SMYD2 glutathionylation contributes to degradation of sarcomeric proteins - Wikidata - wikimedia - TriplyDB

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

http://www.wikidata.org/entity/Q58600320

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SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

http://www.wikidata.org/entity/Q58600320

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article publié dans Nature Communications

@fr

im Oktober 2018 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Nature Communications

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в жовтні 2018

@uk

name

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

@en

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

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type

label

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

@en

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

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prefLabel

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

@en

SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

@nl

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S41467-018-06786-X

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Nature Communications

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SMYD2 glutathionylation contributes to degradation of sarcomeric proteins

@en

P2093

Dhanushka N P Munkanatta Godage

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

Garrett C VanHecke

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

Han-Zhong Feng

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

Jian-Ping Jin

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

Joshua Holcomb

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

Kusal T G Samarasinghe

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

Mark Hiske

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

Zhe Yang

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

P2860

Repression of p53 activity by Smyd2-mediated methylation

Calcium and ROS: A mutual interplay

Mitochondrial reactive oxygen species: a double edged sword in ischemia/reperfusion vs preconditioning

SMYD proteins: key regulators in skeletal and cardiac muscle development and function

Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins

Structure of Human SMYD2 Protein Reveals the Basis of p53 Tumor Suppressor Methylation

4-Hydroxynonenal (HNE) modified proteins in metabolic diseases

SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation

A statistical model for identifying proteins by tandem mass spectrometry

S-glutathionylation of troponin I (fast) increases contractile apparatus Ca2+ sensitivity in fast-twitch muscle fibres of rats and humans

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s41467-018-06786-x

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scholarly article

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10.1038/S41467-018-06786-X

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1

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9

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Charles S Chung

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2018-10-18T00:00:00Z

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30337525

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general chemistry

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6194001

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