Cysteine-based redox switches in enzymes - Wikidata - awgldk - TriplyDB

Cysteine-based redox switches in enzymes

Cysteine-based redox switches in enzymes

http://www.wikidata.org/entity/Q34722134

about

NPGPx (GPx7): a novel oxidative stress sensor/transmitter with multiple roles in redox homeostasis Relationship between Oxidative Stress, Circadian Rhythms, and AMD An unexplored role for Peroxiredoxin in exercise-induced redox signalling?The basics of thiols and cysteines in redox biology and chemistry Diabetes and Alzheimer disease, two overlapping pathologies with the same background: oxidative stress Targeting the redox balance in inflammatory skin conditions Thiol-based redox signaling in the nitrogen-fixing symbiosis A Glutathione-Dependent Detoxification System Is Required for Formaldehyde Resistance and Optimal Survival of Neisseria meningitidis in Biofilms Structural Snapshots of Yeast Alkyl Hydroperoxide Reductase Ahp1 Peroxiredoxin Reveal a Novel Two-cysteine Mechanism of Electron Transfer to Eliminate Reactive Oxygen Species Staphylococcus aureus CymR Is a New Thiol-based Oxidation-sensing Regulator of Stress Resistance and Oxidative Response The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin Therapeutic Strategies for Oxidative Stress-Related Cardiovascular Diseases: Removal of Excess Reactive Oxygen Species in Adult Stem Cells Redox-based regulation of apoptosis: S-glutathionylation as a regulatory mechanism to control cell death Zinc-binding cysteines: diverse functions and structural motifs.Prediction of redox-sensitive cysteines using sequential distance and other sequence-based features.Positive modulation of the α9α10 nicotinic cholinergic receptor by ascorbic acid.Bicarbonate Induced Redox Proteome Changes in Arabidopsis Suspension Cells.Exercise and Glycemic Control: Focus on Redox Homeostasis and Redox-Sensitive Protein Signaling.Thiol-based redox switches Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans.Caloric restriction and the aging process: a critique (Homo)glutathione deficiency impairs root-knot nematode development in Medicago truncatula Oxidative modification of proteins: an emerging mechanism of cell signaling.Thiol/Disulfide redox switches in the regulation of heme binding to proteins.The redoxome: Proteomic analysis of cellular redox networks.Biosynthetic and iron metabolism is regulated by thiol proteome changes dependent on glutaredoxin-2 and mitochondrial peroxiredoxin-1 in Saccharomyces cerevisiae.Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Mechanism-based proteomic screening identifies targets of thioredoxin-like proteins Overview of peroxiredoxins in oxidant defense and redox regulation.Redox regulation of protein kinases.Redox proteomics changes in the fungal pathogen Trichosporon asahii on arsenic exposure: identification of protein responses to metal-induced oxidative stress in an environmentally-sampled isolate The redox stress hypothesis of aging Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay Structural and Mechanistic Insights into the Pseudomonas fluorescens 2-Nitrobenzoate 2-Nitroreductase NbaA Selective Sensitization of Zinc Finger Protein Oxidation by Reactive Oxygen Species through Arsenic Binding.Neutral sphingomyelinase-2 is a redox sensitive enzyme: role of catalytic cysteine residues in regulation of enzymatic activity through changes in oligomeric state.Peroxiredoxins in parasites.S-glutathionylation of cysteine 99 in the APE1 protein impairs abasic endonuclease activity.Quorum-sensing agr mediates bacterial oxidation response via an intramolecular disulfide redox switch in the response regulator AgrA.The Redox Code.

P2860

Q26749241-DD161FAD-AA90-4216-B3FC-BFFD37DCA28D Q26765278-831F848B-7298-4D50-AF5D-2B43FC8E4910 Q26770037-05889F81-9B0C-44C1-8DA5-A61C87BAD8BC Q26991843-770AFDEF-C780-4E59-AF9E-DF390F5F5B5F Q27022552-AF292206-3452-497B-95B4-85D7E811B549 Q27023252-3200961A-17CA-47A1-9840-9A6D55FB8040 Q27024401-F8155E7E-E4FE-47E6-898C-4902D57EDFC7 Q27671818-7CD1CAFE-6DDA-4BE5-8D0F-F3251B081C26 Q27678313-2A164967-9F8F-4548-BC85-0BB3A01960CF Q27678878-02BDC3C0-DAB6-4DE9-BB40-5FF025D9C074 Q27683602-4AB53B33-7054-4739-996A-8B5A97A9B143 Q28077974-E5371E7A-C757-445D-BF62-FAFDC82815DE Q28397611-C7F39292-B297-4258-AF13-CA73BCDE60B1 Q30364031-C38019C3-A05C-4AE0-A00E-2BAD02004CD9 Q30392145-21458481-A910-4F7B-BB2F-41C6009B0FBB Q30443495-3B32F5AB-2E50-4A74-8A5D-0C7CBD206520 Q31160807-9C1FA431-DB73-4055-B741-FE250E9266D1 Q33639120-4E6C924F-A283-4AFA-98D6-2A5E0177E493 Q33762400-EE5DF46C-AD09-4787-8570-11A5B051B301 Q33862472-4261577F-C653-4817-AAB0-4178887EFD8E Q33954183-F0E2C64C-0AAF-4C90-A35E-BB1CF89205C5 Q34126316-A65F38D0-1793-457E-AD6F-E565378ED1D2 Q34304903-02D206A0-9CA2-4CD5-A9E0-E77004DE268A Q34589250-E4976251-9E06-4450-BD55-0AE998BFA0CA Q34725196-C632A77A-877A-499A-B4DC-604DCB2D9D63 Q34869103-8A83FC74-A544-408D-9A15-4E588805E14F Q35001796-CA0C1D09-A2F0-41FB-B5C8-DA7E038F1DF9 Q35126677-0AD4C033-8AED-4A72-85EF-DA55FB730D05 Q35165680-617EDA9C-F874-4177-A679-753F0CFDA24F Q35174581-1288E824-3D9F-4E71-B422-F040CE0DA014 Q35213192-152ACF09-C2F6-4DE0-BE1C-64379D3DC403 Q35705418-7A6D03AF-5782-4AA7-ADD5-7E3FB7F3F1C6 Q35751684-580A21F9-9472-41AA-9E3A-CB4EAA20DDEE Q35829403-4B860444-DBC5-4F38-8417-A37E19DC3F40 Q35883788-C8F86CE1-1389-4EB0-9D2F-E357F2592289 Q35921118-4C71787F-2089-4091-AEB2-55274AAAC431 Q36026850-D11E23F2-C371-44E5-87AC-A2CC20E571A9 Q36027216-298C2C4C-EC8B-453B-8ADB-8FB1C0DB59FE Q36061607-1101B925-767D-4BB9-BDA5-B14FCDE4429C Q36086638-613EC0F9-2308-4961-8C80-5033515D978A

P2860

Cysteine-based redox switches in enzymes

http://www.wikidata.org/entity/Q34722134

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Cysteine-based redox switches in enzymes

@ast

Cysteine-based redox switches in enzymes

@en

Cysteine-based redox switches in enzymes

@nl

type

label

Cysteine-based redox switches in enzymes

@ast

Cysteine-based redox switches in enzymes

@en

Cysteine-based redox switches in enzymes

@nl

prefLabel

Cysteine-based redox switches in enzymes

@ast

Cysteine-based redox switches in enzymes

@en

Cysteine-based redox switches in enzymes

@nl

P1433

Q34722134-50ACD0B6-9884-44FF-9F74-8A4161225287

P1476

Q34722134-93C27D1D-0059-4397-9BA6-C93C6EE01E18

P2093

Q34722134-19BB14D9-8F2D-400A-90E4-C2B2B41A5505

Q34722134-4B049A7B-16FF-4FBC-9E5E-3928E5350B34

Q34722134-542AA300-3EA1-4A5F-BD91-C3E2C5C69C0A

P2860

Q34722134-016A54B3-CFD2-4F83-B701-5DA478C01857

Q34722134-0201CF70-0843-4616-ABC5-1AFCB946F0A9

Q34722134-05748B3C-BB1D-49F5-8603-CDEA4FB501C2

Q34722134-075A875C-1BB8-45D6-AF15-C7F60013690D

Q34722134-09FDBEF8-4359-42D6-97C2-DD9C66B34185

Q34722134-0D43EB13-A512-4C99-A2F6-8BF249B9C19F

Q34722134-0ED61DDF-C7B9-4A27-B1C7-CB39157552DD

Q34722134-0F9F0B52-9663-446C-A70C-F92C08F99F66

Q34722134-173DE445-0FE0-497D-8CD6-389A0EC47F43

Q34722134-187E666D-633A-4C44-B204-858F41BF1C79

P304

Q34722134-2844BE5B-DFE3-4E16-8BB7-D834A8DC1266

P31

Q34722134-067DF644-048B-4F0C-B535-38B26DB62750

P356

Q34722134-809AB283-5BE0-468D-94D5-3599ECD15AFB

P433

Q34722134-927CB762-DD9A-4EC0-B06C-B3D494BFB8D8

P478

Q34722134-2A72C5C7-DFBF-44DD-9F72-2138A8ECB5C6

P577

Q34722134-96A70DE9-BD88-41AD-AFE5-E392B7042E56

P5875

Q34722134-D201C6B4-0811-45C1-8A31-BC22C5567604

P698

Q34722134-99DB89E7-96B0-4E62-B9A0-AED3DFD13A5F

P932

Q34722134-C6FEFE4D-55AA-4021-A130-3285DB038B07

P356

P1433

Antioxidants & Redox Signaling

P1476

Cysteine-based redox switches in enzymes

@en

P2093

Chananat Klomsiri

http://www.w3.org/2001/XMLSchema#string

Leslie B Poole

http://www.w3.org/2001/XMLSchema#string

P Andrew Karplus

http://www.w3.org/2001/XMLSchema#string

P2860

Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site

HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation

Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin

Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

Cysteine p K a Values for the Bacterial Peroxiredoxin AhpC † ‡

Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function.

Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2

Structure, mechanism and regulation of peroxiredoxins

Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid

Protein tyrosine phosphatases: mechanisms of catalysis and regulation

P304

1065-1077

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1089/ARS.2010.3376

http://www.w3.org/2001/XMLSchema#string

P433

6

http://www.w3.org/2001/XMLSchema#string

P478

14

http://www.w3.org/2001/XMLSchema#string

P577

2010-09-17T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

46034202

http://www.w3.org/2001/XMLSchema#string

P698

20799881

http://www.w3.org/2001/XMLSchema#string

P932

3064533

http://www.w3.org/2001/XMLSchema#string