About: A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins

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rdf:type	Item
description	artículu científicu espublizáu en 1997 (ast) vědecký článek publikovaný v roce 1997 (cs) 1997 թվականի փետրվարին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в лютому 1997 (uk) 1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 1997/02/28) (sk) مقالة علمية (نشرت في 28-2-1997) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) wetenschappelijk artikel (gepubliceerd op 1997/02/28) (nl) scientific journal article (en) im Februar 1997 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28579745-C32EB912-284F-43B1-AC01-ACDBA014C8B8
publication date	1997-02-28 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28579745-F89DAC86-EF7F-4681-8D07-4750FCDC57BC
language of work or name	English
author name string	wds:Q28579745-30104063-3208-4F8E-B8F5-9800C9660A67 wds:Q28579745-7CFD39D9-A2CA-422F-B82B-B9DB96FDB5C0 wds:Q28579745-CA0A47E0-7463-4B12-B193-630C084D5066
OpenCitations bibliographic resource ID	wds:Q28579745-35DE57CF-B9E2-4BC8-B9A5-565BB4DCBCB2
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3355434
author name string	E. Knecht J. F. Dice A. M. Cuervo
OpenCitations bibliographic resource ID	3355434
rdfs:label	A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (en) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (nl) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (ast)
skos:prefLabel	A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (en) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (nl) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (ast)
name	A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (en) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (nl) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (ast)
title	wds:Q28579745-0BD6949B-EB13-4C51-97A7-1BE11529AB43
title	A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins (en)
page(s)	wds:Q28579745-E7FB25C8-1031-4F0E-B53B-9721D37CADA3
page(s)	5606–5615
instance of	wds:Q28579745-36D30E14-3DB8-4B35-B2A9-243E62CDD2D4
instance of	scholarly article
PubMed ID	wds:Q28579745-51B6ADD8-AD28-47E9-B36D-7A587C7114D1
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9038169
PubMed ID	9038169
published in	wds:Q28579745-C0B93D5F-3D81-4F20-A21D-65C4A6BBCE64
published in	Journal of Biological Chemistry
issue	wds:Q28579745-0A17C698-46C9-40A6-A64F-262B372E2ED7
volume	wds:Q28579745-4733AA30-EE89-4545-A34F-CA5ECB79F795
issue	9
volume	272
DOI	wds:Q28579745-44E6E7D0-B5CC-4D97-868E-DB1EF74FB37B
DOI	http://dx.doi.org/10.1074/JBC.272.9.5606
DOI	10.1074/JBC.272.9.5606
Fatcat ID	wds:Q28579745-0540D8A0-D114-419B-9C0B-5BDB0371DE49
Fatcat ID	release_qt4iup3eubcmrku4p4xyomf5pq
ResearchGate publication ID	wds:Q28579745-C2C0BC37-0A70-4DE3-AF01-DCFBF1912B24
ResearchGate publication ID	14172986
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28579745
is cites work of	HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting. Chloroquine myopathy suggests that tau is degraded in lysosomes: implication for the formation of paired helical filaments in Alzheimer's disease Protein translocation across membranes Lysosomal degradation of alpha-synuclein in vivo. The elimination of accumulated and aggregated proteins: a role for aggrephagy in neurodegeneration Methods to monitor chaperone-mediated autophagy Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy Chaperone-mediated autophagy: selectivity pays off. Chaperone-mediated autophagy in health and disease Guidelines for the use and interpretation of assays for monitoring autophagy Microautophagy of cytosolic proteins by late endosomes Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection Chaperone-mediated autophagy Identification of regulators of chaperone-mediated autophagy Modulation of deregulated chaperone-mediated autophagy by a phosphopeptide Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes Pharmacological regulators of autophagy and their link with modulators of lupus disease The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles Autophagy in neuronal cells: general principles and physiological and pathological functions IkappaB is a substrate for a selective pathway of lysosomal proteolysis Activation of chaperone-mediated autophagy during oxidative stress Chaperone-mediated autophagy: a unique way to enter the lysosome world Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing Regulation of lamp2a levels in the lysosomal membrane Role of the heat-shock response in the life and death of proteins. Autophagy regulates cholesterol efflux from macrophage foam cells via lysosomal acid lipase Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy Eps8 is recruited to lysosomes and subjected to chaperone-mediated autophagy in cancer cells The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis Role of chaperone mediated autophagy (CMA) in the degradation of misfolded N-CoR protein in non-small cell lung cancer (NSCLC) cells STUB1/CHIP is required for HIF1A degradation by chaperone-mediated autophagy Chaperone-mediated autophagy regulates T cell responses through targeted degradation of negative regulators of T cell activation Phosphorylation-regulated degradation of the tumor-suppressor form of PED by chaperone-mediated autophagy in lung cancer cells. The role of chaperone-mediated autophagy in huntingtin degradation Chaperone-mediated autophagy: machinery, regulation and biological consequences Selective Degradation of Annexins by Chaperone-mediated Autophagy Chaperones in autophagy Altered lipid content inhibits autophagic vesicular fusion Inhibitory effect of dietary lipids on chaperone-mediated autophagy Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy Deficient chaperone-mediated autophagy in liver leads to metabolic dysregulation

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