oxidants (and anti-oxidants) failed to mimic (or prevent) azide effects, arguing that losses in COX activity were not due to resultant compromises in free radical scavenging. Azides 9-14 catalase Homo sapiens 103-111 11796734-3 2002 Although azide treatment also reduced activity (but not content) of both CuZn superoxide dismutase and catalase, a spectrum of pro-oxidants (and anti-oxidants) failed to mimic (or prevent) azide effects, arguing that losses in COX activity were not due to resultant compromises in free radical scavenging. Azides 9-14 cytochrome c oxidase subunit 8A Homo sapiens 227-230 11796734-7 2002 Differential azide effects on COX content relative to COX activity were confirmed using a refined inhibition time course in combination with blue native electrophoresis, and established that holoenzyme dissociation occurs subsequent to losses in catalytic activity. Azides 13-18 cytochrome c oxidase subunit 8A Homo sapiens 30-33 12545210-0 2002 The mechanism of azide activation of polyphenol oxidase II from tobacco. Azides 17-22 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 37-58 11832331-3 2002 Here, we show that azide-sensitive oxidase activity is enriched in the same fractions, correlating subcellular localization of enzyme activity with ceruloplasmin immunoreactivity. Azides 19-24 ceruloplasmin Homo sapiens 148-161 12545210-4 2002 The reason for azide acting as an activator can be attributed to azide complexing with PPO II, thus inducing the formation of CuO(2)(2-)Cu, which is the active site of the peroxide-PPO II complex in which peroxide plays the role of activator. Azides 15-20 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 87-93 12545210-4 2002 The reason for azide acting as an activator can be attributed to azide complexing with PPO II, thus inducing the formation of CuO(2)(2-)Cu, which is the active site of the peroxide-PPO II complex in which peroxide plays the role of activator. Azides 15-20 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 181-187 11904230-0 2002 The effect of anions on azide binding to myoglobin: an unusual functional modulation. Azides 24-29 myoglobin Equus caballus 41-50 11904230-1 2002 The effect of increasing concentrations of several anions on the azide (N(-)(3)) binding properties of sperm whale and horse ferric myoglobin has been studied. Azides 65-70 myoglobin Equus caballus 132-141 12545210-2 2002 The present work shows that azide can also act as an activator of polyphenol oxidase II (PPO II) from tobacco leaves. Azides 28-33 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 66-87 12545210-4 2002 The reason for azide acting as an activator can be attributed to azide complexing with PPO II, thus inducing the formation of CuO(2)(2-)Cu, which is the active site of the peroxide-PPO II complex in which peroxide plays the role of activator. Azides 65-70 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 87-93 12545210-4 2002 The reason for azide acting as an activator can be attributed to azide complexing with PPO II, thus inducing the formation of CuO(2)(2-)Cu, which is the active site of the peroxide-PPO II complex in which peroxide plays the role of activator. Azides 65-70 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 181-187 12545210-2 2002 The present work shows that azide can also act as an activator of polyphenol oxidase II (PPO II) from tobacco leaves. Azides 28-33 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 89-95 11500038-3 2001 Both hydrogen peroxide and superoxide were found to cause release of cytochrome c from the lipid encapsulated protein, which was detected from the distinct spectral changes due to the formation of the azide complex of cytochrome c in the solution. Azides 201-206 cytochrome c, somatic Homo sapiens 69-81 11514664-9 2001 In contrast, azide is bound to the oxidized heme iron in the methemoglobin crystals at an angle of 112 degrees, in a perfect orientation to accept a hydrogen bond from His63. Azides 13-18 hemoglobin subunit gamma 2 Homo sapiens 61-74 11786230-5 2001 Addition of azide (an inhibitor of both catalase and peroxidase) to the MCO systems enhanced the inactivation. Azides 12-17 catalase Homo sapiens 40-48 11500038-3 2001 Both hydrogen peroxide and superoxide were found to cause release of cytochrome c from the lipid encapsulated protein, which was detected from the distinct spectral changes due to the formation of the azide complex of cytochrome c in the solution. Azides 201-206 cytochrome c, somatic Homo sapiens 218-230 11432741-7 2001 Inhibitor studies revealed that the heterologously produced A1 ATPase is insensitive to azide, dicyclohexylcarbodiimide and bafilomycin A1, but sensitive to diethylstilbestrol and its analogues dienestrol and hexestrol. Azides 88-93 ATPase Escherichia coli 63-69 11515379-6 2001 The concentrations of azide, AMP, Pi, fluoride, and ADP, which inhibit the ATPase activity by 50% (IC50), were found to be approximately 100, 0.25, 0.125, 0.04, and 0.035 mM, respectively. Azides 22-27 ATPase GET3-like Solanum tuberosum 75-81 11760120-1 2001 Spectroscopy studies of absorption and circular dichroism of native PPO II and azide PPO II complex demonstrate two new absorptions at 375 nm and 500 nm after azide"s binding with PPO II, which are assigned as the terminal azide to copper charge transfer transitions II(o)nb-to-copper and II(v)nb-to-copper charge transfer transitions respectively. Azides 79-84 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 68-74 11760120-1 2001 Spectroscopy studies of absorption and circular dichroism of native PPO II and azide PPO II complex demonstrate two new absorptions at 375 nm and 500 nm after azide"s binding with PPO II, which are assigned as the terminal azide to copper charge transfer transitions II(o)nb-to-copper and II(v)nb-to-copper charge transfer transitions respectively. Azides 79-84 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 85-91 11760120-1 2001 Spectroscopy studies of absorption and circular dichroism of native PPO II and azide PPO II complex demonstrate two new absorptions at 375 nm and 500 nm after azide"s binding with PPO II, which are assigned as the terminal azide to copper charge transfer transitions II(o)nb-to-copper and II(v)nb-to-copper charge transfer transitions respectively. Azides 79-84 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 85-91 11760120-1 2001 Spectroscopy studies of absorption and circular dichroism of native PPO II and azide PPO II complex demonstrate two new absorptions at 375 nm and 500 nm after azide"s binding with PPO II, which are assigned as the terminal azide to copper charge transfer transitions II(o)nb-to-copper and II(v)nb-to-copper charge transfer transitions respectively. Azides 159-164 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 68-74 11760120-1 2001 Spectroscopy studies of absorption and circular dichroism of native PPO II and azide PPO II complex demonstrate two new absorptions at 375 nm and 500 nm after azide"s binding with PPO II, which are assigned as the terminal azide to copper charge transfer transitions II(o)nb-to-copper and II(v)nb-to-copper charge transfer transitions respectively. Azides 159-164 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 85-91 11760120-1 2001 Spectroscopy studies of absorption and circular dichroism of native PPO II and azide PPO II complex demonstrate two new absorptions at 375 nm and 500 nm after azide"s binding with PPO II, which are assigned as the terminal azide to copper charge transfer transitions II(o)nb-to-copper and II(v)nb-to-copper charge transfer transitions respectively. Azides 159-164 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 85-91 11760120-3 2001 The interaction between azide and PPO II is discussed. Azides 24-29 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 34-40 11760120-4 2001 One terminal azide"s binding with one type-3 copper improves the activity of PPO II and the other three azides" further binding in terminal geometry with the type-3 coppers decreases the activity. Azides 13-18 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 77-83 11760120-4 2001 One terminal azide"s binding with one type-3 copper improves the activity of PPO II and the other three azides" further binding in terminal geometry with the type-3 coppers decreases the activity. Azides 104-110 protoporphyrinogen oxidase, mitochondrial Nicotiana tabacum 77-83 11300898-0 2001 New, azide-free transformation of epoxides into 1,2-diamino compounds: synthesis of the anti-influenza neuraminidase inhibitor oseltamivir phosphate (Tamiflu). Azides 5-10 neuraminidase 1 Homo sapiens 103-116 11297561-11 2001 ATP depletion by 2-deoxyglucose and azide resulted in comparable slowing/immobilization of wild-type and T126M AQP2. Azides 36-41 aquaporin 2 Homo sapiens 111-115 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. Azides 105-110 albumin Homo sapiens 71-74 11422382-7 2001 Apo A-I degradation by activated neutrophils was partially inhibited by the HOCl scavenger methionine, by the heme inhibitor azide, by chloride-free conditions, by the peroxide scavenger catalase, and by a combination of superoxide dismutase (SOD)/catalase, implicating HOCl in the cell-mediated reaction. Azides 125-130 apolipoprotein A1 Homo sapiens 0-5 11386681-4 2001 The use of specific singlet oxygen quenchers (Azide and 9,10-Anthracenedipropionic acid) in ESR and oxygen consumption experiments allowed us to assert that BCA was mainly a type II sensitizer when it was incorporated in DMPC. Azides 46-51 B cell linker Homo sapiens 157-160 11300898-1 2001 A new, azide-free transformation of the key precursor epoxide 6 to the influenza neuraminidase inhibitor prodrug oseltamivir phosphate (1, Tamiflu) is described. Azides 7-12 neuraminidase 1 Homo sapiens 81-94 11236840-4 2001 Therefore, the aim of the present study was to determine the effect of azide on human recombinant and hepatic CYP2E1, CYP1A2, and CYP3A4. Azides 71-76 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 130-136 11300822-1 2001 Myoglobin was reconstituted with the ferric complex of corrphycene, a novel porphyrin isomer with a rearranged tetrapyrrole array, to investigate the influence of porphyrin deformation on the equilibrium between high-spin (S = 5/2) and low-spin (S = 1/2) states in the azide derivative. Azides 269-274 myoglobin Homo sapiens 0-9 11300822-2 2001 The azide affinity, 2.5 x 10(4) M(-1), was 1 order of magnitude lower than the corresponding values of a reference myoglobin containing an electron-deficient diformylheme similar to the corrphycene. Azides 4-9 myoglobin Homo sapiens 115-124 11236840-4 2001 Therefore, the aim of the present study was to determine the effect of azide on human recombinant and hepatic CYP2E1, CYP1A2, and CYP3A4. Azides 71-76 cytochrome P450 family 2 subfamily E member 1 Homo sapiens 110-116 11236840-5 2001 METHODS AND RESULTS: Concentrations of sodium azide as low as 0.1 mM markedly inhibited the specific ethanol oxidation (mean +/- SEM) by recombinant CYP1A2 and CYP3A4 expressed in HepG2 cells (to 16 +/- 1% and 22 +/- 2% of control without azide, respectively; p < 0.01). Azides 46-51 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 149-155 11236840-4 2001 Therefore, the aim of the present study was to determine the effect of azide on human recombinant and hepatic CYP2E1, CYP1A2, and CYP3A4. Azides 71-76 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 118-124 11236840-5 2001 METHODS AND RESULTS: Concentrations of sodium azide as low as 0.1 mM markedly inhibited the specific ethanol oxidation (mean +/- SEM) by recombinant CYP1A2 and CYP3A4 expressed in HepG2 cells (to 16 +/- 1% and 22 +/- 2% of control without azide, respectively; p < 0.01). Azides 46-51 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 160-166 11236840-6 2001 By contrast, the specific activity of CYP2E1 was only slightly (and not significantly) inhibited at this azide concentration (to 79 +/- 12% of control). Azides 105-110 cytochrome P450 family 2 subfamily E member 1 Homo sapiens 38-44 11236840-7 2001 Similarly, in human liver microsomes (n = 6), 0.1 mM azide strongly inhibited CYP1A2-dependent (to 25 +/- 2%) and CYP3A4-dependent (to 15 +/- 2%) ethanol oxidation, whereas CYP2E1 was inhibited only at 10 mM azide (to 60 +/- 10%). Azides 53-58 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 78-84 11236840-7 2001 Similarly, in human liver microsomes (n = 6), 0.1 mM azide strongly inhibited CYP1A2-dependent (to 25 +/- 2%) and CYP3A4-dependent (to 15 +/- 2%) ethanol oxidation, whereas CYP2E1 was inhibited only at 10 mM azide (to 60 +/- 10%). Azides 53-58 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 114-120 11236840-7 2001 Similarly, in human liver microsomes (n = 6), 0.1 mM azide strongly inhibited CYP1A2-dependent (to 25 +/- 2%) and CYP3A4-dependent (to 15 +/- 2%) ethanol oxidation, whereas CYP2E1 was inhibited only at 10 mM azide (to 60 +/- 10%). Azides 53-58 cytochrome P450 family 2 subfamily E member 1 Homo sapiens 173-179 11236840-10 2001 CYP2E1-specific p-nitrophenol hydroxylation was the most sensitive to azide, whereas CYP1A2-dependent 7-methoxyresorufin O-dealkylation was only slightly inhibited. Azides 70-75 cytochrome P450 family 2 subfamily E member 1 Homo sapiens 0-6 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. Azides 168-173 peroxidase 1 Zea mays 85-95 11058036-2 2000 Aryl azide 9, in which the 3"-hydroxyl group of CA-4 is replaced by an azido moiety, demonstrates excellent in vitro cytotoxicity against human cancer cell lines (NCI 60 cell line panel, average GI50 = 4.07 x 10(-8) M) and potent inhibition of tubulin polymerization (IC50 = 1.4+/-0.1 microM). Azides 5-10 carbonic anhydrase 4 Homo sapiens 48-52 11076507-13 2000 Only one cobalt-bound variant, F93I/F95M/W97V CAII, maintains tetrahedral metal coordination geometry; F93S/F95L/W97M CAII binds Co(2+) with trigonal bipyramidal coordination geometry due to the addition of azide anion to the metal coordination polyhedron. Azides 207-218 carbonic anhydrase 2 Homo sapiens 118-122 11071659-8 2000 In agreement with this finding, azide plus 2-deoxy-D-glucose, 2 metabolic blockers, also induced a rapid L-selectin shedding (65% +/- 8%) without affecting the neutrophil viability, activation, or expression level of other surface molecules with soluble isoforms such as CD16 and CD59. Azides 32-37 selectin L Homo sapiens 105-115 11071659-8 2000 In agreement with this finding, azide plus 2-deoxy-D-glucose, 2 metabolic blockers, also induced a rapid L-selectin shedding (65% +/- 8%) without affecting the neutrophil viability, activation, or expression level of other surface molecules with soluble isoforms such as CD16 and CD59. Azides 32-37 Fc gamma receptor IIIa Homo sapiens 271-275 11071659-8 2000 In agreement with this finding, azide plus 2-deoxy-D-glucose, 2 metabolic blockers, also induced a rapid L-selectin shedding (65% +/- 8%) without affecting the neutrophil viability, activation, or expression level of other surface molecules with soluble isoforms such as CD16 and CD59. Azides 32-37 CD59 molecule (CD59 blood group) Homo sapiens 280-284 10887204-5 2000 The inclusion of either azide or GSH partially restored DbetaH activity, suggesting the involvement of the reactive nitrogen oxide species, N(2)O(3). Azides 24-29 dopamine beta-hydroxylase Homo sapiens 56-62 10764744-5 2000 Azide also decreased the elevated caspase-3 activity of mC5 cells. Azides 0-5 caspase-3 Cricetulus griseus 34-43 10764744-5 2000 Azide also decreased the elevated caspase-3 activity of mC5 cells. Azides 0-5 hemolytic complement Mus musculus 56-59 11272537-1 2000 Myoglobin (Mb), in films of dimethyldidodecylammonium bromide (ddab) on graphite electrodes, is used as a catalyst to mediate the electrochemical reduction of nitrous oxide (N2O) as well as the isoelectronic ion azide (N3-) in aqueous solutions. Azides 212-217 myoglobin Homo sapiens 0-9 10970766-8 2000 In addition, calcium chelation abolished the activation of GLUT1 by azide, arsenate, 2,4-dinitrophenol and insulin. Azides 68-73 solute carrier family 2 member 1 Rattus norvegicus 59-64 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)(-). Azides 178-183 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)(-). Azides 178-183 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)(-). Azides 178-183 Cbl proto-oncogene Homo sapiens 213-216 10864893-4 2000 Tolbutamide inhibited azide-induced macroscopic Kir6.2-SUR1 currents, recorded from Xenopus oocytes, with an IC(50) value similar to native K(ATP) channels. Azides 22-27 potassium inwardly rectifying channel subfamily J member 11 Homo sapiens 48-54 10864893-4 2000 Tolbutamide inhibited azide-induced macroscopic Kir6.2-SUR1 currents, recorded from Xenopus oocytes, with an IC(50) value similar to native K(ATP) channels. Azides 22-27 ATP-binding cassette sub-family C member 8 Xenopus laevis 55-59 10864893-7 2000 In the presence of azide, Kir6.2-SUR1 currents were inhibited by englitazone and tolbutamide but not ciclazindol. Azides 19-24 potassium inwardly rectifying channel subfamily J member 11 Homo sapiens 26-32 10864893-7 2000 In the presence of azide, Kir6.2-SUR1 currents were inhibited by englitazone and tolbutamide but not ciclazindol. Azides 19-24 ATP binding cassette subfamily C member 8 Homo sapiens 33-37 10727774-4 2000 Hydroxyl radical scavengers such as azide and mannitol inhibited the fragmentation of ceruloplasmin. Azides 36-41 ceruloplasmin Homo sapiens 86-99 11272537-1 2000 Myoglobin (Mb), in films of dimethyldidodecylammonium bromide (ddab) on graphite electrodes, is used as a catalyst to mediate the electrochemical reduction of nitrous oxide (N2O) as well as the isoelectronic ion azide (N3-) in aqueous solutions. Azides 212-217 myoglobin Homo sapiens 11-13 11674735-6 1999 Coupling (DCC) of a 5"-azido-2"-O-TBDMS-3"-(carboxymethyl)-3",5"-dideoxyuridine intermediate with 5"-amino-5"-deoxynucleosides gave amide-linked dimers (72-78%) that can serve as masked (azide reduction) 5"-amino dimers for analogous synthesis of extended amide-linked oligomers. Azides 187-192 DCC netrin 1 receptor Homo sapiens 10-13 10602307-8 1999 The CL from ABEI-ms with hydrogen peroxide/MPO was completely inhibited by azide. Azides 75-80 myeloperoxidase Homo sapiens 43-46 10550686-0 1999 An X-ray crystallographic study of the binding sites of the azide inhibitor and organic substrates to ceruloplasmin, a multi-copper oxidase in the plasma. Azides 60-65 ceruloplasmin Homo sapiens 102-115 10504390-1 1999 The effect of multiple binding of azide, N3-, on the structural and functional properties of ceruloplasmin (CP) has been reinvestigated by means of both spectroscopic and enzymatic techniques. Azides 34-39 ceruloplasmin Gallus gallus 93-106 10504390-1 1999 The effect of multiple binding of azide, N3-, on the structural and functional properties of ceruloplasmin (CP) has been reinvestigated by means of both spectroscopic and enzymatic techniques. Azides 34-39 ceruloplasmin Gallus gallus 108-110 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. Azides 80-85 solute carrier family 2 member 1 Rattus norvegicus 204-209 10629851-2 1999 Catalase is capable of producing NO from azide and hydroxylamine (Ignarro LJ, FASEB J 1989; 3:31-36). Azides 41-46 catalase Rattus norvegicus 0-8 10629851-8 1999 The catalase activity of the aorta was inhibited by azide and hydroxylamine with the similar IC50 values to EC50 values for relaxation. Azides 52-57 catalase Rattus norvegicus 4-12 10462537-9 1999 )radicals is completely blocked by myeloperoxidase inhibitors, cyanide and azide. Azides 89-94 myeloperoxidase Homo sapiens 49-64 10441390-9 1999 It is concluded that (i) inhibition of oxidative phosphorylation, at any of its steps, leads to a stimulation of glucose transport, and (ii) the mechanism of stimulation of glucose transport in response to azide appears to be predominately mediated by an apparent increase in the number of functional Glut1 sites in the plasma membrane (instead of an increase in their "intrinsic activity"), suggesting an "unmasking" mechanism. Azides 206-211 solute carrier family 2 member 1 Rattus norvegicus 301-306 10393704-8 1999 CML production by neutrophils was inhibited by the H2O2 scavenger catalase and the heme poison azide, implicating myeloperoxidase in the cell-mediated reaction. Azides 95-100 myeloperoxidase Homo sapiens 114-129 10340744-1 1999 The effect of chemical anoxia (azide) in the presence of glucose on the free intracellular Ca2+ concentration ([Ca2+]i) and intracellular pH (pHi) in mouse neocortical neurons was investigated using Fura-2 and BCECF. Azides 31-36 glucose-6-phosphate isomerase 1 Mus musculus 142-145 11390832-2 1999 GLUT-1 expression is also stimulated by hypoxia or azide. Azides 51-56 solute carrier family 2 member 1 Homo sapiens 0-6 10340944-4 1999 Although stimulation of the cells with granulocyte macrophage colony-stimulating factor (GM-CSF) before the assay failed to modulate adhesion, binding was inhibited by up to 50% by treatment of the leukocytes with azide. Azides 214-219 colony stimulating factor 2 Homo sapiens 89-95 9880816-0 1999 An azide-insensitive superoxide dismutase from a hyperthermophilic archaeon, Sulfolobus solfataricus. Azides 3-8 shikimate dehydrogenase Saccharolobus solfataricus 21-41 10217423-1 1999 The ADP(Mg2+)-deactivated, azide-trapped F0 x F1-ATPase of coupled submitochondrial particles is capable of ATP synthesis being incapable of ATP hydrolysis and ATP-dependent delta muH+ generation [FEBS Lett. Azides 27-32 dynein axonemal heavy chain 8 Homo sapiens 49-55 10217423-6 1999 Less than 5% of the original ATPase activity was seen when the reaction (assayed with ATP-regenerating system) was initiated by the addition of ATP to the azide-trapped coupled particles oxidizing succinate either in the presence or in the absence of the uncoupler. Azides 155-160 dynein axonemal heavy chain 8 Homo sapiens 29-35 10391130-4 1999 To delineate the mechanism mediating the stimulation of glucose transport by a azide we employed two strategies: (1) mild cell surface biotinylation followed by isolation of plasma membranes and quantitation of Glut1 sites in Western blots employing anti-Glut1 and anti-myc antibodies, and (2) quantitative immunofluorescence of myc epitopes in plasma membrane sheets. Azides 79-84 solute carrier family 2 member 1 Rattus norvegicus 211-216 10391130-4 1999 To delineate the mechanism mediating the stimulation of glucose transport by a azide we employed two strategies: (1) mild cell surface biotinylation followed by isolation of plasma membranes and quantitation of Glut1 sites in Western blots employing anti-Glut1 and anti-myc antibodies, and (2) quantitative immunofluorescence of myc epitopes in plasma membrane sheets. Azides 79-84 solute carrier family 2 member 1 Rattus norvegicus 255-260 10103024-2 1999 UVA activation of p38 can be inhibited by the singlet oxygen (1O2) quenchers azide and imidazole, but not by the hydroxyl radical scavengers mannitol or dimethylsulfoxide, pointing to the involvement of 1O2. Azides 77-82 mitogen-activated protein kinase 1 Homo sapiens 18-21 10512537-4 1999 This complex displays an MCD spectrum dissimilar from that of the Mb derivative, possibly because of the stabilizing interaction between the azide ligand and the distal arginine of CCP (Arg 48). Azides 141-146 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 181-184 10391130-7 1999 We conclude that the stimulation of glucose transport by azide results mainly from activation of Glut1 transporters pre-existing in the plasma membrane. Azides 57-62 solute carrier family 2 member 1 Rattus norvegicus 97-102 9858764-5 1998 The rate of autoxidation of oxy-myoglobin and azide affinity of met-aquo myoglobin were also found to depend on the orientation of the heme. Azides 46-51 myoglobin Homo sapiens 73-82 9860966-2 1998 The asymmetric stretching vibration of azide bound to carbonic anhydrase II exhibits a pronounced evolution of its vibrational frequency distribution on the time scale of a few picoseconds, which is attributed to modifications of the ligand structure through interactions with the nearby Thr-199. Azides 39-44 carbonic anhydrase 2 Homo sapiens 54-75 9828013-1 1998 Limited cleavage of oxidized and reduced horse heart cytochrome c (Cyt c) and the azide complex of Cyt c by proteinase K at room temperature yields a single cut within the central loop (36-60 in the sequence). Azides 82-87 cytochrome c, somatic Equus caballus 99-104 9828013-4 1998 The results we obtain indicate that oxidized Cyt c is 2.0 kcal mol(-1) less stable than the reduced form, and 0.07 kcal mol(-1) is more stable than the Cyt c: azide complex at 25 degrees C. These values agree in magnitude with results from hydrogen exchange and unfolding studies, suggesting that the stability of a protein can be directly related to its structural dynamics. Azides 159-164 cytochrome c, somatic Equus caballus 45-50 9828013-4 1998 The results we obtain indicate that oxidized Cyt c is 2.0 kcal mol(-1) less stable than the reduced form, and 0.07 kcal mol(-1) is more stable than the Cyt c: azide complex at 25 degrees C. These values agree in magnitude with results from hydrogen exchange and unfolding studies, suggesting that the stability of a protein can be directly related to its structural dynamics. Azides 159-164 cytochrome c, somatic Equus caballus 152-157 9788740-0 1998 Induction of GLUT1 mRNA in response to azide and inhibition of protein synthesis. Azides 39-44 solute carrier family 2 member 1 Rattus norvegicus 13-18 9788740-1 1998 Incubation of Clone 9 cells, a nontransformed rat liver cell line, in the presence of 5 mM azide results in an induction of GLUT1 mRNA which becomes detectable after approximately 3 h of continuous exposure to the agent. Azides 91-96 solute carrier family 2 member 1 Rattus norvegicus 124-129 9788740-7 1998 Finally, SAPK activity was minimally stimulated in cells exposed to azide. Azides 68-73 mitogen-activated protein kinase 9 Rattus norvegicus 9-13 9788740-2 1998 In examining the role of on-going protein synthesis in this response, we found that: (i) the induction of GLUT1 mRNA by azide was not inhibited by anisomycin, (ii) exposure to anisomycin alone also resulted in increased GLUT1 mRNA content, and (iii) the increments in GLUT1 mRNA content in the presence of both azide and anisomycin were additive. Azides 120-125 solute carrier family 2 member 1 Rattus norvegicus 106-111 9788740-2 1998 In examining the role of on-going protein synthesis in this response, we found that: (i) the induction of GLUT1 mRNA by azide was not inhibited by anisomycin, (ii) exposure to anisomycin alone also resulted in increased GLUT1 mRNA content, and (iii) the increments in GLUT1 mRNA content in the presence of both azide and anisomycin were additive. Azides 120-125 solute carrier family 2 member 1 Rattus norvegicus 220-225 9788740-2 1998 In examining the role of on-going protein synthesis in this response, we found that: (i) the induction of GLUT1 mRNA by azide was not inhibited by anisomycin, (ii) exposure to anisomycin alone also resulted in increased GLUT1 mRNA content, and (iii) the increments in GLUT1 mRNA content in the presence of both azide and anisomycin were additive. Azides 120-125 solute carrier family 2 member 1 Rattus norvegicus 220-225 9788740-2 1998 In examining the role of on-going protein synthesis in this response, we found that: (i) the induction of GLUT1 mRNA by azide was not inhibited by anisomycin, (ii) exposure to anisomycin alone also resulted in increased GLUT1 mRNA content, and (iii) the increments in GLUT1 mRNA content in the presence of both azide and anisomycin were additive. Azides 311-316 solute carrier family 2 member 1 Rattus norvegicus 106-111 9839190-5 1998 Furthermore, an azide-insensitive and therefore peroxidase-independent part of CL was found in FMLP-, LDL- and zymosan-stimulated cells. Azides 16-21 formyl peptide receptor 1 Homo sapiens 95-99 9711303-5 1998 When used at low concentrations, azide inhibited more than 70% of cytochrome oxidase (COX) activity without changes in bioenergetics (either lactate production or creatine phosphorylation) or mRNA for mitochondrial enzymes. Azides 33-38 cytochrome c oxidase subunit 8A Homo sapiens 66-84 9685425-7 1998 Reduction of intracellular ATP using azide inhibited Glut 1 and Glut 4 translocation from the LDM to the plasma membrane, insulin receptor autophosphorylation, and IRS-1 tyrosine phosphorylation. Azides 37-42 solute carrier family 2 member 1 Homo sapiens 53-59 9685425-7 1998 Reduction of intracellular ATP using azide inhibited Glut 1 and Glut 4 translocation from the LDM to the plasma membrane, insulin receptor autophosphorylation, and IRS-1 tyrosine phosphorylation. Azides 37-42 solute carrier family 2 member 4 Homo sapiens 64-70 9685425-7 1998 Reduction of intracellular ATP using azide inhibited Glut 1 and Glut 4 translocation from the LDM to the plasma membrane, insulin receptor autophosphorylation, and IRS-1 tyrosine phosphorylation. Azides 37-42 insulin receptor Homo sapiens 122-138 9685425-7 1998 Reduction of intracellular ATP using azide inhibited Glut 1 and Glut 4 translocation from the LDM to the plasma membrane, insulin receptor autophosphorylation, and IRS-1 tyrosine phosphorylation. Azides 37-42 insulin receptor substrate 1 Homo sapiens 164-169 9711303-5 1998 When used at low concentrations, azide inhibited more than 70% of cytochrome oxidase (COX) activity without changes in bioenergetics (either lactate production or creatine phosphorylation) or mRNA for mitochondrial enzymes. Azides 33-38 cytochrome c oxidase subunit 8A Homo sapiens 86-89 9711303-6 1998 Higher azide concentrations resulted in changes in bioenergetic parameters and increases in steady state COX II mRNA levels. Azides 7-12 cytochrome c oxidase subunit 8A Homo sapiens 105-108 9660850-6 1998 No metabolism was detected in neutrophils that had not been activated, and the oxidation was inhibited by azide (which inhibits MPO) and by catalase (which catalyzes the breakdown of H2O2). Azides 106-111 myeloperoxidase Homo sapiens 128-131 9602041-0 1998 1H NMR studies of azide binding to cytochrome c. Azides 18-23 cytochrome c, somatic Homo sapiens 35-47 9576852-0 1998 Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64-->Thr variant. Azides 40-45 myoglobin Equus caballus 71-80 9576852-5 1998 EPR and Fourier transform infrared spectroscopy were used to characterize the myoglobin azide complexes further. Azides 88-93 myoglobin Equus caballus 78-87 9576852-9 1998 The major conformation is comparable to that formed by wild-type myoglobin in which azide is oriented into the distal crevice. Azides 84-89 myoglobin Equus caballus 65-74 9521765-0 1998 Fourier transform infrared analysis of the interaction of azide with the active site of oxidized and reduced bovine Cu,Zn superoxide dismutase. Azides 58-63 superoxide dismutase [Cu-Zn] Bos taurus 116-142 9521765-1 1998 Binding of azide to the native and arginine-modified bovine Cu,Zn superoxide dismutase in the oxidized and reduced form and to the copper-free derivative has been investigated by Fourier transform infrared spectroscopy. Azides 11-16 superoxide dismutase [Cu-Zn] Bos taurus 60-86 9521765-7 1998 It is concluded that azide does not directly coordinate to the copper in the reduced form of Cu,Zn superoxide dismutase but it remains in the active-site pocket in electrostatic interaction with the guanidinium group of Arg141, which is an invariant residue in this class of enzymes. Azides 21-26 superoxide dismutase [Cu-Zn] Bos taurus 93-119 9163514-4 1997 The ferrous myoglobin is capable of strong binding with pyridine, imidazole, cyanide, and azide, and reacts moderately with ammonia. Azides 90-95 myoglobin Homo sapiens 12-21 9494083-5 1998 Azide and carbonyl cyanide p-trifluoromethoxyphenylhydrazone inhibited the thapsigargin-stimulated Ca2+o-induced increase in [Ca2+]c in the presence of increased cAMP (induced by glucagon). Azides 0-5 carbonic anhydrase 2 Rattus norvegicus 99-102 9494083-5 1998 Azide and carbonyl cyanide p-trifluoromethoxyphenylhydrazone inhibited the thapsigargin-stimulated Ca2+o-induced increase in [Ca2+]c in the presence of increased cAMP (induced by glucagon). Azides 0-5 carbonic anhydrase 2 Rattus norvegicus 126-129 9718094-4 1998 Azide can be oxidized by catalase and myeloperoxidase in the presence of H2O2, resulting in the generation of nitric oxide (NO). Azides 0-5 myeloperoxidase Homo sapiens 38-53 9718094-6 1998 Azide-induced migration, and the enhancement by azide of fMLP/CB-induced exocytosis, were blocked by pre-incubating cells with aminotriazole, an inhibitor of catalase and myeloperoxidase, suggesting that the effect of azide was mediated by NO. Azides 0-5 myeloperoxidase Homo sapiens 171-186 9718094-6 1998 Azide-induced migration, and the enhancement by azide of fMLP/CB-induced exocytosis, were blocked by pre-incubating cells with aminotriazole, an inhibitor of catalase and myeloperoxidase, suggesting that the effect of azide was mediated by NO. Azides 48-53 myeloperoxidase Homo sapiens 171-186 9167939-7 1997 The sensitivity to catalase inhibitors, such as aminotriazole, azide, or cyanide varies among the isoforms. Azides 63-68 catalase Mus musculus 19-27 9571774-5 1998 Because azide was an electron donor for the peroxidatic action of catalase, and because 3-amino-1,2,4-triazole inhibited catalase activity by binding with Compound I, peroxynitrite-mediated phenolic nitration was probably accompanied by Compound I formation. Azides 8-13 catalase Homo sapiens 66-74 9571774-5 1998 Because azide was an electron donor for the peroxidatic action of catalase, and because 3-amino-1,2,4-triazole inhibited catalase activity by binding with Compound I, peroxynitrite-mediated phenolic nitration was probably accompanied by Compound I formation. Azides 8-13 catalase Homo sapiens 121-129 9456544-2 1998 Aliquots are acidified, converting azide to volatile hydrazoic acid (HN3) which is then trapped in sodium hydroxide. Azides 35-40 MT-RNR2 like 3 (pseudogene) Homo sapiens 69-72 9398251-12 1997 Since the novel form of clusterin is also expressed in cells exposed to TGFbeta, colchicine, staurosporine, and azide, it may result from toxin-induced disruption of processes of normal cellular protein production. Azides 112-117 clusterin Mus musculus 24-33 9334858-2 1997 Using various parameters of cell death, we demonstrate here that azide is capable of completely inhibiting apoptosis induced by VP-16/etoposide. Azides 65-70 host cell factor C1 Homo sapiens 128-133 9334858-3 1997 Azide was found systematically to protect Jurkat cells against VP-16-induced effects as determined by an array of biochemical and morphological parameters. Azides 0-5 host cell factor C1 Homo sapiens 63-68 9334858-5 1997 We conclude that azide inhibits apoptosis induced by VP-16 at an early point in the apoptotic pathway and that inhibition of apoptosis might be the mechanism of necrosis-induction by azide. Azides 17-22 host cell factor C1 Homo sapiens 53-58 9337622-15 1997 The complementary inhibition of DMPO-OH production by azide and 9,10-anthracenedipropionic acid (ADPA) was consistent with 1O2 production by BCA followed by reaction of 1O2 with DMPO and decay of the intermediate complex to form DMPO-OH and free OH.. All our results seem to indicate that BCA is a 50%/50% type 1/type 2 sensitizer in buffered aqueous solutions and confirmed that the dye-induced hemolysis of erythrocytes was cell caused by a mixed type 1/type 2 mechanism. Azides 54-59 B cell linker Homo sapiens 141-144 9337622-15 1997 The complementary inhibition of DMPO-OH production by azide and 9,10-anthracenedipropionic acid (ADPA) was consistent with 1O2 production by BCA followed by reaction of 1O2 with DMPO and decay of the intermediate complex to form DMPO-OH and free OH.. All our results seem to indicate that BCA is a 50%/50% type 1/type 2 sensitizer in buffered aqueous solutions and confirmed that the dye-induced hemolysis of erythrocytes was cell caused by a mixed type 1/type 2 mechanism. Azides 54-59 B cell linker Homo sapiens 289-292 9339903-8 1997 A radical scavenger, azide anion, inhibited the fragmentation of Cu,Zn-SOD and the formation of .OH whereas ethanol did not. Azides 21-32 superoxide dismutase 1 Homo sapiens 71-74 9339903-9 1997 These results indicated that azide anions had easy access inside the active channel of Cu,Zn-SOD and thus protected the damage of the enzyme by .OH radicals whereas neutral alcohols stayed outside the active channel and could hardly intercept the newly-formed .OH radicals. Azides 29-34 superoxide dismutase 1 Homo sapiens 93-96 9209494-5 1997 This concept was supported by the finding that the proportion of lymphocytes rolling on the higher concentrations of VCAM-1 increased if cells were pretreated with azide to block energy-dependent responses, or if intracellular Ca2+ was chelated. Azides 164-169 vascular cell adhesion molecule 1 Homo sapiens 117-123 9155262-3 1997 The singlet oxygen quenchers, azide, Ni-chelate 1 and Ni-chelate 2, caused smaller inhibitions in the rate of singlet oxygen-mediated inactivation of ACE on K562 cells than ACE in solution. Azides 30-35 acetylcholinesterase (Cartwright blood group) Homo sapiens 150-153 9155262-3 1997 The singlet oxygen quenchers, azide, Ni-chelate 1 and Ni-chelate 2, caused smaller inhibitions in the rate of singlet oxygen-mediated inactivation of ACE on K562 cells than ACE in solution. Azides 30-35 acetylcholinesterase (Cartwright blood group) Homo sapiens 173-176 9034238-7 1997 The formation of 3-chloro PABA was inhibited by azide, catalase, and taurine, which is consistent with the production of the metabolite by the neutrophil myeloperoxidase (MPO) pathway. Azides 48-53 myeloperoxidase Homo sapiens 154-169 9038162-2 1997 glut1 is also up-regulated by inhibitors of oxidative phosphorylation (such as azide) in the presence of oxygen. Azides 79-84 solute carrier family 2 member 1 Rattus norvegicus 0-5 9038162-5 1997 Exposure of a rat liver cell line (Clone 9) to 250 microM cobalt chloride increases GLUT1 mRNA content, which becomes evident at 2 h, reaches a maximal value of approximately 12-fold at 8 h, and remains elevated at approximately 8-fold at 24 h. GLUT1 mRNA was the only GLUT isoform expressed in control cells and in cells exposed to cobalt chloride or azide. Azides 352-357 solute carrier family 2 member 1 Rattus norvegicus 84-89 9038162-5 1997 Exposure of a rat liver cell line (Clone 9) to 250 microM cobalt chloride increases GLUT1 mRNA content, which becomes evident at 2 h, reaches a maximal value of approximately 12-fold at 8 h, and remains elevated at approximately 8-fold at 24 h. GLUT1 mRNA was the only GLUT isoform expressed in control cells and in cells exposed to cobalt chloride or azide. Azides 352-357 glutaminase Rattus norvegicus 84-88 9038162-6 1997 The induction of GLUT1 mRNA by cobalt chloride is associated with a approximately 10-fold stimulation of cytochalasin B-inhibitable 3-O-methyl-D-glucose transport at 24 h. In contrast to the rapid decrease in cell ATP levels and the stimulation of glucose transport in response to azide, cell ATP content and glucose transport remained unaltered during the initial 1-h period of exposure to cobalt chloride. Azides 281-286 solute carrier family 2 member 1 Rattus norvegicus 17-22 9060087-2 1997 Addition to urine of a preservative solution containing benzamidinium chloride, EDTA, tris(hydroxymethyl)-aminomethane and azide prevented the decreases of the concentration values for protein HC and IgG but not for alpha 1-antitrypsin. Azides 123-128 alpha-1-microglobulin/bikunin precursor Homo sapiens 185-195 9060087-2 1997 Addition to urine of a preservative solution containing benzamidinium chloride, EDTA, tris(hydroxymethyl)-aminomethane and azide prevented the decreases of the concentration values for protein HC and IgG but not for alpha 1-antitrypsin. Azides 123-128 serpin family A member 1 Homo sapiens 216-235 9034238-7 1997 The formation of 3-chloro PABA was inhibited by azide, catalase, and taurine, which is consistent with the production of the metabolite by the neutrophil myeloperoxidase (MPO) pathway. Azides 48-53 myeloperoxidase Homo sapiens 171-174 9023770-5 1997 Oocytes injected with SUR1 and either Kir6.2 or Kir6.1 exhibited large inwardly rectifying K+ currents when cytosolic ATP levels were lowered by the metabolic inhibitors azide or FCCP. Azides 170-175 ATP-binding cassette sub-family C member 8 Xenopus laevis 22-26 9023770-5 1997 Oocytes injected with SUR1 and either Kir6.2 or Kir6.1 exhibited large inwardly rectifying K+ currents when cytosolic ATP levels were lowered by the metabolic inhibitors azide or FCCP. Azides 170-175 potassium inwardly rectifying channel subfamily J member 8 L homeolog Xenopus laevis 48-54 8980644-1 1996 A study of the azide reaction with bovine liver catalase in presence of hydrogen peroxide has been performed, using conventional UV-visible spectrometry and activity measurements. Azides 15-20 catalase Bos taurus 48-56 8980644-3 1996 A reaction scheme for peroxidatic degradation of azide by catalase is proposed. Azides 49-54 catalase Bos taurus 58-66 8980644-0 1996 Peroxidatic degradation of azide by catalase and irreversible enzyme inactivation. Azides 27-32 catalase Bos taurus 36-44 8980644-5 1996 Catalase is irreversibly inactivated by prolonged exposure to high levels of H2O2 and azide. Azides 86-91 catalase Bos taurus 0-8 8751892-3 1996 Myeloperoxidase was inhibited with azide, and myeloperoxidase-deficient neutrophils were used. Azides 35-40 myeloperoxidase Homo sapiens 0-15 8892317-1 1996 Treatment of Clone 9 cells incubated in the absence of serum with 5 mM azide for 24 h results in an 8- and 3-fold induction in GLUT1 mRNA and GLUT1 protein, respectively. Azides 71-76 solute carrier family 2 member 1 Rattus norvegicus 127-132 8892317-1 1996 Treatment of Clone 9 cells incubated in the absence of serum with 5 mM azide for 24 h results in an 8- and 3-fold induction in GLUT1 mRNA and GLUT1 protein, respectively. Azides 71-76 solute carrier family 2 member 1 Rattus norvegicus 142-147 8892317-3 1996 Exposure of cells to 5 microM carbonyl cyanide m-chlorophenylhydrazone (CCCP), 0.15 microM oligomycin B, or 5 mM azide resulted in near-equivalent increases in GLUT1 mRNA content. Azides 113-118 solute carrier family 2 member 1 Rattus norvegicus 160-165 8892317-5 1996 We next tested the possibility that an increase in cell SH/SS ratio mediates the enhancement of GLUT1 mRNA in response to azide. Azides 122-127 solute carrier family 2 member 1 Rattus norvegicus 96-101 8892317-7 1996 Moreover, incubation of cells in the presence of 0.3 mM diamide, a known intracellular sulfhydryl oxidizing agent, completely abolishes the induction of GLUT1 mRNA by azide. Azides 167-172 solute carrier family 2 member 1 Rattus norvegicus 153-158 8772449-8 1996 5) Treatment with ionomycin, A-23187, and thapsigargin caused larger increases in glucose-regulated protein 78 and 94 and in 70-kDa heat shock protein mRNAs than in GLUT-1 mRNA, whereas treatment with azide resulted in greater induction of GLUT-1 mRNA. Azides 201-206 solute carrier family 2 member 1 Rattus norvegicus 240-246 8877407-10 1996 Azide, an inhibitor of myeloperoxidase, and catalase which destroys H2O2, essential for MPO-catalyzed oxidations, prevented the generation of C5 activating potency and of chloramines. Azides 0-5 myeloperoxidase Homo sapiens 23-38 8877407-10 1996 Azide, an inhibitor of myeloperoxidase, and catalase which destroys H2O2, essential for MPO-catalyzed oxidations, prevented the generation of C5 activating potency and of chloramines. Azides 0-5 myeloperoxidase Homo sapiens 88-91 8772449-1 1996 Exposure of Clone 9 cells (a rat liver cell line expressing only the GLUT-1 isoform) to 5 mM azide or to 3 microM ionomycin for 12 h results in 3.7 +/- 0.3- and 4.9 +/- 0.4-fold increases in GLUT-1 mRNA content, respectively, suggesting the hypothesis that a rise in cytosolic free calcium concentration ([Ca2+]i) mediates the induction of GLUT-1 mRNA by azide. Azides 93-98 solute carrier family 2 member 1 Rattus norvegicus 69-75 8772449-1 1996 Exposure of Clone 9 cells (a rat liver cell line expressing only the GLUT-1 isoform) to 5 mM azide or to 3 microM ionomycin for 12 h results in 3.7 +/- 0.3- and 4.9 +/- 0.4-fold increases in GLUT-1 mRNA content, respectively, suggesting the hypothesis that a rise in cytosolic free calcium concentration ([Ca2+]i) mediates the induction of GLUT-1 mRNA by azide. Azides 93-98 solute carrier family 2 member 1 Rattus norvegicus 191-197 8772449-1 1996 Exposure of Clone 9 cells (a rat liver cell line expressing only the GLUT-1 isoform) to 5 mM azide or to 3 microM ionomycin for 12 h results in 3.7 +/- 0.3- and 4.9 +/- 0.4-fold increases in GLUT-1 mRNA content, respectively, suggesting the hypothesis that a rise in cytosolic free calcium concentration ([Ca2+]i) mediates the induction of GLUT-1 mRNA by azide. Azides 93-98 solute carrier family 2 member 1 Rattus norvegicus 191-197 8772449-5 1996 2) The increase in GLUT-1 mRNA content by azide was fully preserved in cells preloaded with 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid (BAPTA). Azides 42-47 solute carrier family 2 member 1 Rattus norvegicus 19-25 8760044-10 1996 Preincubating the membranes in MgATP2- in the presence of Ca2+/calmodulin stimulated the subsequent Ca2+ uptake in the presence of oxalate plus MgATP2- and azide. Azides 156-161 calmodulin-3 Sus scrofa 63-73 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. Azides 0-5 cytochrome c, somatic Equus caballus 98-110 8627283-1 1996 Azide, cyanide, fluoride, imidazole, and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative has been investigated, from the thermodynamic viewpoint, at pH 7.5 and 25.0 degrees C. Ligand affinity for ferric and ferrous carboxymethylated cytochrome c is higher by about 30- and 400-fold, respectively, than that observed for the native protein. Azides 0-5 cytochrome c, somatic Equus caballus 99-111 8825615-5 1996 The virucidal effect of eosinophils, PMA, and bromide under these conditions is inhibited by the peroxidase inhibitor azide and catalase, but not heated catalase or superoxide dismutase, implicating the EPO-H2O2-halide system. Azides 118-123 eosinophil peroxidase Homo sapiens 203-206 8825615-7 1996 When the EPO concentration is suboptimal, virucidal activity is increased by bromide, iodide, and, in this instance, thiocyanate and the virucidal activity of the bromide-supplemented system is inhibited by azide and catalase. Azides 207-212 eosinophil peroxidase Homo sapiens 9-12 8825615-7 1996 When the EPO concentration is suboptimal, virucidal activity is increased by bromide, iodide, and, in this instance, thiocyanate and the virucidal activity of the bromide-supplemented system is inhibited by azide and catalase. Azides 207-212 catalase Homo sapiens 217-225 8558444-10 1996 Photoaffinity labeling of porcine coronary artery membrane proteins with the azide derivative of 125I-APE revealed a 45,000-Da binding site. Azides 77-82 apurinic/apyrimidinic endodeoxyribonuclease 1 Homo sapiens 102-105 7711097-5 1995 The ratio of progesterone receptor subunits A:B was determined to be 3.3:1 with both [3H]progestin azide 7 and [3H]-R 5020. Azides 99-104 progesterone receptor Homo sapiens 13-34 7665597-3 1995 To identify the molecular event underlying this apparent increase in GLUT1 intrinsic activity, we studied the acute effects of azide on the substrate binding activity of GLUT1 in Clone 9 cells by measuring glucose-sensitive cytochalasin B binding. Azides 127-132 solute carrier family 2 member 1 Rattus norvegicus 170-175 7665597-5 1995 Furthermore, the cytochalasin B binding activity of purified human erythrocyte GLUT1 reconstituted in liposomes was significantly reduced in the presence of cytosol derived from azide-treated Clone 9 cells but not in the presence of cytosol from control cells; this effect was heat-labile and abolished by the presence of the peptide corresponding to the GLUT1 COOH-terminal sequence. Azides 178-183 solute carrier family 2 member 1 Homo sapiens 79-84 7665597-5 1995 Furthermore, the cytochalasin B binding activity of purified human erythrocyte GLUT1 reconstituted in liposomes was significantly reduced in the presence of cytosol derived from azide-treated Clone 9 cells but not in the presence of cytosol from control cells; this effect was heat-labile and abolished by the presence of the peptide corresponding to the GLUT1 COOH-terminal sequence. Azides 178-183 solute carrier family 2 member 1 Rattus norvegicus 355-360 7665597-6 1995 These results suggest that a cytosolic protein in Clone 9 cells binds to GLUT1 at its COOH-terminal domain and inhibits its substrate binding and that azide-induced metabolic alteration releases GLUT1 from this inhibitory interaction. Azides 151-156 solute carrier family 2 member 1 Rattus norvegicus 73-78 7665597-6 1995 These results suggest that a cytosolic protein in Clone 9 cells binds to GLUT1 at its COOH-terminal domain and inhibits its substrate binding and that azide-induced metabolic alteration releases GLUT1 from this inhibitory interaction. Azides 151-156 solute carrier family 2 member 1 Rattus norvegicus 195-200 7665597-8 1995 We also found a 32P-labeled, 85-kDa protein that binds to GLUT4 but not to GLUT1 and only in cytosol derived from azide-treated cells. Azides 114-119 solute carrier family 2 member 4 Rattus norvegicus 58-63 7665597-9 1995 The roles, if any, of these glucose transporter-binding proteins in the azide-sensitive modulation of GLUT1 substrate binding activity in Clone 9 cells are yet to be determined. Azides 72-77 solute carrier family 2 member 1 Rattus norvegicus 102-107 7493931-5 1995 An enhancer lying 5" to the mouse Glut-1 gene was found to convey responses both to hypoxia and to the mitochondrial inhibitors, azide and rotenone. Azides 129-134 solute carrier family 2 (facilitated glucose transporter), member 1 Mus musculus 34-40 8593745-9 1995 Bcl-2 can delay cell death caused by azide, and inhibit apoptotic changes seen by electron microscopy, but cannot prevent the eventual death of the cells. Azides 37-42 BCL2 apoptosis regulator Homo sapiens 0-5 7626118-3 1995 Consequently, some of the observed inhibition of tyrosinase by azide can be explained by the reaction of enzymatically generated quinones with azide to form azido catechol. Azides 63-68 tyrosinase Homo sapiens 49-59 7626118-3 1995 Consequently, some of the observed inhibition of tyrosinase by azide can be explained by the reaction of enzymatically generated quinones with azide to form azido catechol. Azides 143-148 tyrosinase Homo sapiens 49-59 7789510-2 1995 The initial rates of ATP hydrolysis, oxidative phosphorylation, ATP-dependent, succinate-supported NAD+ reduction, and ATP-induced delta microH+ generation were measured using deactivated ATPase trapped by azide [Biochem. Azides 206-211 dynein axonemal heavy chain 8 Homo sapiens 188-194 7789510-6 1995 The unidirectional effect of azide is not consistent with three alternating binding sites mechanism operating in ATP synthesis and support our hypothesis on the existence of nucleotide(Mg2+)-controlled "synthase" and "hydrolase" states of the mitochondrial F1-F0 ATPase. Azides 29-34 dynein axonemal heavy chain 8 Homo sapiens 263-269 7762668-5 1995 Cytotoxicity was also reduced by inhibiting myeloperoxidase activity with azide or scavenging HOCl with alanine or methionine. Azides 74-79 myeloperoxidase Oryctolagus cuniculus 44-59 7762419-6 1995 Lucigenin-dependent CL of sulphite-treated and subsequently stimulated neutrophils was strongly inhibited by extracellularly added superoxide dismutase, whereas luminol-dependent CL was markedly reduced by the MPO inhibitor azide. Azides 224-229 myeloperoxidase Homo sapiens 210-213 8011626-0 1994 FTIR analysis of the interaction of azide with horse heart myoglobin variants. Azides 36-41 myoglobin Equus caballus 59-68 7999769-0 1994 Low-temperature optical spectroscopy of native and azide-reacted bovine Cu,Zn superoxide dismutase. Azides 51-56 superoxide dismutase [Cu-Zn] Bos taurus 72-98 8028001-0 1994 Crystallographic study of azide-inhibited bovine Cu,Zn superoxide dismutase. Azides 26-31 superoxide dismutase [Cu-Zn] Bos taurus 49-75 8028001-1 1994 The crystal structure of azide-inhibited bovine Cu,Zn superoxide dismutase has been studied and refined based on X-ray synchrotron radiation data, in conjunction with difference Fourier and restrained crystallographic refinement techniques. Azides 25-30 superoxide dismutase [Cu-Zn] Bos taurus 48-74 8011626-1 1994 The interaction of azide with variants of horse heart myoglobin (Mb) has been characterized by Fourier transform infrared (FTIR), electron paramagnetic resonance (EPR), and UV-VIS absorption spectroscopy and by molecular modeling calculations. Azides 19-24 myoglobin Equus caballus 54-63 8250925-5 1993 These findings suggest that nitrite production does not, in this instance, reflect nitric oxide synthase activity by human neutrophils but rather the catalase-catalyzed conversion of azide to nitrite in the presence of H2O2 generated by the stimulated PMN. Azides 183-188 catalase Homo sapiens 150-158 8020498-3 1994 The functionally expressed hybrid ATPase was activated 13-fold at pH 7.5 by the addition of Na+ and inhibited by 1,3-dicyclohexylcarbodiimide, azide and tributyltin chloride. Azides 143-148 ATPase Escherichia coli 34-40 8161207-0 1994 Spin trapping of azidyl and hydroxyl radicals in azide-inhibited rat brain submitochondrial particles. Azides 49-54 spindlin 1 Rattus norvegicus 0-4 7910528-7 1994 Intracellular oxygen radical scavengers (dimethyl sulfoxide, butylated hydroxytoluene, and alpha, alpha"-dipyridyl), the iron chelator desferrioxamine, and the mitochondrial inhibitor azide inhibited the L-NAME-induced neutrophil adhesion, whereas extracellular oxygen radical scavengers (superoxide dismutase and catalase) had no effect. Azides 184-189 catalase Homo sapiens 314-322 7910172-5 1994 Processing of urushiol for presentation to CD8+ T cells was inhibited by azide, monensin, and brefeldin A. Azides 73-78 CD8a molecule Homo sapiens 43-46 8161207-1 1994 Succinate-driven respiration in azide-inhibited rat brain submitochondrial particles (smps) produces azidyl and hydroxyl radicals that were detected by spin trapping with 5,5"-dimethyl-1-pyrroline-N-oxide (DMPO). Azides 32-37 spindlin 1 Rattus norvegicus 152-156 8161207-8 1994 In the azide-inhibited system, reaction of azide anion with H2O2-activated endogenous peroxidase and spin-trapping of the resulting azidyl radical is a convenient monitor of H2O2 production. Azides 7-12 spindlin 1 Rattus norvegicus 101-105 8161207-8 1994 In the azide-inhibited system, reaction of azide anion with H2O2-activated endogenous peroxidase and spin-trapping of the resulting azidyl radical is a convenient monitor of H2O2 production. Azides 43-54 spindlin 1 Rattus norvegicus 101-105 8120009-8 1994 Association of hsp90 (and presumably other heat shock proteins) with cytosolic GRs is drastically reduced by azide treatment, sufficient to account for decreased hormone binding. Azides 109-114 heat shock protein 86, pseudogene 1 Mus musculus 15-20 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). Azides 98-103 myoglobin Homo sapiens 166-175 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 211-216 solute carrier family 2 member 1 Rattus norvegicus 155-160 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 211-216 solute carrier family 2 member 1 Rattus norvegicus 38-43 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 211-216 solute carrier family 2 member 1 Rattus norvegicus 155-160 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 211-216 solute carrier family 2 member 1 Rattus norvegicus 38-43 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 211-216 solute carrier family 2 member 1 Rattus norvegicus 155-160 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 211-216 solute carrier family 2 member 1 Rattus norvegicus 155-160 7694490-9 1993 GLUT1 mRNA half-life was most prolonged (> 12 h) when azide was added subsequent to the addition of actinomycin D, and the half-life continued to be prolonged (6.5 +/- 0.5 h) in cells exposed to azide for 16 h.(ABSTRACT TRUNCATED AT 250 WORDS) Azides 57-62 solute carrier family 2 member 1 Rattus norvegicus 0-5 7694490-9 1993 GLUT1 mRNA half-life was most prolonged (> 12 h) when azide was added subsequent to the addition of actinomycin D, and the half-life continued to be prolonged (6.5 +/- 0.5 h) in cells exposed to azide for 16 h.(ABSTRACT TRUNCATED AT 250 WORDS) Azides 198-203 solute carrier family 2 member 1 Rattus norvegicus 0-5 8388211-5 1993 Azide, an inhibitor of myeloperoxidase, effectively reduced the neutrophil-catalyzed radical yield from the oxidation of MeH but not DMH. Azides 0-5 myeloperoxidase Rattus norvegicus 23-38 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). Azides 256-261 angiotensin I converting enzyme Bos taurus 122-125 8482389-0 1993 The structure of human carbonic anhydrase II in complex with bromide and azide. Azides 73-78 carbonic anhydrase 2 Homo sapiens 23-44 8482389-1 1993 The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Azides 78-83 carbonic anhydrase 2 Homo sapiens 41-62 7694490-1 1993 In previous studies, we have shown that inhibition of oxidative phosphorylation in Clone 9 cells (a nontransformed rat liver cell line) by 5 mM azide results in a marked biphasic stimulation of glucose transport that is mediated by GLUT1 [M. Shetty, J. N. Loeb, and F. Ismail-Beige. Azides 144-149 solute carrier family 2 member 1 Rattus norvegicus 232-237 7694490-7 1993 To investigate the mechanisms mediating GLUT1 mRNA induction, we have examined the effect of incubation in the presence of azide on GLUT1 gene transcription. Azides 123-128 solute carrier family 2 member 1 Rattus norvegicus 132-137 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 126-131 solute carrier family 2 member 1 Rattus norvegicus 38-43 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 126-131 solute carrier family 2 member 1 Rattus norvegicus 155-160 7694490-8 1993 In nuclear run-on assays, the rate of GLUT1 gene transcription was increased 2.5 +/- 0.3-fold in nuclei from cells exposed to azide for 4 h. Additionally, GLUT1 mRNA turnover was decreased in cells treated with azide: upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with half-lives of 2.3 +/- 0.3 and 8.0 +/- 0.5 h in control cells and cells treated with azide for 4 h, respectively. Azides 126-131 solute carrier family 2 member 1 Rattus norvegicus 155-160 8342610-7 1993 The beneficial effect of AZ may be due to its known ability to inhibit one or more enzymes including adenosinetriphosphatase, cytochrome-c oxidase, and myeloperoxidase. Azides 25-27 myeloperoxidase Rattus norvegicus 152-167 1315769-0 1992 Infrared evidence of azide binding to iron, copper, and non-metal sites in heart cytochrome c oxidase. Azides 21-26 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 81-101 8477723-0 1993 Crystallographic studies of azide binding to human carbonic anhydrase II. Azides 28-33 carbonic anhydrase 2 Homo sapiens 51-72 8477723-1 1993 The crystal structures of human carbonic anhydrase II (CAII) at pH 5.7 and 8.0 have been determined at 0.21-nm resolution in the presence of 20 mM azide, which is a noncompetitive inhibitor of the CAII-catalyzed CO2 hydration reaction. Azides 147-152 carbonic anhydrase 2 Homo sapiens 32-53 8477723-1 1993 The crystal structures of human carbonic anhydrase II (CAII) at pH 5.7 and 8.0 have been determined at 0.21-nm resolution in the presence of 20 mM azide, which is a noncompetitive inhibitor of the CAII-catalyzed CO2 hydration reaction. Azides 147-152 carbonic anhydrase 2 Homo sapiens 55-59 8477723-1 1993 The crystal structures of human carbonic anhydrase II (CAII) at pH 5.7 and 8.0 have been determined at 0.21-nm resolution in the presence of 20 mM azide, which is a noncompetitive inhibitor of the CAII-catalyzed CO2 hydration reaction. Azides 147-152 carbonic anhydrase 2 Homo sapiens 197-201 8477723-2 1993 Although azide often facilitates the crystallization of CAII and its variants, this small anion does not cause any significant structural changes in the enzyme active site or in the overall protein structure, and zinc coordination remains tetrahedral over the pH range 5.7-8.0. Azides 9-14 carbonic anhydrase 2 Homo sapiens 56-60 8380332-0 1993 Fourier-transform infrared study of azide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: new evidence for a redox-linked conformational change at the binuclear site. Azides 36-41 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 97-117 8380332-1 1993 Azide binding to the Fea3-CuB site of cytochrome c oxidase purified from bovine heart mitochondria was investigated in various redox levels by Fourier-transform infrared spectroscopy. Azides 0-5 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 38-58 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. Azides 78-83 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 57-77 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. Azides 99-104 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. Azides 26-31 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 5-25 8380332-7 1993 Upon the introduction of 1 electron equivalent to the fully oxidized cytochrome c oxidase-azide complex, an azide band at 2003.5 cm-1 developed. Azides 90-95 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 69-89 8380332-7 1993 Upon the introduction of 1 electron equivalent to the fully oxidized cytochrome c oxidase-azide complex, an azide band at 2003.5 cm-1 developed. Azides 108-113 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 69-89 1429633-6 1992 The ligand binding properties of these recombinant myoglobin proteins were studied by measurements of azide equilibrium and cyanide binding. Azides 102-107 myoglobin Homo sapiens 51-60 1424279-6 1992 Addition of inhibitors to the chemiluminescence system demonstrated that the chemiluminescence response was inhibited by azide and salicylhydroxamic acid and reduced by histidine, suggesting that the chemiluminescence response was due to activation of myeloperoxidase, with generation of singlet oxygen. Azides 121-126 myeloperoxidase Homo sapiens 252-267 1386722-4 1992 Azide sensitivity of ATPase activity and ADP-induced enhancement of bound aurovertin fluorescence, both of which are lost in alpha S373F mutant F1, were regained in alpha C373 F1. Azides 0-5 ATPase Escherichia coli 21-27 8230852-4 1993 The azide response in the pigmented and albino rdy rat was already reduced at the earliest age tested (60 d) and continued to decrease till the age of 2 years. Azides 4-9 MER proto-oncogene, tyrosine kinase Rattus norvegicus 47-50 1468561-2 1992 Resonance Raman spectra are reported for the carbon monoxide (CO) adduct of catalase formed from the reaction of peracetic acid or hydrogen peroxide with the azide adduct of catalase in the presence of CO. Azides 158-163 catalase Homo sapiens 76-84 1468561-2 1992 Resonance Raman spectra are reported for the carbon monoxide (CO) adduct of catalase formed from the reaction of peracetic acid or hydrogen peroxide with the azide adduct of catalase in the presence of CO. Azides 158-163 catalase Homo sapiens 174-182 1390645-1 1992 The mechanism of N-tetrazole ring formation at the distal histidyl imidazole of sperm whale myoglobin (Mb) has been studied by nitrogen-15 (15N) NMR spectroscopy by utilizing 15N-labeled cyanogen bromide (BrCN) and azide ion (N3-). Azides 215-220 myoglobin Physeter catodon 92-101 1615008-3 1992 Plasma ceruloplasmin, determined by azide-inhibitable oxidase activity with two substrates, was 8-fold less in the dog and 9- to 20-fold less in the mouse than in the rat, and, in both dogs and mice, there was 70-75% less ceruloplasmin Cu, determined by atomic absorption after gel filtration. Azides 36-41 ceruloplasmin Canis lupus familiaris 7-20 1319066-3 1992 The viricidal activity of stimulated monocytes was inhibited by the peroxidase inhibitor azide, implicating MPO, and by catalase but not heated catalase or superoxide dismutase, implicating H2O2. Azides 89-94 myeloperoxidase Homo sapiens 108-111 1319066-5 1992 The viricidal activity of stimulated, glucose oxidase-supplemented CGD monocytes and MPO-supplemented MPO-deficient monocytes, like that of normal stimulated monocytes, was inhibited by azide and catalase. Azides 186-191 myeloperoxidase Homo sapiens 85-88 1319066-5 1992 The viricidal activity of stimulated, glucose oxidase-supplemented CGD monocytes and MPO-supplemented MPO-deficient monocytes, like that of normal stimulated monocytes, was inhibited by azide and catalase. Azides 186-191 myeloperoxidase Homo sapiens 102-105 1315769-1 1992 Interactions of azide ion with bovine heart cytochrome c oxidase (CcO) at five redox levels (IV) to (0), obtained by zero to four electron reduction of fully oxidized enzyme CcO(IV), were monitored by infrared and visible/Soret spectra. Azides 16-21 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 44-64 1315769-1 1992 Interactions of azide ion with bovine heart cytochrome c oxidase (CcO) at five redox levels (IV) to (0), obtained by zero to four electron reduction of fully oxidized enzyme CcO(IV), were monitored by infrared and visible/Soret spectra. Azides 16-21 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 66-69 1315769-1 1992 Interactions of azide ion with bovine heart cytochrome c oxidase (CcO) at five redox levels (IV) to (0), obtained by zero to four electron reduction of fully oxidized enzyme CcO(IV), were monitored by infrared and visible/Soret spectra. Azides 16-21 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 174-177 1315769-2 1992 Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3. Azides 33-38 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 18-21 1315769-2 1992 Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3. Azides 33-38 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 96-99 1315769-2 1992 Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3. Azides 33-38 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 96-99 1315769-2 1992 Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3. Azides 33-38 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 96-99 1311041-10 1992 Azide, an inhibitor of MPO, and catalase, a scavenger of H2O2, inhibited the lytic activity of this system. Azides 0-5 myeloperoxidase Homo sapiens 23-26 1352211-5 1992 Myeloperoxidase is likely the enzyme in the leukocyte involved, since the oxidation was inhibited by azide, which inhibits myeloperoxidase, and by catalase, which catalyzes the breakdown of hydrogen peroxide. Azides 101-106 myeloperoxidase Homo sapiens 0-15 1352211-5 1992 Myeloperoxidase is likely the enzyme in the leukocyte involved, since the oxidation was inhibited by azide, which inhibits myeloperoxidase, and by catalase, which catalyzes the breakdown of hydrogen peroxide. Azides 101-106 myeloperoxidase Homo sapiens 123-138 1539639-5 1992 In time course studies an increase in GLUT-1 mRNA content was observed at 4 h and preceded the increment in GLUT-1 which became detectable after 8 h of exposure to azide. Azides 164-169 solute carrier family 2 member 1 Rattus norvegicus 38-44 1539639-5 1992 In time course studies an increase in GLUT-1 mRNA content was observed at 4 h and preceded the increment in GLUT-1 which became detectable after 8 h of exposure to azide. Azides 164-169 solute carrier family 2 member 1 Rattus norvegicus 108-114 1539639-6 1992 A marked induction of GLUT-1 mRNA by azide was also demonstrable in cells incubated in medium containing higher concentrations of glucose (10.6 mM), although the increment was approximately 20% less than when cells were incubated in standard medium (containing 5.6 mM glucose). Azides 37-42 solute carrier family 2 member 1 Rattus norvegicus 22-28 1314821-7 1992 The addition of purified myeloperoxidase to an enzymatic superoxide generating system resulted in the detection of hydroxyl radical that was dependent upon the presence of chloride and was inhibited by superoxide dismutase, catalase, and azide. Azides 238-243 myeloperoxidase Homo sapiens 25-40 1311714-1 1992 Insulin caused a transient increase in H2O2 accumulation in human fat cell suspensions that was observed only in the presence of an inhibitor of catalase and heme-containing peroxidases, such as azide, and reached peak levels of 30 microM within 5 min. Azides 195-200 insulin Homo sapiens 0-7 1733972-2 1992 Analysis of haptoglobin after 150 min of azide incubation shows that its carbohydrates have been processed by Golgi enzymes (Persson, R., Ahlstrom, E., and Fries, E. (1988) J. Azides 41-46 haptoglobin Rattus norvegicus 12-23 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). Azides 126-131 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). Azides 126-131 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). Azides 126-131 myeloperoxidase Homo sapiens 98-101 1769971-7 1991 The hydroxylation was inhibited by salts and azide due to interruption of the electron transport from NAD(P)H to cytochrome b5 and in the terminal enzyme reaction, respectively. Azides 45-50 cytochrome b5 type A Equus caballus 113-126 1930144-5 1991 Specific photocross-linking of 125I-2-(p-azidosalicylamido)-1,3"-dithiopropionate (125I-ASD)-CRP and 125I-ASD-SAP to nuclei revealed transfer of 125I-photoreactive azides to nuclear-envelope proteins of 43, 46, 52 and 70 kDa. Azides 164-170 amyloid P component, serum Rattus norvegicus 110-113 1761490-1 1991 Serum from normal human subjects contained variable amounts of catalase activity, which was inhibitable by heat, azide, trichloroacetic acid (TCA), or aminotriazole treatment. Azides 113-118 catalase Homo sapiens 63-71 2001370-2 1991 Both azides 1 and 2 demonstrate high binding affinity for ER as determined by both a competitive binding assay (relative binding affinities: estradiol = 100; TFAA = 9.3; PAA = 66) and a direct binding assay (Kd: estradiol = 0.24 nM; TFAA = 2.64 nM; PAA = 0.37 nM). Azides 5-11 estrogen receptor 1 Homo sapiens 58-60 1851410-3 1991 Over 95% of the luminol dependent chemiluminescence activated by all samples was inhibited by azide (indicating its dependence upon myeloperoxidase), but anti-(myeloperoxidase) IgG (which specifically inhibits only the extracellular activity of this enzyme) only inhibited the response stimulated by some samples: those fluids which activated the highest luminol dependent chemiluminescence also stimulated the greatest activity of an extracellular myeloperoxidase-H2O2 system. Azides 94-99 myeloperoxidase Homo sapiens 132-147 2001370-4 1991 Specific photocovalent attachment to ER can be effected by irradiation of the tritium-labeled azides; the covalent attachment efficiency is good (1 = 20-30%, 2 = ca. Azides 94-100 estrogen receptor 1 Homo sapiens 37-39 2001370-10 1991 Azides 1 and 2 are the most efficient and selective PAL reagents prepared to date for ER, and they should be useful in further studies of the hormone-binding domain of this protein. Azides 0-6 estrogen receptor 1 Homo sapiens 86-88 1846732-7 1991 All changes observed with the myeloperoxidase system were inhibited by azide or methionine, and were dependent upon the presence of chloride, indicating that they are mediated by HOCl. Azides 71-76 myeloperoxidase Homo sapiens 30-45 1654772-2 1991 Since luminol chemiluminescence (LCL) in neutrophils can be blocked by azide, an inhibitor of myeloperoxidase, LCL has been believed to reflect mainly the myeloperoxidase-catalyzed reaction. Azides 71-76 myeloperoxidase Homo sapiens 94-109 1654772-2 1991 Since luminol chemiluminescence (LCL) in neutrophils can be blocked by azide, an inhibitor of myeloperoxidase, LCL has been believed to reflect mainly the myeloperoxidase-catalyzed reaction. Azides 71-76 myeloperoxidase Homo sapiens 155-170 1849053-6 1991 Addition of azide, an MPO inhibitor, resulted in decreased tetraols from B[a]P-7,8-diol by PMNs or the MPO system. Azides 12-17 myeloperoxidase Homo sapiens 22-25 1849053-6 1991 Addition of azide, an MPO inhibitor, resulted in decreased tetraols from B[a]P-7,8-diol by PMNs or the MPO system. Azides 12-17 myeloperoxidase Homo sapiens 103-106 24197373-2 1990 This is demonstrated by the properties of the associated ATPase: high vanadate sensitivity, azide and nitrate insensitivity, sharp pH optimum around 6.5, and high specificity for ATP as substrate. Azides 92-97 dynein axonemal heavy chain 8 Homo sapiens 57-63 2246244-0 1990 Kinetics and thermodynamics of oxygen, CO, and azide binding by the subcomponents of soybean leghemoglobin. Azides 47-52 leghemoglobin A Glycine max 93-106 1648459-3 1991 Since interaction between the cells and ionomycin was not associated with any notable superoxide production and hydrogen peroxide was induced only in the presence of azide, a potent inhibitor of the hydrogen peroxide-consuming enzymes catalase and myeloperoxidase, we conclude that this stimulus can generate oxygen metabolites intracellularly. Azides 166-171 myeloperoxidase Homo sapiens 248-263 2165113-3 1990 Further, both azide and catalase + superoxide dismutase inhibited the ability of normal neutrophils to damage hyphae, suggesting that this damage is mediated by products of the respiratory burst and by the MPO-halide system. Azides 14-19 myeloperoxidase Homo sapiens 206-209 2171431-4 1990 However, inactivation of catalase in the hepatocytes with azide and addition of the reducing agent ascorbate markedly enhanced the cytotoxicity of the conjugate but did not affect benzoquinone-induced cytotoxicity. Azides 58-63 catalase Homo sapiens 25-33 2169299-5 1990 The luminol response was inhibited by superoxide dismutase (SOD), catalase, and the MPO-inhibitor azide, while the lucigenin response was inhibited by SOD and catalase but stimulated by azide. Azides 98-103 myeloperoxidase Homo sapiens 84-87 2173286-6 1990 Benzo(a)pyrene-7,8-diol chemiluminescence elicited by PMNs from all three species was significantly inhibited by azide, a myeloperoxidase inhibitor. Azides 113-118 myeloperoxidase Rattus norvegicus 122-137 2385230-1 1990 Mammalian A2-adenosine receptor binding subunits (A2AR) can be visualized by covalent labeling with the photoaffinity crosslinking ligand 125I-2-[4-[2-[2-[(4-aminophenyl)methylcarbonylamino] ethylaminocarbonyl]ethyl]phenyl]ethylamino-5"-N-ethylcarboxamidoad enosine or directly with the azide derivative described in this paper. Azides 287-292 adenosine A2a receptor Homo sapiens 50-54 2164216-6 1990 (iii) With H2O2, Cu,Zn-SOD, and DMPO, radical scavengers formate and azide, but not ethanol, decrease DMPO-OH signals while causing new intense signals due to their corresponding DMPO-radical adducts. Azides 69-74 superoxide dismutase 1 Homo sapiens 17-26 1705234-2 1990 Incubation of rat-liver microsomes, previously azide-treated to inhibit catalase, with H2O2 caused a loss of cytochrome P-450 but not of cytochrome b5. Azides 47-52 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 109-125 2111736-7 1990 Both, "spontaneous" and zymosan stimulated CL-Lum responses were inhibited by 100 microM azide and by 0.8 microM superoxide dismutase, suggesting the involvement of hemoproteins and superoxide anion in the measured responses. Azides 89-94 lumican Mus musculus 46-49 2166134-8 1990 On the other hand, azide titration shows that the affinity constant of N-3 for SOD is largely reduced upon PEG modification (K = 154 M-1 and 75 M-1 for the native and modified SOD, respectively). Azides 19-24 superoxide dismutase 1 Homo sapiens 79-82 2166134-8 1990 On the other hand, azide titration shows that the affinity constant of N-3 for SOD is largely reduced upon PEG modification (K = 154 M-1 and 75 M-1 for the native and modified SOD, respectively). Azides 19-24 superoxide dismutase 1 Homo sapiens 176-179 2154520-11 1990 Activities could also be distinguished based on the greater sensitivity of EPO to inhibition by thiocyanate, azide, aminotriazole, and dapsone. Azides 109-114 eosinophil peroxidase Homo sapiens 75-78 2337355-8 1990 Azide inhibited the catalase activity but stimulated the peroxidase activity. Azides 0-5 catalase Homo sapiens 20-28 2157502-2 1990 However, since ionomycin and FMLP activity differ in their requirement for azide, a potent inhibitor of the hydrogen peroxide consuming enzymes catalase and myeloperoxidase, we propose that the two stimuli can activate different pools of the oxidase. Azides 75-80 myeloperoxidase Homo sapiens 157-172 2343183-5 1990 The addition of azide, CuDIPS, or taurine markedly inhibited the induction of SCEs by the combination of BP-7,8-diol and stimulated PMNs, further suggesting the involvement of myeloperoxidase in the activation of the polycyclic aromatic hydrocarbon. Azides 16-21 myeloperoxidase Homo sapiens 176-191 2297707-2 1990 Initial studies indicated that in vitro [3H]MPCU was concentrated 4- to 6-fold in GC3/c1 human colon adenocarcinoma cells in an azide-sensitive manner. Azides 128-133 ankyrin repeat domain 36 Mus musculus 82-85 34967625-6 2022 This was deployed to enzymatically couple an azide group containing peptide sequence to mIL-4, allowing C-terminal bioconjugation of polyethylene glycol or poly(2-ethyl-2-oxazoline). Azides 45-50 interleukin 4 Mus musculus 88-93 33794095-3 2021 Herein, we report vitamin B12 derivatives possessing a photolabile linker suitable for conjugation with amines, azides, and alkynes. Azides 112-118 NADH:ubiquinone oxidoreductase subunit B3 Homo sapiens 26-29 34894657-3 2021 Utilizing DBCORC-TPP, an azide-conjugatable probe with acidity-triggered fluorescence, CALM is operated via DeltaPsim-promoted probe accumulation in mitochondria and thereby bioorthogonal ligation of the trapped probe with azido-choline (Azcholine) metabolically installed on the mitochondrial membrane. Azides 25-30 synaptosome associated protein 91 Homo sapiens 87-91 34931824-3 2022 Herein, a photoresponsive, glutathione, and reactive oxygen species block copolymer mPEG2k-ONB-SS-PO-mPEG2k is prepared by Cu(I)-catalyzed azide-alkyne cycloaddition click polymerization. Azides 139-144 insulin-like growth factor 2 Mus musculus 101-106 34843648-7 2021 Using nonobese diabetic (NOD) mice, we demonstrated that our strategy effectively and selectively conjugates PD-L1 onto beta cells through bioorthogonal stain-promoted azide-alkyne cycloaddition. Azides 168-173 CD274 antigen Mus musculus 109-114 34784173-3 2021 Here we obtain milligram quantities of lig1 of the allosteric homodimer, chorismate mutase, in the form of a mixed isotopically labeled dimer stabilized by Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) between the subunits. Azides 172-177 DNA ligase 1 Homo sapiens 39-43 34784173-3 2021 Here we obtain milligram quantities of lig1 of the allosteric homodimer, chorismate mutase, in the form of a mixed isotopically labeled dimer stabilized by Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) between the subunits. Azides 172-177 superoxide dismutase 1 Homo sapiens 62-71 34287823-2 2021 We report an RNA-controlled reaction system to conditionally restore the N-terminal amino group and thus binding affinity of azide-modified Smac mimetic compounds (SMCs) for their target protein X-linked Inhibitor of Apoptosis Protein (XIAP). Azides 125-130 diablo IAP-binding mitochondrial protein Homo sapiens 140-144 34287823-2 2021 We report an RNA-controlled reaction system to conditionally restore the N-terminal amino group and thus binding affinity of azide-modified Smac mimetic compounds (SMCs) for their target protein X-linked Inhibitor of Apoptosis Protein (XIAP). Azides 125-130 X-linked inhibitor of apoptosis Homo sapiens 195-234 34287823-2 2021 We report an RNA-controlled reaction system to conditionally restore the N-terminal amino group and thus binding affinity of azide-modified Smac mimetic compounds (SMCs) for their target protein X-linked Inhibitor of Apoptosis Protein (XIAP). Azides 125-130 X-linked inhibitor of apoptosis Homo sapiens 236-240 34425200-2 2021 Herein, we selectively introduced high affinity sialoside ligands of Siglec-1 and Siglec-7 to tumor cell surface via in vivo Strain-promoted Azide-Alkyne cyclization of TCCSiaalpha2,3-Lactose or FITCSiaalpha2,6-Lactose with 9-azido sialic acid (AzSia) metabolically installed on tumor cell surface. Azides 141-146 sialic acid binding Ig like lectin 1 Homo sapiens 69-77 34900969-4 2021 As expected, more BMP2p can be conjugated on PEEK after Azide-DOPA4 coating. Azides 56-61 bone morphogenetic protein 2 Rattus norvegicus 18-23 34580438-3 2021 Here, we show that the pharmacokinetics and half-life of IL-2 can be substantially improved by orthogonally conjugating the cytokine to poly(ethylene glycol) (PEG) moieties via a copper-free click reaction through the incorporation of azide-bearing amino acids at defined sites. Azides 235-240 interleukin 2 Mus musculus 57-61 34425200-2 2021 Herein, we selectively introduced high affinity sialoside ligands of Siglec-1 and Siglec-7 to tumor cell surface via in vivo Strain-promoted Azide-Alkyne cyclization of TCCSiaalpha2,3-Lactose or FITCSiaalpha2,6-Lactose with 9-azido sialic acid (AzSia) metabolically installed on tumor cell surface. Azides 141-146 sialic acid binding Ig like lectin 7 Homo sapiens 82-90 34399025-8 2021 A CSD search indicated the frequent and consistent occurrence of this interaction and its role dictating the syn conformation of azide and oxygen in molecules where these groups are separated by 2-4 bonds. Azides 129-134 synemin Homo sapiens 109-112 34473159-4 2021 A probable mechanistic rationalization has been proposed on the basis of theoretical calculations, which suggests systematic fragmentation of HL1 in the presence of azide residue and re-condensation of the fragmented units to yield the final Cu-HLF complex (2). Azides 165-170 asialoglycoprotein receptor 1 Homo sapiens 142-145 34399025-2 2021 Crystal structure analysis revealed that each of these molecules adopts a conformation in which the azide and oxygen groups orient syn to each other with a short O N b contact. Azides 100-105 synemin Homo sapiens 131-134 34473159-4 2021 A probable mechanistic rationalization has been proposed on the basis of theoretical calculations, which suggests systematic fragmentation of HL1 in the presence of azide residue and re-condensation of the fragmented units to yield the final Cu-HLF complex (2). Azides 165-170 HLF transcription factor, PAR bZIP family member Homo sapiens 245-248 34373887-6 2021 PSMA-targeting ligands (i.e., glutamate-urea-lysine derivatives called KuEs) and fluorescent or radiolabelled prosthetic groups were grafted onto the UCNP surface by strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 182-187 folate hydrolase 1 Homo sapiens 0-4 34590180-4 2021 Two conformers of protonated azides - syn- and anti- - were shown to precede corresponding transition states. Azides 29-35 synemin Homo sapiens 38-41 34422774-7 2021 Genetic code expansion was used to incorporate azide chemistry in cytochrome b 562 and alkyne chemistry in GFP so that a permanent triazole covalent linkage can be made between the two proteins. Azides 47-52 mitochondrially encoded cytochrome b Homo sapiens 66-78 34283589-6 2021 Specifically, we investigated the use of both amide bond formation and azide-alkyne ligation for connecting an OMP-targeting macrocyclic peptide to a PMEN building block (obtained by enzymatic degradation of polymyxin E). Azides 71-76 olfactory marker protein Homo sapiens 111-114 34374547-5 2021 We report the detection of frequency fluctuations of an azide anion (N3-) bound in the active site of the protein carbonic anhydrase II, where a low-frequency mode of the protein has been proposed to facilitate proton transfer over two water molecules during the catalyzed reaction. Azides 56-67 carbonic anhydrase 2 Bos taurus 114-135 35536049-5 2022 Then, AA could reduce Cu(II) to produce Cu(I), which plays the role of a catalyst to promote the click reaction of azide terephthalic acid (ATA) and 4-acetylene biphenyl (4-AB), resulting in the SERS signal intensity of free 4-AB in the solution was clearly reduced along with the click reaction carried on, and showed a quantitative relationship with the concentration of ALP. Azides 115-120 alkaline phosphatase, placental Homo sapiens 373-376 34203263-6 2021 Since the PBR28 structure lacks functional moieties that could be exploited for derivatization, in this work we explored a synthetic pathway for the synthesis of a PBR28 derivative carrying an alkyne group (PBR-alkyne), enabling the fast conjugation of the ligand through azide-alkyne cycloaddition, also known as click-chemistry. Azides 272-277 translocator protein Homo sapiens 207-210 35427123-14 2022 We constructed P-selectin targeted microbubbles using an azide-DBCO click reaction, which could detect bowel inflammation in vivo. Azides 57-62 selectin, platelet Mus musculus 15-25 35172039-5 2022 Furthermore, ( Tr L)Co(NC 6 F 5 ) undergoes reductive coupling with another equivalent of azide to furnish the four-coordinate tetrazido complex ( Tr L)Co( kappa 2 -N 4 (C 6 F 5 ) 2 ), expulsion of a fluorine atom to afford ( Tr L)CoF, and N-group transfer reactivity to PPh 3 . Azides 90-95 protein phosphatase 4 catalytic subunit Homo sapiens 271-276 35413191-3 2022 It has been demonstrated that 2 may serve as a synthon for (eta5-1,3-(Me3Si)2C5H3)2U(II) fragment in the presence of Ph2E2 (E = S, Se), alkynes, and a variety of hetero-unsaturated molecules such as diazabutadienes, azine (Ph2C N)2, o-benzoquinone, pyridine N-oxide, CS2, isothiocyanates, and organic azides. Azides 301-307 chorionic somatomammotropin hormone 2 Homo sapiens 267-270 35109860-6 2022 To increase the half-life of the Fab fragment, a 20 kDa PEG chain was attached via strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 99-104 FA complementation group B Homo sapiens 33-36 35245449-3 2022 We used structure-guided engineering of the Dnmt1 methyltransferase to enable catalytic transfer of azide tags onto DNA from a synthetic cofactor analog, Ado-6-azide, in vitro. Azides 100-105 DNA methyltransferase 1 Homo sapiens 44-49 35245449-4 2022 We then CRISPR-edited the Dnmt1 locus in mouse embryonic stem cells to install the engineered codon, which, following pulse internalization of the Ado-6-azide cofactor by electroporation, permitted selective azide tagging of Dnmt1-specific genomic targets in cellulo. Azides 208-213 DNA methyltransferase (cytosine-5) 1 Mus musculus 26-31 35245449-4 2022 We then CRISPR-edited the Dnmt1 locus in mouse embryonic stem cells to install the engineered codon, which, following pulse internalization of the Ado-6-azide cofactor by electroporation, permitted selective azide tagging of Dnmt1-specific genomic targets in cellulo. Azides 208-213 DNA methyltransferase (cytosine-5) 1 Mus musculus 225-230 35106375-7 2022 Glycan array analysis of antisera indicated that the azido-GH glycoconjugate with azide at Gal-C6 of Lac (1-CRM197) elicited the highest antibody response not only to GH, SSEA3, and SSEA4, which share the common SSEA3 epitope, but also to MCF-7 cancer cells, which express these Globo-series glycans. Azides 82-87 gamma-glutamyl hydrolase Homo sapiens 59-61 35106375-7 2022 Glycan array analysis of antisera indicated that the azido-GH glycoconjugate with azide at Gal-C6 of Lac (1-CRM197) elicited the highest antibody response not only to GH, SSEA3, and SSEA4, which share the common SSEA3 epitope, but also to MCF-7 cancer cells, which express these Globo-series glycans. Azides 82-87 lactase Homo sapiens 101-104 35106375-7 2022 Glycan array analysis of antisera indicated that the azido-GH glycoconjugate with azide at Gal-C6 of Lac (1-CRM197) elicited the highest antibody response not only to GH, SSEA3, and SSEA4, which share the common SSEA3 epitope, but also to MCF-7 cancer cells, which express these Globo-series glycans. Azides 82-87 gamma-glutamyl hydrolase Homo sapiens 167-169 2554813-10 1989 Addition of the MPO inhibitor azide to the reaction mixture had no effecting on resulting DMPO-OH or DMPO-CH3 peak amplitudes but increased that of DMPO-OOH. Azides 30-35 myeloperoxidase Homo sapiens 16-19 2557840-10 1989 Inhibition of MPO by azide increased the magnitude, but not the duration, of .OH formation. Azides 21-26 myeloperoxidase Homo sapiens 14-17 2751158-9 1989 Catalase and azide significantly inhibited the lysis of these cells, suggesting the eosinophil peroxidase-catalyzed products of halide oxidation mediated this form of injury. Azides 13-18 eosinophil peroxidase Homo sapiens 84-105 2624761-3 1989 Catalase was found to be instrumental in protecting epithelial cells because when inhibited by either azide or 3-amino-1,2,4-triazole, there was an increase in the cytotoxic effect of exogenous H2O2 and stimulated neutrophils. Azides 102-107 catalase Rattus norvegicus 0-8 2682656-1 1989 An oncogenic 21-kDa (p21) protein (Harvey RAS protein with Val-12) has been covalently modified with a functional reagent that contains a photoactivatable aromatic azide group. Azides 164-169 cyclin-dependent kinase inhibitor 1A (P21) Mus musculus 21-24 2682656-1 1989 An oncogenic 21-kDa (p21) protein (Harvey RAS protein with Val-12) has been covalently modified with a functional reagent that contains a photoactivatable aromatic azide group. Azides 164-169 Harvey rat sarcoma virus oncogene Mus musculus 35-45 2682656-4 1989 To identify the putative intracellular protein(s) that specifically interact with the modified p21 protein, the cells were pulsed with [35S]methionine at selected times after fusion and then UV-irradiated to activate the azide group. Azides 221-226 cyclin-dependent kinase inhibitor 1A (P21) Mus musculus 95-98 2790779-9 1989 (d) If the hepatocytes were compromised with azide or cyanamide to inhibit catalase, cytotoxicity was increased 10-fold or 100-fold if ascorbate was also present. Azides 45-50 catalase Rattus norvegicus 75-83 2775275-5 1989 Furthermore, in ADH-negative deermice, the catalase inhibitor azide (0.1 mM) did not inhibit the increase in ethanol oxidation by oleate and lactate. Azides 62-67 catalase Homo sapiens 43-51 17787990-3 1989 Very sensitive explosives occur within the extended azide family, where X(-) = CNO(-), N(3)(-), NCO(-), or NCS(-) (an isoelectronic set of unsaturated linear triatomic anions). Azides 52-57 biogenesis of lysosomal organelles complex 1 subunit 4 Homo sapiens 79-82 2474836-14 1989 Azide at 5 mM slowed the initial rate of AchE loss by about 75% with E16 and EYMA. Azides 0-5 acetylcholinesterase (Cartwright blood group) Homo sapiens 41-45 2474836-14 1989 Azide at 5 mM slowed the initial rate of AchE loss by about 75% with E16 and EYMA. Azides 0-5 RNA, U105C small nucleolar Homo sapiens 69-72 2544040-4 1989 Supporting the involvement of myeloperoxidase in the enhanced oxidant-generating status of these cells, the luminol-amplified chemiluminescence was found to be azide-, but not superoxide dismutase-inhibitable. Azides 160-165 myeloperoxidase Rattus norvegicus 30-45 2543723-2 1989 However, the presence of azide, a potent inhibitor of the hydrogen peroxide-consuming enzymes catalase and myeloperoxidase, was required to detect any release of hydrogen peroxide induced by ionomycin. Azides 25-30 myeloperoxidase Homo sapiens 107-122 2799756-3 1989 In ancillary experiments, the CL response of PMNs was inhibited by catalase (H2O2-scavenger), -azide (myeloperoxidase-MPO-inhibitor), taurine (hypochlorous acid-HOCl-scavenger) and chloride ion omission. Azides 95-100 myeloperoxidase Homo sapiens 102-117 2542309-5 1989 Both loss of iron binding capacity and transferrin iodination by either the myeloperoxidase system or activated neutrophils were blocked by azide or catalase. Azides 140-145 transferrin Homo sapiens 39-50 2542309-5 1989 Both loss of iron binding capacity and transferrin iodination by either the myeloperoxidase system or activated neutrophils were blocked by azide or catalase. Azides 140-145 myeloperoxidase Homo sapiens 76-91 2712574-6 1989 Second, hepatocyte ethanol metabolism was measured after addition of the catalase inhibitor azide (0.1 mM) and found to be unchanged. Azides 92-97 catalase Homo sapiens 73-81 2540257-3 1989 Azide, a myeloperoxidase (MPO) inhibitor, reduced the CL reaction by more than 80%, which indicates that the CL reaction is dependent on the granule enzyme MPO. Azides 0-5 myeloperoxidase Homo sapiens 9-24 2540257-3 1989 Azide, a myeloperoxidase (MPO) inhibitor, reduced the CL reaction by more than 80%, which indicates that the CL reaction is dependent on the granule enzyme MPO. Azides 0-5 myeloperoxidase Homo sapiens 26-29 2540257-3 1989 Azide, a myeloperoxidase (MPO) inhibitor, reduced the CL reaction by more than 80%, which indicates that the CL reaction is dependent on the granule enzyme MPO. Azides 0-5 myeloperoxidase Homo sapiens 156-159 2538428-0 1989 Single-crystal EPR study of novel azide complex of cyanogen bromide-modified myoglobin. Azides 34-39 myoglobin Homo sapiens 77-86 2538428-2 1989 Stable azide complex of cyanogen bromide-modified met-myoglobin (metMb) was prepared and crystallized. Azides 7-12 myoglobin Homo sapiens 54-63 2494259-9 1989 The response to chymase was non-cytotoxic and was blocked by active site inhibitors of chymase (soybean trypsin inhibitor and chymostatin) and by inhibitors of cellular energy metabolism (azide,2,4-dinitrophenol, dicumarol). Azides 188-193 chymase 1 Canis lupus familiaris 16-23 2535783-5 1989 However, in the presence of azide, a potent inhibitor of the hydrogen peroxide-consuming enzymes, catalase and myeloperoxidase, a pronounced release of hydrogen peroxide was also induced by ionomycin. Azides 28-33 catalase Homo sapiens 98-106 2535783-5 1989 However, in the presence of azide, a potent inhibitor of the hydrogen peroxide-consuming enzymes, catalase and myeloperoxidase, a pronounced release of hydrogen peroxide was also induced by ionomycin. Azides 28-33 myeloperoxidase Homo sapiens 111-126 2824089-3 1987 Azide treatment only slightly affects adhesion of cells to FN, but strongly inhibits cell attachment to DC and NC. Azides 0-5 fibronectin 1 Mus musculus 59-61 2909739-0 1989 Prostaglandin photoaffinity probes: synthesis and biological activity of azide-substituted 16-phenoxy- and 17-phenyl-PGF2 alpha prostaglandins. Azides 73-78 placental growth factor Bos taurus 117-120 2485131-7 1988 Studies on the possible role of the granulocyte enzyme myeloperoxidase in the activation and binding of these arylamines were conducted in vitro and also through the use of azide, an inhibitor of myeloperoxidase activity in cells. Azides 173-178 myeloperoxidase Homo sapiens 55-70 2485131-7 1988 Studies on the possible role of the granulocyte enzyme myeloperoxidase in the activation and binding of these arylamines were conducted in vitro and also through the use of azide, an inhibitor of myeloperoxidase activity in cells. Azides 173-178 myeloperoxidase Homo sapiens 196-211 3414603-2 1988 The HemoCue system measures the hemoglobin level in undiluted capillary or venous blood after conversion of hemoglobin to azide methemoglobin. Azides 122-127 hemoglobin subunit gamma 2 Homo sapiens 128-141 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). Azides 96-101 cytochrome c, somatic Homo sapiens 0-12 3449091-5 1987 The rate of formation of the azidomethyltriazene increasing azide concentration, suggesting either an SN2 mechanism or a significant ionic strength effect on an SN1 reaction. Azides 60-65 solute carrier family 38 member 5 Homo sapiens 102-105 3449091-5 1987 The rate of formation of the azidomethyltriazene increasing azide concentration, suggesting either an SN2 mechanism or a significant ionic strength effect on an SN1 reaction. Azides 60-65 solute carrier family 38 member 3 Homo sapiens 161-164 2826144-0 1987 The uptake of protons by heme-linked ionizable groups on azide binding to methemoglobin. Azides 57-62 hemoglobin subunit gamma 2 Homo sapiens 74-87 2826144-1 1987 When azide ion reacts with methemoglobin in unbuffered solution the pH of the solution increases. Azides 5-10 hemoglobin subunit gamma 2 Homo sapiens 27-40 2826144-3 1987 We have determined as a functional of pH the proton uptake, delta h+, on azide binding to methemoglobin at 20 degrees C. Data for methemoglobins A (human), guinea pig and pigeon are fitted to a theoretical expression based on the electrostatic effect of these sets of heme-linked ionizable groups on the binding of the ligand. Azides 73-78 hemoglobin subunit gamma 2 Homo sapiens 90-103 2966145-9 1987 The chemical modification reagent, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, caused inactivation of the ATPase activity although the enzyme was not inhibited by N,N"-dicyclohexylcarbodiimide, N-ethyl-maleimide, azide or vanadate. Azides 210-215 ATZ20_RS04105 Sulfolobus acidocaldarius 103-109 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. Azides 23-28 thyroid peroxidase Homo sapiens 45-63 3209423-1 1988 A histochemical technique was developed for the quantitative determination of succinic dehydrogenase (SDH) activity in muscle cross-sections using 1-methoxyphenazine methosulphate (mPMS) as the exogenous electron carrier, and azide as an inhibitor of cytochrome oxidase. Azides 226-231 succinate dehydrogenase complex iron sulfur subunit B Homo sapiens 102-105 3397978-5 1988 Inhibition of catalase (with 3-amino 1,2,4 triazole or azide) was found to depress synthesis further, possibly because of exposure to higher steady state levels of H2O2. Azides 55-60 catalase Homo sapiens 14-22 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. Azides 266-271 transmembrane protein 132A Rattus norvegicus 137-140 3349028-15 1988 The concentration of azide required for 50% inhibition of enzyme activity was 20-fold greater for LPO than for SPO. Azides 21-26 lactoperoxidase Homo sapiens 98-101 2974293-3 1988 The enzyme activity was not affected by Na+, K+, ouabain and azide, and exhibited an absolute requirement for Mg2+ ions. Azides 61-66 mucin 7, secreted Homo sapiens 110-113 2887427-15 1987 The ATPase is insensitive to azide or vanadate but is inhibited by relatively low concentrations of nitrate. Azides 29-34 ATZ20_RS04105 Sulfolobus acidocaldarius 4-10 2821114-13 1987 Moreover, the mononuclear leukocytes contain an azide-sensitive factor, probably catalase, which provides partial protection against injury by neutrophil products. Azides 48-53 catalase Homo sapiens 81-89 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. Azides 102-107 RP1 axonemal microtubule associated Homo sapiens 0-3 2952501-7 1987 The ATPase activity is not inhibited by N,N"-dicyclohexylcarbodiimide, azide or vanadate, but it is by the vascular ATPase inhibitor nitrate with an [I]50 of 8 mM. Azides 71-76 ATZ20_RS04105 Sulfolobus acidocaldarius 4-10 16665635-3 1987 The H(+)-ATPase was associated with a low density membrane population having a peak density of 1.11 grams per cubic centimeter, and its activity was inhibited by NO(3) (-), N,N"-dicyclohexylcarbodiimide and diethylstilbestrol but not by vanadate, azide, molybdate, or oligomycin. Azides 247-252 plasma membrane ATPase 1 Solanum lycopersicum 4-15 2822016-3 1987 This was inhibited by azide and methionine, indicating that inactivation was due to myeloperoxidase-derived oxidants. Azides 22-27 myeloperoxidase Homo sapiens 84-99 3312184-6 1987 Trp-130 of rabbit skeletal myosin heavy chain, which was reported to cross-link to an azide derivative of ATP by Okamoto and Yount (Proc. Azides 86-91 myosin, heavy chain 15 Gallus gallus 27-33 3555347-5 1987 Azide (0.1 mM), a potent inhibitor of catalase in vitro, also did not affect ethanol oxidation in control cells. Azides 0-5 catalase Homo sapiens 38-46 3031158-15 1987 The reaction could also be inhibited by superoxide dismutase and azide, indicating that O-2 and heme or an iron-dependent enzyme were required for the reaction. Azides 65-70 immunoglobulin kappa variable 1D-39 Homo sapiens 88-91 3029204-9 1987 Catalase and azide substantially inhibited the lysis produced by the EPO-H2O2-halide system, suggesting that EPO-catalyzed products of halide oxidation mediated this form of injury. Azides 13-18 eosinophil peroxidase Homo sapiens 69-72 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. Azides 10-15 myeloperoxidase Homo sapiens 174-189 3029204-9 1987 Catalase and azide substantially inhibited the lysis produced by the EPO-H2O2-halide system, suggesting that EPO-catalyzed products of halide oxidation mediated this form of injury. Azides 13-18 eosinophil peroxidase Homo sapiens 109-112 3793732-2 1987 In contrast, reconstituted azide or CO myoglobin initially exhibited less circular dichroism in the Soret wavelength region than native myoglobin. Azides 27-32 myoglobin Physeter catodon 136-145 3756179-8 1986 Acta 829, 327-334), the spin equilibrium constants of methemoglobin subunits are calculated from kinetic and equilibrium binding parameters with azide ion as ligand. Azides 145-150 hemoglobin subunit gamma 2 Homo sapiens 54-67 3793764-6 1987 Upon visualization with fluorescent alpha-bungarotoxin, some AChR in azide-treated samples appear as small, bright spots. Azides 69-74 cholinergic receptor nicotinic alpha 2 subunit Rattus norvegicus 61-65 3793764-9 1987 During reformation of AChR clusters upon removal of azide, IMP concentration in receptor domains increases. Azides 52-57 cholinergic receptor nicotinic alpha 2 subunit Rattus norvegicus 22-26 3032797-9 1987 Azide inhibited the effects of the MPO-H2O2-Cl- system. Azides 0-5 myeloperoxidase Homo sapiens 35-38 2989289-1 1985 Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide. Azides 79-84 myeloperoxidase Homo sapiens 38-53 3017930-9 1986 The findings suggest that O-2, formed during phagocytosis, is converted to H2O2 within phagosomes and then diffuses out into the extracellular medium when its decomposition by catalase and/or peroxidases is blocked by azide. Azides 218-223 immunoglobulin kappa variable 1D-39 Homo sapiens 26-29 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). Azides 140-145 myeloperoxidase Homo sapiens 46-61 3008887-2 1986 The lysis was inhibited by azide, catalase, chloride-free medium and amino acids, suggesting the requirement for myeloperoxidase (MPO), hydrogen peroxide (H2O2), chloride ions (Cl-), and hypochlorous acid (HOC1), respectively. Azides 27-32 eosinophil peroxidase Gallus gallus 113-128 3016275-1 1986 The lysis of human red blood cells (HRBC) by neutrophil polymorphonuclear leukocytes (PMN), triggered with opsonized zymosan (OPZ) particles, was inhibited by azide, catalase, Cl- -free medium and amino acids indicating the involvement of myeloperoxidase (MPO), hydrogen peroxide (H2O2), Cl- ions and hypochlorous acid (HOCl) respectively. Azides 159-164 catalase Homo sapiens 166-174 3016275-1 1986 The lysis of human red blood cells (HRBC) by neutrophil polymorphonuclear leukocytes (PMN), triggered with opsonized zymosan (OPZ) particles, was inhibited by azide, catalase, Cl- -free medium and amino acids indicating the involvement of myeloperoxidase (MPO), hydrogen peroxide (H2O2), Cl- ions and hypochlorous acid (HOCl) respectively. Azides 159-164 myeloperoxidase Homo sapiens 239-254 3016275-1 1986 The lysis of human red blood cells (HRBC) by neutrophil polymorphonuclear leukocytes (PMN), triggered with opsonized zymosan (OPZ) particles, was inhibited by azide, catalase, Cl- -free medium and amino acids indicating the involvement of myeloperoxidase (MPO), hydrogen peroxide (H2O2), Cl- ions and hypochlorous acid (HOCl) respectively. Azides 159-164 myeloperoxidase Homo sapiens 256-259 3955232-5 1986 The method for quantitating cytochrome b was modified by using PMN sonicates incubated with azide plus hydrogen peroxide. Azides 92-97 mitochondrially encoded cytochrome b Homo sapiens 28-40 2863267-5 1985 Apart from resistance to azide, the tonoplast-type ATPase was strikingly similar in its inhibitor sensitivities to the mitochondrial ATPase. Azides 25-30 dynein axonemal heavy chain 8 Homo sapiens 51-57 4037797-7 1985 Chicken ceruloplasmin catalyzed the azide-sensitive oxidation of p-phenylenediamine (PPD) and N,N"-dimethyl-p-phenylenediamine (DPD), and showed ferroxidase activity similar to that of human ceruloplasmin. Azides 36-41 ceruloplasmin Gallus gallus 8-21 4037797-7 1985 Chicken ceruloplasmin catalyzed the azide-sensitive oxidation of p-phenylenediamine (PPD) and N,N"-dimethyl-p-phenylenediamine (DPD), and showed ferroxidase activity similar to that of human ceruloplasmin. Azides 36-41 ceruloplasmin Homo sapiens 191-204 2989289-8 1985 Glutathione-glutathione peroxidase (GSH-GSH peroxidase), an extracellular H2O2 scavenger, totally protected neutrophil myeloperoxidase from inactivation by azide plus glucose-glucose oxidase. Azides 156-161 myeloperoxidase Homo sapiens 119-134 2989289-9 1985 In addition, when a mixture of normal and CGD cells was stimulated with PMA in the presence of azide, 90% of the myeloperoxidase in CGD neutrophils was inactivated. Azides 95-100 myeloperoxidase Homo sapiens 113-128 2989289-11 1985 In contrast, myeloperoxidase in normal polymorphonuclear leukocytes stimulated with PMA in the presence of azide and GSH-GSH peroxidase was 75% inactivated. Azides 107-112 myeloperoxidase Homo sapiens 13-28 2989289-2 1985 It is well known that catalase is transformed to nitric oxide-Fe2+-catalase by hydrogen peroxide (H2O2) plus azide. Azides 109-114 catalase Homo sapiens 22-30 2989289-2 1985 It is well known that catalase is transformed to nitric oxide-Fe2+-catalase by hydrogen peroxide (H2O2) plus azide. Azides 109-114 catalase Homo sapiens 67-75 2989289-3 1985 In this report, we show that myeloperoxidase is also inactivated by H2O2 plus azide. Azides 78-83 myeloperoxidase Homo sapiens 29-44 2989289-5 1985 Stimulation of neutrophils with phorbol myristate acetate (PMA, 100 ng/ml) plus azide (5 mM) for 30 min completely inactivated intragranular myeloperoxidase and reduced cytosolic catalase to 35% of resting cells. Azides 80-85 myeloperoxidase Homo sapiens 141-156 2989289-5 1985 Stimulation of neutrophils with phorbol myristate acetate (PMA, 100 ng/ml) plus azide (5 mM) for 30 min completely inactivated intragranular myeloperoxidase and reduced cytosolic catalase to 35% of resting cells. Azides 80-85 catalase Homo sapiens 179-187 2989289-7 1985 Incubation of neutrophils with azide and a H2O2 generating system (glucose-glucose oxidase) inactivated 41% of neutrophil myeloperoxidase. Azides 31-36 myeloperoxidase Homo sapiens 122-137 2857551-0 1985 Interaction of azide with beef heart mitochondrial ATPase. Azides 15-20 ATP synthase F1 subunit epsilon Homo sapiens 37-57 2861789-8 1985 Also, if endogenous catalase is inhibited by azide, rabbit liver microsomes catalyze the inactivation of glutamine synthetase. Azides 45-50 catalase Oryctolagus cuniculus 20-28 2991910-2 1985 Cu(II)(3,5-diisopropylsalicylic acid)2 (CuDIPS), a biomimetic superoxide dismutase, and azide, a myeloperoxidase inhibitor, inhibited both of these reactions, indicating a dependency on oxygen-derived oxidants in these hydrocarbon-activation processes. Azides 88-93 myeloperoxidase Homo sapiens 97-112 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. Azides 173-178 NADH:ubiquinone oxidoreductase subunit B3 Homo sapiens 12-15 6325409-6 1984 Fluorescent changes accompanying phagocytosis of serum-opsonized 5-isothiocyanatofluorescein-zymosan were also consistent with chlorination of the label; the changes were shown to be myeloperoxidase-dependent by use of myeloperoxidase-deficient or azide-treated cells. Azides 248-253 myeloperoxidase Homo sapiens 183-198 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. Azides 33-38 myeloperoxidase Bos taurus 125-140 3155777-6 1985 Several parameters that could affect the binding of C3b-coated microspheres to neutrophils were studied; these included time and temperature of incubation of the microspheres with the cells, the diameter of the microspheres, the C3b content of the C3b-coated microspheres, the presence of metal ions, azide, EDTA, protein (BSA, IgG), soybean trypsin inhibitor in the buffers, and the method of isolation of the neutrophils. Azides 301-306 endogenous retrovirus group K member 3 Homo sapiens 52-55 6151045-3 1984 Effective inhibition by normal alpha 1-antitrypsin occurred at much lower concentrations when azide or catalase was added, or when normal neutrophils were replaced by those from a donor with chronic granulomatous disease. Azides 94-99 serpin family A member 1 Homo sapiens 31-50 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. Azides 243-248 C-C motif chemokine ligand 4 Rattus norvegicus 28-32 6095975-3 1984 The optical absorption of P. mirabilis PR catalase in the presence of various anionic species (cyanide, azide, formate) was examined. Azides 104-109 catalase Bos taurus 42-50 4036175-5 1985 SubMIC penicillin pretreatment of S. pneumoniae R36A specifically promoted the susceptibility of these organisms to killing by myeloperoxidase (MPO)-mediated mechanisms (enhancement lost using MPO-deficient or azide-treated cells). Azides 210-215 myeloperoxidase Homo sapiens 127-142 4036175-5 1985 SubMIC penicillin pretreatment of S. pneumoniae R36A specifically promoted the susceptibility of these organisms to killing by myeloperoxidase (MPO)-mediated mechanisms (enhancement lost using MPO-deficient or azide-treated cells). Azides 210-215 myeloperoxidase Homo sapiens 144-147 6696880-2 1984 In the noncooperative system, azide binding to methemoglobin, the alterations in exchange kinetics are proportional to the average degree of ligation. Azides 30-35 hemoglobin subunit gamma 2 Homo sapiens 47-60 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. Azides 41-46 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. Azides 41-46 myeloperoxidase Homo sapiens 102-117 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. Azides 41-46 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. Azides 41-46 eosinophil peroxidase Homo sapiens 174-195 16663096-1 1983 When assayed in the presence of azide, NO(3) (-) was shown to be a specific inhibitor of a proton-translocating ATPase present in corn (Zea mays L. cv WF9 x M017) root microsomal membranes. Azides 32-37 ATPase Zea mays 112-118 6657916-8 1983 When human serum albumin (HSA) was oxidized using radiolytically generated azide radicals, a radical transformation involving TrpH and TyrOH residues occurred with k = 3.8 X 10(3) sec-1. Azides 75-80 albumin Homo sapiens 11-30 6657916-8 1983 When human serum albumin (HSA) was oxidized using radiolytically generated azide radicals, a radical transformation involving TrpH and TyrOH residues occurred with k = 3.8 X 10(3) sec-1. Azides 75-80 tryptophan hydroxylase 1 Homo sapiens 126-130 6657916-8 1983 When human serum albumin (HSA) was oxidized using radiolytically generated azide radicals, a radical transformation involving TrpH and TyrOH residues occurred with k = 3.8 X 10(3) sec-1. Azides 75-80 secretory blood group 1, pseudogene Homo sapiens 180-185 6311062-4 1983 This loss of elastase binding activity was abrogated by the addition of azide or catalase but not superoxide dismutase or heated catalase. Azides 72-77 elastase, neutrophil expressed Homo sapiens 13-21 6683096-6 1983 Azide, which inhibits contaminating catalase in microsomes, increased the oxidation of dimethyl sulfoxide and 2-keto-4-thiomethylbutyric acid by both microsomal preparations. Azides 0-5 catalase Rattus norvegicus 36-44 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. Azides 28-33 myeloperoxidase Homo sapiens 163-178 6189586-4 1983 However, glucose or azide increased the fraction of dihydrofolate reductase associated with methotrexate and abolished the effect of tetrahydrofolates on this intracellular component. Azides 20-25 dihydrofolate reductase Mus musculus 52-75 6289706-7 1982 The "antioxidant" activity of ceruloplasmin is inhibited by azide. Azides 60-65 ceruloplasmin Homo sapiens 30-43 6295926-2 1983 The target cell lysis was prevented by azide, suggesting the involvement of the myeloperoxidase enzyme. Azides 39-44 myeloperoxidase Homo sapiens 80-95 6220498-1 1983 The nuclei of the rat liver, heart, thymus and of the mouse liver isolated in sucrose gradient reveal ATPase sensitive to bicarbonate, sulfite, azide and thiocyanate. Azides 144-149 dynein, axonemal, heavy chain 8 Mus musculus 102-108 6131444-2 1982 This synthesis involves the linkage of Boc-Phe-D-Trp-Lys[Z(pCl)]-Thr-Phe-Thr-Ser-OH to H-Hcy(CH2-CO-Lys[Z(oCl)]-Asn-Phe-OMe)-NH2 and subsequent azide cyclization. Azides 144-149 BOC cell adhesion associated, oncogene regulated Rattus norvegicus 39-42 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. Azides 64-69 myeloperoxidase Homo sapiens 24-39 7142703-4 1982 It requires low numbers of viable neutrophils and physiologic concentrations of chloride and is blocked by addition of azide, cyanide, catalase, or methionine, but not methionine sulfoxide, superoxide dismutase, or heated catalase. Azides 119-124 catalase Homo sapiens 222-230 16593251-2 1982 Its phosphorylation, like that of plasma membrane ATPase, was dependent on Mg(2+), substrate specific for ATP, insensitive to azide, oligomycin, or molybdate, and sensitive to N,N"-dicyclohexylcarbodiimide, diethylstilbestrol, or vanadate. Azides 126-131 ATPase Zea mays 50-56 6280725-5 1982 In the absence of the catalase inhibitor azide, methanol may be oxidized primarily by the peroxidatic activity of catalase since there was little effect on methanol oxidation by competing hydroxyl radical scavengers. Azides 41-46 catalase Rattus norvegicus 114-122 6281334-7 1982 Incubation of eosinophils with azide that inhibits EPO, and catalase that degrades H2O2, significantly increased the amount of SRS activity detected in the extracellular medium after A23187 stimulation. Azides 31-36 eosinophil peroxidase Equus caballus 51-54 6802924-8 1982 Cytolysis was also completely inhibitable by azide (50 percent inhibition, 2.6 X 10 -5 M), indicating a requirement for enzymatic activity of EPO. Azides 45-50 eosinophil peroxidase Equus caballus 142-145 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. Azides 86-91 SagB/ThcOx family dehydrogenase Methanobacterium formicicum 21-34 6280725-6 1982 Azide, which inhibited catalase activity greater than 95%, inhibited NADPH-dependent oxidation of methanol by 30-50%. Azides 0-5 catalase Rattus norvegicus 23-31 6280725-7 1982 The azide-insensitive (catalase-independent) pathway of methanol oxidation was inhibited by scavengers of hydroxyl radicals. Azides 4-9 catalase Rattus norvegicus 23-31 6277912-3 1982 The addition of catalase or the myeloperoxidase inhibitor, azide, protected all three prostaglandins from the phorbol-stimulated neutrophils. Azides 59-64 myeloperoxidase Homo sapiens 32-47 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. Azides 260-265 myeloperoxidase Homo sapiens 150-165 7054281-6 1982 The peroxidase inhibitor azide inhibited the killing of staph-EPO by these mononuclear phagocytes without affecting the killing of control staphylococci; in the presence azide, the killing curve with staph-EPO returned to that seen with control organisms. Azides 25-30 AT695_RS02070 Staphylococcus aureus 4-14 7054281-6 1982 The peroxidase inhibitor azide inhibited the killing of staph-EPO by these mononuclear phagocytes without affecting the killing of control staphylococci; in the presence azide, the killing curve with staph-EPO returned to that seen with control organisms. Azides 170-175 AT695_RS02070 Staphylococcus aureus 4-14 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. Azides 93-98 myeloperoxidase Homo sapiens 165-180 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. Azides 204-209 myeloperoxidase Homo sapiens 53-68 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. Azides 76-81 catalase Homo sapiens 97-105 7262080-6 1981 Direct measurements of pH changes during catalase interaction with these ligands also indicate stoichiometric uptake of one proton per haem group upon addition of formate or azide at pH 6, but at greater pH values the proton uptake declines, suggesting the involvement of a secondary site in the liganding reaction. Azides 174-179 catalase Homo sapiens 41-49 16661370-5 1980 The bean ABP auxin binding site is similar to the corn endoplasmic reticulum auxin-binding sites in specificity for auxins and sensitivity to thiol reagents and azide. Azides 161-166 auxin-binding protein 4 Zea mays 9-12 7009832-4 1981 Inhibition of catalase by azide affected the activity of the non-ADH pathway by less than 10%. Azides 26-31 catalase Rattus norvegicus 14-22 7009832-4 1981 Inhibition of catalase by azide affected the activity of the non-ADH pathway by less than 10%. Azides 26-31 aldo-keto reductase family 1 member A1 Rattus norvegicus 65-68 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. Azides 199-204 myeloperoxidase Homo sapiens 87-102 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. Azides 45-50 cytochrome c, somatic Equus caballus 79-91 6252248-5 1980 Azide, which in addition to its blocking action on oxydative phosphorylation also inhibits catalase and myeloperoxidase, resulted in a approximately equal to 40% stimulation of ADCC by cells from normals but was without effect of ADCC by cells from CGD patients. Azides 0-5 catalase Homo sapiens 91-99 6252248-5 1980 Azide, which in addition to its blocking action on oxydative phosphorylation also inhibits catalase and myeloperoxidase, resulted in a approximately equal to 40% stimulation of ADCC by cells from normals but was without effect of ADCC by cells from CGD patients. Azides 0-5 myeloperoxidase Homo sapiens 104-119 7426622-0 1980 Resonance Raman spectra of manganese myoglobin and its azide complex. Azides 55-60 myoglobin Homo sapiens 37-46 7426622-2 1980 The enhancement of bound azide vibrations at 650 [depolarized (dp), bending] and 2039 cm-1 (dp, antisymmetric stretch) upon excitation at approximately 400-460 nm indicates the existence of a new charge-transfer transition in manganese(III) myoglobin-azide complex. Azides 25-30 myoglobin Homo sapiens 241-250 6773547-6 1980 The stimulation by Fe-EDTA appears to represent a pathway involving hydroxyl radicals rather than catalase because (1) stimulation occurred in the presence of azide, which inhibits catalase, (2) stimulation occurred in the presence of 1-butanol, which is not an effective substrate for catalase, and (3) stimulation was blocked by hydroxyl radical scavenging agents, which do not affect catalase-mediated oxidation of ethanol. Azides 159-164 catalase Homo sapiens 181-189 6773547-6 1980 The stimulation by Fe-EDTA appears to represent a pathway involving hydroxyl radicals rather than catalase because (1) stimulation occurred in the presence of azide, which inhibits catalase, (2) stimulation occurred in the presence of 1-butanol, which is not an effective substrate for catalase, and (3) stimulation was blocked by hydroxyl radical scavenging agents, which do not affect catalase-mediated oxidation of ethanol. Azides 159-164 catalase Homo sapiens 181-189 6773547-6 1980 The stimulation by Fe-EDTA appears to represent a pathway involving hydroxyl radicals rather than catalase because (1) stimulation occurred in the presence of azide, which inhibits catalase, (2) stimulation occurred in the presence of 1-butanol, which is not an effective substrate for catalase, and (3) stimulation was blocked by hydroxyl radical scavenging agents, which do not affect catalase-mediated oxidation of ethanol. Azides 159-164 catalase Homo sapiens 181-189 6244848-2 1980 The reaction of myeloperoxidase with fluoride, chloride and azide has been studied by EPR. Azides 60-65 myeloperoxidase Homo sapiens 16-31 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. Azides 151-156 erythropoietin Cavia porcellus 4-7 226523-0 1979 Azide binding to the cytochrome c ferric heme octapeptide. Azides 0-5 cytochrome c, somatic Homo sapiens 21-33 6159758-0 1980 Azide reversibly raises cyclic GMP levels in hepatic slices and activates guanylate cyclase. Azides 0-5 5'-nucleotidase, cytosolic II Homo sapiens 31-34 7352984-5 1980 A model study of the azide-methemoglobin complex suggested that the increase of the high-spin character of the beta heme iron is due to a conformational change of the proximal histidine which weakens the interaction between the heme iron and the proximal base. Azides 21-26 hemoglobin subunit gamma 2 Homo sapiens 27-40 291908-2 1979 In the first, an aryl azide derivative of insulin, 125I-labeled 4-azido-2-nitrophenyl-insulin, was synthesized and used to photolabel the binding region of the insulin receptor in rat liver membranes and human placenta membranes. Azides 17-27 insulin receptor Rattus norvegicus 160-176 388210-0 1979 Azide-induced mutagenesis in gram-negative bacteria is recA-and lexA-independent. Azides 0-5 DNA repair system Escherichia coli 64-68 511929-8 1979 Small AChR aggregates also appear to be precursors of clusters which form on myotubes never exposed to azide. Azides 103-108 cholinergic receptor nicotinic alpha 2 subunit Rattus norvegicus 6-10 388210-3 1979 The mutagenic effect of azide was also observed in uvrA lexA mutants of E. coli K12 and E. coli B/r. Azides 24-29 DNA repair system Escherichia coli 56-60 427108-2 1979 Inhibition by both compounds was more effective in the presence of the catalase inhibitor, azide. Azides 91-96 catalase Homo sapiens 71-79 158207-3 1979 Inhibitors of oxidative phosphorylation (oligomycin, azide and amytal) had a more potent inhibitory effect on the hydrolytic activity of ATPase in its reduced form. Azides 53-58 dynein axonemal heavy chain 8 Homo sapiens 137-143 435305-0 1979 Chain heterogeneity in the methemoglobin-azide equilibrium. Azides 41-46 hemoglobin subunit gamma 2 Homo sapiens 27-40 212502-5 1978 Ethylene formation from methional by phagocytosing eosinophils and by H2O2 in the presence or absence of catalase was stimulated by azide. Azides 132-137 catalase Homo sapiens 105-113 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. Azides 33-38 myoglobin Homo sapiens 64-73 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 33-38 myeloperoxidase Homo sapiens 16-19 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 33-38 myeloperoxidase Homo sapiens 163-166 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 103-108 myeloperoxidase Homo sapiens 16-19 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 103-108 myeloperoxidase Homo sapiens 163-166 656407-7 1978 Azide acts non-competitively towards cytochrome c when the latter is oxidized by cytochrome aa3-containing proteoliposomes both in the energized and deenergized (plus p-trifluoromethoxy carbonyl cyanide phenylhydrazone and valinomycin) conditions. Azides 0-5 cytochrome c, somatic Homo sapiens 37-49 16660337-5 1978 The soluble fraction also contained an active ATPase, which was inhibited by azide and stimulated by sodium chloride and trypsin. Azides 77-82 ATPase Zea mays 46-52 658858-2 1978 The total blood hemoglobin content was determined by the azide-methemoglobin method instead of the well-known cyanmethemoglobin method. Azides 57-62 hemoglobin subunit gamma 2 Homo sapiens 63-76 624406-0 1978 The monovalent anions chloride and azide as potent activators of NaF- and p(NH)ppG-stimulation of pancreatic adenylate cyclase. Azides 35-40 C-X-C motif chemokine ligand 8 Homo sapiens 65-68 597572-0 1977 Binding of azide ion to methemoglobin at elevated temperatures and the reality of the "compensation" temperature. Azides 11-16 hemoglobin subunit gamma 2 Homo sapiens 24-37 202316-6 1978 EPR spectra of the azide, sulfide and formate complexes of cytochrome c oxidase in mitochondria in situ obtained as a function of the orientation of the applied magnetic field relative to the planes of the membrane multilayers showed that both hemes of the oxidase were oriented in such a way that the angle between the heme normal and the membrane normal was approx. Azides 19-24 cytochrome c, somatic Homo sapiens 59-71 22333-0 1977 The effect of methemoglobin on the inhibition of cytochrome c oxidase by cyanide, sulfide or azide. Azides 93-98 hemoglobin subunit gamma 2 Homo sapiens 14-27 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. Azides 154-159 leghemoglobin A Glycine max 60-73 194005-8 1977 As would be expected, inhibition of catalase by azide virtually abolished the oxidation of formate, but the burst in HMPS activity associated with phagocytosis was augmented further. Azides 48-53 catalase Homo sapiens 36-44 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. Azides 46-51 catalase Bos taurus 4-12 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. Azides 46-51 catalase Bos taurus 121-129 7191621-4 1980 After inhibition of alcohol dehydrogenase (ADH) by pyrazole (2 mM) and the catalase by azide (1 mM) approximately 25% of the ethanol oxidizing activity remained. Azides 87-92 aldo-keto reductase family 1 member A1 Rattus norvegicus 20-41 7191621-4 1980 After inhibition of alcohol dehydrogenase (ADH) by pyrazole (2 mM) and the catalase by azide (1 mM) approximately 25% of the ethanol oxidizing activity remained. Azides 87-92 catalase Rattus norvegicus 75-83 13072-14 1977 The spectrum of horse cytochrome c with added azide, cyanide, hydroxide, or imidazole as axial ligands has also been examined. Azides 46-51 cytochrome c, somatic Equus caballus 22-34 180060-5 1976 Light emission by normal leukocytes is strongly inhibited by both superoxide dismutase and azide, whereas that of myeloperoxidase-deficient leukocytes, while still strongly inhibited by superoxide dismutase is considerably less sensitive to azide. Azides 242-247 myeloperoxidase Homo sapiens 114-129 180060-7 1976 Light emission by the xanthine oxidase model system is strongly inhibited by superoxide dismutase and is not inhibited by azide, whereas the myeloperoxidase-dependent model system is strongly inhibited by azide but only slightly inhibited by superoxide dismutase. Azides 205-210 myeloperoxidase Homo sapiens 141-156 5828-5 1976 Changing the solvent from water to D2O or by quenching experiments in presence of azide ions it could be shown that the desactivation of lysozyme is caused exclusively by singlet oxygen. Azides 82-87 lysozyme Homo sapiens 137-145 956135-2 1976 During reduction of aniline and azide complexes with cytochrome P-450, an intermediate spectrum developed in the fast phase and changed to that of the reduced form in the slow phase. Azides 32-37 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 53-69 956135-7 1976 These results indicate that reduction of the aniline and azide complexes of cytochrome P-450 involves two steps: first reduction of cytochrome P-450 and then some changes in reduced state. Azides 57-62 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 76-92 956135-7 1976 These results indicate that reduction of the aniline and azide complexes of cytochrome P-450 involves two steps: first reduction of cytochrome P-450 and then some changes in reduced state. Azides 57-62 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 132-148 786861-6 1976 The Fc receptor, in common with many other membrane components, may be capped by polyvalent ligands under permissive conditions and capping is inhibited by azide. Azides 156-161 Fc receptor Mus musculus 4-15 12504-2 1976 The volume changes associated with the binding of cyanide and azide ions to methemoglobin are pH-dependent. Azides 62-67 hemoglobin subunit gamma 2 Homo sapiens 76-89 170101-6 1975 Chlorination in neutrophils is inhibited by the iodide and myeloperoxidase inhibitors azide and cyanide. Azides 86-91 myeloperoxidase Homo sapiens 59-74 167834-1 1975 Azide and imidazole complexes of ferric cytochrome c. Azides 0-5 cytochrome c, somatic Equus caballus 40-52 1169971-7 1975 The peculiarity of hyperfine-shifted methyl proton signals for other myoglobin complexes such as azide and imidazole derivatives is also discussed briefly in terms of constraint of heme side methyl group buried in a hydrophobic cleft. Azides 97-102 myoglobin Equus caballus 69-78 235996-0 1975 The conversion of glyceraldehyde-3-phosphate dehydrogenase to an acylphosphatase by trinitroglycerin and inactivation of this activity by azide and ascorbate. Azides 138-143 glyceraldehyde-3-phosphate dehydrogenase Sus scrofa 18-58 235996-6 1975 Treatment of the sulfenic acid form of glyceraldehyde-3-phosphate dehydrogenase at pH 5.3 with a 10-fold molar excess of azide over the concentration of enzyme subunit completely inactivates the acylphosphatase reaction catalyzed by the oxidized enzyme. Azides 121-126 glyceraldehyde-3-phosphate dehydrogenase Sus scrofa 39-79 1094115-3 1975 DesGly10-LH-RH hydrazide was used as a precursor in the synthesis of desGly10-LH-RH allylamide and desGly10-LH-RH propargylamide by conversion to the azide and reaction with allylamine and propargylamine, respectively. Azides 19-24 gonadotropin releasing hormone 1 Rattus norvegicus 9-14 1094115-3 1975 DesGly10-LH-RH hydrazide was used as a precursor in the synthesis of desGly10-LH-RH allylamide and desGly10-LH-RH propargylamide by conversion to the azide and reaction with allylamine and propargylamine, respectively. Azides 19-24 gonadotropin releasing hormone 1 Rattus norvegicus 78-83 1094115-3 1975 DesGly10-LH-RH hydrazide was used as a precursor in the synthesis of desGly10-LH-RH allylamide and desGly10-LH-RH propargylamide by conversion to the azide and reaction with allylamine and propargylamine, respectively. Azides 19-24 gonadotropin releasing hormone 1 Rattus norvegicus 78-83 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. Azides 212-217 carbonic anhydrase 2 Homo sapiens 111-131 234444-9 1975 The effect of IHP on azide-binding kinetics with methemoglobin has also been examined. Azides 21-26 hemoglobin subunit gamma 2 Homo sapiens 49-62 4333944-0 1972 Infrared studies of azide bound to myoglobin and hemoglobin. Azides 20-25 myoglobin Homo sapiens 35-44 4477160-2 1974 Volume changes on the formation of azide-methemoglobin from deoxyhemoglobin. Azides 35-40 hemoglobin subunit gamma 2 Homo sapiens 41-54 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. Azides 0-5 heterogeneous nuclear ribonucleoprotein C Homo sapiens 36-39 4562475-6 1972 The dispersion of crude oil by either RAG-1 or the enrichment culture was absolutely dependent on exogenous sources of nitrogen and phosphorous and completely inhibited by 10(-2)m azide. Azides 180-185 recombination activating 1 Homo sapiens 38-43 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. Azides 0-5 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. Azides 0-5 myeloperoxidase Homo sapiens 236-251 6048304-0 1967 The properties of hemoglobin M. Reactivity of methemoglobin M to cyanide, azide and fluoride. Azides 74-79 hemoglobin subunit gamma 2 Homo sapiens 46-59 11945940-0 1971 Kinetic studies of ceruloplasmin-azide interaction. Azides 33-38 ceruloplasmin Homo sapiens 19-32 4322320-1 1970 A thermal equilibrium between the high- and low-spin states in the catalase-azide compound. Azides 76-81 catalase Homo sapiens 67-75 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. Azides 0-5 myeloperoxidase Homo sapiens 76-91 5900720-0 1966 An azide-methemoglobin method for hemoglobin determination in blood. Azides 3-8 hemoglobin subunit gamma 2 Homo sapiens 9-22 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. Azides 103-108 cytochrome c, somatic Homo sapiens 0-12 33852279-2 2021 We report here the design and development of the first amyloid-beta (Abeta)-targeted, blood-brain barrier (BBB) penetrable theranostic Gd(DOTA)-cyanine dyad, which was synthesized by the conjugation of Gd(DOTA) complex and carbazole-based cyanine dye by the copper(I)-catalyzed azide-alkyne cycloaddition click reaction for imaging of Abeta in vivo and ex vivo in AD mouse models. Azides 278-283 amyloid beta (A4) precursor protein Mus musculus 69-74 5878175-0 1965 [Comparison between the absorption spectra of azide-methemoglobin and cianomethemoglobin]. Azides 46-51 hemoglobin subunit gamma 2 Homo sapiens 52-65 14479448-0 1962 The reduction of catalase by azide and peroxides. Azides 29-34 catalase Homo sapiens 17-25 6007241-0 1966 [Azide-methemoglobin method for the quantitative measurement of hemoglobins]. Azides 1-6 hemoglobin subunit gamma 2 Homo sapiens 7-20 34006109-2 2021 Here we present a density matrix renormalization group self-consistent field (DMRG-SCF) study of the azide photodissociation mechanism of trans,trans,trans-[Pt(N3)2(OH)2(NH3)2], including spin-orbit coupling. Azides 101-106 spindlin 1 Homo sapiens 188-192 34037037-2 2021 No reaction of 2 with internal alkynes was observed, but it reacts in the presence of various heterounsaturated molecules such as CS2, isothiocyanates, aldehydes, imines, diazenes, carbodiimides, nitriles, isonitriles, diazoalkane, and organic azides, forming carbodithioates, sulfidos, oxidos, metallaheterocycles, and imido complexes, in good yields. Azides 244-250 chorionic somatomammotropin hormone 2 Homo sapiens 130-133 33453208-4 2021 This work shows effects of azide on aggregation of two highly purified reference proteins, both a bovine serum albumin (BSA) as well as a monoclonal antibody (NISTmAb). Azides 27-32 albumin Homo sapiens 105-118 33844532-4 2021 Click chemistry synthesis on an alkyne E3 ligase engagers panel and an azide variant of 7 rapidly generated bispecific nanomolar degraders of ERalpha, with PROTACs 18 and 21 inhibiting ER+ MCF7 tumor growth in a mouse xenograft model of breast cancer. Azides 71-76 estrogen receptor 1 (alpha) Mus musculus 142-149 33887091-0 2021 Corrigendum: Modular Medical Imaging Agents Based on Azide-Alkyne Huisgen Cycloadditions: Synthesis and Pre-Clinical Evaluation of 18F-Labeled PSMA-Tracers for Prostate Cancer Imaging. Azides 53-58 folate hydrolase 1 Homo sapiens 143-147 33846725-4 2021 PhotoClick cholesterol showed saturable photoaffinity labelling of TSPO that could be specifically immunoprecipitated with anti-TSPO antibody, following the click reaction with the fluorescent-azide probe, tetramethylrhodamine (TAMRA)-azide. Azides 193-198 translocator protein Mus musculus 67-71 33846725-4 2021 PhotoClick cholesterol showed saturable photoaffinity labelling of TSPO that could be specifically immunoprecipitated with anti-TSPO antibody, following the click reaction with the fluorescent-azide probe, tetramethylrhodamine (TAMRA)-azide. Azides 193-198 translocator protein Mus musculus 128-132 33846725-4 2021 PhotoClick cholesterol showed saturable photoaffinity labelling of TSPO that could be specifically immunoprecipitated with anti-TSPO antibody, following the click reaction with the fluorescent-azide probe, tetramethylrhodamine (TAMRA)-azide. Azides 235-240 translocator protein Mus musculus 67-71 33846725-4 2021 PhotoClick cholesterol showed saturable photoaffinity labelling of TSPO that could be specifically immunoprecipitated with anti-TSPO antibody, following the click reaction with the fluorescent-azide probe, tetramethylrhodamine (TAMRA)-azide. Azides 235-240 translocator protein Mus musculus 128-132 33802220-0 2021 Metabolic Glycoengineering in hMSC-TERT as a Model for Skeletal Precursors by Using Modified Azide/Alkyne Monosaccharides. Azides 93-98 telomerase reverse transcriptase Homo sapiens 35-39 33672039-3 2021 We previously prolonged the plasma half-life of GLP-1 via site-specific conjugation of human serum albumin (HSA) at position 16 of recombinant GLP-1 using site-specific incorporation of p-azido-phenylalanine (AzF) and strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 234-239 glucagon Homo sapiens 48-53 33047427-1 2021 Linear uniform oligomers synthesized via a two-step iterative cycle are postmodified with uniform octaethylene glycol monomethyl ether and finally coupled via azide-alkyne cycloaddition to yield uniform star-shaped block macromolecules with a mass ranging from 10 to 14 kDa. Azides 159-164 steroidogenic acute regulatory protein Homo sapiens 203-207 33672039-3 2021 We previously prolonged the plasma half-life of GLP-1 via site-specific conjugation of human serum albumin (HSA) at position 16 of recombinant GLP-1 using site-specific incorporation of p-azido-phenylalanine (AzF) and strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 234-239 albumin Homo sapiens 93-106 33644004-7 2020 Introduction of an azide group in the P2 position expanded the selectivity window for cathepsin S, but rendered the probe undetectable, as demonstrated in bio-orthogonal competitive activity-based protein profiling. Azides 19-24 cathepsin S Homo sapiens 86-97 33644004-8 2020 Incorporation of an additional azide handle for click chemistry on the solvent-exposed P1 position allowed for selective labeling of cathepsin S. Azides 31-36 cathepsin S Homo sapiens 133-144 33244548-5 2020 Specifically, erlotinib (Er), a hydrophobic small molecule drug targeting the epidermal growth factor receptor (EGFR), is covalently conjugated with azide (N3) modified DNA strands and subsequently self-assembled on spatially programmable erlotinib-grafted 6 x 6 x 64 nt DNA nanostructures. Azides 149-154 epidermal growth factor receptor Homo sapiens 112-116 32898852-25 2021 MetRS* harbors a mutation (L247G) in the amino acid binding site which preferentially tags nascent proteins with an azide-tagged methionine analog, azidonorleucine (Anl). Azides 116-121 methionine-tRNA synthetase 2 (mitochondrial) Mus musculus 0-5 33053236-1 2021 RATIONALE: Oxygen isotope ratio measurements of NO2 - and NO3 - by the azide method and denitrifier method are sensitive to the delta18 O of sample water. Azides 71-76 NBL1, DAN family BMP antagonist Homo sapiens 58-61 33300344-4 2021 One system involves azide-DNA-functionalized QDs, which are used for bioconjugation with dibenzocyclooctyne (DBCO)-modified glucose oxidase (GOx) to form a GOx-QDs complex. Azides 20-25 hydroxyacid oxidase 1 Homo sapiens 124-139 33300344-4 2021 One system involves azide-DNA-functionalized QDs, which are used for bioconjugation with dibenzocyclooctyne (DBCO)-modified glucose oxidase (GOx) to form a GOx-QDs complex. Azides 20-25 hydroxyacid oxidase 1 Homo sapiens 141-144 33300344-4 2021 One system involves azide-DNA-functionalized QDs, which are used for bioconjugation with dibenzocyclooctyne (DBCO)-modified glucose oxidase (GOx) to form a GOx-QDs complex. Azides 20-25 hydroxyacid oxidase 1 Homo sapiens 156-159 33271741-3 2020 A human anti-gp41 antibody (7B2) was conjugated to two photosensitizers (PSs) with different charges through different linking strategies; "Click" conjugation by using an azide-bearing porphyrin attached via a disulfide bridge linker with a drug-to-antibody ratio (DAR) of exactly 4, and "Lysine" conjugation by using phthalocyanine IRDye 700DX dye with average DARs of 2.1, 3.0 and 4.4. Azides 171-176 secretogranin V Homo sapiens 28-31 32897074-5 2020 These observations are rationalized in terms of the greater electron-withdrawing ability of the azides in the pseudaminic acid donor compared to the corresponding acetoxy groups in the KDO resulting in reaction through tighter ion pairs even at the SN1 end of the general glycosylation mechanism. Azides 96-102 solute carrier family 38 member 3 Homo sapiens 249-252 32767537-6 2020 Furthermore, an azide-modified tandem Knoevenagel building block enabled the synthesis of branched PEG-linkers and the conjugation of two fluorophores, resulting in an improved signal-to-noise ratio in live cell fluorescence imaging experiments targeting the EGF-receptor. Azides 16-21 epidermal growth factor receptor Homo sapiens 259-271 33238707-4 2020 We herein report a catalytic approach that is highly effective for controlling enantioselectivity as well as reactivity of the intermolecular radical C-H amination of carboxylic acid esters with organic azides via Co(II)-based metalloradical catalysis (MRC). Azides 203-209 mitochondrially encoded cytochrome c oxidase II Homo sapiens 214-220 33302417-2 2020 The proposed platform contains a urea-based, PSMA-targeting Glu-Urea-Lys (EuK) fragment as a vector moiety and tripeptide linker with terminal amide and azide groups for subsequent addition of two different therapeutic and diagnostic agents. Azides 153-158 folate hydrolase 1 Homo sapiens 45-49 33211494-1 2020 Hydrazoic acid (HN3) is the simplest covalent azide, potentially explosive, and strongly toxic with both a low boiling and a low melting point (309 and 193 K, respectively). Azides 46-51 MT-RNR2 like 3 (pseudogene) Homo sapiens 16-19 32989852-6 2020 We proceeded to catalogue the response of all bud-expressed ERFs, and identified additional ERFs that respond similarly to ethylene, HC, azide and hypoxia. Azides 137-142 HBS1 like translational GTPase Homo sapiens 92-96 32864887-4 2020 This utilizes copper-catalyzed or strain-promoted azide-alkyne cycloaddition (CuAAC/SPAAC) "click" chemistry to covalently attach cyclo(RGDfK) peptides to the azide group of l-azidohomoalanine, a methionine analogue previously site specifically incorporated into the primary sequence of a thioredoxin (TRX)-tagged silk fusion protein, TRX-4RepCT, to give TRX3Aha -4RepCT3Aha . Azides 50-55 thioredoxin Homo sapiens 289-300 32864887-4 2020 This utilizes copper-catalyzed or strain-promoted azide-alkyne cycloaddition (CuAAC/SPAAC) "click" chemistry to covalently attach cyclo(RGDfK) peptides to the azide group of l-azidohomoalanine, a methionine analogue previously site specifically incorporated into the primary sequence of a thioredoxin (TRX)-tagged silk fusion protein, TRX-4RepCT, to give TRX3Aha -4RepCT3Aha . Azides 50-55 thioredoxin Homo sapiens 302-305 32864887-4 2020 This utilizes copper-catalyzed or strain-promoted azide-alkyne cycloaddition (CuAAC/SPAAC) "click" chemistry to covalently attach cyclo(RGDfK) peptides to the azide group of l-azidohomoalanine, a methionine analogue previously site specifically incorporated into the primary sequence of a thioredoxin (TRX)-tagged silk fusion protein, TRX-4RepCT, to give TRX3Aha -4RepCT3Aha . Azides 159-164 thioredoxin Homo sapiens 289-300 32864887-4 2020 This utilizes copper-catalyzed or strain-promoted azide-alkyne cycloaddition (CuAAC/SPAAC) "click" chemistry to covalently attach cyclo(RGDfK) peptides to the azide group of l-azidohomoalanine, a methionine analogue previously site specifically incorporated into the primary sequence of a thioredoxin (TRX)-tagged silk fusion protein, TRX-4RepCT, to give TRX3Aha -4RepCT3Aha . Azides 159-164 thioredoxin Homo sapiens 302-305 32392042-5 2020 Anti-human serum albumin pAbF antibody was modified with azide groups and conjugated to UCNP@PEG-alkyne via click reaction; alternatively, the antibody, after mild reduction of its disulfide bonds, was conjugated to UCNP@PEG-maleimide. Azides 57-62 albumin Homo sapiens 11-24 32952647-0 2020 In vitro effects of azide-containing human CRP isoforms and oxLDL on U937-derived macrophage production of atherosclerosis-related cytokines. Azides 20-25 C-reactive protein Homo sapiens 43-46 32952647-3 2020 Azide, the commercial preservative of CRP, may influence its action in vitro. Azides 0-5 C-reactive protein Homo sapiens 38-41 32952647-4 2020 The present study aimed to determine the effects of both isoforms of azide-containing CRP (mCRP and pCRP) with and without oxLDL on cytokine production by U937-derived macrophages. Azides 69-74 C-reactive protein Homo sapiens 86-89 32952647-4 2020 The present study aimed to determine the effects of both isoforms of azide-containing CRP (mCRP and pCRP) with and without oxLDL on cytokine production by U937-derived macrophages. Azides 69-74 C-reactive protein, pentraxin-related Mus musculus 91-95 32952647-10 2020 By contrast, double azide caused a significant decrease in the levels of IFN-gamma and IL-6. Azides 20-25 interferon gamma Homo sapiens 73-82 32952647-10 2020 By contrast, double azide caused a significant decrease in the levels of IFN-gamma and IL-6. Azides 20-25 interleukin 6 Homo sapiens 87-91 32952647-11 2020 The results of the present study indicated that mCRP, pCRP, oxLD and possibly azide, individually or in different combinations, had the tendency to upregulate the expression of IL-4 and to downregulate that of the pro-atherogenic cytokines, IFN-gamma and IL-6, suggesting that the intima microenvironment serves a crucial role in atherogenesis. Azides 78-83 C-reactive protein, pentraxin-related Mus musculus 48-52 32952647-11 2020 The results of the present study indicated that mCRP, pCRP, oxLD and possibly azide, individually or in different combinations, had the tendency to upregulate the expression of IL-4 and to downregulate that of the pro-atherogenic cytokines, IFN-gamma and IL-6, suggesting that the intima microenvironment serves a crucial role in atherogenesis. Azides 78-83 interleukin 4 Homo sapiens 177-181 32952647-11 2020 The results of the present study indicated that mCRP, pCRP, oxLD and possibly azide, individually or in different combinations, had the tendency to upregulate the expression of IL-4 and to downregulate that of the pro-atherogenic cytokines, IFN-gamma and IL-6, suggesting that the intima microenvironment serves a crucial role in atherogenesis. Azides 78-83 interferon gamma Homo sapiens 241-250 32952647-11 2020 The results of the present study indicated that mCRP, pCRP, oxLD and possibly azide, individually or in different combinations, had the tendency to upregulate the expression of IL-4 and to downregulate that of the pro-atherogenic cytokines, IFN-gamma and IL-6, suggesting that the intima microenvironment serves a crucial role in atherogenesis. Azides 78-83 interleukin 6 Homo sapiens 255-259 32955854-5 2020 We demonstrate this technology by tracking the reaction of azide with microcrystalline myoglobin, using only a fraction of the sample required for a mix-and-inject experiment. Azides 59-64 myoglobin Homo sapiens 87-96 32996488-3 2020 A bifunctional macromolecule, structured as azide-poly(ethylene glycol)-porphyrin (termed TPA), was synthesized. Azides 44-49 plasminogen activator, tissue type Homo sapiens 90-93 32558100-3 2020 Triplet syn -2-formyl-3-fluorophenylnitrene, generated in argon matrices by UV-irradiation of an azide precursor, was found to spontaneously cyclize to singlet 4-fluoro-2,1-benzisoxazole. Azides 97-102 synapsin II Homo sapiens 8-14 32315486-0 2020 Modular medical imaging agents based on azide-alkyne Huisgen cycloadditions: Synthesis and pre-clinical evaluation of 18F-labeled PSMA-tracers for prostate cancer imaging. Azides 40-45 folate hydrolase 1 Homo sapiens 130-134 32813490-3 2020 To meet these requirements, we functionalized QDs with photo-patternable and semiconducting poly(vinyltriphenylamine-random-azidostyrene) (PTPA-N3-SH) ligands in which hole-transporting triphenylamine and UV-crosslinkable azide (-N3) groups are integrated. Azides 222-227 protein phosphatase 2 phosphatase activator Homo sapiens 139-143 32800119-0 2020 Highly sensitive detection of carcinoembryonic antigen using copper-free click chemistry on the surface of azide cofunctionalized graphene oxide. Azides 107-112 CEA cell adhesion molecule 3 Homo sapiens 30-54 32800119-1 2020 In this study, we reported a highly sensitive method for detecting carcinoembryonic antigen (CEA) based on an azide cofunctionalized graphene oxide (GO-N3) and carbon dot (CDs) biosensor system. Azides 110-115 CEA cell adhesion molecule 3 Homo sapiens 67-91 32800119-1 2020 In this study, we reported a highly sensitive method for detecting carcinoembryonic antigen (CEA) based on an azide cofunctionalized graphene oxide (GO-N3) and carbon dot (CDs) biosensor system. Azides 110-115 CEA cell adhesion molecule 3 Homo sapiens 93-96 32658470-5 2020 sgR-CLK employs a novel posttranscriptional chemo-enzymatic labeling platform wherein a terminal uridylyl transferase (TUTase) was repurposed to generate clickable sgRNA of choice by site-specific tailoring of multiple azide-modified nucleotide analogs at the 3" end. Azides 219-224 terminal uridylyl transferase 1, U6 snRNA-specific Homo sapiens 88-117 32658470-5 2020 sgR-CLK employs a novel posttranscriptional chemo-enzymatic labeling platform wherein a terminal uridylyl transferase (TUTase) was repurposed to generate clickable sgRNA of choice by site-specific tailoring of multiple azide-modified nucleotide analogs at the 3" end. Azides 219-224 terminal uridylyl transferase 1, U6 snRNA-specific Homo sapiens 119-125 32643920-2 2020 In this study, a sensitive and specific electrochemiluminescence (ECL) biosensor combined highly specific Cu+ catalyzed azide-alkyne cycloaddition (CuAAC) with high efficiency of hybridization chain reaction (HCR) for the purpose of detecting pyrophosphatase has been designed. Azides 120-125 inorganic pyrophosphatase 1 Homo sapiens 243-258 32543833-0 2020 Optimised methods for the production and bioconjugation of site-specific, alkyne-modified glucagon-like peptide-1 (GLP-1) analogs to azide-modified delivery platforms using copper-catalysed alkyne-azide cycloaddition. Azides 133-138 glucagon Homo sapiens 90-113 32543833-0 2020 Optimised methods for the production and bioconjugation of site-specific, alkyne-modified glucagon-like peptide-1 (GLP-1) analogs to azide-modified delivery platforms using copper-catalysed alkyne-azide cycloaddition. Azides 133-138 glucagon Homo sapiens 115-120 32276227-3 2020 When H2S is present, the azide group in SP2 was reduced to amine group, resulting in a turn-on fluorescence signal. Azides 25-30 Sp2 transcription factor Homo sapiens 40-43 32045045-5 2020 The mechanism studies indicates that the one-electron oxidative intermediate Rh 2 (II,III)N 3 is responsible for the azide transfer. Azides 117-122 Rh associated glycoprotein Homo sapiens 77-81 32596210-8 2020 Finally, the adhesive azidopentanoyl-modified GGGRGDSGGGY-NH2 (RGDS) peptide was immobilized on the NaYF4:Yb3+/Er3+@NaYF4:Nd3+-PEG-Alk particles via Cu(I)-catalyzed azide-alkyne cycloaddition. Azides 165-170 ral guanine nucleotide dissociation stimulator Homo sapiens 49-53 32463677-6 2020 Reactivity studies comparing 3-OCN to the azide analogue [(CpiPr4)2U(mu-eta1:eta1-N3)]4 (3-N3) demonstrated significant differences in the chemistry of cyanates and azides with trivalent uranium. Azides 42-47 secreted phosphoprotein 1 Homo sapiens 72-76 32463677-6 2020 Reactivity studies comparing 3-OCN to the azide analogue [(CpiPr4)2U(mu-eta1:eta1-N3)]4 (3-N3) demonstrated significant differences in the chemistry of cyanates and azides with trivalent uranium. Azides 42-47 secreted phosphoprotein 1 Homo sapiens 77-81 32566878-4 2020 The two liposomes exhibit different azide placement mechanisms; C18-ether-AAM-treated cells have azido placement through direct insertion, while C18-ester-AAM-treated cells express azido more through metabolic glycoengineering. Azides 36-41 Bardet-Biedl syndrome 9 Homo sapiens 64-67 32392255-2 2020 Kinetic data obtained for the binding reaction of azide to myoglobin demonstrate the feasibility of the method for high-frequency EPR. Azides 50-55 myoglobin Homo sapiens 59-68 31665825-3 2020 An azide labeled SW probe was synthesized for protein target fishing, and the results demonstrated that AKT could be captured specifically. Azides 3-8 AKT serine/threonine kinase 1 Homo sapiens 104-107 32011889-4 2020 Therefore, we applied click chemistry-based 18F-fluoroglcosylation using 2-deoxy-2-[18F]fluoroglucosyl azide or 6-deoxy-6-[18F]fluoroglucosyl azide as prosthetic groups for the radiosynthesis of the 18F-fluoroglycosylated glutamate-urea-lysine based PSMA inhibitors 2-[18F]FGlc-PSMA ([18F]7) and 6-[18F]FGlc-PSMA ([18F]8). Azides 73-108 folate hydrolase 1 Homo sapiens 250-254 32289483-3 2020 Herein, we designed the protein-drug conjugate HSAP-DC-CAT (human serum albumin/Pt (IV)-dibenzocyclooctyne/chlorin e6-catalase) by modification of CAT and cisplatin pro-drug loaded HSA with pH-sensitive azide linker 3-(azidomethyl)-4-methyl-2,5-furandione (AzMMMan) followed by click chemistry assembly with DC. Azides 203-208 mutS homolog 6 Homo sapiens 47-51 32289483-3 2020 Herein, we designed the protein-drug conjugate HSAP-DC-CAT (human serum albumin/Pt (IV)-dibenzocyclooctyne/chlorin e6-catalase) by modification of CAT and cisplatin pro-drug loaded HSA with pH-sensitive azide linker 3-(azidomethyl)-4-methyl-2,5-furandione (AzMMMan) followed by click chemistry assembly with DC. Azides 203-208 catalase Homo sapiens 55-58 32289483-3 2020 Herein, we designed the protein-drug conjugate HSAP-DC-CAT (human serum albumin/Pt (IV)-dibenzocyclooctyne/chlorin e6-catalase) by modification of CAT and cisplatin pro-drug loaded HSA with pH-sensitive azide linker 3-(azidomethyl)-4-methyl-2,5-furandione (AzMMMan) followed by click chemistry assembly with DC. Azides 203-208 albumin Homo sapiens 66-79 32241912-7 2020 Copurification experiments suggested that the MBD binds to iron and that azide disrupts iron binding. Azides 73-78 outer membrane receptor FepA Escherichia coli 88-92 32316169-6 2020 A "clickable" non-natural amino acid-p-azido-l-phenylalanine (AzF)-was incorporated into three specific sites (V16, Y19, and F28) of a GLP-1 variant, followed by conjugation with HSA through strain-promoted azide-alkyne cycloaddition. Azides 207-212 AZF1 Homo sapiens 62-65 32316169-6 2020 A "clickable" non-natural amino acid-p-azido-l-phenylalanine (AzF)-was incorporated into three specific sites (V16, Y19, and F28) of a GLP-1 variant, followed by conjugation with HSA through strain-promoted azide-alkyne cycloaddition. Azides 207-212 glucagon Homo sapiens 135-140 32011889-4 2020 Therefore, we applied click chemistry-based 18F-fluoroglcosylation using 2-deoxy-2-[18F]fluoroglucosyl azide or 6-deoxy-6-[18F]fluoroglucosyl azide as prosthetic groups for the radiosynthesis of the 18F-fluoroglycosylated glutamate-urea-lysine based PSMA inhibitors 2-[18F]FGlc-PSMA ([18F]7) and 6-[18F]FGlc-PSMA ([18F]8). Azides 73-108 folate hydrolase 1 Homo sapiens 278-282 32011889-4 2020 Therefore, we applied click chemistry-based 18F-fluoroglcosylation using 2-deoxy-2-[18F]fluoroglucosyl azide or 6-deoxy-6-[18F]fluoroglucosyl azide as prosthetic groups for the radiosynthesis of the 18F-fluoroglycosylated glutamate-urea-lysine based PSMA inhibitors 2-[18F]FGlc-PSMA ([18F]7) and 6-[18F]FGlc-PSMA ([18F]8). Azides 73-108 folate hydrolase 1 Homo sapiens 278-282 31733428-5 2020 In contrast, azide, thiocyanate and imidazole binding to Hb(III), Hp1-1:Hb(III) and Hp2-2:Hb(III) follows a two-step process, whereas ligand binding to alpha(III) and beta(III) chains follows a simple behavior. Azides 13-18 chromobox 5 Homo sapiens 66-69 31887957-1 2020 For the first time, the novel type of guided bone regeneration composite nanofibers were prepared by grafting polycaprolactone (PCL) to chitosan (CS) using the copper (I) - catalyzed azide-alkyne cycloaddition (CuAAC) reaction. Azides 183-188 citrate synthase Homo sapiens 146-148 33463203-3 2020 Therefore, we deployed genetic codon expansion to integrate an azide functionality to the FGF-2 N-terminus, which was site-directly decorated with poly(ethylene glycol) (PEG) through bioorthogonal strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 63-68 fibroblast growth factor 2 Mus musculus 90-95 33463203-3 2020 Therefore, we deployed genetic codon expansion to integrate an azide functionality to the FGF-2 N-terminus, which was site-directly decorated with poly(ethylene glycol) (PEG) through bioorthogonal strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 213-218 fibroblast growth factor 2 Mus musculus 90-95 32011889-4 2020 Therefore, we applied click chemistry-based 18F-fluoroglcosylation using 2-deoxy-2-[18F]fluoroglucosyl azide or 6-deoxy-6-[18F]fluoroglucosyl azide as prosthetic groups for the radiosynthesis of the 18F-fluoroglycosylated glutamate-urea-lysine based PSMA inhibitors 2-[18F]FGlc-PSMA ([18F]7) and 6-[18F]FGlc-PSMA ([18F]8). Azides 112-147 folate hydrolase 1 Homo sapiens 250-254 32011889-4 2020 Therefore, we applied click chemistry-based 18F-fluoroglcosylation using 2-deoxy-2-[18F]fluoroglucosyl azide or 6-deoxy-6-[18F]fluoroglucosyl azide as prosthetic groups for the radiosynthesis of the 18F-fluoroglycosylated glutamate-urea-lysine based PSMA inhibitors 2-[18F]FGlc-PSMA ([18F]7) and 6-[18F]FGlc-PSMA ([18F]8). Azides 112-147 folate hydrolase 1 Homo sapiens 278-282 32011889-4 2020 Therefore, we applied click chemistry-based 18F-fluoroglcosylation using 2-deoxy-2-[18F]fluoroglucosyl azide or 6-deoxy-6-[18F]fluoroglucosyl azide as prosthetic groups for the radiosynthesis of the 18F-fluoroglycosylated glutamate-urea-lysine based PSMA inhibitors 2-[18F]FGlc-PSMA ([18F]7) and 6-[18F]FGlc-PSMA ([18F]8). Azides 112-147 folate hydrolase 1 Homo sapiens 278-282 32023915-1 2020 A new energetic curing reagent, Glycidyl azide polymer grafted tetrafunctional isocyanate (N100-g-GAP) was synthesized and characterized by FT-IR and GPC approaches. Azides 32-46 glycophorin C (Gerbich blood group) Homo sapiens 140-153 31746532-4 2020 Azide-modified exosomes derived from M1 macrophages are conjugated with dibenzocyclooctyne-modified antibodies of CD47 and SIRPalpha (aCD47 and aSIRPalpha) through pH-sensitive linkers. Azides 0-5 CD47 molecule Homo sapiens 114-118 31733428-6 2020 However, azide, thiocyanate and imidazole binding to Hb(III), Hp1-1:Hb(III) and Hp2-2:Hb(III) is characterized by a simple equilibrium, reflecting the compensation of kinetic parameters. Azides 9-14 chromobox 5 Homo sapiens 62-65 31733428-7 2020 The fast and the slow step of azide, thiocyanate and imidazole binding to Hb(III), Hp1-1:Hb(III) and Hp2-2:Hb(III) mirror the ligand binding properties of the beta(III) and alpha(III) chains, respectively. Azides 30-35 chromobox 5 Homo sapiens 83-86 31608910-2 2019 The multiple binding modes of the tert-butoxysiloxide ligand have proven very well suited to stabilize highly reactive homo- and heteropolymetallic complexes of uranium that have shown an unusual high reactivity towards small molecules such as CO2, CS2, chalcogens and azides. Azides 269-275 chorionic somatomammotropin hormone 2 Homo sapiens 249-252 31657567-3 2019 The reaction, carried out with a variety of organic azides containing free alcohol, acid, Boc-protected amine, ester, protected sugars, long chain alkanes, benzyl, 9-methylanthracenyl and cholesteryl groups were found to be general in nature, which afforded a plethora of new chemical entities; reactions of diazides generated mostly the desired and a few unexpected products. Azides 52-58 BOC cell adhesion associated, oncogene regulated Homo sapiens 90-93 31647241-7 2019 We have synthesized new azide-terminated coumarin linkers that we react with the amine groups of insulin. Azides 24-29 insulin Homo sapiens 97-104 32110322-4 2019 Herein, we report that the accumulated Cu in Abeta plaques can effectively catalyze an azide-alkyne bioorthogonal cycloaddition reaction for fluorophore activation and drug synthesis in living cells, a transgenic AD model of Caenorhabditis elegans CL2006, and brain slices of triple transgenic AD mice. Azides 87-92 amyloid beta (A4) precursor protein Mus musculus 45-50 31550138-4 2019 Here we report the first X-ray crystal structure of a reactive Rh2 nitrenoid, enabled by N2 elimination from an organic azide ligand within a single-crystal matrix. Azides 120-125 Rh associated glycoprotein Homo sapiens 63-66 31325418-0 2019 Targeting specific membranes with an azide derivative of the pore-forming peptide ceratotoxin A. Azides 37-42 ceratotoxin-A Ceratitis capitata 82-95 31325418-4 2019 In this work, we modified CtxA at its N-terminus with an azide group and investigated its pore-forming characteristics in planar lipid bilayer experiments. Azides 57-62 ceratotoxin-A Ceratitis capitata 26-30 31557873-4 2019 The C-14 hydroxyl and C-10 ketone were installed via SmI2-mediated radical cyclization, and oxidation of a benzylic alcohol (obtained from an intermediate nitrate azide), respectively. Azides 155-168 homeobox C10 Homo sapiens 22-26 31456406-2 2019 The azidolipids bear an azide group at different positions of the sn-1 or sn-2 alkyl chain and they further differ in the type of linkage (ester vs ether) of the sn-2 alkyl chain. Azides 24-29 solute carrier family 38 member 3 Homo sapiens 66-70 31456406-2 2019 The azidolipids bear an azide group at different positions of the sn-1 or sn-2 alkyl chain and they further differ in the type of linkage (ester vs ether) of the sn-2 alkyl chain. Azides 24-29 solute carrier family 38 member 5 Homo sapiens 74-78 31414819-0 2019 Benzene Triimide Cage as a Selective Container of Azide. Azides 50-55 DEAD-box helicase 53 Homo sapiens 17-21 31414819-2 2019 Here, we report the first BTI-based cage composed of two face-to-face BTIs pillared by three m-xylylene spacers and efficient and selective binding of azide through cooperative anion-pi interactions. Azides 151-156 DEAD-box helicase 53 Homo sapiens 36-40 30561864-2 2019 For this, a well-defined water-soluble beta-CD-core star mPEG with aldehyde groups (CD-star(ald)PEG, III) is first designed and synthesized via the copper-catalyzed azide-alkyne click reaction. Azides 165-170 ACD shelterin complex subunit and telomerase recruitment factor Homo sapiens 39-46 31844845-3 2019 An azide modified bovine serum albumin (azBSA) was employed as the linker. Azides 3-8 albumin Homo sapiens 25-38 31844845-5 2019 Attachment of the emitting payload to the particle through azide-modified bovine serum albumin (BSA) quenches emission, which can be again activated with digestion of the azBSA. Azides 59-64 albumin Homo sapiens 81-94 30798218-3 2019 In this study, a novel fluorescent probe, QN-1, based on azide group and quinoline derivatives was developed for detecting H2S. Azides 57-62 centrosomal protein 162 Homo sapiens 42-46 30860635-1 2019 With the aim of developing a new approach to obtain improved aptamers, a cyclic thrombin-binding aptamer (TBA) analogue (cycTBA) has been prepared by exploiting a copper(I)-assisted azide-alkyne cycloaddition. Azides 182-187 coagulation factor II, thrombin Homo sapiens 80-88 31252450-4 2019 The resultant alkyne-containing PHEMA was then used to modify the azide-terminated oligopeptides [Arg-Gly-Asp-Ser (RGDS)] with a photolabile 3-amino-3-(2-nitrophenyl)propanoic acid moiety via the copper-catalyzed alkyne-azide click chemistry. Azides 66-71 ral guanine nucleotide dissociation stimulator Mus musculus 115-119 30985840-1 2019 A series of dicopper azacryptand complexes was evaluated in copper-catalysed azide-alkyne cycloaddition (CuAAC) in water at 37 C. It was found that they showed high activity at concentrations as low as 5 muM. Azides 77-82 latexin Homo sapiens 205-208 31091124-10 2019 After azide or cisplatin treatment, more dead cells were found in knockdown cells compared with controls, accompanied by increases in cleaved/active caspase-3. Azides 6-11 caspase 3 Mus musculus 149-158 31016975-6 2019 Kinetic studies revealed that pyridine binding slows down the formation of the tetrazido complex by blocking azide coordination to the CoIII imido. Azides 109-114 mitochondrially encoded cytochrome c oxidase III Homo sapiens 135-140 30672956-3 2019 Peripheral amines were labeled with multiple copies of a metal isotope, whereas the azide functionality at the focal point was employed in conjugation to a single anti-human CD4 antibody. Azides 84-89 CD4 molecule Homo sapiens 174-177 30946565-0 2019 Site-Selective Synthesis of Insulin Azides and Bioconjugates. Azides 36-42 insulin Homo sapiens 28-35 30807110-3 2019 Here, we have prepared a trastuzumab-chelator conjugate by using affinity-guided conjugation, in which an azide was attached to the antibody prior to a strain promoted azide-alkyne cycloaddition reaction with DBCO-PEG4-NOTA. Azides 106-111 small nuclear ribonucleoprotein N Mus musculus 214-218 30706146-0 2019 Fluoride and azide binding to ferric human hemoglobin:haptoglobin complexes highlights the ligand-dependent inequivalence of the alpha and beta hemoglobin chains. Azides 13-18 haptoglobin Homo sapiens 54-65 30706146-3 2019 Here, kinetics and thermodynamics of fluoride and azide binding to ferric human Hb (Hb(III)) complexed with the human Hp phenotypes 1-1 and 2-2 (Hp1-1:Hb(III) and Hp2-2:Hb(III), respectively) are reported (pH 7.0 and 20.0 C). Azides 50-55 chromobox 5 Homo sapiens 145-150 30706146-3 2019 Here, kinetics and thermodynamics of fluoride and azide binding to ferric human Hb (Hb(III)) complexed with the human Hp phenotypes 1-1 and 2-2 (Hp1-1:Hb(III) and Hp2-2:Hb(III), respectively) are reported (pH 7.0 and 20.0 C). Azides 50-55 ADP ribosylation factor like GTPase 6 interacting protein 5 Homo sapiens 163-168 30706146-5 2019 In contrast, kinetics of azide binding to and dissociation from Hp1-1:Hb(III)(-N3-) and Hp2-2:Hb(III)(-N3-) follow a two-step process. Azides 25-30 chromobox 5 Homo sapiens 64-69 30706146-5 2019 In contrast, kinetics of azide binding to and dissociation from Hp1-1:Hb(III)(-N3-) and Hp2-2:Hb(III)(-N3-) follow a two-step process. Azides 25-30 ADP ribosylation factor like GTPase 6 interacting protein 5 Homo sapiens 88-93 30706146-6 2019 However, azide binding to Hp1-1:Hb(III) and Hp2-2:Hb(III) is characterized by a simple equilibrium, reflecting the compensation of kinetic parameters. Azides 9-14 chromobox 5 Homo sapiens 26-31 30706146-7 2019 The fast and the slow step of azide binding to Hp1-1:Hb(III) and Hp2-2:Hb(III) should reflect azide binding to the ferric beta and alpha chains, respectively, as also proposed for the similar behavior observed in Hb(III). Azides 30-35 chromobox 5 Homo sapiens 47-52 30706146-7 2019 The fast and the slow step of azide binding to Hp1-1:Hb(III) and Hp2-2:Hb(III) should reflect azide binding to the ferric beta and alpha chains, respectively, as also proposed for the similar behavior observed in Hb(III). Azides 30-35 ADP ribosylation factor like GTPase 6 interacting protein 5 Homo sapiens 65-70 30706146-7 2019 The fast and the slow step of azide binding to Hp1-1:Hb(III) and Hp2-2:Hb(III) should reflect azide binding to the ferric beta and alpha chains, respectively, as also proposed for the similar behavior observed in Hb(III). Azides 94-99 chromobox 5 Homo sapiens 47-52 31018636-5 2019 Specially, breast cancer stem cells (BCSCs) are first captured by nucleolin aptamer immobilized on the electrode surface and then selectively recognized by MNFs through the binding with CD44, thereby offering a large number of azide groups for signal labeling. Azides 227-232 nucleolin Homo sapiens 66-75 30683555-3 2019 In our pursuit of a CA IX-specific PET probe, we designed and synthesized a peptide-based CA IX imaging probe by the efficient click reaction of 1,3-dipolar cycloaddition of terminal alkynes and organic azides. Azides 203-209 carbonic anhydrase 9 Homo sapiens 20-25 30683555-3 2019 In our pursuit of a CA IX-specific PET probe, we designed and synthesized a peptide-based CA IX imaging probe by the efficient click reaction of 1,3-dipolar cycloaddition of terminal alkynes and organic azides. Azides 203-209 carbonic anhydrase 9 Homo sapiens 90-95 30706146-7 2019 The fast and the slow step of azide binding to Hp1-1:Hb(III) and Hp2-2:Hb(III) should reflect azide binding to the ferric beta and alpha chains, respectively, as also proposed for the similar behavior observed in Hb(III). Azides 94-99 ADP ribosylation factor like GTPase 6 interacting protein 5 Homo sapiens 65-70 30717597-2 2019 To tackle these issues, we fabricate a flexible copper azide film (CA-C film@PF) via employing the metal-organic framework (MOF) film produced by electrospinning technique as the precursor, followed by pyrolysis treatment, in situ azide reaction, and perfluorinated coating procedures. Azides 55-60 lysine acetyltransferase 8 Homo sapiens 99-128 30640328-2 2019 Compounds 1-7 were fully characterized, also by single-crystal X-ray diffraction analysis, and applied as homogeneous catalysts for the azide-alkyne cycloaddition (AAC) reaction to afford 1,4-disubstituted 1,2,3-triazoles. Azides 136-141 glycine-N-acyltransferase Homo sapiens 164-167 30594453-3 2019 The chelator-peptide conjugation was performed via a Cu(I)-assisted click reaction of the alkyne-bearing chelator (2) with an azide-functionalized sst2-ANT peptide (3), to yield NSO-sst2-ANT (4). Azides 126-131 somatostatin receptor 2 Mus musculus 147-151 30594453-3 2019 The chelator-peptide conjugation was performed via a Cu(I)-assisted click reaction of the alkyne-bearing chelator (2) with an azide-functionalized sst2-ANT peptide (3), to yield NSO-sst2-ANT (4). Azides 126-131 solute carrier family 25 member 6 Homo sapiens 152-155 30553624-4 2019 Structural evolution of 37 produced the azide-containing cis-49a, which had good properties in three important respects: (1) selectivity for CYP1B1 over CYP1A1 and CYP1A2 (120-times and 150-times, respectively), (2) greater inhibitory potency of >2 times that of ANF, and (3) improved solubility. Azides 40-45 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 141-147 30553624-4 2019 Structural evolution of 37 produced the azide-containing cis-49a, which had good properties in three important respects: (1) selectivity for CYP1B1 over CYP1A1 and CYP1A2 (120-times and 150-times, respectively), (2) greater inhibitory potency of >2 times that of ANF, and (3) improved solubility. Azides 40-45 cytochrome P450 family 1 subfamily A member 1 Homo sapiens 153-159 30553624-4 2019 Structural evolution of 37 produced the azide-containing cis-49a, which had good properties in three important respects: (1) selectivity for CYP1B1 over CYP1A1 and CYP1A2 (120-times and 150-times, respectively), (2) greater inhibitory potency of >2 times that of ANF, and (3) improved solubility. Azides 40-45 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 164-170 30657688-4 2019 In this method, the O-GlcNAc moiety on peptides was labeled with UDP-GalNAz followed by copper-free azide-alkyne cycloaddition with a multifunctional reagent bearing a terminal cyclooctyne, a disulfide bridge, and a biotin handle. Azides 100-105 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 20-28 30512211-1 2019 Alkenes can be cleaved by means of the (3+2) cycloaddition and subsequent cycloreversion of 1,3-dipoles, classically ozone (O3 ), but the azide (R-N3 ) variant is rare. Azides 138-143 drosha ribonuclease III Homo sapiens 145-149 30960224-4 2019 The cyclic backbone (c-P2) was then coupled with azide-containing polymer double-chain (l-PS-PhN3) via CuAAC reaction to construct a novel cyclic double-grafted polymer (c-P2-g-Ph-PS). Azides 49-54 ceruloplasmin Homo sapiens 21-25 30960224-4 2019 The cyclic backbone (c-P2) was then coupled with azide-containing polymer double-chain (l-PS-PhN3) via CuAAC reaction to construct a novel cyclic double-grafted polymer (c-P2-g-Ph-PS). Azides 49-54 ceruloplasmin Homo sapiens 170-174 31459462-5 2019 Dialkyne 3 was successfully employed for "peptide stapling" of a p53-based diazido peptide, whereby two azides are bridged to give a product with a stabilized conformation. Azides 104-110 tumor protein p53 Homo sapiens 65-68 31161513-3 2019 The lipoic acid ligase variant, LplAW37V, functionalizes proteins by covalently attaching an azide-bearing lipoic acid derivative to a 13-amino acid recognition sequence known as the lipoic acid ligase acceptor peptide (LAP). Azides 93-98 LAP Homo sapiens 220-223 31161513-5 2019 The versatility of the attached azide group is complemented by the modular nature of the LAP sequence, which can be introduced within a protein at internal and/or terminal sites as well as at multiple sites simultaneously. Azides 32-37 LAP Homo sapiens 89-92 31161513-7 2019 Additionally, methods for the modification and immobilization of azide-functionalized LAP-GFP are discussed. Azides 65-70 LAP Homo sapiens 86-89 31332748-8 2019 Finally, we describe the modification of a nanoparticle surface with scFv attachment via two methods: (1) direct Sortase-mediated conjugation; or (2) a two-step system which consists of scFv Sortase-mediated conjugation followed by strain promoted azide-alkyne cycloaddition. Azides 248-253 immunglobulin heavy chain variable region Homo sapiens 69-73 31332756-8 2019 In addition, a variety of isoprenoid analogs containing different bioorthogonal functional groups, including azides, alkynes, and aldehydes, have been developed to enable conjugation to various cargos after being incorporated onto the target protein by PFTase. Azides 109-115 protein farnesyltransferase Saccharomyces cerevisiae S288C 253-259 31332756-9 2019 In this protocol, we present a detailed procedure for labeling Designed Ankyrin Repeat Proteins (DARPins) engineered with a C-terminal CVIA sequence using an azide-containing FPP analog by yeast PFTase (yPFTase). Azides 158-163 protein farnesyltransferase Saccharomyces cerevisiae S288C 195-201 30496416-3 2018 Here, we propose a strategy for a rapid screening for ability of any EGF-LD to be O-fucosylated, using copper-catalyzed azide-alkyne cycloaddition (CuAAC). Azides 120-125 epidermal growth factor Homo sapiens 69-72 31330414-2 2019 METHODS: The ethinyl group of ethisterone, a PR targeting pharmacophore, was coupled with azide modified PEG-OTs by click chemistry to obtain the labeling precursor. Azides 90-95 progesterone receptor Rattus norvegicus 45-47 30566283-4 2019 Meanwhile, activated T cells are treated with Ac4 GalNAz to introduce azide (N3 ) on the cell surface, initiating specific tumor targeting through a bio-orthogonal click reaction between N3 and BCN. Azides 70-75 adenylate cyclase 4 Homo sapiens 46-49 30655958-2 2019 Modified versions of the PAR1 antagonist RWJ-58259 containing alkyne adapters were connected via cycloaddition reactions to azide-capped polyethylene glycol (PEG) spacers attached to imidazopyridazine-based PAR2 antagonists. Azides 124-129 coagulation factor II thrombin receptor Homo sapiens 25-29 30351969-0 2018 RuHCl(CO)(PPh3)3-Catalyzed Direct Amidation of Arene C-H Bond with Azides. Azides 67-73 protein phosphatase 4 catalytic subunit Homo sapiens 10-14 30351969-1 2018 We first report the direct ortho C-H amidation of arenes with azides by using a novel and inexpensive RuHCl(CO)(PPh3)3 catalyst. Azides 62-68 protein phosphatase 4 catalytic subunit Homo sapiens 112-116 30077971-0 2018 X-ray structural analyses of azide-bound cytochrome c oxidases reveal that the H-pathway is critically important for the proton-pumping activity. Azides 29-34 LOC104968582 Bos taurus 41-53 30350619-2 2018 Lactose was equipped with an azide-functionalized linker and was supplemented to bacterial cultures as an artificial substrate for bacterial beta-galactosidase enzyme. Azides 29-34 galactosidase beta 1 Homo sapiens 141-159 30351095-4 2018 In contrast, the azide splits off N2 and furnishes a transient triplet sulfonyl nitrene intermediate (OCN)S(O)2N upon a 266 nm laser irradiation in solid Ne-matrix at 2.8 K. Subsequent photolysis of the nitrene with visible light (lambda = 380-450 nm) results in oxygen-shifted Curtius rearrangement to a novel nitroso sulfoxide (OCN)S(O)NO. Azides 17-22 bone gamma-carboxyglutamate protein Homo sapiens 102-105 30351095-4 2018 In contrast, the azide splits off N2 and furnishes a transient triplet sulfonyl nitrene intermediate (OCN)S(O)2N upon a 266 nm laser irradiation in solid Ne-matrix at 2.8 K. Subsequent photolysis of the nitrene with visible light (lambda = 380-450 nm) results in oxygen-shifted Curtius rearrangement to a novel nitroso sulfoxide (OCN)S(O)NO. Azides 17-22 bone gamma-carboxyglutamate protein Homo sapiens 330-333 30336590-3 2018 To achieve this, we encapsulated rat aNSCs in chitosan-based hydrogels functionalized with immobilized azide-tagged interferon-gamma inside a chitosan conduit. Azides 103-108 interferon gamma Rattus norvegicus 116-132 30209482-0 2018 tert-Butyl nitrite mediated nitrogen transfer reactions: synthesis of benzotriazoles and azides at room temperature. Azides 89-95 telomerase reverse transcriptase Homo sapiens 0-4 30077971-5 2018 To experimentally test this, we examined X-ray structures of the azide-bound, oxidized bovine CcO and found that an azide derivative (N3--Fe a33+, CuB2+-N3-) induces a translational movement of the heme a3 plane. Azides 65-70 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 94-97 30077971-5 2018 To experimentally test this, we examined X-ray structures of the azide-bound, oxidized bovine CcO and found that an azide derivative (N3--Fe a33+, CuB2+-N3-) induces a translational movement of the heme a3 plane. Azides 116-121 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 94-97 30160117-3 2018 Mechanistic studies suggested that the Rh2(II,II)-bound azide intermediate, rather than the free azide radical, is the key active species in the reaction. Azides 56-61 Rh blood group D antigen Homo sapiens 39-48 29846671-3 2018 We conceived a novel chemo-enzymatic method termed terminal deoxynucleotidyl transferase (TdT)-assisted, copper-catalyzed azide-alkyne cycloaddition (CuAAC)-mediated ssDNA ligation (TCS ligation). Azides 122-127 DNA nucleotidylexotransferase Homo sapiens 51-88 29846671-3 2018 We conceived a novel chemo-enzymatic method termed terminal deoxynucleotidyl transferase (TdT)-assisted, copper-catalyzed azide-alkyne cycloaddition (CuAAC)-mediated ssDNA ligation (TCS ligation). Azides 122-127 DNA nucleotidylexotransferase Homo sapiens 90-93 29846671-4 2018 In this method, TdT is used to incorporate a single 3"-azide-modified dideoxyribonucleotide onto the 3"-end of target ssDNA, followed by CuAAC-mediated click ligation of the azide-incorporated 3"-end to a 5"-ethynylated synthetic adaptor. Azides 55-60 DNA nucleotidylexotransferase Homo sapiens 16-19 30125079-4 2018 The nine azide ELP guest residues served as conjugation sites for site-specific modification with dibenzocyclooctyne (DBCO)-functionalized single-domain antibodies (SdAbs) through strain-promoted alkyne-azide cycloaddition (SPAAC). Azides 9-14 nuclear receptor subfamily 5 group A member 1 Homo sapiens 15-18 30001617-3 2018 In this paper, we report the modular synthesis of protein-brush hybrids containing elastin-like polypeptides (ELP) as model proteins by copper-catalyzed azide-alkyne cycloaddition. Azides 153-158 nuclear receptor subfamily 5 group A member 1 Homo sapiens 83-108 30001617-3 2018 In this paper, we report the modular synthesis of protein-brush hybrids containing elastin-like polypeptides (ELP) as model proteins by copper-catalyzed azide-alkyne cycloaddition. Azides 153-158 nuclear receptor subfamily 5 group A member 1 Homo sapiens 110-113 30001617-4 2018 We exploit the recently discovered imidazole-1-sulfonyl azide (ISA) in a diazotransfer reaction to introduce an N-terminal azide onto an ELP. Azides 56-61 nuclear receptor subfamily 5 group A member 1 Homo sapiens 137-140 30001617-5 2018 Next, we use a click reaction to couple the azido-ELP to an alkyne-terminated amine-rich polymer followed by a second diazotransfer step to produce an azide-rich backbone that serves as a scaffold. Azides 151-156 nuclear receptor subfamily 5 group A member 1 Homo sapiens 50-53 29767512-2 2018 In this study, nine novel dye- and azide-conjugated CTZ analogues were synthesized by conjugating a series of fluorescent dyes or an azide group to the C-2 or C-6 position of the nCTZ backbone to obtain bulkiness-driven substrate specificity and potential chemiluminescence/bioluminescence resonance energy transfer (C/BRET). Azides 35-40 complement C2 Homo sapiens 152-155 30019040-1 2018 An efficient strategy for reliable quantitative SERS analysis in common fluids was proposed by amphiphilic functionalization of graphitic silver nanoparticles with inherent internal standards by azides, and has the merits of high accuracy, enhanced dispersity and outstanding stability in fluids. Azides 195-201 seryl-tRNA synthetase 2, mitochondrial Homo sapiens 48-52 29946609-1 2018 Here we report the 18F labeling of a prostate specific membrane antigen (PSMA) ligand via a strain promoted oxa-dibenzocyclooctyne (ODIBO)- or bicyclo[6.1.0]nonyne (BCN)-azide reaction. Azides 170-175 folate hydrolase 1 Homo sapiens 37-71 29946609-1 2018 Here we report the 18F labeling of a prostate specific membrane antigen (PSMA) ligand via a strain promoted oxa-dibenzocyclooctyne (ODIBO)- or bicyclo[6.1.0]nonyne (BCN)-azide reaction. Azides 170-175 folate hydrolase 1 Homo sapiens 73-77 29946609-2 2018 Although ODIBO reacts with azide 20 fold faster than BCN, in vivo PET imaging suggests that 18F-BCN-azide-PSMA demonstrated much higher tumor uptake and a much higher tumor to background contrast. Azides 27-32 folate hydrolase 1 Homo sapiens 106-110 29663810-3 2018 Redox activation of the Cu(OTf)2 precatalyst by indole results in catalytically competent Cu(I) required for azide-metallocarbene coupling. Azides 109-114 POU class 2 homeobox 2 Homo sapiens 24-32 29915035-6 2018 More importantly, we found that the activation of GLUT1 by azide or MbetaCD did not increase its membrane expression but induced the decrease of the large clusters. Azides 59-64 solute carrier family 2 member 1 Homo sapiens 50-55 29767512-2 2018 In this study, nine novel dye- and azide-conjugated CTZ analogues were synthesized by conjugating a series of fluorescent dyes or an azide group to the C-2 or C-6 position of the nCTZ backbone to obtain bulkiness-driven substrate specificity and potential chemiluminescence/bioluminescence resonance energy transfer (C/BRET). Azides 35-40 complement C6 Homo sapiens 159-162 29767512-2 2018 In this study, nine novel dye- and azide-conjugated CTZ analogues were synthesized by conjugating a series of fluorescent dyes or an azide group to the C-2 or C-6 position of the nCTZ backbone to obtain bulkiness-driven substrate specificity and potential chemiluminescence/bioluminescence resonance energy transfer (C/BRET). Azides 133-138 complement C2 Homo sapiens 152-155 29880804-7 2018 First, rGAA and M6PgPs were modified with crosslinkers containing azide and dibenzocyclooctyne, respectively. Azides 66-71 alpha glucosidase Rattus norvegicus 7-11 29880804-8 2018 In the second reaction using copper-free click chemistry, the azide-functionalized rGAA was conjugated with dibenzocyclooctyne-functionalized M6PgPs without the loss of enzyme activity. Azides 62-67 alpha glucosidase Rattus norvegicus 83-87 29863301-3 2018 Proof of concept was achieved with a deactivatable tracer consisting of a CXCR4-specific peptide functionalized with a Cy5 dye bearing a chemoselective azide handle (N3 -Cy5-AcTZ14011). Azides 152-157 C-X-C motif chemokine receptor 4 Homo sapiens 74-79 29664293-3 2018 This study shows that PMS without explicit activation undergoes direct reaction with a variety of compounds, including antibiotics, pharmaceuticals, phenolics, and commonly used singlet-oxygen (1O2) traps and quenchers, specifically furfuryl alcohol (FFA), azide, and histidine. Azides 257-262 proline rich protein BstNI subfamily 1 Homo sapiens 22-25 29938019-2 2018 The linearly connected heterocyclic compounds were synthesized by thermal Huisgen 1,3-dipolar cycloaddition between previously unknown pyridine SF4-alkynes and readily available azides, providing a series of rod-like SF4-connected N-heterocycles in good to excellent yields. Azides 178-184 SURP and G-patch domain containing 1 Homo sapiens 217-220 29361211-8 2018 We demonstrated that an optimized dual-functionalized dendrimer can undergo rapid strain-promoted azide-alkyne cycloaddition with the DBCO-functionalized alpha-CD20 at the physiological conditions. Azides 98-103 membrane-spanning 4-domains, subfamily A, member 1 Mus musculus 160-164 29534937-1 2018 In a previous study, we evaluated a HER2-specific single domain antibody fragment (sdAb) 2Rs15d labeled with 18F via conjugation of a residualizing prosthetic agent that was synthesized by copper-catalyzed azide-alkyne cycloaddition (CuAAC). Azides 206-211 erb-b2 receptor tyrosine kinase 2 Homo sapiens 36-40 29534937-3 2018 The HER2-targeted sdAb 2Rs15d and a nonspecific sdAb R3B23 were pre-conjugated with a moiety containing both azide- and guanidine functionalities. Azides 109-114 erb-b2 receptor tyrosine kinase 2 Homo sapiens 4-8 29600859-3 2018 In this report, we have demonstrated the formation of regioselective 1,4-disubstituted 1,2,3-triazoles from various types of aryl terminal alkynes and azidoformates, which are electron-deficient azides, using a commercialized [Cu(CH3CN)4]PF6 copper(I) catalyst under mild conditions. Azides 195-201 sperm associated antigen 17 Homo sapiens 238-241 29896385-2 2018 Herein, an efficient and versatile way to synthesize polymerizable 9,10-azaboraphenanthrene (BNP)-containing monomers by aromaticity-driven ring expansion reactions between highly antiaromatic borafluorene and azides is reported, and the corresponding conjugated small molecules and polymers are developed as well. Azides 210-216 natriuretic peptide B Homo sapiens 93-96 29470911-1 2018 Broken symmetry density functional theory has been used to calculate g-tensor, 55Mn, 14N, and 17O hyperfine couplings for active site models of superoxidized MnIII/MnIV manganese catalase both in its native and azide-inhibited form. Azides 211-216 catalase Homo sapiens 179-187 29534020-6 2018 A novel method of synthesis involving copper free "click" chemistry (Dibenzocyclooctyl, DBCO) moiety with an azide-labeled reaction partner, known as Strain-Promoted Alkyne Azide Cycloaddition (SPAAC) along with a desolvation method for PTX loading were used in the present study to arrive at the CA IX selective nano-carriers, HSA-PTX-ATZ. Azides 109-114 carbonic anhydrase 9 Homo sapiens 297-302 29441791-5 2018 In contrast to what is seen for 2, receptor 3 forms a CsN3 complex in 20% CD3OD in CDCl3, wherein the azide anion is bound only vertically to the NH protons of the calix[4]pyrrole and the cesium cation is complexed within the cone shaped-calix[4]pyrrole bowl. Azides 102-113 casein kappa Homo sapiens 54-58 29265682-0 2018 Visible-light-driven Efficient Photocatalytic Reduction of Organic Azides to Amines over CdS Sheet-rGO Nanocomposite. Azides 67-73 CDP-diacylglycerol synthase 1 Homo sapiens 89-92 29265682-3 2018 In the adopted strategy, CdS not only accelerates the formation of nitrene through photoactivation of azide but also enhances the decomposition of azide to a certain extent, which entirely suppressed formation of the azo compound. Azides 102-107 CDP-diacylglycerol synthase 1 Homo sapiens 25-28 29265682-3 2018 In the adopted strategy, CdS not only accelerates the formation of nitrene through photoactivation of azide but also enhances the decomposition of azide to a certain extent, which entirely suppressed formation of the azo compound. Azides 147-152 CDP-diacylglycerol synthase 1 Homo sapiens 25-28 28493513-3 2017 In this paper, soluble multifunctional polytriazoles (PIa and PIb) with high weight-average molecular weights (Mw up to 32 000) are prepared via the developed metal-free poly-cycloaddition of activated azide and alkynes in high yields (up to 90%). Azides 202-207 RPTOR independent companion of MTOR complex 2 Homo sapiens 54-57 29131928-8 2018 RESULTS: NO3- /NO2- nitrogen is routed to the 15 Nalpha position of N2 O in the azide reaction; hence the delta15 Nalpha value should be used for N2 O laser spectrometry results. Azides 80-85 NBL1, DAN family BMP antagonist Homo sapiens 9-12 29052959-8 2018 The lysine residue was also converted into an azide group in both a linear and reversed cyclic peptide sequences cyclo(K(N3)larllt) (Cyclo.L1.1) to allow for subsequent "click" conjugation. Azides 46-51 immunoglobulin kappa variable 1-6 Homo sapiens 139-143 29172484-3 2017 Here, we report a new method for the total chemical synthesis of IGF-1 analogs, which entails the solid-phase synthesis of two IGF-1 precursor chains that is followed by the CuI-catalyzed azide-alkyne cycloaddition ligation and by biomimetic formation of a native pattern of disulfides. Azides 188-193 insulin like growth factor 1 Homo sapiens 65-70 29172484-3 2017 Here, we report a new method for the total chemical synthesis of IGF-1 analogs, which entails the solid-phase synthesis of two IGF-1 precursor chains that is followed by the CuI-catalyzed azide-alkyne cycloaddition ligation and by biomimetic formation of a native pattern of disulfides. Azides 188-193 insulin like growth factor 1 Homo sapiens 127-132 29269881-6 2017 Combination of site-specific incorporation of a clickable p-azido-L-phenylalanine to Uox and strain-promoted azide-alkyne cycloaddition allowed the conjugation of fatty acid (palmitic acid analog) to Uox with the HSA binding capacity and retained enzyme activity. Azides 109-114 urate oxidase (pseudogene) Homo sapiens 200-203 28780139-1 2017 Quaternary amine functionalized metal-organic framework MIL-101(Cr) (MIL-101(Cr)-NMe3) was prepared as the sorbent for the magnetic solid-phase extraction (MSPE) of azide from sartan drugs before ion chromatography determination. Azides 165-170 NME/NM23 nucleoside diphosphate kinase 3 Homo sapiens 81-85 29200285-8 2018 As proof of principle, purified, azide-modified scFv was conjugated to the antioxidant enzyme, catalase, resulting in robust endothelial targeting of functional cargo in vitro and in vivo. Azides 33-38 immunglobulin heavy chain variable region Homo sapiens 48-52 29200285-8 2018 As proof of principle, purified, azide-modified scFv was conjugated to the antioxidant enzyme, catalase, resulting in robust endothelial targeting of functional cargo in vitro and in vivo. Azides 33-38 catalase Homo sapiens 95-103 29206443-0 2018 Site-Specific 64Cu Labeling of the Serine Protease, Active Site Inhibited Factor Seven Azide (FVIIai-N3), Using Copper Free Click Chemistry. Azides 87-92 coagulation factor II, thrombin Homo sapiens 35-50 29113793-2 2018 AuNPs are co-functionalized with doxorubicin (DOX) and an azide-terminated polymer (DOX/N3@AuNPs), and the DOX/N3@AuNPs are associated into DOX@AuNCs in the presence of an alkyne-terminated MMP-2 cleavable peptide (alkyne-peptide-alkyne; APA) by click chemistry. Azides 58-63 matrix metallopeptidase 2 Mus musculus 190-195 29306432-8 2018 Finally, we discuss several applications of the copper-catalyzed azide-alkyne cycloaddition "click" reaction to attach various alkyne-containing chemical probes to GalNAz and demonstrate how this functionalization of O-GlcNAc-modified proteins can be used to realize (1)-(3) above. Azides 65-70 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 217-225 29104923-6 2017 The resultant azidolipids are then fluorescently tagged using the strain-promoted azide-alkyne cycloaddition, enabling visualization of cellular membranes bearing active PLD enzymes. Azides 82-87 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 170-173 28718966-5 2017 Then, the regioselective anti-addition of HN3 to triple bond of active silver-acetylide or ethynyl carbinols affords product vinyl azide via Ag-C sigma-bond activation or Ag...C pi-coordination activation modes, and the former one is more favorable. Azides 131-136 MT-RNR2 like 3 (pseudogene) Homo sapiens 42-45 28771266-3 2017 Azide-terminated NiII, CoII, CuII, ZnII-templated [2]pseudorotaxanes were explored to generate [2]rotaxane, ROT, via reaction with an alkyne-terminated triphenylene unit as a stopper under the mild reaction condition of the CuI-catalyzed azide-alkyne cycloaddition reaction. Azides 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-27 28771266-3 2017 Azide-terminated NiII, CoII, CuII, ZnII-templated [2]pseudorotaxanes were explored to generate [2]rotaxane, ROT, via reaction with an alkyne-terminated triphenylene unit as a stopper under the mild reaction condition of the CuI-catalyzed azide-alkyne cycloaddition reaction. Azides 238-243 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-27 28218815-6 2017 Azide-modified ManNAc analogues widely used in MGE also enhanced esterase activity and provided a way to enrich targeted glycoengineered proteins (such as CES2), thereby providing unambiguous evidence that the compounds were converted to sialosides and installed into the glycan structures of esterases as intended. Azides 0-5 carboxylesterase 2 Homo sapiens 155-159 28636039-3 2017 Herein, we report the conjugation of three azide-bearing BODIPYs with similar core structures but widely different emission wavelengths (green, red and NIR) to tyrosine residues of a model globular protein (BSA) via a common linking methodology. Azides 43-48 NOC2 like nucleolar associated transcriptional repressor Homo sapiens 152-155 28747761-5 2017 BMP2 covalently immobilized on an MC hydrogel (MC-BMP2) was prepared quantitatively by a simple biorthogonal reaction between alkyne groups on BMP2-OpgY and azide groups on MC-N3 via a Cu(I)-catalyzed click reaction. Azides 157-162 bone morphogenetic protein 2 Homo sapiens 0-4 28747761-5 2017 BMP2 covalently immobilized on an MC hydrogel (MC-BMP2) was prepared quantitatively by a simple biorthogonal reaction between alkyne groups on BMP2-OpgY and azide groups on MC-N3 via a Cu(I)-catalyzed click reaction. Azides 157-162 bone morphogenetic protein 2 Homo sapiens 50-54 28747761-5 2017 BMP2 covalently immobilized on an MC hydrogel (MC-BMP2) was prepared quantitatively by a simple biorthogonal reaction between alkyne groups on BMP2-OpgY and azide groups on MC-N3 via a Cu(I)-catalyzed click reaction. Azides 157-162 bone morphogenetic protein 2 Homo sapiens 50-54 28649697-5 2017 Both normal and cancerous prostate tissues were sliced and cultured in the presence of the azide-functionalized sialic acid biosynthetic precursor Ac4 ManNAz. Azides 91-96 adenylate cyclase 4 Homo sapiens 147-150 27836606-4 2017 Covalent binding of capturing biomolecule (anti-TNF-alpha antibody) on off-surface matrix was achieved via azide group activity of 4-fluoro-3-nitro-azidobenzene (FNAB), which act as cross-linker and further covalently binds to anti-TNF-alpha antibody via thermal reaction. Azides 107-112 tumor necrosis factor Homo sapiens 48-57 28461152-2 2017 The azide anion is a potent competitive inhibitor that binds directly to the metal and is used as a substrate analog to superoxide in studies of SOD. Azides 4-15 superoxide dismutase 2 Homo sapiens 145-148 28461152-3 2017 The crystal structure of human MnSOD-azide complex was solved and shows the putative binding position of superoxide, providing a model for binding to the active site. Azides 37-42 superoxide dismutase 2 Homo sapiens 31-36 28426192-5 2017 We successfully attached the azide as a chemical warhead to cellular substrates of wild-type p300 and engineered GCN5. Azides 29-34 E1A binding protein p300 Homo sapiens 93-97 28426192-5 2017 We successfully attached the azide as a chemical warhead to cellular substrates of wild-type p300 and engineered GCN5. Azides 29-34 lysine acetyltransferase 2A Homo sapiens 113-117 27836606-4 2017 Covalent binding of capturing biomolecule (anti-TNF-alpha antibody) on off-surface matrix was achieved via azide group activity of 4-fluoro-3-nitro-azidobenzene (FNAB), which act as cross-linker and further covalently binds to anti-TNF-alpha antibody via thermal reaction. Azides 107-112 tumor necrosis factor Homo sapiens 232-241 28524847-3 2017 We design a small-molecule anticoagulant drug (Warfarin) containing an azide group that acts as a safety pin. Azides 71-76 dynein light chain LC8-type 1 Homo sapiens 105-108 28474886-5 2017 "Click SAgA" (cSAgAPLP:LABL) uses hydrolytically stable covalent conjugation chemistry (Copper-catalyzed Azide-Alkyne Cycloaddition (CuAAC)) rather than a hydrolyzable oxime bond to attach PLP and LABL to HA. Azides 105-110 proteolipid protein 1 Homo sapiens 19-22 28493627-2 2017 Described herein is that the platinum (boryl)iminomethane (BIM) complex [Pt(kappa2 -N,B-Cy2 BIM)(CNArDipp2 )] can effect the oxidative insertion of a range of unsaturated organic substrates, including azides, isocyantes, and nitriles, as well as CO2 and elemental sulfur (S8 ). Azides 201-207 nudix hydrolase 4 Homo sapiens 97-106 28510447-0 2017 Synthesis of a Highly Azide-Reactive and Thermosensitive Biofunctional Reagent for Efficient Enrichment and Large-Scale Identification of O-GlcNAc Proteins by Mass Spectrometry. Azides 22-27 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 138-146 28510447-5 2017 In this work, we designed and synthesized a novel thermosensitive immobilized triarylphosphine reagent as a convenient tool for efficient enrichment of azide-labeled O-GlcNAc proteins from complex biological samples. Azides 152-157 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 166-174 28510447-7 2017 As a result, facilitated coupling is achieved between triarylphosphine and azide-labeled O-GlcNAc proteins via Staudinger ligation, due to the increased triarylphosphine concentration, reduced interfacial mass transfer resistance, and steric hindrance in homogeneous reaction. Azides 75-80 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 89-97 27862453-1 2017 The reaction between [UO2 F2 ] and an excess of Me3 SiN3 in acetonitrile solution results in fluoride-azide exchange and the uranium(VI) dioxodiazide adduct [UO2 (N3 )2 CH3 CN] was isolated in quantitative yield. Azides 102-107 SIN3 transcription regulator family member A Homo sapiens 52-56 28383264-1 2017 An iridium-catalyzed ortho-C(sp2)-H amidation reaction of benzaldehydes with organic azides has been developed. Azides 85-91 Sp2 transcription factor Homo sapiens 27-32 28323404-5 2017 Azide-terminated lysozyme aptamers were clicked onto the rGO/PEI/Ph-alkynyl matrix and used for the sensing of lysozyme levels in patients suffering from inflammatory bowel disease (IBD), where lysozyme levels are up-regulated. Azides 0-5 lysozyme Homo sapiens 17-25 28323404-5 2017 Azide-terminated lysozyme aptamers were clicked onto the rGO/PEI/Ph-alkynyl matrix and used for the sensing of lysozyme levels in patients suffering from inflammatory bowel disease (IBD), where lysozyme levels are up-regulated. Azides 0-5 lysozyme Homo sapiens 111-119 28323404-5 2017 Azide-terminated lysozyme aptamers were clicked onto the rGO/PEI/Ph-alkynyl matrix and used for the sensing of lysozyme levels in patients suffering from inflammatory bowel disease (IBD), where lysozyme levels are up-regulated. Azides 0-5 lysozyme Homo sapiens 111-119 28296399-6 2017 The amido products arise from highly reactive Co(III) imido radical intermediates that are the kinetic products of the reactions of 1 or 1-THF with the azide reagents. Azides 152-157 mitochondrially encoded cytochrome c oxidase III Homo sapiens 46-52 28161574-4 2017 An engineered interferon-gamma (IFN-gamma) fusion protein was tagged with an N-terminal azide group, and immobilized to two different dibenzocyclooctyne-functionalized biomimetic polysaccharides (chitosan and hyaluronan). Azides 88-93 interferon gamma Rattus norvegicus 14-30 28161574-4 2017 An engineered interferon-gamma (IFN-gamma) fusion protein was tagged with an N-terminal azide group, and immobilized to two different dibenzocyclooctyne-functionalized biomimetic polysaccharides (chitosan and hyaluronan). Azides 88-93 interferon gamma Rattus norvegicus 32-41 28161574-5 2017 We successfully immobilized azide-tagged IFN-gamma under a wide variety of reaction conditions, both in solution and to bulk hydrogels. Azides 28-33 interferon gamma Rattus norvegicus 41-50 28161574-13 2017 We found that adding an N-terminal azide-tag to interferon-gamma enabled stable and robust Cu-free "click" immobilization under a variety of physiologic conditions. Azides 35-40 interferon gamma Rattus norvegicus 48-64 27882694-2 2017 Herein, by making use of the copper-free strain-promoted alkyne-azide cycloaddition (SPAAC) reaction between difluorinated cyclooctynes (DIFOs) and various azide-containing compounds, we showed for the first time that potential caspase-1 inhibitors could be rapidly synthesized. Azides 64-69 caspase 1 Homo sapiens 228-237 28080030-1 2017 Cytochrome P450 enzymes have been engineered to catalyze abiological C-H bond amination reactions, but the yields of these reactions have been limited by low chemoselectivity for the amination of C-H bonds over competing reduction of the azide substrate to a sulfonamide. Azides 238-243 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 28935106-8 2017 EPO was engineered to carry azide-tagged Man3GlcNAc2 glycans that could be further modified via click chemistry to introduce other functional groups. Azides 28-33 erythropoietin Homo sapiens 0-3 27734553-2 2017 Azide-terminated PSt and P4VP are synthesized via post- and pre-atom transfer radical polymerization modification, respectively. Azides 0-5 sulfotransferase family 1A member 1 Homo sapiens 17-20 28695504-3 2017 AO-alkyne can be used to detect auto-ADP-ribosylation of PARP10 in cells following Cu-catalyzed click conjugation to an azide reporter. Azides 120-125 poly(ADP-ribose) polymerase family member 10 Homo sapiens 57-63 28695507-4 2017 Recently, we developed a robust NAD+ analog-sensitive approach for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subsequent copper-catalyzed azide-alkyne cycloaddition ("click chemistry") reactions. Azides 181-186 poly(ADP-ribose) polymerase 1 Homo sapiens 67-72 28695507-4 2017 Recently, we developed a robust NAD+ analog-sensitive approach for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subsequent copper-catalyzed azide-alkyne cycloaddition ("click chemistry") reactions. Azides 181-186 poly(ADP-ribose) polymerase 1 Homo sapiens 67-71 27778291-3 2017 This chapter demonstrates the power of a triple bioorthogonal ligation strategy which addresses the three activities of the proteasome: the beta5-subunit selective norbornene-tagged probe is reacted with fluorescent tetrazine, the beta1-selective azide-functionalized probe was addressed with a biotinylated phosphine, followed by an alkyne-substituted pan-reactive probe to label the remaining beta2 activity to which an azide-coupled fluorophore was ligated. Azides 247-252 potassium calcium-activated channel subfamily M regulatory beta subunit 1 Homo sapiens 231-236 27935613-2 2016 We report the design and synthesis of azide-tagged boronic acid salicylidenehydrazone (BASHY) dyes and their use for site-selective labelling of Annexin V. Azides 38-43 annexin A5 Homo sapiens 145-154 28144361-4 2016 By this method, two series of azide group-terminated polyrotaxanes (benzylazide: PRX-Bn-N3, phenylazide: PRX-Ph-N3,) were synthesized for functionalization via click reactions. Azides 30-35 periaxin Homo sapiens 81-84 28144361-4 2016 By this method, two series of azide group-terminated polyrotaxanes (benzylazide: PRX-Bn-N3, phenylazide: PRX-Ph-N3,) were synthesized for functionalization via click reactions. Azides 30-35 periaxin Homo sapiens 105-108 28144361-6 2016 Additionally, the terminal azide groups of the PRX-Bn-N3 could be modified with dibenzylcyclooctyne (DBCO)-conjugated fluorescent molecules via a copper-free click reaction; this fluorescently labeled PRX was utilized for intracellular fluorescence imaging. Azides 27-32 periaxin Homo sapiens 47-50 28144361-6 2016 Additionally, the terminal azide groups of the PRX-Bn-N3 could be modified with dibenzylcyclooctyne (DBCO)-conjugated fluorescent molecules via a copper-free click reaction; this fluorescently labeled PRX was utilized for intracellular fluorescence imaging. Azides 27-32 periaxin Homo sapiens 201-204 27751588-2 2016 FLT3-specific peptides were conjugated onto modified poloxamer 407 using the copper-catalyzed azide-alkyne cycloaddition reaction. Azides 94-99 fms related receptor tyrosine kinase 3 Homo sapiens 0-4 27396685-1 2016 Different azides and alkynes have been coupled via Cu-catalyzed 1,3-dipolar Huisgen cycloaddition to afford a novel family of N1- and C5-substituted 1,2,3-triazole derivatives that feature the propargylamine group typical of irreversible MAO-B inhibitors at the C4-side chain of the triazole ring. Azides 10-16 monoamine oxidase B Homo sapiens 238-243 27762044-3 2016 A cathepsin B-specific cleavable substrate (KGRR) conjugated with triacetylated N-azidoacetyl-d-mannosamine (RR-S-Ac3 ManNAz) was developed to enable tumor cells to generate unnatural glycans that contain azide groups. Azides 205-210 cathepsin B Mus musculus 2-13 27723299-4 2016 For this purpose, defined amounts of azide-functionalized IL-2 were linked to alkyne-functionalized hydroxyethyl starch nanocapsules via copper-free click reactions. Azides 37-42 interleukin 2 Homo sapiens 58-62 27238725-5 2016 The new compounds 1-4 differed in their presumed AChE peripheral site binding moiety, which ranged from an azide group to functionalized heterocycles. Azides 107-112 acetylcholinesterase (Cartwright blood group) Homo sapiens 49-53 27882199-3 2016 Through strategic selection of the mammalian expression host, we were able to introduce azide-functionalized glycans onto a homogeneously glycosylated anti-EphA2 monoclonal antibody in one step. Azides 88-93 EPH receptor A2 Homo sapiens 156-161 27256882-2 2016 Here we report a robust NAD(+) analog-sensitive approach for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subsequent copper-catalyzed azide-alkyne cycloaddition reactions. Azides 175-180 poly(ADP-ribose) polymerase 1 Homo sapiens 61-66 27289322-6 2016 The presented results demonstrate the usefulness of strain-promoted azide-alkyne cycloaddition in the labelling of highly lipophilic lipopeptides without disturbing the in vitro activity of these conjugates with respect to activation of TLR-2. Azides 68-73 toll like receptor 2 Homo sapiens 237-242 27171861-5 2016 Insulin modified with either one or two light cleavable azide groups is polymerized with a tridentate alkyne-bridging monomer using a click reaction. Azides 56-61 insulin Homo sapiens 0-7 27409454-3 2016 Post-DNA synthesis copper-catalyzed azide-alkyne cycloaddition (CuAAC) reactions with a variety of spin labels enable the use of double electron-electron resonance experiments to measure a number of distances on the duplex, affording a high level of detailed structural information. Azides 36-41 spindlin 1 Homo sapiens 99-103 27373419-7 2016 However, resveratrol prevented these effects, protecting hippocampal astrocytes against azide-induced cytotoxicity through the heme-oxygenase-1 (HO-1) pathway and inhibiting p38 mitogen-activated protein kinase (p38 MAPK) and nuclear factor kappa B (NFkappaB) activation. Azides 88-93 heme oxygenase 1 Homo sapiens 127-143 27373419-7 2016 However, resveratrol prevented these effects, protecting hippocampal astrocytes against azide-induced cytotoxicity through the heme-oxygenase-1 (HO-1) pathway and inhibiting p38 mitogen-activated protein kinase (p38 MAPK) and nuclear factor kappa B (NFkappaB) activation. Azides 88-93 mitogen-activated protein kinase 14 Homo sapiens 212-220 27373419-7 2016 However, resveratrol prevented these effects, protecting hippocampal astrocytes against azide-induced cytotoxicity through the heme-oxygenase-1 (HO-1) pathway and inhibiting p38 mitogen-activated protein kinase (p38 MAPK) and nuclear factor kappa B (NFkappaB) activation. Azides 88-93 nuclear factor kappa B subunit 1 Homo sapiens 226-248 27373419-7 2016 However, resveratrol prevented these effects, protecting hippocampal astrocytes against azide-induced cytotoxicity through the heme-oxygenase-1 (HO-1) pathway and inhibiting p38 mitogen-activated protein kinase (p38 MAPK) and nuclear factor kappa B (NFkappaB) activation. Azides 88-93 nuclear factor kappa B subunit 1 Homo sapiens 250-258 27384259-7 2016 Although the oxidants tested were unsuccessful, electrophiles, particularly NBS, enabled the coupling reaction to occur in good yield with a broad range of secondary and tertiary boronic esters, bearing different steric demands and functional groups (esters, azides, nitriles, alcohols, and ethers). Azides 259-265 nibrin Homo sapiens 76-79 27256882-2 2016 Here we report a robust NAD(+) analog-sensitive approach for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subsequent copper-catalyzed azide-alkyne cycloaddition reactions. Azides 175-180 poly(ADP-ribose) polymerase 1 Homo sapiens 61-65 27458323-0 2016 Efficient access to sp3-rich tricyclic amine scaffolds through Diels-Alder reactions of azide-containing silyloxydienes. Azides 88-93 Sp3 transcription factor Homo sapiens 20-23 27355959-5 2016 Performing the SPAAC click reaction (Strain-Promoted Azide-Alkyne Cycloaddition) by the use of a dibenzylcyclooctyne-fluorophore (DBCO-fluorophore) led to a specifically labeled human protein kinase CK2alpha. Azides 53-58 casein kinase 2 alpha 2 Homo sapiens 199-207 27128971-7 2016 Moreover, metabolic labeling using myristic acid, azide showed a considerable decrease in the myristoylation of proteins in parasites treated with NMT inhibitors, providing evidence of the on-target activity of the inhibitors. Azides 50-55 N-myristoyltransferase 1 Homo sapiens 147-150 28328022-1 2016 RATIONALE: The azide method for measuring the stable isotope ratios of nitrate (NO3- ) is easy to set up. Azides 15-20 NBL1, DAN family BMP antagonist Homo sapiens 80-83 26952080-4 2016 Here, we describe a direct comparison of tetrazine ligation and strain promoted azide-alkyne cycloaddition using benzimidazole based probes to bind their known target, the gastric proton pump, ATP4A. Azides 80-85 ATPase H+/K+ transporting subunit alpha Homo sapiens 193-198 26930274-5 2016 Importantly, DBCO-650-labeled chondrocytes presented strong NIRF signals with relatively low cytotoxicity and the amounts of azide groups and DBCO-650 could be easily controlled by feeding different amounts of Ac4ManNAz and DBCO-650 to the cell culture system. Azides 125-130 immunoglobulin kappa variable 4-63 Mus musculus 210-213 26792724-6 2016 The leucine residue was substituted for the alkyne-bearing proparcylglycine to facilitate conjugation of an azide-tagged reporter group using click chemistry, following irreversible inhibition of CTSS. Azides 108-113 cathepsin S Homo sapiens 196-200 26938787-4 2016 Modification with a cyclic RGD peptide and a heparin binding peptide (HBP) was realized by an efficient on-resin combination of Diels-Alder reaction with inverse electron demand and Cu(I) catalyzed azide-alkyne cycloaddition. Azides 198-203 azurocidin 1 Homo sapiens 45-68 26938787-4 2016 Modification with a cyclic RGD peptide and a heparin binding peptide (HBP) was realized by an efficient on-resin combination of Diels-Alder reaction with inverse electron demand and Cu(I) catalyzed azide-alkyne cycloaddition. Azides 198-203 azurocidin 1 Homo sapiens 70-73 26812170-5 2016 X-ray photoelectron spectroscopy studies showed successful dialkyne incorporation with minimal Si surface oxidation, and monitoring of the C 1s and N 1s core-level spectra showed successful azide-alkyne cycloaddition. Azides 190-195 heterogeneous nuclear ribonucleoprotein C Homo sapiens 139-142 26731630-6 2016 Despite precursor binding to crystalline AChE, coupling of rapid electric field fluctuations in the gorge with proper alignments of the azide and alkyne reactants to form the triazole remains a likely limiting step. Azides 136-141 acetylcholinesterase (Cartwright blood group) Homo sapiens 41-45 33418637-0 2016 Azide-Incorporated Clickable Silk Fibroin Materials with the Ability to Photopattern. Azides 0-5 fibroin light chain Bombyx mori 34-41 33418637-4 2016 We demonstrated that azide groups in AzPhe incorporated into silk fibroin can be selectively modified by bioorthogonal azide-alkyne cycloaddition reactions (click chemistry). Azides 21-26 fibroin light chain Bombyx mori 66-73 33418637-4 2016 We demonstrated that azide groups in AzPhe incorporated into silk fibroin can be selectively modified by bioorthogonal azide-alkyne cycloaddition reactions (click chemistry). Azides 119-124 fibroin light chain Bombyx mori 66-73 26900445-0 2016 Efficient conversion of primary azides to aldehydes catalyzed by active site variants of myoglobin. Azides 32-38 myoglobin Homo sapiens 89-98 26731630-2 2016 These features launched AChE as a reaction vessel for in situ click-chemistry synthesis of high-affinity TZ2PA6 and TZ2PA5 inhibitors, forming a syn-triazole upon cycloaddition within the gorge from alkyne and azide reactants bound at the two sites, respectively. Azides 210-215 acetylcholinesterase (Cartwright blood group) Homo sapiens 24-28 26731630-2 2016 These features launched AChE as a reaction vessel for in situ click-chemistry synthesis of high-affinity TZ2PA6 and TZ2PA5 inhibitors, forming a syn-triazole upon cycloaddition within the gorge from alkyne and azide reactants bound at the two sites, respectively. Azides 210-215 synemin Homo sapiens 78-81 26683093-5 2016 The conjugation approach allowed the controlled attachment of doxorubicin through an acid-labile hydrazone linkage, an Alexa Fluor dye through an amide bond, and a glycan-based ligand for the cell surface receptor CD22 of B-cells using strain promoted azide-alkyne cycloaddition. Azides 252-257 CD22 molecule Homo sapiens 214-218 26693734-2 2016 Most synthetic methodologies leading to vitamin B12 conjugates involve functionalization at the 5" position via either carbamate-based linkages or using copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC), resulting in stable conjugates that are not cleaved within the cell. Azides 173-178 NADH:ubiquinone oxidoreductase subunit B3 Homo sapiens 48-51 26792393-3 2016 Here, we aimed to stabilize and modulate the receptor-compatible conformation of insulin by covalent intra-chain crosslinking within its B22-B30 segment, using the Cu(I)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction of azides and alkynes. Azides 226-232 insulin Homo sapiens 81-88 26900445-2 2016 Here, we demonstrate that engineered variants of the hemoprotein myoglobin can catalyze this transformation with high efficiency (up to 8,500 turnovers) and selectivity across a range of structurally diverse aryl-substituted primary azides. Azides 233-239 myoglobin Homo sapiens 65-74 26900445-3 2016 Mutagenesis of the "distal" histidine residue was particularly effective in enhancing the azide oxidation reactivity of myoglobin, enabling these reactions to proceed in good to excellent yields (37-89%) and to be carried out at a synthetically useful scale. Azides 90-95 myoglobin Homo sapiens 120-129 26768534-2 2015 While [WO(N3 )4 ] was formed through fluoride-azide exchange in the reaction of Me3 SiN3 with WOF4 in SO2 solution, the reaction with MoOF4 resulted in a reduction of Mo(VI) to Mo(V) and formation of [MoO(N3 )3 ]. Azides 46-51 SIN3 transcription regulator family member A Homo sapiens 84-88 28791106-2 2016 The signal probe, prepared using a Raman signal molecule and dibenzocyclooctyne-amine to functionalize a 10 nm Au nanoparticle, exhibits a negligible SERS effect and can recognize and link the azide-tagged glycan via a click reaction. Azides 193-198 seryl-tRNA synthetase 2, mitochondrial Homo sapiens 150-154 26431832-2 2015 Our group recently demonstrated that guanosine exhibits glioprotective effects in the C6 astroglial cell line by associating the heme oxygenase-1 (HO-1) signaling pathway with protection against azide-induced oxidative stress. Azides 195-200 heme oxygenase 1 Homo sapiens 129-145 26512733-0 2015 Azide vs Alkyne Functionalization in Pt(II) Complexes for Post-treatment Click Modification: Solid-State Structure, Fluorescent Labeling, and Cellular Fate. Azides 0-5 solute carrier family 35 member G1 Homo sapiens 58-62 26512733-2 2015 Post-treatment fluorescent labeling of functionalized Pt(II)-based agents using the bioorthogonal Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) reaction has recently been reported as a promising approach. Azides 114-119 solute carrier family 35 member G1 Homo sapiens 0-4 26431832-2 2015 Our group recently demonstrated that guanosine exhibits glioprotective effects in the C6 astroglial cell line by associating the heme oxygenase-1 (HO-1) signaling pathway with protection against azide-induced oxidative stress. Azides 195-200 heme oxygenase 1 Homo sapiens 147-151 26717597-1 2015 We demonstrated using Ca(2+)-sensitive fluorescent probe, mitochondria binding dyes, and confocal laser scanning microscopy, that elimination of electrochemical potential of uterus myocytes" inner mitochondrial membrane by aprotonophore carbonyl cyanide m-chlorophenyl hydrazone (10 muM), and by a respiratory chain complex IV inhibitor sodium azide (1 mM) is associated with substantial increase of Ca2+ concentration in myoplasm in the case of the protonophore effect only, but not in the case of the azide effect. Azides 344-349 latexin Homo sapiens 283-286 26453409-3 2015 This paper reports the synthesis by a copper-catalyzed azide-alkyne cycloaddition reaction as the key reaction, of bivalent CXCR4 ligands with near infrared (NIR) dyes at the terminus or the center of the poly-L-proline linker. Azides 55-60 C-X-C motif chemokine receptor 4 Homo sapiens 124-129 26257399-4 2015 Analysis of this complex shows that the substrate analog, azide, binds end-on to the manganese center as a sixth ligand and that it ligates directly to a third and new solvent molecule also positioned within interacting distance to the His30 and Tyr34 residues of the substrate access funnel. Azides 58-63 Histone H2A Caenorhabditis elegans 236-241 26308144-4 2015 Site-selective chemical cross-linking of SOD introduces a bioorthogonal azide group on the cross-link so that two SODs react efficiently with a bis-alkyne through phase-directed copper-catalyzed azide-alkyne cycloaddition (PDCuAAC). Azides 72-77 superoxide dismutase 1 Homo sapiens 41-44 26308144-4 2015 Site-selective chemical cross-linking of SOD introduces a bioorthogonal azide group on the cross-link so that two SODs react efficiently with a bis-alkyne through phase-directed copper-catalyzed azide-alkyne cycloaddition (PDCuAAC). Azides 195-200 superoxide dismutase 1 Homo sapiens 41-44 26512633-2 2015 This scaffold holds two alkyne arms in a free and TIPS-protected form for consecutive CuAAC (copper(I)-catalyzed azide-alkyne cycloaddition), one Fmoc-protected hydrazide arm for reaction with aldehydes, and one carboxylic acid arm with CF2 groups for attachment to the resin and (19)F-NMR quantification. Azides 113-118 ATPase H+ transporting accessory protein 1 Homo sapiens 237-240 26119004-1 2015 [Cu(dap)2]Cl effectively catalyzes azide addition from the Zhdankin reagent to styrene-type double bonds, and subsequent addition of a third component to the benzylic position. Azides 35-40 DLG associated protein 2 Homo sapiens 4-9 26308144-0 2015 Bioorthogonal phase-directed copper-catalyzed azide-alkyne cycloaddition (PDCuAAC) coupling of selectively cross-linked superoxide dismutase dimers produces a fully active bis-dimer. Azides 46-51 superoxide dismutase 1 Homo sapiens 120-140 26037613-5 2015 Specifically, azide- and alkyne-functionalized N-mustard analogs serve as cofactor mimics of SAM and are enzymatically transferred to a model peptide substrate in a PRMT1-dependent fashion. Azides 14-19 protein arginine methyltransferase 1 Homo sapiens 165-170 25822161-2 2015 The click-chemical ligation between an azide-modified probe DNA and a dibenzocyclooctyne-modified probe DNA occurred through the hybridization of target miRNA (miR-141). Azides 39-44 microRNA 141 Homo sapiens 160-167 25980911-2 2015 First, O-GlcNAc-modified peptides were enzymatically labeled with an azide-containing GalNAc analog. Azides 69-74 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 7-15 25999035-2 2015 We optimized a protocol for bio-orthogonal TRAP conjugation via Cu(I)-catalyzed Huisgen-cycloaddition of terminal azides and alkynes (CuAAC), including a detailed investigation of kinetic properties of Cu(II)-TRAP complexes. Azides 114-120 TRAP Homo sapiens 43-47 25999035-3 2015 TRAP building blocks for CuAAC, TRAP(alkyne)3 and TRAP(azide)3 were obtained by amide coupling of propargylamine/3-azidopropyl-1-amine, respectively. Azides 55-60 TRAP Homo sapiens 0-4 25862515-6 2015 Incorporation of p-azido-l-phenylalanine into two predetermined positions of Uox allowed site-specific linkage of dibenzocyclooctyne-derivatized human serum albumin (HSA) through strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 195-200 urate oxidase Mus musculus 77-80 28706718-4 2015 In silico modelling was used to design TEM beta-lactamase variants with the non-natural amino acid p-azido-l-phenylalanine (azF) placed at functionally strategic positions permitting residue-specific modification with alkyne adducts by exploiting strain-promoted azide-alkyne cycloaddition. Azides 263-268 AZF1 Homo sapiens 124-127 25805211-0 2015 Azide-alkyne cycloaddition-mediated cyclization of phosphonopeptides and their evaluation as PTP1B binders and enrichment tools. Azides 0-5 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 93-98 25805211-4 2015 Here, we aimed to study if azide-alkyne cycloaddition-mediated cyclization of a peptide inhibitor could increase its selectivity toward PTP1B over TCPTP, and if cyclic and linear peptide binders can be applied as enrichment tools of endogenous PTP1B. Azides 27-32 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 136-141 25805211-4 2015 Here, we aimed to study if azide-alkyne cycloaddition-mediated cyclization of a peptide inhibitor could increase its selectivity toward PTP1B over TCPTP, and if cyclic and linear peptide binders can be applied as enrichment tools of endogenous PTP1B. Azides 27-32 protein tyrosine phosphatase non-receptor type 2 Homo sapiens 147-152 25805211-4 2015 Here, we aimed to study if azide-alkyne cycloaddition-mediated cyclization of a peptide inhibitor could increase its selectivity toward PTP1B over TCPTP, and if cyclic and linear peptide binders can be applied as enrichment tools of endogenous PTP1B. Azides 27-32 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 244-249 25962668-1 2015 Genetically encoded p-azido-phenylalanine (azF) residues in G protein-coupled receptors (GPCRs) can be targeted with dibenzocyclooctyne-modified (DIBO-modified) fluorescent probes by means of strain-promoted [3+2] azide-alkyne cycloaddition (SpAAC). Azides 214-219 AZF1 Homo sapiens 43-46 26120211-1 2015 Oligomers incorporating the tetrapeptide MSH4, the minimum active sequence of melanocyte stimulating hormone, were synthesized by an A2 + B2 strategy involving microwave-assisted copper-catalyzed azide-alkyne cycloaddition. Azides 196-201 mutS homolog 4 Homo sapiens 41-45 25611563-1 2015 Polymer-peptide conjugates were produced via the copper-catalyzed azide-alkyne cycloaddition of poly(tert-butyl acrylate) (PtBA) and elastin-like peptides. Azides 66-71 elastin Homo sapiens 133-140 25623286-1 2015 An azide (-N3) group attached at the -ortho carbon atom to the aniline moiety of 2-anilino-4,6-di-tert-butylphenol formed a diradical-containing Co(II) complex via inter-ligand azo (N=N) bond formation. Azides 3-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-151 25336437-5 2015 Azide-modified transferrin is attached to these particles, and their high colloidal stability and successful targeting to cancer cells overexpressing the transferrin receptor are demonstrated. Azides 0-5 transferrin Homo sapiens 15-26 25336437-5 2015 Azide-modified transferrin is attached to these particles, and their high colloidal stability and successful targeting to cancer cells overexpressing the transferrin receptor are demonstrated. Azides 0-5 transferrin Homo sapiens 154-165 25893040-3 2015 On the basis of the in vitro study results, di-cRGD-PEG5-ADIBOT-(18)F was prepared from a SPAAC reaction with (18)F-labeled azide and subsequent chemo-orthogonal scavenger-assisted separation without high performance liquid chromatography (HPLC) purification in 92% decay-corrected radiochemical yield (dcRCY) with high specific activity for further in vivo positron emission tomography (PET) imaging study. Azides 124-129 neuronatin Homo sapiens 52-56 25122513-4 2014 This was carried out by the synthesis of a glyco-N-carboxyanhydride (glyco-NCA) containing an azide group at the sixth position of the carbohydrate ring. Azides 94-99 CEA cell adhesion molecule 6 Homo sapiens 75-78 25434878-0 2015 3D Co(II) coordination polymer with ferrimagnetic-like layers based on azide and tetrazolate bridges showing slow magnetic dynamics. Azides 71-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 3-8 25394493-3 2014 Herein we report azide functionalized metal-organic framework (MOF) as a selective turn-on fluorescent probe for H2S detection. Azides 17-22 lysine acetyltransferase 8 Homo sapiens 38-67 25129803-2 2014 Azide functionalities were introduced onto chitosan, through mesylation of C-6 hydroxyl groups, and reacted with a di-alkyne PEO by a regioselective Cu(I)-catalyzed cycloaddition. Azides 0-5 complement C6 Homo sapiens 75-78 25338703-3 2015 In the search for novel FAAH inhibitors, a series of O-(1,2,3-triazol-4-yl)methyl carbamate derivatives were designed and synthesized exploiting a copper- catalyzed [3+2] cycloaddition reaction between azides and alkynes (click chemistry). Azides 202-208 fatty-acid amide hydrolase-like Rattus norvegicus 24-28 25579846-4 2015 By using two mutually compatible, bioorthogonal reactions (copper-catalyzed azide-alkyne cycloaddition chemistry and TCO-tetrazine ligation), we demostrate small molecule-based multiplex bioimaging for simultaneous in situ monitoring of two important cell-cycle regulating kinases (AKA and CDK1). Azides 76-81 aurora kinase A Homo sapiens 282-285 25579846-4 2015 By using two mutually compatible, bioorthogonal reactions (copper-catalyzed azide-alkyne cycloaddition chemistry and TCO-tetrazine ligation), we demostrate small molecule-based multiplex bioimaging for simultaneous in situ monitoring of two important cell-cycle regulating kinases (AKA and CDK1). Azides 76-81 cyclin dependent kinase 1 Homo sapiens 290-294 32262013-4 2014 In this method, azide-beta-CD molecules were first assembled around the templates by formation of template-monomer complexes, and thus the mutual positions of azide-beta-CD molecules were fixed. Azides 16-21 ACD shelterin complex subunit and telomerase recruitment factor Homo sapiens 22-29 32262013-4 2014 In this method, azide-beta-CD molecules were first assembled around the templates by formation of template-monomer complexes, and thus the mutual positions of azide-beta-CD molecules were fixed. Azides 16-21 ACD shelterin complex subunit and telomerase recruitment factor Homo sapiens 165-172 32262013-5 2014 Then, azide-beta-CD molecules were anchored to the walls of the nano-pores of SBA-15 via click chemistry. Azides 6-11 ACD shelterin complex subunit and telomerase recruitment factor Homo sapiens 12-19 25478165-4 2014 The bioorthogonal Staudinger ligation scheme was used to chemoselectively crosslink azide functionalized hyperbranched alginate (alginate-hN3) to methyl-2-diphenylphosphino-terephthalate (MDT) linked PAMAM dendrimer (PAMAM-MDT). Azides 84-89 MT-RNR2 like 3 (pseudogene) Homo sapiens 138-141 25122513-5 2014 Subsequently, the NCA was polymerized to obtain azide-containing glycopolypeptides having good control over molecular weight and polydispersity index (PDI) in high yields. Azides 48-53 CEA cell adhesion molecule 6 Homo sapiens 18-21 25162488-3 2014 The negatively charged co(CEA-AAm) NP was conjugated with a nucleolin-targeting F3 peptide using a highly efficient and specific copper(I) catalyzed azide-alkyne click reaction. Azides 149-154 nucleolin Homo sapiens 60-69 25164984-6 2014 Small molecule modules with precisely positioned alkyne and azide moieties bind adjacent internal loops in r(CCUG)(exp), the causative agent of myotonic dystrophy type 2 (DM2), and are transformed into oligomeric, potent inhibitors of DM2 RNA dysfunction by a Huisgen 1,3-dipolar cycloaddition reaction, a variant of click chemistry. Azides 60-65 immunoglobulin heavy diversity 1-14 (non-functional) Homo sapiens 171-174 25164984-6 2014 Small molecule modules with precisely positioned alkyne and azide moieties bind adjacent internal loops in r(CCUG)(exp), the causative agent of myotonic dystrophy type 2 (DM2), and are transformed into oligomeric, potent inhibitors of DM2 RNA dysfunction by a Huisgen 1,3-dipolar cycloaddition reaction, a variant of click chemistry. Azides 60-65 immunoglobulin heavy diversity 1-14 (non-functional) Homo sapiens 235-238 25191696-0 2014 Copper-catalyzed C(sp2)-H amidation with azides as amino sources. Azides 41-47 Sp2 transcription factor Homo sapiens 17-22 24673378-6 2014 Azide treatment of these cells resulted in several detrimental effects, including induction of cytotoxicity and mitochondrial dysfunction, increased levels of reactive oxygen/nitrogen species, inducible nitric oxide synthase expression and NADPH oxidase, decreased glutamate uptake and EAAC1 glutamate transporter expression, decreased glutathione (GSH) levels, and decreased activities of glutamine synthetase (GS), superoxide dismutase and catalase (CAT). Azides 0-5 solute carrier family 1 member 1 Homo sapiens 286-291 25121958-0 2014 Transition-state structure for the quintessential SN2 reaction of a carbohydrate: reaction of alpha-glucopyranosyl fluoride with azide ion in water. Azides 129-134 solute carrier family 38 member 5 Homo sapiens 50-53 25121958-1 2014 We report that the SN2 reaction of alpha-d-glucopyranosyl fluoride with azide ion proceeds through a loose (exploded) transition-state (TS) structure. Azides 72-77 solute carrier family 38 member 5 Homo sapiens 19-22 25023539-1 2014 The 2-[(18)F]fluoro-3-pent-4-yn-1-yloxypyridine ([(18)F]FPyKYNE) analog of the potent non-peptide angiotensin II type 1 receptor (AT1R) blocker losartan was produced via click chemistry linking [(18)F]FPyKYNE to azide-modified tetrazole-protected losartan followed by TFA deprotection. Azides 212-217 angiotensin II receptor, type 1b Rattus norvegicus 98-128 24857763-3 2014 The CS-b-PLA(n) were synthesized using click-grafting onto method implying reducing-end alkynation of low-molecular weight depolymerized CS (M(w) = 5000 g mol(-1)) and azide-terminated functionalization of PLAn (M(w) = 6500 g mol(-1) (n = 46) and M(w) = 1700 g mol(-1) (n = 20)). Azides 168-173 chorionic somatomammotropin hormone 2 Homo sapiens 4-8 24884258-3 2014 The azide groups incorporated in fibroin were active as chemical handles for click chemistry in both the solubilized and the solid (fibrous) states. Azides 4-9 fibroin light chain Bombyx mori 33-40 24884258-4 2014 The azides survived degumming in the boiling alkaline solution that is required for complete removal of the sericin layer, demonstrating that AzPhe-incorporated silk fibroin could be a versatile platform to produce "clickable" silk materials in various forms. Azides 4-10 fibroin light chain Bombyx mori 166-173 24945908-3 2014 For this purpose, ELP and PEG blocks were functionalized with azide and cyclooctyne moieties, respectively. Azides 62-67 nuclear receptor subfamily 5 group A member 1 Homo sapiens 18-21 24945908-4 2014 Azides were introduced by applying a recently developed pH-controlled diazotransfer reaction on the primary amines present in ELP (N-terminus and lysine side chains). Azides 0-6 nuclear receptor subfamily 5 group A member 1 Homo sapiens 126-129 24945908-5 2014 By varying pH, ELP-blocks with one or two azides were obtained, which subsequently allowed us to synthesize both ELP-PEG diblock copolymers and miktoarm star polymers. Azides 42-48 nuclear receptor subfamily 5 group A member 1 Homo sapiens 15-18 25005084-0 2014 Azide inhibition of urate oxidase. Azides 0-5 urate oxidase (pseudogene) Homo sapiens 20-33 25005084-1 2014 The inhibition of urate oxidase (UOX) by azide was investigated by X-ray diffraction techniques and compared with cyanide inhibition. Azides 41-46 urate oxidase (pseudogene) Homo sapiens 18-31 25005084-1 2014 The inhibition of urate oxidase (UOX) by azide was investigated by X-ray diffraction techniques and compared with cyanide inhibition. Azides 41-46 urate oxidase (pseudogene) Homo sapiens 33-36 25005084-4 2014 UOX was co-crystallized with azide (N3) in the presence or absence of either uric acid (UA, the natural substrate) or 8-azaxanthine (8AZA, a competitive inhibitor). Azides 29-34 urate oxidase (pseudogene) Homo sapiens 0-3 25000540-4 2014 The structure of 2 is very similar but one of the azide ions acts as mu1,1 and the other as mu1,3 to form an alternating chain. Azides 50-55 glutathione S-transferase mu 1 Homo sapiens 69-74 25000540-4 2014 The structure of 2 is very similar but one of the azide ions acts as mu1,1 and the other as mu1,3 to form an alternating chain. Azides 50-55 glutathione S-transferase mu 1 Homo sapiens 92-97 25084947-4 2014 The phase transition to chain like structure (P-1 phase) occurs at a modest pressure 51 GPa, the azide ions N3 (-) (linear chains of three N atoms with covalent bonds and interact weakly with each other) begin to show remarkable polymeric N properties in the CsN3 system. Azides 97-102 casein kappa Homo sapiens 259-263 24673378-6 2014 Azide treatment of these cells resulted in several detrimental effects, including induction of cytotoxicity and mitochondrial dysfunction, increased levels of reactive oxygen/nitrogen species, inducible nitric oxide synthase expression and NADPH oxidase, decreased glutamate uptake and EAAC1 glutamate transporter expression, decreased glutathione (GSH) levels, and decreased activities of glutamine synthetase (GS), superoxide dismutase and catalase (CAT). Azides 0-5 glutamate-ammonia ligase Homo sapiens 390-410 24673378-6 2014 Azide treatment of these cells resulted in several detrimental effects, including induction of cytotoxicity and mitochondrial dysfunction, increased levels of reactive oxygen/nitrogen species, inducible nitric oxide synthase expression and NADPH oxidase, decreased glutamate uptake and EAAC1 glutamate transporter expression, decreased glutathione (GSH) levels, and decreased activities of glutamine synthetase (GS), superoxide dismutase and catalase (CAT). Azides 0-5 glutamate-ammonia ligase Homo sapiens 349-351 24673378-6 2014 Azide treatment of these cells resulted in several detrimental effects, including induction of cytotoxicity and mitochondrial dysfunction, increased levels of reactive oxygen/nitrogen species, inducible nitric oxide synthase expression and NADPH oxidase, decreased glutamate uptake and EAAC1 glutamate transporter expression, decreased glutathione (GSH) levels, and decreased activities of glutamine synthetase (GS), superoxide dismutase and catalase (CAT). Azides 0-5 catalase Homo sapiens 442-450 24673378-6 2014 Azide treatment of these cells resulted in several detrimental effects, including induction of cytotoxicity and mitochondrial dysfunction, increased levels of reactive oxygen/nitrogen species, inducible nitric oxide synthase expression and NADPH oxidase, decreased glutamate uptake and EAAC1 glutamate transporter expression, decreased glutathione (GSH) levels, and decreased activities of glutamine synthetase (GS), superoxide dismutase and catalase (CAT). Azides 0-5 catalase Homo sapiens 452-455 24887377-4 2014 In the present study, we incorporated an alkyne-bearing NAA into an enzyme, murine dihydrofolate reductase (mDHFR), in high cell density cultivation of Escherichia coli, and performed CuAAC conjugation with fluorescent azide dyes to evaluate enzyme compatibility of various CuAAC conditions comprising combination of commercially available Cu(I)-chelating ligands and reductants. Azides 219-224 dihydrofolate reductase Mus musculus 108-113 24652439-2 2014 The dimeric NGR peptide (NGR2) was conjugated with an alkyne-containing PEG unit followed by mixing with an azide-terminated Cy5.5 fluorophore (Cy5.5-N3) to afford Cy5.5-NGR2. Azides 108-113 reticulon 4 receptor Homo sapiens 12-15 24652439-2 2014 The dimeric NGR peptide (NGR2) was conjugated with an alkyne-containing PEG unit followed by mixing with an azide-terminated Cy5.5 fluorophore (Cy5.5-N3) to afford Cy5.5-NGR2. Azides 108-113 reticulon 4 receptor like 2 Homo sapiens 25-29 32261313-2 2014 Azide-terminated poly(N-vinylcaprolactam) (PVCL-N3), prepared a priori via xanthate-mediated reversible addition-fragmentation chain transfer (RAFT) polymerization of N-vinylcaprolactam (VCL), was then linked to HPCL chains through Cu(i)-catalyzed alkyne-azide click reaction. Azides 0-5 2-hydroxyacyl-CoA lyase 1 Homo sapiens 212-216 24807699-0 2014 Adjusting the surface areal density of click-reactive azide groups by kinetic control of the azide substitution reaction on bromine-functional SAMs. Azides 54-59 methionine adenosyltransferase 1A Homo sapiens 143-147 24807699-0 2014 Adjusting the surface areal density of click-reactive azide groups by kinetic control of the azide substitution reaction on bromine-functional SAMs. Azides 93-98 methionine adenosyltransferase 1A Homo sapiens 143-147 24715520-6 2014 Conversion into the corresponding azide followed by copper-catalyzed azide-alkyne cycloaddition afforded multivalent glycoconjugates of Gb3 for further investigation as anti-cancer therapeutics. Azides 34-39 alpha 1,4-galactosyltransferase (P blood group) Homo sapiens 136-139 24715520-6 2014 Conversion into the corresponding azide followed by copper-catalyzed azide-alkyne cycloaddition afforded multivalent glycoconjugates of Gb3 for further investigation as anti-cancer therapeutics. Azides 69-74 alpha 1,4-galactosyltransferase (P blood group) Homo sapiens 136-139 24664183-2 2014 A trimethylguanosine synthase was engineered to transfer a terminal azido moiety to the 5"-cap which could be further modified using strain-promoted azide-alkyne cycloaddition (SPAAC). Azides 149-154 trimethylguanosine synthase 1 Homo sapiens 2-29 24548078-7 2014 The utility of the new cross-linker has been demonstrated by conjugation of azide functionalized bovine serum albumin (azido-BSA) with azido-fluorescein and by the immobilization of the latter protein on azide-derivatized silica beads. Azides 76-81 albumin Homo sapiens 104-117 24548078-7 2014 The utility of the new cross-linker has been demonstrated by conjugation of azide functionalized bovine serum albumin (azido-BSA) with azido-fluorescein and by the immobilization of the latter protein on azide-derivatized silica beads. Azides 204-209 albumin Homo sapiens 104-117 24522410-1 2014 Two new azide bound cobalt(III) complexes, [Co(L(1))(N3)3] (fac-1) and [Co(L(2))(N3)3] (mer-2), where L(1) is bis(2-pyridylmethyl)amine and L(2) is (2-pyridylmethyl)(2-pyridylethyl)amine, derived from tridentate reduced Schiff-base ligands have been reported. Azides 8-13 bromodomain PHD finger transcription factor Homo sapiens 60-65 24522410-1 2014 Two new azide bound cobalt(III) complexes, [Co(L(1))(N3)3] (fac-1) and [Co(L(2))(N3)3] (mer-2), where L(1) is bis(2-pyridylmethyl)amine and L(2) is (2-pyridylmethyl)(2-pyridylethyl)amine, derived from tridentate reduced Schiff-base ligands have been reported. Azides 8-13 CD151 molecule (Raph blood group) Homo sapiens 88-93 24568284-1 2014 The copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) click reaction was used to incorporate alkyne-functionalized dipicolylamine (DPA) ligands (1 and 3) for fac-[M(I)(CO)3](+) (M = Re/(99m)Tc) complexation into an alpha-melanocyte stimulating hormone (alpha-MSH) peptide analogue. Azides 24-29 pro-opiomelanocortin-alpha Mus musculus 220-256 24568284-1 2014 The copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) click reaction was used to incorporate alkyne-functionalized dipicolylamine (DPA) ligands (1 and 3) for fac-[M(I)(CO)3](+) (M = Re/(99m)Tc) complexation into an alpha-melanocyte stimulating hormone (alpha-MSH) peptide analogue. Azides 24-29 pro-opiomelanocortin-alpha Mus musculus 258-267 24568284-5 2014 An alpha-MSH peptide functionalized with an azide was labeled with fac-[M(I)(CO)3](+) using both click, then chelate (CuAAC reaction with 1 or 3 followed by metal complexation) and chelate, then click (metal complexation of 1 and 3 followed by CuAAC with the peptide) strategies to assess the effects of CuAAC conditions on fac-[M(I)(CO)3](+) complexation within a peptide framework. Azides 44-49 pro-opiomelanocortin-alpha Mus musculus 3-12 24370415-9 2014 The Quantum yield of 4-methyl-7-propargylcoumarin (7P4MC) was enhanced after triazole formation with azide functionalized PEG (methoxy-PEG350 azide). Azides 101-106 progestagen associated endometrial protein Homo sapiens 122-125 24370415-9 2014 The Quantum yield of 4-methyl-7-propargylcoumarin (7P4MC) was enhanced after triazole formation with azide functionalized PEG (methoxy-PEG350 azide). Azides 101-106 progestagen associated endometrial protein Homo sapiens 127-147 24342725-4 2014 The pretargeting component, anti-HER2 humanized monoclonal antibody, trastuzumab, functionalized with azide groups labels cancer cells that overexpress HER2 surface receptors. Azides 102-107 erb-b2 receptor tyrosine kinase 2 Homo sapiens 33-37 24342725-4 2014 The pretargeting component, anti-HER2 humanized monoclonal antibody, trastuzumab, functionalized with azide groups labels cancer cells that overexpress HER2 surface receptors. Azides 102-107 erb-b2 receptor tyrosine kinase 2 Homo sapiens 152-156 24096390-3 2014 Incorporation of acetylene legs into the structure allowed the motors to be grafted to azide-modified quartz and silicon substrates using the "click" 1,3-dipolar cycloaddition reaction. Azides 87-92 doublecortin like kinase 1 Homo sapiens 143-151 24243841-6 2014 We coupled an azide-modified VPg peptide to an RNA primer harboring a cyclooctyne [bicyclo[6.1.0]nonyne (BCN)] by a copper-free "click" reaction, leading to a VPg-triazole-RNA construct that was "non-cleavable" by TDP2. Azides 14-19 tyrosyl-DNA phosphodiesterase 2 Homo sapiens 214-218 24211082-3 2014 Two RGD derivatives (RGDS and iRGD) with azide-terminated groups were conjugated to bicyclononyne-functionalized PSi nanoparticles via copper-free azide-alkyne cycloaddition. Azides 41-46 ral guanine nucleotide dissociation stimulator Homo sapiens 21-25 24192930-4 2014 A preliminary investigation of the catalytic activity of these compounds indicated that the unusual mononuclear complex 6 [(NSHC)2CuBr] is an active catalyst for the Huisgen 1,3-dipolar cycloaddition of azide and alkynes while complexes 1-5 and 7 were marginally less active. Azides 203-208 SHC adaptor protein 3 Homo sapiens 124-128 24345448-0 2014 Azide-alkyne cycloaddition affording enzymatically tunable bisubstrate based inhibitors of histone acetyltransferase PCAF. Azides 0-5 lysine acetyltransferase 2B Homo sapiens 117-121 24211082-3 2014 Two RGD derivatives (RGDS and iRGD) with azide-terminated groups were conjugated to bicyclononyne-functionalized PSi nanoparticles via copper-free azide-alkyne cycloaddition. Azides 147-152 ral guanine nucleotide dissociation stimulator Homo sapiens 21-25 23877838-3 2013 Diagnostic IR stretches support the presence of mu1,1-bridged (end-on, 2075 cm(-1)) azide groups in 1 and mu1,3-bridged (end-to-end, 2117 cm(-1)) thiocyanate groups in 2. Azides 84-89 glutathione S-transferase mu 1 Homo sapiens 48-51 23988352-1 2013 Using Cu(I)-catalyzed azide-alkyne cycloaddition in a mixed classical organic phase and solid phase peptide synthesis approach, we synthesized four analogs of Leu-enkephalin to systematically replace amides by 1,4-disubstituted[1,2,3]triazoles. Azides 22-27 prodynorphin Homo sapiens 159-173 23932248-5 2013 Polymeric nanoparticles comprised of poly(lactide-co-2-methyl, 2-carboxytrimethylene carbonate)-g-polyethylene glycol-furan/azide are click-modified with both anti-HER2 antibodies and nucleic acids on the exterior PEG corona. Azides 124-129 erb-b2 receptor tyrosine kinase 2 Homo sapiens 164-168 23767880-2 2013 To provide homogeneous and stable structures with this motif, the synthesis of a C-linked mimic, C-GlcNAc Ser, has been prepared from the C-Glc Ser by a double inversion strategy using azide to insert the C-2 nitrogen functionality. Azides 185-190 complement C2 Homo sapiens 205-208 23880865-7 2013 The expressions of ZmCHC1 and ZmCHC2 genes in maize are down-regulated by azide or cold treatment, further revealing the energy requirement of CME and suggesting that CME in plants is sensitive to low temperatures. Azides 74-79 Clathrin heavy chain 1 Zea mays 30-36 23834026-0 2013 Overcoming synthetic challenges of oridonin A-ring structural diversification: regio- and stereoselective installation of azides and 1,2,3-triazoles at the C-1, C-2, or C-3 position. Azides 122-128 heterogeneous nuclear ribonucleoprotein C Homo sapiens 156-159 23834026-0 2013 Overcoming synthetic challenges of oridonin A-ring structural diversification: regio- and stereoselective installation of azides and 1,2,3-triazoles at the C-1, C-2, or C-3 position. Azides 122-128 complement C2 Homo sapiens 161-164 23834026-0 2013 Overcoming synthetic challenges of oridonin A-ring structural diversification: regio- and stereoselective installation of azides and 1,2,3-triazoles at the C-1, C-2, or C-3 position. Azides 122-128 complement C3 Homo sapiens 169-172 23834026-1 2013 Efficient and concise synthetic approaches have been developed for the rapid and diverse installation of azide functionalities at the C-1, C-2, or C-3 positions of oridonin (1) with highly controlled regio- and stereoselectivity, while keeping key reactive pharmacophores intact by utilizing unique preactivation strategies based on the common synthon 4. Azides 105-110 heterogeneous nuclear ribonucleoprotein C Homo sapiens 134-137 23834026-1 2013 Efficient and concise synthetic approaches have been developed for the rapid and diverse installation of azide functionalities at the C-1, C-2, or C-3 positions of oridonin (1) with highly controlled regio- and stereoselectivity, while keeping key reactive pharmacophores intact by utilizing unique preactivation strategies based on the common synthon 4. Azides 105-110 complement C2 Homo sapiens 139-142 23834026-1 2013 Efficient and concise synthetic approaches have been developed for the rapid and diverse installation of azide functionalities at the C-1, C-2, or C-3 positions of oridonin (1) with highly controlled regio- and stereoselectivity, while keeping key reactive pharmacophores intact by utilizing unique preactivation strategies based on the common synthon 4. Azides 105-110 complement C3 Homo sapiens 147-150 31986714-1 2013 The FeIII azide complexes [FeIII (N3 )cyclam-ac]PF6 (1 PF6 ), [FeIII (N3 )Me3 cyclam-ac]PF6 (2 PF6 ), and trans-[FeIII (N3 )2 cyclam]ClO4 (3 ClO4 ) (cyclam=1,4,8,11-tetraazacyclotetradecane; cyclam-ac=1,4,8,11-tetraazacyclotetradecane-1-acetate; Me3 cyclam-ac=4,8,11-trimethyl-1,4,8,11-tetraazacyclotetra-decane-1-acetate) are studied in the gas phase with special emphasis on the formation of high-valent iron nitrides by collision-induced dissociation. Azides 10-15 sperm associated antigen 17 Homo sapiens 48-51 23683595-2 2013 The prosthetic groups were conjugated to azide- and PEG3-modified bombesin(6-14) analogues via copper-catalyzed azide-alkyne cycloaddition couplings to yield mono- and di-mini-PEGylated ligands for PET imaging of the gastrin- releasing peptide receptor. Azides 41-46 gastrin releasing peptide receptor Mus musculus 217-252 23683595-2 2013 The prosthetic groups were conjugated to azide- and PEG3-modified bombesin(6-14) analogues via copper-catalyzed azide-alkyne cycloaddition couplings to yield mono- and di-mini-PEGylated ligands for PET imaging of the gastrin- releasing peptide receptor. Azides 112-117 paternally expressed 3 Mus musculus 52-56 23444389-11 2013 The metabolic inhibitor azide (3 mM), the KATP channel opener diazoxide (340 muM), and the Ca2+ channel blocker nifedipine (20 muM) significantly reversed Rb1-mediated GLP1 secretion. Azides 24-29 RB transcriptional corepressor 1 Homo sapiens 155-158 23695978-4 2013 A single-domain antibody (A12) that specifically targets PlexinD1 (a transmembrane protein overexpressed in tumor vasculature) is equipped with an azide-functionality using expressed protein ligation. Azides 147-152 plexin D1 Homo sapiens 57-65 23651235-7 2013 Homogeneous ultrafine PCL fibers, decorated with azide functions, have been made completely hydrophilic upon coupling with propargyl-alpha-d-mannoside and propargyl-beta-d-galactoside. Azides 49-54 PHD finger protein 1 Homo sapiens 22-25 23444389-11 2013 The metabolic inhibitor azide (3 mM), the KATP channel opener diazoxide (340 muM), and the Ca2+ channel blocker nifedipine (20 muM) significantly reversed Rb1-mediated GLP1 secretion. Azides 24-29 glucagon like peptide 1 receptor Homo sapiens 168-172 23876273-6 2013 In all cases, blaIMP-8 was transferred by conjugation to azide-resistant Escherichia coli J53. Azides 57-62 BlaIMP-8 Enterobacter cloacae 14-22 23411399-3 2013 It was found that Cu(I)-catalyzed alkyne-azide cycloaddition reaction (click chemistry) between the alkyne-labeled glycan and the azide-tagged HSA led to an efficient formation of the glycoconjugates. Azides 41-46 albumin Homo sapiens 143-146 23161861-3 2013 The mutual influence between the alkali-metal azides and the pi rings or Zn centers of the involved MOF derivatives are studied by considering the interactions both of the alkali-metal cations with model aromatic centers and of the alkali-metal azides with distinct sites of differently sized models of IRMOF-1 and IRMOF-3. Azides 46-52 lysine acetyltransferase 8 Homo sapiens 100-103 22926664-4 2013 While maximal activities of respiration of saponin-permeabilized muscle fibers and digitonin-permeabilized fibroblasts were only slightly affected by the MFN2 mutations, the sensitivity of active state oxygen consumption to azide, a cytochrome c oxidase (COX) inhibitor, was increased. Azides 224-229 mitofusin 2 Homo sapiens 154-158 23301498-3 2013 In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin. Azides 147-152 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 62-70 24900659-3 2013 Docking studies show that Abl is able to allow the in situ click chemistry between specific azide and alkyne fragments by binding to Abl-active sites. Azides 92-97 ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens 26-29 24900659-3 2013 Docking studies show that Abl is able to allow the in situ click chemistry between specific azide and alkyne fragments by binding to Abl-active sites. Azides 92-97 ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens 133-136 23161861-1 2013 Interactions between alkali-metal azides and metal-organic framework (MOF) derivatives, namely, the first and third members of the isoreticular MOF (IRMOF) family, IRMOF-1 and IRMOF-3, are studied within the density functional theory (DFT) paradigm. Azides 34-40 lysine acetyltransferase 8 Homo sapiens 45-74 23161861-1 2013 Interactions between alkali-metal azides and metal-organic framework (MOF) derivatives, namely, the first and third members of the isoreticular MOF (IRMOF) family, IRMOF-1 and IRMOF-3, are studied within the density functional theory (DFT) paradigm. Azides 34-40 lysine acetyltransferase 8 Homo sapiens 70-73 23338847-3 2013 The two mononuclear complexes 3 and 4 display distorted TBP and tetrahedral geometry, respectively with the azide ions acting as monodentate ligands. Azides 108-113 TATA-box binding protein Homo sapiens 56-59 23461511-3 2013 Treatment of hydrides OsHCl(CO)(PPh3)2L (2), first with triflic acid and then with an excess of RN3 afforded organic azide complexes [OsCl(eta(1)-N3R)(CO)(PPh3)2L]BPh4 (5-7) [R = 4-CH3C6H4CH2, C6H5CH2, C6H5; L = P(OEt)3]. Azides 117-122 drosha ribonuclease III Homo sapiens 96-99 23333444-3 2013 The alpha-linked disaccharide obtained was subsequently transformed into alpha-galactosyl ceramide in four steps involving Z-selective Wittig olefination at C-1, stereo-inversion at C-4 using azide, one-pot reduction of azide and amidation, and global deprotection. Azides 192-197 complement C4A (Rodgers blood group) Homo sapiens 182-185 23512694-5 2013 Cycloaddition of a biotinylated azide with the propargylated c-di-GMP diester under click conditions provides the biotinylated c-di-GMP conjugate in an isolated yield of 62%. Azides 32-37 5'-nucleotidase, cytosolic II Homo sapiens 66-69 23512694-5 2013 Cycloaddition of a biotinylated azide with the propargylated c-di-GMP diester under click conditions provides the biotinylated c-di-GMP conjugate in an isolated yield of 62%. Azides 32-37 5'-nucleotidase, cytosolic II Homo sapiens 132-135 23161861-3 2013 The mutual influence between the alkali-metal azides and the pi rings or Zn centers of the involved MOF derivatives are studied by considering the interactions both of the alkali-metal cations with model aromatic centers and of the alkali-metal azides with distinct sites of differently sized models of IRMOF-1 and IRMOF-3. Azides 245-251 lysine acetyltransferase 8 Homo sapiens 100-103 23161861-5 2013 Remarkably, it is found that, with increasing alkali-metal atom size, the latter decrease for cations interacting with the pi-ring systems and increase for the azides interacting with the MOF fragments. Azides 160-166 lysine acetyltransferase 8 Homo sapiens 188-191 23172365-0 2013 Site-selective azide incorporation into endogenous RNase A via a "chemistry" approach. Azides 15-20 ribonuclease A family member 1, pancreatic Homo sapiens 51-58 23172365-8 2013 Finally, the water soluble azide-reactive phosphine probe, rho-TEO-phosphine (21) (rho: rhodamine), has been designed and applied to attach a chromophore to azido-(K1)RNase A via Staudinger ligation at physiological pH indicating that the introduced azido group is accessible and could be addressed by other established azide-reactive bioorthogonal reaction schemes. Azides 27-32 ribonuclease A family member 1, pancreatic Homo sapiens 167-174 23172365-8 2013 Finally, the water soluble azide-reactive phosphine probe, rho-TEO-phosphine (21) (rho: rhodamine), has been designed and applied to attach a chromophore to azido-(K1)RNase A via Staudinger ligation at physiological pH indicating that the introduced azido group is accessible and could be addressed by other established azide-reactive bioorthogonal reaction schemes. Azides 320-325 ribonuclease A family member 1, pancreatic Homo sapiens 167-174 22670768-0 2012 RuH2(CO)(PPh3)3 catalyzed selective formation of 1,4-disubstituted triazoles from cycloaddition of alkynes and organic azides. Azides 119-125 caveolin 1 Homo sapiens 9-13 23330670-8 2013 We investigate the effect of azide and 8-hydroxyquinoline binding to Cu-Abeta and demonstrate the presence of a water-derived ligand and a second exchangeable ligand coordinated to copper at physiological pH, along the equatorial plane of a square-pyramidal active site. Azides 29-34 amyloid beta precursor protein Homo sapiens 72-77 23083520-1 2012 Selective generation of an amine-terminated self-assembled monolayer bound to silicon wafers via a silicon-carbon linkage was realized by photocatalytically reducing the corresponding azide-terminated, self-assembled monolayers (Az-SAMs). Azides 184-189 methionine adenosyltransferase 1A Homo sapiens 232-236 26605631-10 2012 Finally, the antisymmetric stretch vibrational frequency is computed for an azide ion in FDH and in aqueous solution. Azides 76-81 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 89-92 22988919-3 2012 To this end, we describe the development of copper-catalyzed azide-alkyne cycloaddition (CuAAC, a click chemistry reaction) for site-specific PEGylation of interferon beta-1b (IFNb) containing azidohomoalanine (Aha) at the N-terminus. Azides 61-66 interferon beta 1 Rattus norvegicus 176-180 22996637-0 2012 Conjugation of transferrin to azide-modified CdSe/ZnS core-shell quantum dots using cyclooctyne click chemistry. Azides 30-35 transferrin Homo sapiens 15-26 22925760-5 2012 The benzylamine 15alpha and the dimethylamine 16alpha were obtained by reduction of the azide 6 and subsequent reductive alkylation. Azides 88-93 ATPase H+ transporting accessory protein 1 Homo sapiens 46-53 22861903-2 2012 Here we perform the first atomistic simulation of an azide energetic material, HN3, from the beginning to the end of the chemical evolution and find that the time scale for complete decomposition is a mere 10 ps, orders of magnitude shorter than that of secondary explosives and approaching the fundamental limiting time scale for chemistry; i.e., vibrational time scale. Azides 53-58 MT-RNR2 like 3 (pseudogene) Homo sapiens 79-82 22963672-5 2013 The reduced stomatal apertures of siz1 were inhibited by the application of peroxidase inhibitors, salicylhydroxamic acid and azide, which inhibits SA-dependent reactive oxygen species (ROS) production, but not by an NADPH oxidase inhibitor, diphenyl iodonium chloride, which inhibits ABA-dependent ROS production. Azides 126-131 DNA-binding protein with MIZ/SP-RING zinc finger, PHD-finger and SAP domain-containing protein Arabidopsis thaliana 34-38 22963672-5 2013 The reduced stomatal apertures of siz1 were inhibited by the application of peroxidase inhibitors, salicylhydroxamic acid and azide, which inhibits SA-dependent reactive oxygen species (ROS) production, but not by an NADPH oxidase inhibitor, diphenyl iodonium chloride, which inhibits ABA-dependent ROS production. Azides 126-131 peroxidase Arabidopsis thaliana 76-86 22918759-4 2013 In the work described in this chapter, new alpha-melanocyte stimulating hormone (alpha-MSH) peptide analogs were synthesized and cyclized by copper-catalyzed terminal azide-alkyne cycloaddition "click" chemistry techniques. Azides 167-172 pro-opiomelanocortin-alpha Mus musculus 43-79 22918759-4 2013 In the work described in this chapter, new alpha-melanocyte stimulating hormone (alpha-MSH) peptide analogs were synthesized and cyclized by copper-catalyzed terminal azide-alkyne cycloaddition "click" chemistry techniques. Azides 167-172 pro-opiomelanocortin-alpha Mus musculus 81-90 23106307-0 2012 Interactions of soluble guanylate cyclase with a P-site inhibitor: effects of gaseous heme ligands, azide, and allosteric activators on the binding of 2"-deoxy-3"-GMP. Azides 100-105 5'-nucleotidase, cytosolic II Homo sapiens 163-166 22887038-0 2012 Reversible crystal-to-amorphous structural conversion in the single end-on azide-bridged Co(II) complex: concomitant color and magnetic modulations. Azides 75-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 89-95 22887038-1 2012 Crystal clear: An end-on (EO) azide-bridged Co(II) layer (see scheme; 1) with coordinated water molecules, long spacer p-XBP4 ligands, and unbound azide anions was evacuated to generate a dehydrated sample of 2. Azides 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 22876975-1 2012 The efficient synthesis of multivalent neoglycoconjugates of MUC1 is reported, which utilizes Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddition (CuACC) of azide-functionalized GlcNAc-centered neoglycotetrasaccharide clusters to the MUC1 peptide sequence that was equipped with a propargylglycine residue for "click chemistry". Azides 110-115 mucin 1, cell surface associated Homo sapiens 61-65 22876975-1 2012 The efficient synthesis of multivalent neoglycoconjugates of MUC1 is reported, which utilizes Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddition (CuACC) of azide-functionalized GlcNAc-centered neoglycotetrasaccharide clusters to the MUC1 peptide sequence that was equipped with a propargylglycine residue for "click chemistry". Azides 110-115 mucin 1, cell surface associated Homo sapiens 237-241 22876975-1 2012 The efficient synthesis of multivalent neoglycoconjugates of MUC1 is reported, which utilizes Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddition (CuACC) of azide-functionalized GlcNAc-centered neoglycotetrasaccharide clusters to the MUC1 peptide sequence that was equipped with a propargylglycine residue for "click chemistry". Azides 160-165 mucin 1, cell surface associated Homo sapiens 61-65 22876975-1 2012 The efficient synthesis of multivalent neoglycoconjugates of MUC1 is reported, which utilizes Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddition (CuACC) of azide-functionalized GlcNAc-centered neoglycotetrasaccharide clusters to the MUC1 peptide sequence that was equipped with a propargylglycine residue for "click chemistry". Azides 160-165 mucin 1, cell surface associated Homo sapiens 237-241 22180026-4 2012 We demonstrate that these azide- and alkyne-functionalized TG2 substrates are cell permeable and suitable for specific labeling of TG2 glutamine-donor substrates in HeLa and Movas cells. Azides 26-31 transglutaminase 2 Homo sapiens 59-62 22180026-4 2012 We demonstrate that these azide- and alkyne-functionalized TG2 substrates are cell permeable and suitable for specific labeling of TG2 glutamine-donor substrates in HeLa and Movas cells. Azides 26-31 transglutaminase 2 Homo sapiens 131-134 22180026-5 2012 Both the Cu(I)-catalyzed and strain promoted azide-alkyne cycloaddition proved applicable for subsequent derivatization of the TG2 substrate proteins with the desired probe. Azides 45-50 transglutaminase 2 Homo sapiens 127-130 22753337-1 2012 AVOIDING THE COPPERS: A continuous-flow synthesis for the Cu(I) -catalyzed azide-alkyne cycloaddition reaction using [Cu(phenanthroline)(PPh3)2]NO3 as a homogeneous catalyst is developed (up to 92 % isolated yield). Azides 75-80 caveolin 1 Homo sapiens 137-141 22187146-8 2012 Fourth, after removal of the reversible blockage under mild acidic condition, europium-loaded DOTA with an azide moiety was introduced to the two-chain relaxin-3 carrying the alkyne moiety through click chemistry. Azides 107-112 relaxin 3 Homo sapiens 152-161 22634249-11 2012 This was efficiently prevented by addition of azide or ROS scavengers during the IA treatment or by pre-activation of the Nrf2 system. Azides 46-51 NFE2 like bZIP transcription factor 2 Rattus norvegicus 122-126 22678989-3 2012 For this purpose, azide and alkynyl groups were loaded on the membranes of BPs through the co-assembly method to obtain N(3)-BPs and Alk-BPs, respectively. Azides 18-23 ALK receptor tyrosine kinase Homo sapiens 133-136 22548282-2 2012 Compared with Cu(I)-catalyzed click chemistry, this metal-free strategy provides the following advantages for Cu-64 labeling of the core of SCK-NPs: (1) elimination of copper exchange between nonradioactive Cu in the catalyst and DOTA-chelated Cu-64; (2) elimination of the internal click reactions between the azide and acetylene groups in the same NPs; and (3) increased efficiency of the click reaction because water-soluble Cu(I) does not need to reach the hydrophobic core of the NPs. Azides 311-316 SHC adaptor protein 2 Homo sapiens 140-143 22533503-1 2012 We have synthesized elastin mimetic hybrid polymers (EMHPs) via the step-growth polymerization of azide-functionalized poly(ethylene glycol) (PEG) and alkyne-terminated peptide (AKAAAKA)(2) (AK2) that is abundant in the cross-linking domains of the natural elastin. Azides 98-103 elastin Homo sapiens 20-27 22533503-1 2012 We have synthesized elastin mimetic hybrid polymers (EMHPs) via the step-growth polymerization of azide-functionalized poly(ethylene glycol) (PEG) and alkyne-terminated peptide (AKAAAKA)(2) (AK2) that is abundant in the cross-linking domains of the natural elastin. Azides 98-103 adenylate kinase 2 Homo sapiens 191-194 22533503-1 2012 We have synthesized elastin mimetic hybrid polymers (EMHPs) via the step-growth polymerization of azide-functionalized poly(ethylene glycol) (PEG) and alkyne-terminated peptide (AKAAAKA)(2) (AK2) that is abundant in the cross-linking domains of the natural elastin. Azides 98-103 elastin Homo sapiens 257-264 22684063-0 2012 Purification, crystallization and preliminary X-ray crystallographic analysis of the ATPase domain of human TAP in nucleotide-free and ADP-, vanadate- and azide-complexed forms. Azides 155-160 SEC14 like lipid binding 2 Homo sapiens 108-111 22537861-1 2012 Triazolyl glycolipid derivatives constructed via Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddition reaction (Cue-AAC) represent a new range of carbohydrate-based scaffolds for use in many fields of the chemical research. Azides 65-70 glycine-N-acyltransferase Homo sapiens 118-121 22052741-5 2011 By incorporating artificial amino acids that carry an azide (Aha) or an alkyne (Plk) in their side chains, into ubiquitin (Ub) and PCNA, respectively, we were able to link the two proteins site-specifically by the Cu(I) -catalyzed azide-alkyne cycloaddition. Azides 54-59 proliferating cell nuclear antigen Homo sapiens 131-135 22394239-8 2012 Instead of the in situ protein-templated azide-alkyne cycloaddition reaction occurring at a localized, sequestered enzyme active center as previously shown, we demonstrate that the in situ reaction can take place at the subunit interfaces of an oligomeric protein and can thus be used as a tool for identifying novel candidate nAChR ligands. Azides 41-46 cholinergic receptor nicotinic alpha 4 subunit Homo sapiens 327-332 22239252-5 2012 Second, we evaluated a panel of five different cyclooctyne structures and found that fluorophore conjugates to aza-dibenzocyclooctyne (ADIBO) gave the highest and most specific derivatization of azide-conjugated LAP in cells. Azides 195-200 LAP Homo sapiens 212-215 22224833-5 2012 To obtain the protein-DNA conjugate for assembly of the PPH, we report here the first direct copper catalyzed azide-alkyne cycloaddition-based protein-DNA conjugation. Azides 110-115 enolase 1 Homo sapiens 56-59 23028680-4 2012 Azide-terminal GA (ATGA) was synthesized and applied to human embryonic kidney 293 (HEK293) cells expressing fusion beta2AR, and the electron spin resonance (ESR) technique was utilized. Azides 0-5 adrenoceptor beta 2 Homo sapiens 116-123 22372823-5 2012 The BMP peptide was grafted by the reaction between the azide moiety of Az-mPEG-BMP and the propargyl moiety in the hydrogel. Azides 56-61 bone morphogenetic protein 1 Homo sapiens 4-7 22372823-5 2012 The BMP peptide was grafted by the reaction between the azide moiety of Az-mPEG-BMP and the propargyl moiety in the hydrogel. Azides 56-61 bone morphogenetic protein 1 Homo sapiens 80-83 22052741-5 2011 By incorporating artificial amino acids that carry an azide (Aha) or an alkyne (Plk) in their side chains, into ubiquitin (Ub) and PCNA, respectively, we were able to link the two proteins site-specifically by the Cu(I) -catalyzed azide-alkyne cycloaddition. Azides 231-236 polo like kinase 1 Homo sapiens 80-83 22052741-5 2011 By incorporating artificial amino acids that carry an azide (Aha) or an alkyne (Plk) in their side chains, into ubiquitin (Ub) and PCNA, respectively, we were able to link the two proteins site-specifically by the Cu(I) -catalyzed azide-alkyne cycloaddition. Azides 231-236 proliferating cell nuclear antigen Homo sapiens 131-135 21939187-1 2011 Click phosphorylation of a propargylated unprotected peptide and phosphoryl azide using chaotrope-assisted Cu(I)-catalyzed 1,3-dipolar cycloaddition enabled a high-yielding and rapid synthesis of a nucleoside diphosphate kinase (NDPK) phosphocarrier domain. Azides 76-81 cytidine/uridine monophosphate kinase 2 Homo sapiens 198-227 22011743-0 2011 Isomorphous Co(II) and Ni(II) antiferromagnets based on mixed azide- and carboxylate-bridged chains: metamagnetism and single-chain dynamics. Azides 62-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 22011743-1 2011 Two isomorphous Co(II) and Ni(II) coordination polymers with azide and the 4-(4-pyridyl)benzoic acid N-oxide ligand (4,4-Hopybz) were synthesized, and structurally and magnetically characterized. Azides 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-22 21939187-1 2011 Click phosphorylation of a propargylated unprotected peptide and phosphoryl azide using chaotrope-assisted Cu(I)-catalyzed 1,3-dipolar cycloaddition enabled a high-yielding and rapid synthesis of a nucleoside diphosphate kinase (NDPK) phosphocarrier domain. Azides 76-81 cytidine/uridine monophosphate kinase 2 Homo sapiens 229-233 21812426-0 2011 Blockade of Her2/neu binding to Hsp90 by emodin azide methyl anthraquinone derivative induces proteasomal degradation of Her2/neu. Azides 48-53 erb-b2 receptor tyrosine kinase 2 Homo sapiens 12-20 22012888-1 2011 New hybrid organic-inorganic dyes based on an azide-functionalized cubic octasilsesquioxane (POSS) as the inorganic part and a 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene (BDP) chromophore as the organic component have been synthesized by copper(I)-catalyzed 1,3-dipolar cycloaddition of azides to alkynes. Azides 46-51 AT-rich interaction domain 3B Homo sapiens 171-174 24900276-1 2011 The strain-promoted click 1,3-dipolar cycloaddition reactions involving azides and cyclooctynes for the synthesis of triazoles offer the advantage of being able to be performed in biological settings via copper-free chemistries. Azides 72-78 doublecortin like kinase 1 Homo sapiens 20-27 21174193-4 2011 The immobilization of the B14-ligand onto an azide-group-modified surface was performed with a copper (I)-mediated Click reaction. Azides 45-50 NADH:ubiquinone oxidoreductase subunit A6 Homo sapiens 26-29 21812426-0 2011 Blockade of Her2/neu binding to Hsp90 by emodin azide methyl anthraquinone derivative induces proteasomal degradation of Her2/neu. Azides 48-53 heat shock protein 90 alpha family class A member 1 Homo sapiens 32-37 21812426-0 2011 Blockade of Her2/neu binding to Hsp90 by emodin azide methyl anthraquinone derivative induces proteasomal degradation of Her2/neu. Azides 48-53 erb-b2 receptor tyrosine kinase 2 Homo sapiens 121-129 21657220-0 2011 Magnetic systems with mixed carboxylate and azide bridges: slow relaxation in Co(II) metamagnet and spin frustration in Mn(II) compound. Azides 44-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-84 21552627-4 2011 A click chemistry reaction was used to connect the azide to lipophilic alkynes selected to interact selectively with the S1" subunit of MMP2, as shown by docking and molecular dynamic experiments of the designed compounds. Azides 51-56 matrix metallopeptidase 2 Homo sapiens 136-140 21616091-11 2011 In addition, RTA at 9 muM produced a cytotoxic activity that could not be explained exclusively by the presence of azide in the RTA buffer. Azides 115-120 MAS related GPR family member F Homo sapiens 13-16 21431191-0 2011 Pin-point chemical modification of RNA with diverse molecules through the functionality transfer reaction and the copper-catalyzed azide-alkyne cycloaddition reaction. Azides 131-136 dynein light chain LC8-type 1 Homo sapiens 0-3 21506176-0 2011 Stereo- and regioselective azide/alkyne cycloadditions in carbonic anhydrase II via tethering, monitored by crystallography and mass spectrometry. Azides 27-32 carbonic anhydrase 2 Homo sapiens 58-79 21506176-1 2011 The carbonic anhydrase II mutant His64Cys was prepared and applied to tethered alkyne/azide cycloaddition reactions. Azides 86-91 carbonic anhydrase 2 Homo sapiens 4-25 21325828-4 2011 10 mM azide for 30 minutes (chemical anoxia) significantly inhibited the activity of ERK2 (measured as phospho-ERK) but the ERK-2 activity is rapidly increased in a MEK-independen manner, when azide is washed out of the cells. Azides 6-11 mitogen-activated protein kinase 1 Mus musculus 85-89 21160028-4 2011 In HeLa cells, overexpression of mitofusins attenuated mitochondrial fragmentation during cisplatin- and azide-induced cell injury, which was accompanied by less apoptosis and less cytochrome c release from mitochondria. Azides 105-110 cytochrome c, somatic Homo sapiens 181-193 21160028-7 2011 Consistently, in rat kidney proximal tubular cells, small interfering RNA knockdown of Drp1 prevented mitochondrial fragmentation during azide-induced ATP depletion, which was accompanied by less Bax activation, insertion, and oligomerization in mitochondria. Azides 137-142 collapsin response mediator protein 1 Rattus norvegicus 87-91 21160028-7 2011 Consistently, in rat kidney proximal tubular cells, small interfering RNA knockdown of Drp1 prevented mitochondrial fragmentation during azide-induced ATP depletion, which was accompanied by less Bax activation, insertion, and oligomerization in mitochondria. Azides 137-142 BCL2 associated X, apoptosis regulator Rattus norvegicus 196-199 21300897-5 2011 O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes. Azides 175-180 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 0-8 21384852-0 2011 [CuBr(PPh3)3] for azide-alkyne cycloaddition reactions under strict Click conditions. Azides 18-23 caveolin 1 Homo sapiens 6-10 21094119-7 2011 Azide (N(3)(-)) was found to be a very strong inhibitor of the heCAT (IC(50)=0.2 nM) but a relatively weak CAT inhibitor (IC(50)~10 muM) in human hemolysates. Azides 0-5 catalase Homo sapiens 65-68 21433193-3 2011 Using (Cu(I)Br(PPh3)3) as catalyst for the azide/alkyne-"click"-reaction, crosslinking of the two components at 40 C is observed within 380 min and as fast as 10 min at 80 C. Significant recovery of the tensile storage modulus was observed in a material containing 10 wt.-% and accordingly 5 wt.-% capsules including the reactive components within 5 d at room temperature, thus proving a new concept for materials with self-healing properties. Azides 43-48 caveolin 1 Homo sapiens 15-19 21214250-2 2011 Cooling a solution of the linear and macrocyclic components required for the rotaxane increases the population of the target pseudorotaxane, which is then captured by a rapid capping reaction between an azide and PPh(3). Azides 203-208 caveolin 1 Homo sapiens 213-219 21126012-1 2011 Linear reduction-degradable cationic polymers with different secondary amine densities (S2 and S3) and their nonreducible counterparts (C2 and C3) were synthesized by Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) step-growth polymerization of the dialkyne-oligoamine monomers and the diazide monomers. Azides 183-188 complement C2 Homo sapiens 136-145 21325828-4 2011 10 mM azide for 30 minutes (chemical anoxia) significantly inhibited the activity of ERK2 (measured as phospho-ERK) but the ERK-2 activity is rapidly increased in a MEK-independen manner, when azide is washed out of the cells. Azides 6-11 mitogen-activated protein kinase 1 Mus musculus 124-129 21325828-4 2011 10 mM azide for 30 minutes (chemical anoxia) significantly inhibited the activity of ERK2 (measured as phospho-ERK) but the ERK-2 activity is rapidly increased in a MEK-independen manner, when azide is washed out of the cells. Azides 6-11 midkine Mus musculus 165-168 21325828-4 2011 10 mM azide for 30 minutes (chemical anoxia) significantly inhibited the activity of ERK2 (measured as phospho-ERK) but the ERK-2 activity is rapidly increased in a MEK-independen manner, when azide is washed out of the cells. Azides 193-198 mitogen-activated protein kinase 1 Mus musculus 85-89 21325828-4 2011 10 mM azide for 30 minutes (chemical anoxia) significantly inhibited the activity of ERK2 (measured as phospho-ERK) but the ERK-2 activity is rapidly increased in a MEK-independen manner, when azide is washed out of the cells. Azides 193-198 mitogen-activated protein kinase 1 Mus musculus 124-129 21090615-3 2010 The click-chemistry inhibitor TZ2PA6 links the active center ligand, tacrine, to the peripheral site ligand, propidium, through a biorthogonal reaction of an acetylene and an azide that forms either a syn1 or an anti1 triazole. Azides 175-180 synapsin I Mus musculus 201-205 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. Azides 186-191 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. Azides 209-214 2,4-dienoyl-CoA reductase 1 Homo sapiens 62-67 20542427-1 2010 Glycosyl 1,2,3-triazoles with alpha-D-gluco, beta-D-gluco, alpha-D-galacto, beta-D-galacto and beta-2-acetamido-2-deoxygluco (GlcNAc) stereochemistry were prepared by reaction of the corresponding azides with vinyl acetate under microwave irradiation. Azides 197-203 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 95-101 20958070-7 2010 To further probe the role of the metals, we studied how small molecules such as nitrite (NO(2)(-)), azide (N(3)(-)), and carbon monoxide (CO) interact with the PHM copper ions. Azides 100-105 peptidylglycine alpha-amidating monooxygenase Homo sapiens 160-163 20857965-2 2010 The POH chain end C-Br bonds were subjected to a nucleophilic attack by NaN(3), resulting in azide-terminated POH (POH-N(3)). Azides 93-98 carbonyl reductase 1 Homo sapiens 18-22 20635454-6 2010 The cefotaxime and ceftazidime resistance of the ESBL-producers were transferred to azide-resistant E. coli J53 by conjugation. Azides 84-89 EsbL Escherichia coli 49-53 20586543-5 2010 RESULTS: Both hydroxyl and azide radicals induce centrin 2 polymerisation as we characterised several intermolecular cross-links generating dimers, trimers, tetramers and higher molecular mass species. Azides 27-32 centrin 2 Homo sapiens 49-58 19850004-7 2010 Genomic DNA recovered from E. coli that had been subjected to phagocytosis by human neutrophils occasionally showed small increases in 5-chlorocytosine content when compared to analogous cellular reactions where myeloperoxidase activity was inhibited by azide ion. Azides 254-259 myeloperoxidase Homo sapiens 212-227 20172905-4 2010 We conducted a proteomics scale study to identify candidate trans ligands of CD22 on B-cells by UV photocross-linking CD22-Fc chimera bound to B-cell glycoproteins engineered to carry sialic acids with a 9-aryl azide moiety. Azides 211-216 CD22 molecule Homo sapiens 77-81 20172905-4 2010 We conducted a proteomics scale study to identify candidate trans ligands of CD22 on B-cells by UV photocross-linking CD22-Fc chimera bound to B-cell glycoproteins engineered to carry sialic acids with a 9-aryl azide moiety. Azides 211-216 CD22 molecule Homo sapiens 118-122 20184343-1 2010 A highly effective Co(II)-based system has been developed for catalytic intramolecular C-H amination with phosphoryl azides without the need of terminal oxidant or other additives, resulting in the high-yielding production of cyclophosphoramidates with nitrogen gas as the byproduct. Azides 117-123 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-24 20473435-1 2010 Reactions of MnX(2) meltsalt (X = Cl and ClO(4)) and a quinquedentate Schiff base ligand together with its coligand azides in MeOH produced the unprecedented assembly of novel octa- and hexadecanuclear manganese clusters containing two and four alternant tetrahedral Mn(III)(3)Mn(II) cores bridged by Schiff base ligands and versatile azides groups. Azides 116-122 keratin 86 Homo sapiens 13-16 20473435-1 2010 Reactions of MnX(2) meltsalt (X = Cl and ClO(4)) and a quinquedentate Schiff base ligand together with its coligand azides in MeOH produced the unprecedented assembly of novel octa- and hexadecanuclear manganese clusters containing two and four alternant tetrahedral Mn(III)(3)Mn(II) cores bridged by Schiff base ligands and versatile azides groups. Azides 335-341 keratin 86 Homo sapiens 13-16 20354629-2 2010 "Click addition" of azide to a CN group in 1 gives the oligomeric tetrazolato complex Ru{N(3)N[Na(OEt(2))]=CC(CN)=CCPh=C(CN)(2)}(PPh(3))Cp 3, also containing a RuC(3)N ring. Azides 20-25 protein phosphatase 4 catalytic subunit Homo sapiens 129-140 20232865-3 2010 In the same vessel, the desired functionalized MOF then is obtained by the Huisgen 1,3-dipolar cycloaddition of azides to alkynes, otherwise known as the "click" reaction. Azides 112-118 lysine acetyltransferase 8 Homo sapiens 47-50 20017521-1 2010 Enantioenriched allenylsilanes are used in three-component propargylation reactions with aldehydes and silyl ethers to form syn-homopropargylic ethers that contain an imbedded azide. Azides 176-181 synemin Homo sapiens 124-127 19537804-6 2009 Infrared spectroscopy demonstrated an uptake of 2 equiv of PPNN(3) cocatalyst by the strap mimic catalyst, while only 1 equiv of azide was able to bind to the catalyst containing the full strap, supporting the design function of both complexes. Azides 129-134 serine/threonine kinase receptor associated protein Homo sapiens 188-193 20023923-2 2009 Azide, a singlet oxygen quencher, greatly reduced the p53 photocrosslinking, consistent with the idea that singlet oxygen is the reactive oxygen species involved in p53 photocrosslinking. Azides 0-5 tumor protein p53 Homo sapiens 54-57 20023923-2 2009 Azide, a singlet oxygen quencher, greatly reduced the p53 photocrosslinking, consistent with the idea that singlet oxygen is the reactive oxygen species involved in p53 photocrosslinking. Azides 0-5 tumor protein p53 Homo sapiens 165-168 20024266-1 2009 The study describes for the first time the application of Cu(I)-mediated 1,3-dipolar [3+2]cycloaddition for the labelling of proteins with the short-lived positron emitter fluorine-18 as exemplified with azide-functionalized human serum albumin (HSA). Azides 204-209 albumin Homo sapiens 231-244 19840997-8 2009 The effects of azide on TREK occlude subsequent channel inhibition by AMPK and are attenuated by expression of a dominant negative catalytic subunit of AMPK (dnAMPK), suggesting that metabolic stress modulates TREK channels by an AMPK mechanism. Azides 15-20 potassium two pore domain channel subfamily K member 2 Homo sapiens 24-28 19840997-8 2009 The effects of azide on TREK occlude subsequent channel inhibition by AMPK and are attenuated by expression of a dominant negative catalytic subunit of AMPK (dnAMPK), suggesting that metabolic stress modulates TREK channels by an AMPK mechanism. Azides 15-20 protein kinase AMP-activated catalytic subunit alpha 2 Homo sapiens 70-74 19840997-8 2009 The effects of azide on TREK occlude subsequent channel inhibition by AMPK and are attenuated by expression of a dominant negative catalytic subunit of AMPK (dnAMPK), suggesting that metabolic stress modulates TREK channels by an AMPK mechanism. Azides 15-20 protein kinase AMP-activated catalytic subunit alpha 2 Homo sapiens 152-156 19840997-8 2009 The effects of azide on TREK occlude subsequent channel inhibition by AMPK and are attenuated by expression of a dominant negative catalytic subunit of AMPK (dnAMPK), suggesting that metabolic stress modulates TREK channels by an AMPK mechanism. Azides 15-20 potassium two pore domain channel subfamily K member 2 Homo sapiens 210-214 19840997-8 2009 The effects of azide on TREK occlude subsequent channel inhibition by AMPK and are attenuated by expression of a dominant negative catalytic subunit of AMPK (dnAMPK), suggesting that metabolic stress modulates TREK channels by an AMPK mechanism. Azides 15-20 protein kinase AMP-activated catalytic subunit alpha 2 Homo sapiens 152-156 19821579-4 2009 Two copies of Abeta-binding motifs (either curcumin or the KLVFFA peptide) are clicked via copper(I)-mediated azide-alkyne cycloaddition on a constrained cyclopeptide scaffold designed to interfere with Abeta aggregation. Azides 110-115 amyloid beta precursor protein Homo sapiens 14-19 19746954-5 2009 The chloro ligands in cis-2 are readily displaced by reaction with thiocyanate, azide, and carbonate to give cis- and trans-[Fe(NCS)(2)L(2)] (cis- and trans-3), cis- and trans-[Fe(N(3))(2)L(2)] (cis- and trans-4), and [Fe(kappa(2)-O(2)CO)L(2)] (5), respectively. Azides 80-85 suppressor of cytokine signaling 2 Homo sapiens 22-27 19637848-1 2009 We present three-pulse vibrational echo measurements of azide ion bound to the active site Zn of human carbonic anhydrase II (HCA II) and of two separate active-site mutants Thr199 --> Ala (T199A) and Leu198 --> Phe (L198F). Azides 56-61 carbonic anhydrase 2 Homo sapiens 103-124 19568620-0 2009 "Clickable" elastins: elastin-like polypeptides functionalized with azide or alkyne groups. Azides 68-73 elastin Homo sapiens 12-19 19568620-1 2009 Elastin-like polypeptides (ELPs) functionalized with azide or alkyne groups were produced biosynthetically and coupled via the Cu-catalyzed azide-alkyne cycloaddition to a variety of (bio)molecules. Azides 53-58 elastin Homo sapiens 0-7 19568620-1 2009 Elastin-like polypeptides (ELPs) functionalized with azide or alkyne groups were produced biosynthetically and coupled via the Cu-catalyzed azide-alkyne cycloaddition to a variety of (bio)molecules. Azides 140-145 elastin Homo sapiens 0-7 19243105-1 2009 The active site electronic structure of the azide complex of substrate-bound human heme oxygenase 1 (hHO) has been investigated by (1)H NMR spectroscopy to shed light on the orbital/spin ground state as an indicator of the unique distal pocket environment of the enzyme. Azides 44-49 heme oxygenase 1 Homo sapiens 83-99 19076073-5 2009 Modelling of mouse ceruloplasmin against the known X-ray structure of human ceruloplasmin indicated subtle but potentially significant changes in the pPD- and azide-binding sites. Azides 159-164 ceruloplasmin Mus musculus 19-32 19076073-5 2009 Modelling of mouse ceruloplasmin against the known X-ray structure of human ceruloplasmin indicated subtle but potentially significant changes in the pPD- and azide-binding sites. Azides 159-164 ceruloplasmin Homo sapiens 76-89 19097642-3 2009 A tetra-hydroxy terminated 4-arm PEG was functionalized with acetylene and was reacted with peptide azide/diazide and/or PEG diazide to produce hydrogels via a copper mediated 1,3-cycloaddition (Click chemistry) generating a triazole linkage as the networking forming reaction. Azides 100-105 progestagen associated endometrial protein Homo sapiens 33-36 18723823-9 2008 Consistent with this, heteromeric SUR1+SUR2A channels were sensitive to azide, diazoxide, and pinacidil, and their single-channel burst duration was 2-fold longer than that of the T1 channels. Azides 72-77 ATP binding cassette subfamily C member 8 Homo sapiens 34-38 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. Azides 52-57 carbonic anhydrase 15 Mus musculus 164-170 19178353-8 2009 Calculation of the k(1) values (nucleophile attack as RDS) for the reactions of 1a-h with N(3)(-) indicates that azide ion is more reactive than OH(-) toward the thione esters, although the former is over 11 pK(a) units less basic than the latter. Azides 113-118 peripherin 2 Homo sapiens 54-57 19479916-2 2009 The structurally uniform alkyne-terminated mucin mimetic glycopolymers (see picture; TR = fluorophore) were printed on azide-functionalized chips by microcontact printing in the presence of a copper catalyst. Azides 119-124 LOC100508689 Homo sapiens 43-48 18837524-6 2008 The PEGylated BMP peptide was reacted with 4-carboxybenzenesulfonazide to produce an azide functionalized Az-mPEG-BMP peptide. Azides 65-70 bone morphogenetic protein 1 Homo sapiens 14-17 18837524-6 2008 The PEGylated BMP peptide was reacted with 4-carboxybenzenesulfonazide to produce an azide functionalized Az-mPEG-BMP peptide. Azides 65-70 bone morphogenetic protein 1 Homo sapiens 114-117 18989078-2 2008 Each azide ligand bridges three Pb(II) ions in a mu(1,1,3) coordination mode to form a two-dimensional three-connected 6(3) topology network extending in the bc plane. Azides 5-10 submaxillary gland androgen regulated protein 3B Homo sapiens 32-38 18701654-3 2008 Using mouse fibroblasts of AMPK wild type and AMPK knockout, we documented that the expression of AMPK is essential for the glucose transport response to both azide and 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside (AICAR). Azides 159-164 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 27-31 18701654-3 2008 Using mouse fibroblasts of AMPK wild type and AMPK knockout, we documented that the expression of AMPK is essential for the glucose transport response to both azide and 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside (AICAR). Azides 159-164 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 46-50 18701654-3 2008 Using mouse fibroblasts of AMPK wild type and AMPK knockout, we documented that the expression of AMPK is essential for the glucose transport response to both azide and 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside (AICAR). Azides 159-164 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 46-50 18701654-5 2008 In Clone 9 cells, AMPK wild-type fibroblasts, and H9c2 heart cells, azide or hypoxia selectively increased p-ERK1/2, whereas, in contrast, AICAR selectively stimulated p-p38; phosphorylation of JNK was unaffected. Azides 68-73 mitogen activated protein kinase 3 Rattus norvegicus 109-115 18701654-5 2008 In Clone 9 cells, AMPK wild-type fibroblasts, and H9c2 heart cells, azide or hypoxia selectively increased p-ERK1/2, whereas, in contrast, AICAR selectively stimulated p-p38; phosphorylation of JNK was unaffected. Azides 68-73 mitogen activated protein kinase 14 Rattus norvegicus 170-173 18701654-5 2008 In Clone 9 cells, AMPK wild-type fibroblasts, and H9c2 heart cells, azide or hypoxia selectively increased p-ERK1/2, whereas, in contrast, AICAR selectively stimulated p-p38; phosphorylation of JNK was unaffected. Azides 68-73 mitogen-activated protein kinase 8 Rattus norvegicus 194-197 18701654-6 2008 Azide"s effect on p-ERK1/2 abundance and glucose transport in Clone 9 cells was partially abolished by the MEK1/2 inhibitor U0126. Azides 0-5 mitogen activated protein kinase 3 Rattus norvegicus 20-26 18701654-6 2008 Azide"s effect on p-ERK1/2 abundance and glucose transport in Clone 9 cells was partially abolished by the MEK1/2 inhibitor U0126. Azides 0-5 mitogen activated protein kinase kinase 1 Rattus norvegicus 107-113 18701654-7 2008 SB 203580, an inhibitor of p38, prevented the phosphorylation of p38 and the glucose transport response to AICAR and, unexpectedly, to azide. Azides 135-140 mitogen activated protein kinase 14 Rattus norvegicus 27-30 18701654-11 2008 We conclude that although azide, hypoxia, and AICAR all activate AMPK, the downstream signaling pathways are distinct, with azide and hypoxia stimulating ERK1/2 and AICAR stimulating the p38 pathway. Azides 26-31 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 65-69 18701654-11 2008 We conclude that although azide, hypoxia, and AICAR all activate AMPK, the downstream signaling pathways are distinct, with azide and hypoxia stimulating ERK1/2 and AICAR stimulating the p38 pathway. Azides 26-31 mitogen activated protein kinase 3 Rattus norvegicus 154-160 18701654-11 2008 We conclude that although azide, hypoxia, and AICAR all activate AMPK, the downstream signaling pathways are distinct, with azide and hypoxia stimulating ERK1/2 and AICAR stimulating the p38 pathway. Azides 26-31 mitogen activated protein kinase 14 Rattus norvegicus 187-190 18701654-11 2008 We conclude that although azide, hypoxia, and AICAR all activate AMPK, the downstream signaling pathways are distinct, with azide and hypoxia stimulating ERK1/2 and AICAR stimulating the p38 pathway. Azides 124-129 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 65-69 18723823-9 2008 Consistent with this, heteromeric SUR1+SUR2A channels were sensitive to azide, diazoxide, and pinacidil, and their single-channel burst duration was 2-fold longer than that of the T1 channels. Azides 72-77 ATP binding cassette subfamily C member 8 Homo sapiens 39-44 18723823-12 2008 Finally, the response of the SUR1+SUR2A channels to azide was found to be intermediate to those of the homomeric channels. Azides 52-57 ATP binding cassette subfamily C member 8 Homo sapiens 29-33 18723823-12 2008 Finally, the response of the SUR1+SUR2A channels to azide was found to be intermediate to those of the homomeric channels. Azides 52-57 ATP binding cassette subfamily C member 8 Homo sapiens 34-39 18721805-5 2008 Between 12 and 30 h of azide treatment, cardiomyocytes showed progressive cell death accompanied by release of intact cTnI (29 kDa), intact cTnT (39 kDa), four cTnI degradation products of 26, 20, 17 and 12 kDa, and three cTnT degradation products of 37, 27 and 14 kDa. Azides 23-28 troponin I3, cardiac type Homo sapiens 118-122 18555981-6 2008 In this communication we describe rationale for using purified recombinant Drosophila AChE as a template for in situ reaction of tacrine and propidium based libraries of acetylene and azide building blocks. Azides 184-189 Acetylcholine esterase Drosophila melanogaster 86-90 18555981-10 2008 Moreover, the preferred site of acetylene+azide reaction in insect AChE and the resulting triazole ring formation shifts from near the base of the gorge to closer to its rim due to substantial differences of the gorge geometry in Drosophila AChE. Azides 42-47 Acetylcholine esterase Drosophila melanogaster 67-71 18555981-10 2008 Moreover, the preferred site of acetylene+azide reaction in insect AChE and the resulting triazole ring formation shifts from near the base of the gorge to closer to its rim due to substantial differences of the gorge geometry in Drosophila AChE. Azides 42-47 Acetylcholine esterase Drosophila melanogaster 241-245 18681416-6 2008 Evolution of HN 3 is detected from the azides. Azides 39-45 MT-RNR2 like 3 (pseudogene) Homo sapiens 13-17 18665287-0 2008 Reactivity of a Co(I) [N(2)P(2)] complex with azides: evidence for a transient Co(III) imido species. Azides 46-52 mitochondrially encoded cytochrome c oxidase I Homo sapiens 16-21 18721805-5 2008 Between 12 and 30 h of azide treatment, cardiomyocytes showed progressive cell death accompanied by release of intact cTnI (29 kDa), intact cTnT (39 kDa), four cTnI degradation products of 26, 20, 17 and 12 kDa, and three cTnT degradation products of 37, 27 and 14 kDa. Azides 23-28 troponin T2, cardiac type Homo sapiens 140-144 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. Azides 188-193 exonuclease 1 Homo sapiens 0-5 18721805-5 2008 Between 12 and 30 h of azide treatment, cardiomyocytes showed progressive cell death accompanied by release of intact cTnI (29 kDa), intact cTnT (39 kDa), four cTnI degradation products of 26, 20, 17 and 12 kDa, and three cTnT degradation products of 37, 27 and 14 kDa. Azides 23-28 troponin I3, cardiac type Homo sapiens 160-164 18721805-5 2008 Between 12 and 30 h of azide treatment, cardiomyocytes showed progressive cell death accompanied by release of intact cTnI (29 kDa), intact cTnT (39 kDa), four cTnI degradation products of 26, 20, 17 and 12 kDa, and three cTnT degradation products of 37, 27 and 14 kDa. Azides 23-28 troponin T2, cardiac type Homo sapiens 222-226 21201721-3 2008 The axial disposition of the azide group is consistent with the clean inversion of stereochemistry at C-3 under Mitsunobu conditions. Azides 29-34 complement C3 Homo sapiens 102-105 18420387-0 2008 Combined NMR and computational study for azide binding to human manganese superoxide dismutase. Azides 41-46 superoxide dismutase 2 Homo sapiens 64-94 21203059-2 2008 The Mn(III) ion is hexa-coordinated by two N and two O atoms from two phenolate ligands and two N atoms from two azide ligands. Azides 113-118 hexosaminidase subunit alpha Homo sapiens 19-23 18420387-1 2008 Human manganese superoxide dismutase (MnSOD) labeled with 3-fluorotyrosine (Tyf) was complexed with the (15)N-labeled inhibitor azide ([(15)N(3)(-)]). Azides 128-133 superoxide dismutase 2 Homo sapiens 6-36 18420387-1 2008 Human manganese superoxide dismutase (MnSOD) labeled with 3-fluorotyrosine (Tyf) was complexed with the (15)N-labeled inhibitor azide ([(15)N(3)(-)]). Azides 128-133 superoxide dismutase 2 Homo sapiens 38-43 18420387-9 2008 As a consequence the azide forms an H bond with Gln143 instead with Tyf34, in contrast to non-(19)F-labeled MnSOD, where the azide is hydrogen bonded to the hydroxy group of Tyr34. Azides 125-130 superoxide dismutase 2 Homo sapiens 108-113 18493649-5 2008 In addition, DAz-1 contains an azide chemical handle that can be selectively detected with phosphine reagents via the Staudinger ligation for identification, enrichment and visualization of modified proteins. Azides 31-36 deleted in azoospermia 1 Homo sapiens 13-18 18325999-6 2008 In concordance with these observations, ATP production in the NOR-1 silent interfering RNA (but not control)-transfected cells was resistant to (azide-mediated) inhibition of oxidative metabolism and expressed significantly higher levels of hypoxia inducible factor-1alpha. Azides 145-150 nuclear receptor subfamily 4, group A, member 3 Mus musculus 62-67 18284212-5 2008 Of the anions studied, particularly intriguing in terms of observed trends in substrate kinetics and their novel atomic compositions were the nitrite, nitrate, and azide anions, the latter of which was found to enhance the relative activity of human pancreatic alpha-amylase by nearly 5-fold. Azides 164-169 amylase alpha 2A Homo sapiens 250-274 18361486-0 2008 Model studies of azide binding to functional analogues of CcO. Azides 17-22 ryanodine receptor 1 Homo sapiens 58-61 18433119-4 2008 Intriguingly, the LMCT transition energies correlate almost linearly with the Fe(3+/2+) reduction potentials of the corresponding Fe(3+)-bound SOD species in the absence of azide, which span a range of approximately 1 V (see the preceding paper). Azides 173-178 superoxide dismutase 2 Homo sapiens 143-146 18357998-0 2008 A convenient preparation of 5-iodo-1,4-disubstituted-1,2,3-triazole: multicomponent one-pot reaction of azide and alkyne mediated by CuI-NBS. Azides 104-109 nibrin Homo sapiens 137-140 18284212-12 2008 In a completely unexpected turn of events, structural studies show that in azide-bound human pancreatic alpha-amylase, the normally resident chloride ion is retained in its binding site and an azide anion is found bound in an embedded side pocket in the substrate binding cleft. Azides 75-80 amylase alpha 2A Homo sapiens 93-117 18284212-12 2008 In a completely unexpected turn of events, structural studies show that in azide-bound human pancreatic alpha-amylase, the normally resident chloride ion is retained in its binding site and an azide anion is found bound in an embedded side pocket in the substrate binding cleft. Azides 193-204 amylase alpha 2A Homo sapiens 93-117 26620794-5 2008 The confinement of the species Cs2(N3)2 forces the azide moieties to get closer together. Azides 51-56 chorionic somatomammotropin hormone 2 Homo sapiens 31-34 18225870-2 2008 After photolysis of these four aryl azides in room temperature solutions, only one species was observed in the TR3 spectra for each azide, respectively at the probe wavelengths employed in the TR3 experiments. Azides 36-41 nuclear receptor subfamily 4 group A member 1 Homo sapiens 111-114 18225870-2 2008 After photolysis of these four aryl azides in room temperature solutions, only one species was observed in the TR3 spectra for each azide, respectively at the probe wavelengths employed in the TR3 experiments. Azides 36-41 nuclear receptor subfamily 4 group A member 1 Homo sapiens 193-196 18239831-0 2008 Assembling metals (Co II and Mn II) with pyridylcarboxylates in the presence of azide: synthesis, structural aspects and magnetic behavior of three coordination polymers. Azides 80-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-34 18198892-8 2008 The unstable HN5/N5- produced at -40 degrees C did not build up in the solution but degraded to azide ion and nitrogen gas with a short lifetime. Azides 96-101 MT-RNR2 like 5 (pseudogene) Homo sapiens 13-16 18067996-7 2008 CONCLUSIONS: Azide-induced chemical hypoxia increased glucose uptake and GLUT-4 translocation in neonatal rat cardiomyocytes through a mechanism that at least was partially mediated by AMPK activation. Azides 13-18 solute carrier family 2 member 4 Rattus norvegicus 73-79 18478709-0 2008 A highly active and reusable copper(I)-tren catalyst for the "click" 1,3-dipolar cycloaddition of azides and alkynes. Azides 98-104 doublecortin like kinase 1 Homo sapiens 61-70 17957036-10 2008 GLUT1 mRNA expression remained unchanged, whereas GLUT4 mRNA expression increased following azide treatment. Azides 92-97 solute carrier family 2 member 4 Homo sapiens 50-55 18067996-2 2008 This study aimed at investigating whether AMPK was involved in glucose transporter-4 (GLUT-4) translocation induced by azide-induced chemical hypoxia in primary cultured neonatal rat cardiomyocytes. Azides 119-124 solute carrier family 2 member 4 Rattus norvegicus 63-84 18067996-2 2008 This study aimed at investigating whether AMPK was involved in glucose transporter-4 (GLUT-4) translocation induced by azide-induced chemical hypoxia in primary cultured neonatal rat cardiomyocytes. Azides 119-124 solute carrier family 2 member 4 Rattus norvegicus 86-92 18067996-5 2008 RESULTS: Azide-induced chemical hypoxia and AICAR both increased glucose uptake and GLUT-4 translocation in cardiomyocytes, and AICAR had an additive effect on insulin action. Azides 9-14 solute carrier family 2 member 4 Rattus norvegicus 84-90 17900108-0 2007 Uncommon ferromagnetic interactions in a homometallic Co(II) chain bridged by a single end-to-end azide. Azides 98-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 17999512-2 2007 The concept is based on ion exchange and is initiated by an azide-promoted SN2-reaction at the alkyl sulfonate followed by trapping of the resulting aryl sulfonate anion with an ion-exchange resin. Azides 60-65 solute carrier family 38 member 5 Homo sapiens 75-78 17900108-2 2007 Magnetic data show that intrachain ferromagnetic couplings via the single end-to-end azide group are observed, which is an extraordinary case among the azide-bridged Co(II) systems. Azides 85-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-172 17900108-2 2007 Magnetic data show that intrachain ferromagnetic couplings via the single end-to-end azide group are observed, which is an extraordinary case among the azide-bridged Co(II) systems. Azides 152-157 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-172 17448660-1 2007 A regiochemical and stereochemical mixture of flexible linkers bearing terminal azide functionality was synthesized in two steps from squalene and was used to connect two high affinity NDP-alpha-MSH ligands or two low affinity MSH(4) ligands. Azides 80-85 mutS homolog 4 Homo sapiens 227-233 17496043-1 2007 The absorption and resonance Raman spectra and the azide binding kinetics of ferric horse heart myoglobin (Mb) and mini myoglobin (a chemically truncated form of horse heart Mb containing residues 32-139) have been compared. Azides 51-56 myoglobin Equus caballus 96-105 17496043-5 2007 Azide binds to horse heart Mb much more slowly than to sperm whale Mb. Azides 0-5 myoglobin Equus caballus 27-29 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. Azides 204-209 Rru_A1356 Rhodospirillum rubrum ATCC 11170 136-144 17828368-3 2007 Complex 1 is composed of a neutral 3D coordination framework based on unprecedented hexanuclear copper(ii) clusters which features three types of bridging modes for azide (mu-1,1, mu-1,3 and mu-1,1,3). Azides 165-170 glutathione S-transferase mu 1 Homo sapiens 172-186 17603931-3 2007 To challenge this hypothesis, we performed one-electron oxidation experiments with human centrin 2, starting from azide radicals. Azides 114-119 centrin 2 Homo sapiens 89-98 17530811-3 2007 The (PAA-Az/PAA-Alk)-coated particles were subsequently functionalized by exploiting the free alkyne click moieties present in the film upon exposure to an azide-modified rhodamine dye. Azides 156-161 ALK receptor tyrosine kinase Homo sapiens 16-19 17461574-0 2007 1D and 2D end-to-end azide-bridged cobalt(II) complexes: syntheses, crystal structures, and magnetic properties. Azides 21-26 leiomodin 1 Homo sapiens 0-9 17388412-1 2007 Steady-state and time-resolved infrared spectroscopy of the azide (N(3)-) anion has been used to characterize aqueous mixtures both with the ionic liquid (IL) 1-butyl-3-methylimidazolium tetrafluoroborate ([BMIM][BF(4)]) and with dimethyl sulfoxide (DMSO). Azides 60-65 interleukin 1 alpha Homo sapiens 141-160 17127063-7 2007 The best hCA VI inhibitors were cyanide, azide, sulfamide, and sulfamate, with inhibition constants in the range of 70-90microM. Azides 41-46 carbonic anhydrase 6 Homo sapiens 9-15 17131385-6 2007 After 24 h of exposure to azide the precursor and nuclear forms of SREBP-2 protein decreased by approximately 80% and approximately 50%, respectively. Azides 26-31 sterol regulatory element binding transcription factor 2 Rattus norvegicus 67-74 17373846-1 2007 Molecular modeling demonstrates that the first excited state of the triplet ketone (T1K) in azide 1b has a (pi,pi*) configuration with an energy that is 66 kcal/mol above its ground state and its second excited state (T2K) is 10 kcal/mol higher in energy and has a (n,pi*) configuration. Azides 92-97 TANK binding kinase 1 Homo sapiens 218-221 17373846-7 2007 Thus, T1K (pi,pi*) in azide 1b leads to energy transfer to form nitrene 2b; however, alpha-cleavage is not observed since the energy of T2K (n,pi*) is 10 kcal/mol higher in energy than T1K, and therefore, T2K is not populated. Azides 22-27 TANK binding kinase 1 Homo sapiens 205-208 17389990-1 2007 Horse spleen apoferritin, the hollow protein shell derived from ferritin, a special biological nanoparticle, can be chemoselectively modified at the lysine residues, which affords a robust scaffold for further chemical reactions including Cu(i)-catalyzed azide-alkyne cycloaddition reaction and atom transfer radical polymerization reaction. Azides 255-260 ferritin heavy chain Equus caballus 13-24 17338513-1 2007 This report describes the rapid and slow thermal decomposition of an energetically unstable polycyclic and heterocyclic azide, triazido-s-heptazine (C6N16), to produce nitrogen-rich CNx materials (x > 1.2). Azides 120-125 calnexin Homo sapiens 182-185 17257840-6 2007 The best hCA XII inhibitors were cyanide (K(I) of 1 microM) and azide (K(I) of 80 microM). Azides 64-69 carbonic anhydrase 12 Homo sapiens 9-16 17222729-0 2007 Persistent activation of nuclear factor kappa-B signaling pathway in patients with unstable angina and elevated levels of C-reactive protein evidence for a direct proinflammatory effect of azide and lipopolysaccharide-free C-reactive protein on human monocytes via nuclear factor kappa-B activation. Azides 189-194 nuclear factor kappa B subunit 1 Homo sapiens 25-47 17222729-0 2007 Persistent activation of nuclear factor kappa-B signaling pathway in patients with unstable angina and elevated levels of C-reactive protein evidence for a direct proinflammatory effect of azide and lipopolysaccharide-free C-reactive protein on human monocytes via nuclear factor kappa-B activation. Azides 189-194 C-reactive protein Homo sapiens 122-140 17222729-0 2007 Persistent activation of nuclear factor kappa-B signaling pathway in patients with unstable angina and elevated levels of C-reactive protein evidence for a direct proinflammatory effect of azide and lipopolysaccharide-free C-reactive protein on human monocytes via nuclear factor kappa-B activation. Azides 189-194 nuclear factor kappa B subunit 1 Homo sapiens 265-287 16943243-4 2007 Use of small interference RNA (siRNA) directed against AMPKalpha(1) or AMPKalpha(1) + AMPKalpha(2) (total AMPKalpha) resulted in a significant inhibition of the glucose transport response and the content of phosphorylated AMPKalpha(1) + phosphorylated AMPKalpha(2) (total p-AMPKalpha) and phosphorylated acetyl-CoA carboxylase (p-ACC) in response to azide. Azides 350-355 protein kinase AMP-activated catalytic subunit alpha 1 Rattus norvegicus 55-67 16885151-10 2007 Azide-induced Bax translocation and cytochrome c release, two critical mitochondrial events of apoptosis, were abrogated in death-resistant clones. Azides 0-5 BCL2 associated X, apoptosis regulator Homo sapiens 14-17 16885151-10 2007 Azide-induced Bax translocation and cytochrome c release, two critical mitochondrial events of apoptosis, were abrogated in death-resistant clones. Azides 0-5 cytochrome c, somatic Homo sapiens 36-48 16943243-7 2007 Incubation of cells with compound C, an inhibitor of AMPK, abrogated the glucose transport response and abolished the increase in total p-AMPK in azide-treated or hypoxia-exposed cells. Azides 146-151 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 53-57 16943243-7 2007 Incubation of cells with compound C, an inhibitor of AMPK, abrogated the glucose transport response and abolished the increase in total p-AMPK in azide-treated or hypoxia-exposed cells. Azides 146-151 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 138-142 17427165-0 2007 Cu2(OTf)2-catalyzed and microwave-controlled preparation of tetrazoles from nitriles and organic azides under mild, safe conditions. Azides 97-103 POU class 2 homeobox 2 Homo sapiens 0-9 17283953-5 2007 During azide dosage, the GAC biofilters still removed geosmin and MIB nearly unaffectedly. Azides 7-12 glutaminase Homo sapiens 25-28 16943243-4 2007 Use of small interference RNA (siRNA) directed against AMPKalpha(1) or AMPKalpha(1) + AMPKalpha(2) (total AMPKalpha) resulted in a significant inhibition of the glucose transport response and the content of phosphorylated AMPKalpha(1) + phosphorylated AMPKalpha(2) (total p-AMPKalpha) and phosphorylated acetyl-CoA carboxylase (p-ACC) in response to azide. Azides 350-355 protein kinase AMP-activated catalytic subunit alpha 1 Rattus norvegicus 71-83 16943243-4 2007 Use of small interference RNA (siRNA) directed against AMPKalpha(1) or AMPKalpha(1) + AMPKalpha(2) (total AMPKalpha) resulted in a significant inhibition of the glucose transport response and the content of phosphorylated AMPKalpha(1) + phosphorylated AMPKalpha(2) (total p-AMPKalpha) and phosphorylated acetyl-CoA carboxylase (p-ACC) in response to azide. Azides 350-355 protein kinase AMP-activated catalytic subunit alpha 1 Rattus norvegicus 71-83 16984172-5 2006 It was also demonstrated that azides can be incorporated into inhibitors of other caspases (e.g. 3, 8) and cathepsins (e.g. K, S, B), indicating the versatility of this valuable new approach to cysteine protease inhibition. Azides 30-36 caspase 1 Homo sapiens 82-90 17038762-0 2006 A disposable, screen-printed electrode for the amperometric determination of azide based on the immobilization with catalase or tyrosinase. Azides 77-82 catalase Homo sapiens 116-124 17038762-0 2006 A disposable, screen-printed electrode for the amperometric determination of azide based on the immobilization with catalase or tyrosinase. Azides 77-82 tyrosinase Homo sapiens 128-138 17038762-1 2006 A disposable, screen-printed electrode based on the immobilization of catalase or tyrosinase was developed to construct biosensors for the amperometric determination of azide. Azides 169-174 catalase Homo sapiens 70-78 17038762-1 2006 A disposable, screen-printed electrode based on the immobilization of catalase or tyrosinase was developed to construct biosensors for the amperometric determination of azide. Azides 169-174 tyrosinase Homo sapiens 82-92 17047746-0 2006 Ferromagnetic vs. antiferromagnetic coupling in bis(mu2-1,1-azido)dinickel(II) complexes with syn- and anti-conformations of the end-on azide bridges. Azides 136-141 synemin Homo sapiens 94-97 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. Azides 344-349 tyrosinase Homo sapiens 33-43 17034128-4 2006 Ab initio QM/MM results show that the reaction in the AChE gorge occurs when 3/azide and 4/acetylene are extended in a parallel orientation. Azides 79-84 acetylcholinesterase (Cartwright blood group) Homo sapiens 54-58 17034128-9 2006 All of these results, thus, imply that inside the AChE gorge, the azide group of 3 and the acetylene group of 4 always remain parallel, with the consequence that 1 is the only product. Azides 66-71 acetylcholinesterase (Cartwright blood group) Homo sapiens 50-54 16908148-0 2006 Application of azide-alkyne cycloaddition "click chemistry" for the synthesis of Grb2 SH2 domain-binding macrocycles. Azides 15-20 growth factor receptor bound protein 2 Homo sapiens 81-85 16908148-1 2006 Copper (I) promoted [3+2] Huisgen cycloaddition of azides with terminal alkynes was used to prepare triazole-containing macrocycles based on the Grb2 SH2 domain-binding motif, "Pmp-Ac(6)c-Asn", where Pmp and Ac(6)c stand for 4-phosphonomethylphenylalanine and 1-aminocyclohexanecarboxylic acid, respectively. Azides 51-57 growth factor receptor bound protein 2 Homo sapiens 145-149 16889691-3 2006 Radical scavengers, such as azide, mannitol, and ethanol, significantly inhibited the cytochrome c/H2O2 system-mediated DNA cleavage. Azides 28-33 cytochrome c, somatic Homo sapiens 86-98 16581013-6 2006 Pre-incubation of membrane vesicles with azide and Mg2+, without exogenous ADP, resulted in almost complete inhibition of the initial rate of ATPase when assayed at 10 degrees C, but had little effect at 37 degrees C. Rates of ATP synthesis following this pre-incubation were not affected at any temperature. Azides 41-46 ATPase Escherichia coli 142-148 16841919-6 2006 Soybean trypsin inhibitor was functionalized with N-(4-pentynoyloxy)succinimide to carry alkyne groups and then allowed to react with the azide-containing beads to produce an affinity sorbent for trypsin. Azides 138-143 kunitz trypsin protease inhibitor Glycine max 8-25 16752921-13 2006 Besides becoming resistant to detergent inhibition, the soluble human E-NTPDase 8 ECD displays greater activity with Ca nucleotide substrates, an increased affinity for ATP, different pH dependence, and a decreased sensitivity to azide inhibition when compared to the membrane-bound enzyme. Azides 230-235 ectonucleoside triphosphate diphosphohydrolase 8 Homo sapiens 70-81 16611641-7 2006 CDO was also rendered inactive upon complexation with the metal-binding inhibitors azide and cyanide. Azides 83-88 cysteine dioxygenase type 1 Rattus norvegicus 0-3 16603468-10 2006 Azide response amplitudes were significantly larger in the HGF-treated eyes than in the untreated eyes (p < 0.05). Azides 0-5 hepatocyte growth factor Rattus norvegicus 59-62 16519441-4 2006 Acetylenes possessing redox-active ferrocene substituents react with the azide-terminated mixed SAMs and electrochemical measurements of the ferrocene-modified SAM electrodes have been used to quantify the redox centers attached to these platforms. Azides 73-78 methionine adenosyltransferase 1A Homo sapiens 96-100 16226717-5 2005 Reductase-catalyzed deformylation is unaffected by metal ion chelators and oxygen radical scavengers, but is strongly inhibited by catalase, and the catalase-mediated inhibition is prevented by azide. Azides 194-199 catalase Homo sapiens 131-139 16408927-4 2006 The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies. Azides 36-41 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 27-35 16408927-4 2006 The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies. Azides 36-41 O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens 77-85 16226717-5 2005 Reductase-catalyzed deformylation is unaffected by metal ion chelators and oxygen radical scavengers, but is strongly inhibited by catalase, and the catalase-mediated inhibition is prevented by azide. Azides 194-199 catalase Homo sapiens 149-157 16316130-0 2005 Interaction of azide ion with hemin and cytochrome c immobilized on Au and Ag nanoparticles. Azides 15-20 cytochrome c, somatic Homo sapiens 40-52 16316130-1 2005 This paper presents a set of investigations on the binding of a metabolic inhibitor, azide with prosthetic heme group of biomolecules, hemin chloride (Hem) and cytochrome c (Cyt c) immobilized on Au and Ag nanoparticles. Azides 85-90 cytochrome c, somatic Homo sapiens 174-179 16316130-6 2005 Azide binding of Cyt c requires thermal activation due to reduced accessibility of the heme center, unlike in the case of hemin. Azides 0-5 cytochrome c, somatic Homo sapiens 17-22 16287266-1 2005 Cp*RuCl(PPh3)2 is an effective catalyst for the regioselective "fusion" of organic azides and terminal alkynes, producing 1,5-disubstituted 1,2,3-triazoles. Azides 83-89 caveolin 1 Homo sapiens 8-12 16202884-0 2005 A biosensor based on catalase for determination of highly toxic chemical azide in fruit juices. Azides 73-78 catalase Homo sapiens 21-29 16287257-3 2005 The ligated substrates included complex sugars, peptides, poly(ethylene oxide) polymers, and the iron carrier protein transferrin, with routine success even for cases that were previously resistant to azide-alkyne coupling using the conventional ligand tris(triazolyl)amine (1). Azides 201-206 transferrin Homo sapiens 118-129 16202884-1 2005 In this work, an amperometric biosensor based on catalase enzyme was developed for the determination of azide. Azides 104-109 catalase Homo sapiens 49-57 16202884-2 2005 The principle of the measurements was based on the determination of the decrease in the differentiation of oxygen level which had been caused by the inhibition of catalase in the bioactive layer of the biosensor by azide. Azides 215-220 catalase Homo sapiens 163-171 15846409-1 2005 Azide terminally functional poly(methyl methacrylate)s (Mn = 4000-6000, PDI = 1.21-1.28) have been prepared by living radical polymerization and successfully reacted with alkynes in a Huisgen cycloaddition (click) reaction in one pot using the same catalyst for both processes. Azides 0-5 peptidyl arginine deiminase 1 Homo sapiens 72-79 15802626-0 2005 C-reactive protein-induced in vitro endothelial cell activation is an artefact caused by azide and lipopolysaccharide. Azides 89-94 C-reactive protein Homo sapiens 0-18 15976313-7 2005 This study has implications for interpretation of in vitro studies using CRP preparations containing azide at equivalent or higher concentrations. Azides 101-106 C-reactive protein Homo sapiens 73-76 16024637-4 2005 Methimazole, 4-aminobenzoic acid hydrazide, or azide inhibits the reaction, suggesting that it is mediated by the cellular myeloperoxidase, an enzyme naturally present in large amounts in HL-60 cells. Azides 37-42 myeloperoxidase Homo sapiens 123-138 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. Azides 100-105 alpha/beta fold hydrolase Anoxybacillus gonensis 18-26 15683235-1 2005 The geometric and electronic structures of the six-coordinate azide adduct of oxidized manganese superoxide dismutase (Mn3+ SOD) that is formed at low temperatures, LT N3-Mn3+ SOD, has been examined in detail through a combined spectroscopic/computational approach. Azides 62-67 superoxide dismutase 1 Homo sapiens 119-127 15683235-1 2005 The geometric and electronic structures of the six-coordinate azide adduct of oxidized manganese superoxide dismutase (Mn3+ SOD) that is formed at low temperatures, LT N3-Mn3+ SOD, has been examined in detail through a combined spectroscopic/computational approach. Azides 62-67 superoxide dismutase 1 Homo sapiens 124-127 15531583-13 2005 MPO nonnitrosative oxidation of IQ with 0.3 mm NO(2)(-) at pH 5.5 was inhibited by azide, but not NADH, demonstrating differences between MPO oxidation of IQ with NO compared with NO(2)(-). Azides 83-88 myeloperoxidase Homo sapiens 0-3 15326527-2 2004 The radical precursors, trans- and cis-1-bromo-(2-isocyanatocyclopropyl)benzene and (2-bromophenyl)-3-isocyanatooxirane, were prepared from the corresponding bromophenylcyclopropane and bromophenyloxirane carboxylic acids via Curtius rearrangements of the derived azides. Azides 264-270 suppressor of cytokine signaling 1 Homo sapiens 35-40 15488471-2 2004 Acute exposure (90 min) to 5mM azide stimulated glucose transport by approximately 4.7-fold and increased the abundance of Glut1 in the non-DRM fraction of the plasma membrane by approximately 2.9-fold while the abundance of Glut1 in the DRMs was not changed. Azides 31-36 solute carrier family 2 member 1 Rattus norvegicus 123-128 15488471-2 2004 Acute exposure (90 min) to 5mM azide stimulated glucose transport by approximately 4.7-fold and increased the abundance of Glut1 in the non-DRM fraction of the plasma membrane by approximately 2.9-fold while the abundance of Glut1 in the DRMs was not changed. Azides 31-36 solute carrier family 2 member 1 Rattus norvegicus 225-230 15488471-3 2004 In parallel experiments, approximately 17 h exposure to azide further increased the rate of glucose transport over that observed at 90 min by approximately 33% and increased plasma membrane Glut1 content by approximately 3.5-fold over control. Azides 56-61 solute carrier family 2 member 1 Rattus norvegicus 190-195 15488471-5 2004 We conclude that acute exposure to azide increases Glut1 content in the non-DRM fractions, while prolonged exposure to azide increases the Glut1 content in both non-DRM and DRM fractions. Azides 35-40 solute carrier family 2 member 1 Rattus norvegicus 51-56 15488471-5 2004 We conclude that acute exposure to azide increases Glut1 content in the non-DRM fractions, while prolonged exposure to azide increases the Glut1 content in both non-DRM and DRM fractions. Azides 119-124 solute carrier family 2 member 1 Rattus norvegicus 139-144 15506782-1 2004 The reaction of azide with organotellurium(VI) halides Ph(5)TeBr and cis-(biphen)(2)TeF(2) (biphen = 2,2"-biphenyldiyl) resulted in the formation and isolation of Ph(5)TeN(3) (1) and cis-(biphen)(2)Te(N(3))(2) (2), which are the first tellurium(VI)-azide species. Azides 16-21 TEF transcription factor, PAR bZIP family member Homo sapiens 84-87 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. Azides 279-284 carbonic anhydrase 13 Mus musculus 116-124 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). Azides 153-158 carbonic anhydrase 13 Mus musculus 9-17 15389841-8 2004 For the azide-exposed native cell line, addition of the antioxidant trolox to the medium abrogated both Hsp70/Hsp40 translocation and upregulation. Azides 8-13 heat shock protein family A (Hsp70) member 4 Homo sapiens 104-109 15389841-8 2004 For the azide-exposed native cell line, addition of the antioxidant trolox to the medium abrogated both Hsp70/Hsp40 translocation and upregulation. Azides 8-13 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 110-115 15575746-3 2004 When TMSN(3) or LiN(3) are used as azide-based nucleophiles, a 1,2-syn-addition pathway is also observed. Azides 35-40 synemin Homo sapiens 67-70 15563139-2 2004 Spirodiepoxides derived from allenes by oxidation are shown to give syn disubstituted ketones and their derivatives, including ortho ester, oxazoline, azido epoxide, as well as sulfonamide-, amide-, and azide-containing hydroxy ketones. Azides 203-208 synemin Homo sapiens 68-71 15257594-10 2004 The reactivity of these [PhBP3]NiIL and [PhBPiPr3]NiIL complexes with respect to oxidative group transfer reactions from organic azides and diazoalkanes is discussed. Azides 129-135 PHB1 pseudogene 3 Homo sapiens 25-30 15278148-1 2004 Ligandless palladium-catalyzed Suzuki-Miyaura coupling converted an inert p-bromobenzyl ether to a DDQ-labile p-(3,4-dimethoxyphenyl) benzyl ether in the presence of azide functionality and this strategy serves as a key step for the convergent synthesis of a fully lipidated malaria GPI disaccharide. Azides 166-171 glucose-6-phosphate isomerase Homo sapiens 283-286 15203186-10 2004 MPO-mediated lipid oxidation was inhibited by heme poisons (azide, cyanide) and catalase. Azides 60-65 myeloperoxidase Homo sapiens 0-3 15469714-5 2004 Radical scavengers, azide, N-acetylcysteine, and catalase inhibited the oxidized catecholamine-mediated Cu,Zn-SOD aggregation. Azides 20-25 superoxide dismutase 1 Homo sapiens 110-113 15134448-8 2004 Azide binding to PHM is used as a spectroscopic and electronic structure analogue to OOH(-) binding to provide a starting point for developing a geometric and electronic structural model for the putative Cu(II)(M)-OOH intermediate in the H-atom abstraction reaction of PHM. Azides 0-5 peptidylglycine alpha-amidating monooxygenase Homo sapiens 17-20 15039448-7 2004 A thiol-blocking reagent, N-ethylmaleimide, as well as myeloperoxidase inhibitors (succinyl acetone and azide), blocked formation of fluorescent acridine-piperidine. Azides 104-109 myeloperoxidase Homo sapiens 55-70 15134448-8 2004 Azide binding to PHM is used as a spectroscopic and electronic structure analogue to OOH(-) binding to provide a starting point for developing a geometric and electronic structural model for the putative Cu(II)(M)-OOH intermediate in the H-atom abstraction reaction of PHM. Azides 0-5 peptidylglycine alpha-amidating monooxygenase Homo sapiens 269-272 15123248-2 2004 Recently, we introduced a tag-free strategy for activity-based protein profiling (ABPP) that utilizes the copper(I)-catalyzed azide-alkyne cycloaddition reaction ("click chemistry") to analyze the functional state of enzymes in living cells and organisms. Azides 126-131 amyloid beta precursor protein Homo sapiens 82-86 15047532-3 2004 Conjugation experiments were done with azide-resistant E. coli J53 as the recipient and selection with azide and sulfonamide, a resistance frequently linked to qnr. Azides 103-108 Qnr Escherichia coli 160-163 14611231-1 2003 A novel end-on azide-bridged homospin 1D chain, Co(bt)(N3)2 (1) (bt = 2,2"-bithiazoline), is constructed by sharing edges of Co(II) distorted octahedrons to form a helix, which shows magnetic hysteresis with steps and slow relaxation below 5-6 K, typical of single-chain magnet behavior. Azides 15-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-130 14759599-0 2004 Azide binding to yeast cytochrome c peroxidase and horse metmyoglobin: comparative thermodynamic investigation using isothermal titration calorimetry. Azides 0-5 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 23-46 14759599-5 2004 CcP and Mb differ significantly in their reactivity toward the azide anion, N3-. Azides 63-74 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 0-3 14757816-2 2004 However, considerable rate acceleration is observed when this reaction occurs inside the active center gorge of acetylcholinesterase (AChE) between certain azide and acetylene reactants, attached via methylene chains to specific inhibitor moieties selective for the active center and peripheral site of the enzyme. Azides 156-161 acetylcholinesterase Mus musculus 112-132 14757816-2 2004 However, considerable rate acceleration is observed when this reaction occurs inside the active center gorge of acetylcholinesterase (AChE) between certain azide and acetylene reactants, attached via methylene chains to specific inhibitor moieties selective for the active center and peripheral site of the enzyme. Azides 156-161 acetylcholinesterase Mus musculus 134-138 14696937-1 2003 Carbon disulfide (CS2) was determined at trace levels by its induction effect on the reaction of triiodide with azide in acidic media. Azides 112-117 chorionic somatomammotropin hormone 2 Homo sapiens 18-21 12938025-6 2003 Azide effect on PS2 expression was completely inhibited by the addition of an antioxidant suggesting that the imbalance of the cellular redox homeostasis modulates the expression of this gene. Azides 0-5 presenilin 2 Homo sapiens 16-19 14578187-10 2003 Stimulation of glycolysis by azide inhibition of oxidative phosphorylation was impaired by 44% in GT1(+/-), with impaired up-regulation of GLUT1 protein. Azides 29-34 beta-1,4-galactosyltransferase 1 Homo sapiens 98-101 12816487-3 2003 An exclusive selectivity in the reduction of anomeric azides is observed, while the C-2 and C-6 azides are left untouched. Azides 96-102 complement C6 Homo sapiens 92-95 12971747-0 2003 The first azide(mu1,1)-bridged binuclear cobalt(II)-imino nitroxide complex with ferromagnetic behavior. Azides 10-15 glutathione S-transferase mu 1 Homo sapiens 16-21 12971747-1 2003 The first azide(mu1,1)-bridged binuclear cobalt(II) complex with a chelated imino nitroxide radical, [Co2(immepy)2(N3)(4)].2EtOH, was structurally and magnetically characterized, where immepy = 4,4,5,5-tetramethyl-2-(6"-methyl-2"-pyridyl) imidazoline-1-oxyl. Azides 10-15 glutathione S-transferase mu 1 Homo sapiens 16-21 12874386-3 2003 We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety. Azides 308-313 O-GlcNAcase Homo sapiens 173-184 12686514-1 2003 We have previously shown that the acute stimulation of glucose transport in Clone 9 cells in response to azide is mediated by activation of Glut1 and that stomatin, a Glut1-binding protein, appears to inhibit Glut1 function. Azides 105-110 solute carrier family 2 member 1 Rattus norvegicus 140-145 12686514-3 2003 Acute exposure to azide resulted in 40 and 50% decreases in the content of Glut1 in DRMs of Clone 9 cells and 3T3-L1 fibroblasts, respectively, whereas the distribution of stomatin and caveolin-1 in Clone 9 cells remained unchanged. Azides 18-23 solute carrier family 2 member 1 Rattus norvegicus 75-80 12686514-3 2003 Acute exposure to azide resulted in 40 and 50% decreases in the content of Glut1 in DRMs of Clone 9 cells and 3T3-L1 fibroblasts, respectively, whereas the distribution of stomatin and caveolin-1 in Clone 9 cells remained unchanged. Azides 18-23 caveolin 1 Rattus norvegicus 185-195 12686514-4 2003 In addition, treatment of Clone 9 cells with azide resulted in a approximately 50% decrease in the content of Glut1 in the DRM fraction of plasma membranes. Azides 45-50 solute carrier family 2 member 1 Rattus norvegicus 110-115 12686514-5 2003 We conclude that 1) a significant fraction of Glut1 is localized in DRMs, and 2) treatment of cells with azide results in a partial redistribution of Glut1 out of the DRM fraction. Azides 105-110 solute carrier family 2 member 1 Rattus norvegicus 46-51 12686514-5 2003 We conclude that 1) a significant fraction of Glut1 is localized in DRMs, and 2) treatment of cells with azide results in a partial redistribution of Glut1 out of the DRM fraction. Azides 105-110 solute carrier family 2 member 1 Rattus norvegicus 150-155 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. Azides 221-226 catalase Homo sapiens 15-23 12767819-4 2003 In recombinant murine Mb, azide affinities are only slightly dependent on the Cys(E9) oxidation state. Azides 26-31 myoglobin Mus musculus 22-24 12762694-1 2003 [reaction: see text] The construction of multivalent neoglycoconjugates is efficiently achieved by the regiospecific catalytic cycloaddition of alkynes and azides using the organic-soluble copper complexes (Ph(3)P)(3).CuBr and (EtO)(3)P.CuI. Azides 156-162 RUNX1 partner transcriptional co-repressor 1 Homo sapiens 228-231 12820649-5 2003 Daf-21 mutants also acquire sodium azide-induced thermotolerance, whereas 3 non-Hsp, constitutive dauer-forming mutants exhibited a variable response to azide exposure. Azides 35-40 Heat shock protein 90 Caenorhabditis elegans 0-6 12627943-7 2003 This is supported by comparison of the crystal structure of H30V MnSOD with that of azide bound to Mn(III)SOD from Thermus thermophilus and by visible absorption spectra showing that azide binding to the metal in H30V Mn(III)SOD is abolished. Azides 84-89 superoxide dismutase 2 Homo sapiens 65-70 12627943-7 2003 This is supported by comparison of the crystal structure of H30V MnSOD with that of azide bound to Mn(III)SOD from Thermus thermophilus and by visible absorption spectra showing that azide binding to the metal in H30V Mn(III)SOD is abolished. Azides 183-188 superoxide dismutase 2 Homo sapiens 65-70 12717622-5 2003 Coincubation with either catalase, with the myeloperoxidase inhibitor azide, or with the hypochlorous acid scavenger methionine almost completely prevented activation, but not the release, of MMP-9, in supernatants of human PMNs stimulated with hiR6. Azides 70-75 myeloperoxidase Homo sapiens 44-59 12683828-2 2003 The uranium(III) complex reacts with organic azides to yield uranium(IV) azido as well as uranium(V) imido complexes, [((ArO)(3)tacn)U(IV)(N(3))] and [((ArO)(3)tacn)U(V)(NSi(CH(3))(3))]. Azides 45-51 cytochrome P450 family 19 subfamily A member 1 Homo sapiens 121-124 12683828-2 2003 The uranium(III) complex reacts with organic azides to yield uranium(IV) azido as well as uranium(V) imido complexes, [((ArO)(3)tacn)U(IV)(N(3))] and [((ArO)(3)tacn)U(V)(NSi(CH(3))(3))]. Azides 45-51 cytochrome P450 family 19 subfamily A member 1 Homo sapiens 153-156 12446267-3 2003 The scavenging activity was inhibited 60 +/- 4% by azide (an inhibitor of heme-containing peroxidases and catalase) and 42 +/- 9% by dapsone (an inhibitor of lactoperoxidase). Azides 51-56 catalase Homo sapiens 106-114 12693212-12 2003 The bridging azide complex [Ru2(trpy)2(6,6"-Me2dppz)mu-N3](PF6)2 (10b) is formed by reaction of 6b with (CH3)3-SiN3. Azides 13-18 sperm associated antigen 17 Homo sapiens 59-62 12504251-0 2003 NMR study of the conformational transition of cytochrome c upon the displacement of Met80 by exogenous ligand: structural and magnetic characterization of azidoferricytochrome c. As the exogenous ligand-cytochrome c complexes were purported to represent models for the unfolding intermediate of cytochrome c, NMR spectroscopy has been utilized to study the azide adduct of horse heart cytochrome c. Azides 357-362 cytochrome c, somatic Equus caballus 46-58 12485374-8 2003 Con A-primed but not resident macrophages have a significant content of myeloperoxidase (MPO) and inhibition of MPO by azide completely blocked chemiluminescence and AFMK production. Azides 119-124 myeloperoxidase Mus musculus 112-115