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1,1-bis(4-hydroxyphenyl)ethane
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i.e.bisphenol E, 15% inhibition at 0.0125 mM
1,3-diphenylpropane
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8% inhibition at 0.0125 mM
12-O-Tetradecanoylphorbol 13-acetate
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binds to and moderately inhibits PDI
16F16
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irreversible inhibition
2',3,3',4',5'-pentachlorobiphenyl
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strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity
2',3,3',5,5',6'-hexachlorobiphenyl
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strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity
2,2-bis(4-hydroxyphenyl)propane
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i.e. bisphenol A, 30% inhibition at 0.0125 mM
2,4-dinitrochlorobenzene
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2-(2-carboxy-4-nitro-phenyl) disulfonyl-5-nitrobenzoic acid
i.e. NSC517871. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
2-nitro-5-sulfo-sulfonyl-benzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
2-Nitro-5-thiocyanobenzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
2-[[4-(cyclopropanecarbonyl)piperazin-1-yl]methyl]-1,2-benzothiazol-3(2H)-one
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potent, reversible inhibition
3,3',5-triiodo-L-thyronine
3,3',5-triiodothyronine
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4,4'-diisothiocyano-2,2'-stilbene disulfonic acid
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considerably more effective after preincubation with DTT
4,4'-methylenebisphenol
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12% inhibition at 0.0125 mM
4-(6-methylimidazo[1,2-a]pyridin-2-yl)benzene-1,2-diol
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4-alpha-cumylphenol
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18% inhibition at 0.0125 mM
4-amino-phenylarsine oxide
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0.0058 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
4-chloromercuribenzoic acid
4-hydroxy-2-nonenal
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44% inhibition at 0.03 mM
5,5'-dithiobis(2-nitrobenzoic acid)
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0.0049 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
5-(3-carboxy-4-nitro-phenyl) sulfonyl-2-nitrobenzoic acid
i.e. NSC695265. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
8-azido-ATP
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for the ATPase activity, binds at the same site as ATP
acrolein
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79% inhibition at 0.03 mM
anti-PDI Fab fragments
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-
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Ca2+
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1 mM, 40% inhibition
Diazobenzene sulfonic acid
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considerably more effective after preincubation with DTT
Dithionitrobenzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
dithiothreitol
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treatment decreases the content of 52 kDa isoform by half
E-64
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0.01 mM, 11% inhibition after treatment with 0.01 mM DTT. No inhibition without DTT
ethyl N-[[[(cyanocarbonyl)(2,4-dimethoxyphenyl)amino]thiophen-2-yl]acetyl]glycinate
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genistein
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suppresses binding of proinsulin to PDI, inhibits 66% of PDIs chaperone activity
gentamycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
kanamycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
MA3 018
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inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
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MA3 019
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inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
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methyl-methanethiosulfonate
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abolishes PDI oxidoreductase but not chaperone activity
Mg2+
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1 mM, 20% inhibition
N-acetylated-triiodothyronine
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0.07 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
N-Iodoacetyl-N'-(5-sulfo)-1-naphthyl-diaminoethane
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incubation after pretreatment with DTT or GSH
N-[2-methyl-2-(morpholin-4-yl)propyl]-1,2-benzothiazol-3-amine
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NEM
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incubation after pretreatment with DTT or GSH
neomycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
nitazoxanide
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a broad-spectrum anti-parasitic drug
nitazoxanide thiazolide derivatives
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PDI is inhibited by those thiazolides that also affected parasite proliferation
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paromomycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
peptides
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study of the inhibition of enzyme catalyzed reduction of insulin by GSH by peptides of various length and amino acid composition
phenyl vinyl sulfonate
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Phenylarsine oxide
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complete inhibition at 0.01-0.1 mM in vivo
quercetin 3-rutinoside
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S-nitrosocysteine
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S-nitrosates endogenous or overexpressed PDI in HEK-293T cells
sisomycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
streptomycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
tert-2-hexenal
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32% inhibition at 1 mM
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thionitrobenzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
tizoxanide
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deacetylated metabolite of nitazoxanide
Vancomycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
vincristine
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inhibits chaperone activity but not isomerase activity of both isoforms PDI and P5 in vitro. A 100:1 molar ratio of vincristine to enzyme is sufficient to almost completely inhibit chaperone activity
zinc bacitracin
specific inhibition; specific inhibition; specific inhibition
Zn2+
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1 mM, 70% inhibition
3,3',5-triiodo-L-thyronine
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and analogs
3,3',5-triiodo-L-thyronine
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inhibits PDI isomerase activity
3,3',5-triiodo-L-thyronine
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inhibits PDI isomerase activity
3,3',5-triiodo-L-thyronine
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30% inhibition at 0.0125 mM
3,3',5-triiodo-L-thyronine
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inhibits PDI isomerase activity
3,4-dichlorophenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
3,4-dichlorophenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
3,4-dichlorophenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-chloromercuribenzoic acid
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4-chloromercuribenzoic acid
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4-nonylphenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-nonylphenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-nonylphenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
bacitracin
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bacitracin
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commercial bacitracin consists of 65% bacitracin A and B
bacitracin
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a PDI-specific inhibitor
bacitracin
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inhibition of protein disulfide isomerase results in enhanced stress response and apoptosis
bacitracin
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inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
bacitracin
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a PDI-specific inhibitor
bacitracin
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full inhibition of reductase activity at 0.2 mM
bacitracin
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infusion of blood vessels inhibits platelet thrombus formation and fibrin generation
bacitracin A
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bisphenol A
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i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview. Inhibits also PDI family members ERp57 and ERp72
bisphenol A
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i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview
bisphenol A
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i.e. 2,2-bis-(4-hydroxyphenyl) propane, BPA, binds to the enzyme and inhibits its enzymatic and hormone-binding activities
bisphenol A
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halogenated derivatives of bisphenol A as well as bisphenol A itself bind to PDI and thereby suppress the oxidative refolding of reduced RNaseA by PDI
bisphenol A
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i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview
Cd2+
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iodoacetamide
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iodoacetamide
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pH-dependent inactivation
iodoacetamide
alkylation of PDIp by iodoacetamide fully abolishes its enzymatic activity while it still retains most of its chaperone activity
iodoacetamide
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incubation after pretreatment with DTT or GSH
iodoacetate
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iodoacetate
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inactivation by alkylation follows pseudo-first-order kinetics
iodoacetate
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1 mM, almost complete inhibition after reduction with 0.01 mM DTT. No inhibition in absence of DTT
iodoacetate
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inactivation by alkylation follows pseudo-first-order kinetics
N-ethylmaleimide
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pH-independent inactivation within the range of pH 6.3-7.0
N-ethylmaleimide
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abolishes PDI oxidoreductase but not chaperone activity
Pentachlorophenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
Pentachlorophenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
Pentachlorophenol
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inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
quercetin-3-rutinoside
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quercetin-3-rutinoside
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ribostamycin
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aminoglycoside antibiotic, inhibits the chaperone activity of PDI, isomerase activity is not inhibited
ribostamycin
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analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
tetrabromobisphenyl A
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TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrabromobisphenyl A
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TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrabromobisphenyl A
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TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrachlorobisphenyl A
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TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrachlorobisphenyl A
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TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrachlorobisphenyl A
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TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
additional information
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in presence of light, the level of protein disulfide isomerase protein decreases by 80%
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additional information
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malonaldehyde bis(diethyl acetal) is a poor inhibitor, pH-dependency of inhibition by alkylating inhibitors and SH-reagents
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additional information
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pressure conditions at 400 MPa decrease the enzyme isomerase activity
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additional information
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both GmPDIL-3a and GmPDIL-3b are resistant to protease treatment in the absence of detergent, and are degraded when detergent is added
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additional information
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in absence of DTT, the enzyme, at a concentration above 0.001 mM, inhibits reactivation of creatinine kinase involving Cys36 and Cys295 of PDI
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additional information
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inhibition by PDI-specific antibodiy RL90
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additional information
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functional inhibition of protein disulfide isomerase by S-nitrosylation
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additional information
no inhibition of PDI oxido-reductase activity with di(o-aminobenzyl)-labeled oxidized glutathione by DELTA-somatostatin
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additional information
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no inhibition of PDI oxido-reductase activity with di(o-aminobenzyl)-labeled oxidized glutathione by DELTA-somatostatin
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additional information
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although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords
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additional information
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ribostamycin has very slight inhibitory effect on protein disulfide isomerase chaperone activity and no effect on both reductase and isomerase activities
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additional information
no inhibition of CxPR2 activity by treatment with cysteine and serine protease inhibitors E-64 and DCI
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additional information
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although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords
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additional information
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CxRP2 activity is partially depleted by immobilized RNK-16 granule proteins, no inhibition of CxPR2 activity by treatment with cysteine and serine protease inhibitors E-64 and DCI
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additional information
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no effects of nonhydroxylated biphenyls on 3,3',5-triiodo-L-thyronine binding
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additional information
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although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords
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