Role of Carbonyl Modifications on Aging-Associated Protein Aggregation. - Wikidata - wikimedia - TriplyDB

Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

http://www.wikidata.org/entity/Q36500213

about

The age- and sex-specific decline of the 20s proteasome and the Nrf2/CncC signal transduction pathway in adaption and resistance to oxidative stress in Drosophila melanogaster Effect of peroxynitrite on human serum albumin: a multi technique approach.Age-Dependent Protein Aggregation Initiates Amyloid-β Aggregation.Reduced Insulin/IGF-1 Signaling Restores the Dynamic Properties of Key Stress Granule Proteins during Aging.Elevated oxidative stress in the aortic media of patients with bicuspid aortic valve.Protein Posttranslational Modifications: Roles in Aging and Age-Related Disease.A Tale of Two Concepts: Harmonizing the Free Radical and Antagonistic Pleiotropy Theories of Aging.Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans.More stressed out with age? Check your RNA granule aggregation.Identification of ageing biomarkers in human dermis biopsies by thermal analysis (DSC) combined with Fourier transform infrared spectroscopy (FTIR/ATR).Origin and pathophysiology of protein carbonylation, nitration and chlorination in age-related brain diseases and aging.

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Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

http://www.wikidata.org/entity/Q36500213

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

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Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

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Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

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Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

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Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

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Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

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Scientific Reports

P1476

Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

@en

P2093

Aleksandra M Urbanska

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

Barbara Roda

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

Kateryna Morozova

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

Liling Huang

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

Maya Tanase

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

Michael Goldberg

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

Pierluigi Reschiglian

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

Valerio Zolla

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P2860

Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.

Activation of chaperone-mediated autophagy during oxidative stress

Chaperone-mediated autophagy: a unique way to enter the lysosome world

Widespread protein aggregation as an inherent part of aging in C. elegans

GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides

Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy

Impairment of the ubiquitin-proteasome system by protein aggregation

The role of autophagy in neurodegenerative disease

Aggresomes, inclusion bodies and protein aggregation

Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain

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19311

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scholarly article

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10.1038/SREP19311

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P478

6

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Laura Santambrogio

Cristina C Clement

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2016-01-18T00:00:00Z

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291136666

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26776680

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4726109

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