Proteomic approaches to the characterization of protein thiol modification. - Wikidata - wikimedia - TriplyDB

Proteomic approaches to the characterization of protein thiol modification.

Proteomic approaches to the characterization of protein thiol modification.

http://www.wikidata.org/entity/Q34925199

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The basics of thiols and cysteines in redox biology and chemistry Staphylococcal response to oxidative stress Chemical approaches to detect and analyze protein sulfenic acids The electrophile responsive proteome: integrating proteomics and lipidomics with cellular function Silica Nanoparticles Induce Oxidative Stress and Autophagy but Not Apoptosis in the MRC-5 Cell Line Measurement of Reactive Oxygen Species, Reactive Nitrogen Species, and Redox-Dependent Signaling in the Cardiovascular System: A Scientific Statement From the American Heart Association.Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I.Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detection Thiol-dependent antioxidant activity of interphotoreceptor retinoid-binding protein.Lipocalin-type prostaglandin D synthase protects against oxidative stress-induced neuronal cell death.A comparative 'bottom up' proteomics strategy for the site-specific identification and quantification of protein modifications by electrophilic lipids.Basis for half-site ligand binding in yeast NAD(+)-specific isocitrate dehydrogenase.Using the heat-shock response to discover anticancer compounds that target protein homeostasis.Redox regulation of cell migration and adhesion Geopyxins A-E, ent-kaurane diterpenoids from endolichenic fungal strains Geopyxis aff. majalis and Geopyxis sp. AZ0066: structure-activity relationships of geopyxins and their analogues.Reactive oxygen species scavenger N-acetyl cysteine reduces methamphetamine-induced hyperthermia without affecting motor activity in mice.Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria.Genetic modifier screens to identify components of a redox-regulated cell adhesion and migration pathway Increased nitroxidative stress promotes mitochondrial dysfunction in alcoholic and nonalcoholic fatty liver disease.Detection of electrophile-sensitive proteins.Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly Modulating protein function through reversible oxidation: Redox-mediated processes in plants revealed through proteomics.Post-translational modifications and the Warburg effect.Characterisation of the active/de-active transition of mitochondrial complex I.S-nitrosation and neuronal plasticity.Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.Measurement and meaning of cellular thiol:disufhide redox status.Protein Thiol Redox Signaling in Monocytes and Macrophages.Redox Control of Skeletal Muscle Regeneration.Biophysical and proteomic characterization strategies for cysteine modifications in Ras GTPases.Chasing cysteine oxidative modifications: proteomic tools for characterizing cysteine redox status.Identification and quantification of protein S-nitrosation by nitrite in the mouse heart during ischemia.Methylsulfonyl benzothiazole (MSBT): a selective protein thiol blocking reagent.A twist on quantification: measuring the site occupancy of S-nitrosylation.The STIM-Orai Pathway: Regulation of STIM and Orai by Thiol Modifications.Mitochondrial reactive oxygen species and adipose tissue thermogenesis: Bridging physiology and mechanisms.Stress turns on the heat: Regulation of mitochondrial biogenesis and UCP1 by ROS in adipocytes.The transcriptional response to oxidative stress is part of, but not sufficient for, insulin resistance in adipocytes.Impaired fertilizing ability of superoxide dismutase 1-deficient mouse sperm during in vitro fertilization.A simple method for determining the ligand affinity toward a zinc-enzyme model by using a TAMRA/TAMRA interaction.

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Proteomic approaches to the characterization of protein thiol modification.

http://www.wikidata.org/entity/Q34925199

description

2010 nî lūn-bûn

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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Proteomic approaches to the characterization of protein thiol modification.

@ast

Proteomic approaches to the characterization of protein thiol modification.

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Proteomic approaches to the characterization of protein thiol modification.

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type

label

Proteomic approaches to the characterization of protein thiol modification.

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Proteomic approaches to the characterization of protein thiol modification.

@en

Proteomic approaches to the characterization of protein thiol modification.

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prefLabel

Proteomic approaches to the characterization of protein thiol modification.

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Proteomic approaches to the characterization of protein thiol modification.

@en

Proteomic approaches to the characterization of protein thiol modification.

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J.CBPA.2010.11.003

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Current Opinion in Chemical Biology

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Proteomic approaches to the characterization of protein thiol modification.

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Andrew M James

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Edward T Chouchani

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Ian M Fearnley

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Kathryn S Lilley

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Michael P Murphy

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P2860

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

Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

Difference gel electrophoresis: a single gel method for detecting changes in protein extracts

Palmitoylation: policing protein stability and traffic

Blue native PAGE

Iodophenylarsine oxide and arsenical affinity chromatography: new probes for dithiol proteins. Application to tubulins and to components of the insulin receptor-glucose transporter signal transduction pathway

Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation

Mitochondria, oxidants, and aging

Protein S-nitrosylation: purview and parameters

Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple

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