Methionine in proteins defends against oxidative stress. - Wikidata - wikimedia - TriplyDB

Methionine in proteins defends against oxidative stress.

Methionine in proteins defends against oxidative stress.

http://www.wikidata.org/entity/Q37072433

about

The sRNA RyhB regulates the synthesis of the Escherichia coli methionine sulfoxide reductase MsrB but not MsrA The Impact of Non-Enzymatic Reactions and Enzyme Promiscuity on Cellular Metabolism during (Oxidative) Stress Conditions The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions Methionine oxidation and reduction in proteins Reducing systems protecting the bacterial cell envelope from oxidative damage Structural basis for the phototoxicity of the fluorescent protein KillerRed NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: insight into its biological role Characterization and Solution Structure of Mouse Myristoylated Methionine Sulfoxide Reductase A 1.2 Å resolution crystal structure of Escherichia coli WrbA holoprotein Glutathione redox control of asthma: from molecular mechanisms to therapeutic opportunities Adaptation in Bacillus cereus: From Stress to Disease Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A Role of cysteines in the stability and DNA-binding activity of the hypochlorite-specific transcription factor HypT Methionine mutations of outer membrane protein X influence structural stability and beta-barrel unfolding Dual sites of protein initiation control the localization and myristoylation of methionine sulfoxide reductase A High hydrostatic pressure activates gene expression that leads to ethanol production enhancement in a Saccharomyces cerevisiae distillery strain Genome-wide transcriptomic responses of a human isolate of Lactobacillus plantarum exposed to p-coumaric acid stress.Lysine biotinylation and methionine oxidation in the heat shock protein HSP60 synergize in the elimination of reactive oxygen species in human cell cultures.Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.High hydrostatic pressure activates transcription factors involved in Saccharomyces cerevisiae stress tolerance.Abiotic methanogenesis from organosulphur compounds under ambient conditions.Quantitative Evaluation of the Compatibility Effects of Huangqin Decoction on the Treatment of Irinotecan-Induced Gastrointestinal Toxicity Using Untargeted Metabolomics Metabolomic profiling in a Hedgehog Interacting Protein (Hhip) murine model of chronic obstructive pulmonary disease.Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage.Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detection Adaptive translation as a mechanism of stress response and adaptation.Deciphering nitric oxide stress in bacteria with quantitative modeling.Mitochondrially encoded methionine is inversely related to longevity in mammals.Promiscuous methionyl-tRNA synthetase mediates adaptive mistranslation to protect cells against oxidative stress.Chemical probes for analysis of carbonylated proteins: a review.Mistranslation of the genetic code.Convergent signaling pathways--interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation Synergistic roles of Helicobacter pylori methionine sulfoxide reductase and GroEL in repairing oxidant-damaged catalase.Identification of crucial amino acids of bacterial Peptide deformylases affecting enzymatic activity in response to oxidative stress Methionine sulfoxide reductases protect against oxidative stress in Staphylococcus aureus encountering exogenous oxidants and human neutrophils.RNA binding targets aminoacyl-tRNA synthetases to translating ribosomes.Methionine sulfoxide reductase A is a stereospecific methionine oxidase.Methionine sulfoxide reductase A negatively controls microglia-mediated neuroinflammation via inhibiting ROS/MAPKs/NF-κB signaling pathways through a catalytic antioxidant function Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2 Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury.

P2860

Q21133532-B3691ACB-3BE3-44D0-9E10-0607EDA97468 Q26785889-6E413A29-116F-45A3-9EE4-6118FBB8FF16 Q26864476-B23C50A2-23C9-4B36-B0B3-CDB9E465A6F8 Q26996948-DDF96745-2D16-4741-BF33-5849D238EFF8 Q27015968-7CA1E443-7FF9-4F1A-AE2C-4A0610BCB221 Q27656817-0D526582-EF0B-4D18-93F6-F40231C081D8 Q27664111-1A6414C0-42EE-4353-A3BC-FDCBE8B47A82 Q27679469-6B723E9E-FFE7-42D0-97B7-762F0F199B23 Q27685448-8A642D95-0809-4E1A-8C74-B7014FA11597 Q27694579-B437F67C-F82A-43B5-B8BD-906C8E126498 Q28079646-7B991EA7-57A9-4D8C-8EB0-2B813CF54260 Q28250197-E2CB4B58-E8AF-40D4-BAE9-138BD3F42B17 Q28534166-9756193C-1877-45F6-BD42-496A4E70E67B Q28535036-DDDBF4DA-C875-4C8E-877D-9757B2FCEF4A Q28591385-1A64D96D-A3B4-43BA-990B-6B6866D47E7E Q28603591-48F51183-717E-47F4-98F5-1039F5B52781 Q30223975-2744EC9E-C0B9-4708-9103-2C4E95DC8022 Q30359623-7E903746-522F-4945-8DCF-F520ED68B862 Q33403195-83B370B8-A0D8-4632-994B-CB1CD24624D9 Q33456116-CAFCEFCF-41B8-49A1-B89D-D2F27EB5AB6E Q33462001-FF986E6B-886B-4E30-B88E-C2F3B1CFD6DF Q33586138-A7AE19D9-C268-4B67-B76B-B387DE97B4D3 Q33746937-0487E163-4A68-4C64-A720-EDBCC19CF7C0 Q33760122-12C8398C-74D4-40E6-997D-24C80FC13D96 Q33767975-99A18FD5-F79A-445A-B3D9-2AF80A1A0087 Q33944973-FEB7B1CE-1911-4D20-A3E3-8F19F4C5292C Q34033314-5E296091-74AF-4424-B142-D8A9D891E842 Q34151866-A6526DD1-2DB9-48C9-A037-C606CDF14719 Q34264532-54C1827C-1C8A-48FF-94C0-A04AF29EF56E Q34372674-C887FF72-B2F9-4D64-91B4-DFC00E492469 Q34438631-34D2F703-1C03-4610-9815-A98AE540AB21 Q34629007-C3654B5E-14BE-4A74-A722-252FDBE161A0 Q34998318-5807566E-200B-4AA3-A232-2CBC21E37257 Q35021437-E139E179-B062-4C94-8412-C0B5F2C812F4 Q35046066-2FECB025-BCD7-4B51-B015-3109BC416507 Q35063447-522208AC-C356-474B-B5ED-A134849DB6F7 Q35081449-EDDBE961-59BE-4ACC-97DD-89EF5ADD7017 Q35199303-F9923C60-6FF4-41D2-8F2C-5FC894DADC6D Q35344420-6AC81C10-8E19-4C0C-9F01-1B896D780C24 Q35395827-9FF2C1AC-C636-49B2-BCC5-5FF63E5C070D

P2860

Methionine in proteins defends against oxidative stress.

http://www.wikidata.org/entity/Q37072433

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 09 October 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Methionine in proteins defends against oxidative stress.

@en

Methionine in proteins defends against oxidative stress.

@nl

type

label

Methionine in proteins defends against oxidative stress.

@en

Methionine in proteins defends against oxidative stress.

@nl

prefLabel

Methionine in proteins defends against oxidative stress.

@en

Methionine in proteins defends against oxidative stress.

@nl

P1433

Q37072433-3465C132-C740-4138-BA77-0A95CB4CCC71

P1476

Q37072433-94A6EC53-C96E-44D6-90A5-E730289C97CC

P2093

Q37072433-40ECACDD-9D46-4CCF-9056-C666D790224F

Q37072433-C7512290-03F7-443A-B457-FD0E40280C39

P2860

Q37072433-013DB8AE-7751-452A-919B-B77AEC3A777B

Q37072433-07EC69B3-8FA7-4F1E-B2DE-BFED85526E43

Q37072433-1993EA44-A12E-4976-A66C-264936B0F3D0

Q37072433-1FE4BE4D-EB46-49E3-98FE-41CF3F3217EF

Q37072433-21E26A68-8D77-4AF4-A435-F25DDBE51E8A

Q37072433-2206F919-A7B2-4061-A443-2840B0E1D4ED

Q37072433-26569612-5CBD-4EF3-B988-AF533BEA0EF5

Q37072433-2A80B1EE-68B2-43B7-A8CB-BB3797EA4E64

Q37072433-2F9DFA6A-0817-4069-B027-FE2F5E5DE822

Q37072433-462F2EBB-3EFB-446D-905C-2834FBD99BC7

P304

Q37072433-663FFD16-325E-421A-972F-6691F8678999

P31

Q37072433-1B35ED3A-1BC3-426B-97B7-A5D3FBA9B61E

P356

Q37072433-8495477F-8BE4-4F15-8CA8-757D9682AFA4

P407

Q37072433-5E61E85A-0BE6-4701-A608-076B494BE006

P433

Q37072433-AA896566-B167-48B7-A144-F2585C9814BE

P478

Q37072433-4B1CCAB5-5A86-487D-B979-36AFAAED746A

P577

Q37072433-5941C62D-9E19-4834-8CAB-AEC7ED6E3ED3

P5875

Q37072433-8998FE7F-BDCE-43A9-B63C-C3FCBA0C939D

P698

Q37072433-BCEB351B-12DE-4F3C-87A3-35B8979FAD29

P932

Q37072433-2DC8D7F0-3123-4346-9F49-45CF4E8EFEE7

P356

P1433

P1476

Methionine in proteins defends against oxidative stress.

@en

P2093

Rodney L Levine

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

Shen Luo

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

P2860

Protein oxidation implicated as the primary determinant of bacterial radioresistance

The Werner syndrome protein is a DNA helicase

High-quality life extension by the enzyme peptide methionine sulfoxide reductase

Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics

Methionine residues as endogenous antioxidants in proteins

Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution

Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure

The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo.

Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates

P304

464-472

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

P31

scholarly article

P356

10.1096/FJ.08-118414

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

P407

P433

2

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

P478

23

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

P577

2008-10-09T00:00:00Z

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

P5875

23310076

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

P698

18845767

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

P932

2630790

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