about
Quantitative Cross-linking/Mass Spectrometry Using Isotope-labeled Cross-linkers and MaxQuantBiological and Chemical Adaptation to Endogenous Hydrogen Peroxide Production in Streptococcus pneumoniae D39Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative foldingT-REX on-demand redox targeting in live cells.European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).Reactivity, Selectivity, and Stability in Sulfenic Acid Detection: A Comparative Study of Nucleophilic and Electrophilic Probes.Systematic and quantitative assessment of hydrogen peroxide reactivity with cysteines across human proteomes.Dependence of the structure and mechanics of metaphase chromosomes on oxidized cysteines.Regulated methionine oxidation by monooxygenases.ROS in Cancer: The Burning Question.The Myeloablative Drug Busulfan Converts Cysteine to Dehydroalanine and Lanthionine in Redoxins.The STIM-Orai Pathway: Regulation of STIM and Orai by Thiol Modifications.Mitochondrial reactive oxygen species and adipose tissue thermogenesis: Bridging physiology and mechanisms.Detecting Protein Sulfenylation in Cells Exposed to a Toxicant.Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation.Features of reactive cysteines discovered through computation: from kinase inhibition to enrichment around protein degrons.Stress-Activated Chaperones: A First Line of Defense.Discovery of Heteroaromatic Sulfones As a New Class of Biologically Compatible Thiol-Selective Reagents.Competitive profiling of celastrol targets in human cervical cancer HeLa cells via quantitative chemical proteomics.Quantitative proteomics identifies redox switches for global translation modulation by mitochondrially produced reactive oxygen species.Maintaining a Healthy Proteome during Oxidative Stress.Peroxidatic cysteine residue of peroxiredoxin 2 separated from human red blood cells treated by tert-butyl hydroperoxide is hyperoxidized into sulfinic and sulfonic acids.Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker.Ube2V2 Is a Rosetta Stone Bridging Redox and Ubiquitin Codes, Coordinating DNA Damage Responses.Comprehensive Redox Profiling of the Thiol Proteome of Clostridium difficile.Redox regulation of cell proliferation: Bioinformatics and redox proteomics approaches to identify redox-sensitive cell cycle regulators.Adductomic signatures of benzene exposure provide insights into cancer induction.Dynamic redox balance directs the oocyte-to-embryo transition via developmentally controlled reactive cysteine changesComputational Structural Biology of -nitrosylation of Cancer Targets
P2860
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P2860
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
The Expanding Landscape of the Thiol Redox Proteome.
@ast
The Expanding Landscape of the Thiol Redox Proteome.
@en
type
label
The Expanding Landscape of the Thiol Redox Proteome.
@ast
The Expanding Landscape of the Thiol Redox Proteome.
@en
prefLabel
The Expanding Landscape of the Thiol Redox Proteome.
@ast
The Expanding Landscape of the Thiol Redox Proteome.
@en
P2860
P356
P1476
The Expanding Landscape of the Thiol Redox Proteome.
@en
P2093
P2860
P356
10.1074/MCP.O115.056051
P577
2015-10-30T00:00:00Z