Thiol-based redox switches in eukaryotic proteins. - Wikidata - awgldk - TriplyDB

Thiol-based redox switches in eukaryotic proteins.

Thiol-based redox switches in eukaryotic proteins.

http://www.wikidata.org/entity/Q37322426

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A redox switch in angiotensinogen modulates angiotensin release.Relationship between Oxidative Stress, Circadian Rhythms, and AMD The Measurement of Reversible Redox Dependent Post-translational Modifications and Their Regulation of Mitochondrial and Skeletal Muscle Function Strategies for profiling native S-nitrosylation The role of peroxiredoxin II in chemoresistance of breast cancer cells Selenium cytotoxicity in cancer The basics of thiols and cysteines in redox biology and chemistry The thioredoxin/peroxiredoxin/sulfiredoxin system: current overview on its redox function in plants and regulation by reactive oxygen and nitrogen species Oxr1 is essential for protection against oxidative stress-induced neurodegeneration Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia.Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity Sending Out an SOS: Mitochondria as a Signaling Hub Redox regulation by reversible protein S-thiolation in bacteria Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function ROSics: chemistry and proteomics of cysteine modifications in redox biology.Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology Prediction of redox-sensitive cysteines using sequential distance and other sequence-based features.Redox biology: computational approaches to the investigation of functional cysteine residues Click-PEGylation - A mobility shift approach to assess the redox state of cysteines in candidate proteins Cofactor binding protects flavodoxin against oxidative stress.Thiol-based regulation of glyceraldehyde-3-phosphate dehydrogenase in blood bank-stored red blood cells: a strategy to counteract oxidative stress.Photons and particles emitted from cold atmospheric-pressure plasma inactivate bacteria and biomolecules independently and synergistically.Protein redox modification as a cellular defense mechanism against tissue ischemic injury.Thiol redox biochemistry: insights from computer simulations Resin-assisted enrichment of thiols as a general strategy for proteomic profiling of cysteine-based reversible modifications H2S and its role in redox signaling.Thiol-based redox switches Protection of a single-cysteine redox switch from oxidative destruction: On the functional role of sulfenyl amide formation in the redox-regulated enzyme PTP1B.Caloric restriction and the aging process: a critique Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes.YCF1-mediated cadmium resistance in yeast is dependent on copper metabolism and antioxidant enzymes.Proteome-wide light/dark modulation of thiol oxidation in cyanobacteria revealed by quantitative site-specific redox proteomics.Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans Cysteine-based redox switches in enzymes The redoxome: Proteomic analysis of cellular redox networks.Proteomic and carbonylation profile analysis of rat skeletal muscles following acute swimming exercise Transcriptome-wide mapping of pea seed ageing reveals a pivotal role for genes related to oxidative stress and programmed cell death

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Thiol-based redox switches in eukaryotic proteins.

http://www.wikidata.org/entity/Q37322426

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on May 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Thiol-based redox switches in eukaryotic proteins.

@en

Thiol-based redox switches in eukaryotic proteins.

@nl

type

label

Thiol-based redox switches in eukaryotic proteins.

@en

Thiol-based redox switches in eukaryotic proteins.

@nl

prefLabel

Thiol-based redox switches in eukaryotic proteins.

@en

Thiol-based redox switches in eukaryotic proteins.

@nl

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Antioxidants & Redox Signaling

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Thiol-based redox switches in eukaryotic proteins.

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Nicolas Brandes

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

Sebastian Schmitt

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

Ursula Jakob

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

P2860

Triose phosphate isomerase deficiency is caused by altered dimerization--not catalytic inactivity--of the mutant enzymes

Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress

Cell transformation by the superoxide-generating oxidase Mox1

PTP1B contributes to the oncogenic properties of colon cancer cells through Src activation

Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2

SIAH-1 promotes apoptosis and tumor suppression through a network involving the regulation of protein folding, unfolding, and trafficking: identification of common effectors with p53 and p21(Waf1)

Protein thiol modifications visualized in vivo

Nitric oxide: physiology, pathophysiology, and pharmacology

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B

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997-1014

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scholarly article

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10.1089/ARS.2008.2285

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5

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11

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2009-05-01T00:00:00Z

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18999917

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2787739

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