Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation. - Wikidata - awgldk - TriplyDB

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

http://www.wikidata.org/entity/Q36672895

about

Integration of cardiac proteome biology and medicine by a specialized knowledgebase A large dataset of protein dynamics in the mammalian heart proteome Post-translational modifications of the cardiac proteome in diabetes and heart failure Characterization, design, and function of the mitochondrial proteome: from organs to organisms Quantitative proteomics in cardiovascular research: global and targeted strategies Lysine ubiquitination and acetylation of human cardiac 20S proteasomes.Mitochondrial Aging: Is There a Mitochondrial Clock?Immobilized Metal Affinity Chromatography Coupled to Multiple Reaction Monitoring Enables Reproducible Quantification of Phospho-signaling Regulation of acetylation restores proteolytic function of diseased myocardium in mouse and human.Assessing Cardiac Metabolism: A Scientific Statement From the American Heart Association.The selected reaction monitoring/multiple reaction monitoring-based mass spectrometry approach for the accurate quantitation of proteins: clinical applications in the cardiovascular diseases.Proteomics in cardiovascular disease: recent progress and clinical implication and implementation.Mitochondrial remodeling: Rearranging, recycling, and reprogramming.Proteomics Research in Cardiovascular Medicine and Biomarker Discovery.Phosphoproteome mapping of cardiomyocyte mitochondria in a rat model of heart failure Rapid Phosphoproteomic Effects of Abscisic Acid (ABA) on Wild-Type and ABA Receptor-Deficient A. thaliana Mutants.

P2860

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P2860

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

http://www.wikidata.org/entity/Q36672895

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

@zh-cn

name

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

@ast

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

@en

type

label

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

@ast

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

@en

prefLabel

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

@ast

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

@en

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J.JPROT.2012.09.015

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Journal of Proteomics

P1476

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

@en

P2093

Christopher M Ryan

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

David A Liem

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

Jun Zhang

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Kym F Faull

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Maggie P Y Lam

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Sarah B Scruggs

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Tae-Young Kim

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P2860

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis

PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

Systematic characterization of the murine mitochondrial proteome using functionally validated cardiac mitochondria

Assay development for the determination of phosphorylation stoichiometry using multiple reaction monitoring methods with and without phosphatase treatment: application to breast cancer signaling pathways

A tissue-specific atlas of mouse protein phosphorylation and expression

Tyrosine phosphorylation by Src within the cavity of the adenine nucleotide translocase 1 regulates ADP/ATP exchange in mitochondria.

Study of mitochondria in rat liver. Quantitative electron microscopy.

Phosphoproteome analysis of isoflurane-protected heart mitochondria: phosphorylation of adenine nucleotide translocator-1 on Tyr194 regulates mitochondrial function.

Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions.

Regulation of pyruvate dehydrogenase complex activity by reversible phosphorylation.

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15-23

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scholarly article

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10.1016/J.JPROT.2012.09.015

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81

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phosphorylation

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3593810

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