About: The BAG proteins: a ubiquitous family of chaperone regulators

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scientific article published on May 2008

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 2008 (ast) наукова стаття, опублікована в травні 2008 (uk) مقالة علمية نشرت في مايو 2008 (ar) scientific article published on May 2008 (en)
publication date	wds:Q37081047-B023B183-3BA9-4110-8DFF-8ADD7932D4C1
publication date	2008-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37081047-A95541F6-C681-4E5F-999A-4DD3E472CCA7
language of work or name	English
exact match	wds:Q37081047-1DA99CA9-2CEF-4B9F-B68C-846A391E91F0
exact match	https://scigraph.springernature.com/pub.10.1007/s00018-008-7535-2
author name string	wds:Q37081047-9B387D1A-C8AD-407F-87DE-A7D8FC82003B wds:Q37081047-E5D58502-69D1-4BB5-A600-F58959204B4D
author name string	M B Dickman M Kabbage
rdfs:label	The BAG proteins: a ubiquitous family of chaperone regulators (en) The BAG proteins: a ubiquitous family of chaperone regulators (nl) The BAG proteins: a ubiquitous family of chaperone regulators (ast)
skos:prefLabel	The BAG proteins: a ubiquitous family of chaperone regulators (en) The BAG proteins: a ubiquitous family of chaperone regulators (nl) The BAG proteins: a ubiquitous family of chaperone regulators (ast)
name	The BAG proteins: a ubiquitous family of chaperone regulators (en) The BAG proteins: a ubiquitous family of chaperone regulators (nl) The BAG proteins: a ubiquitous family of chaperone regulators (ast)
title	wds:Q37081047-C288257D-B3CF-4F69-B80D-A2559B26867E
title	The BAG proteins: a ubiquitous family of chaperone regulators (en)
page(s)	wds:Q37081047-82D03D3C-79F5-47D5-9EB3-E06EF80D9E91
page(s)	1390-1402
instance of	wds:Q37081047-3A0FDB18-B628-4B9E-B492-3E72F84EBAE6 wds:Q37081047-c5c9dca3-633d-493a-b7e4-d8f7ba2527c1
instance of	review article scholarly article
main subject	wds:Q37081047-EA382088-ECA0-48F5-9D50-96E6101E8DFA
main subject	molecular chaperones
PubMed ID	wds:Q37081047-E756732B-9BB0-4667-B3A6-474E9C1EC17B
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18264803
PubMed ID	18264803
published in	wds:Q37081047-FBC5C116-5C92-4717-853B-F55C43B40E2D
published in	Cellular and Molecular Life Sciences
issue	wds:Q37081047-89E33553-6FCD-4B87-B985-14E7949E0F09
volume	wds:Q37081047-E8845AAF-B5CB-42BE-8FA1-06B811205B85
issue	9
volume	65
DOI	wds:Q37081047-2206E2E1-D822-409C-ACF8-B9AB0DF68DBD
DOI	http://dx.doi.org/10.1007/S00018-008-7535-2
DOI	10.1007/S00018-008-7535-2
ResearchGate publication ID	wds:Q37081047-A80033E6-D411-4037-AF6A-57A5E8576799
ResearchGate publication ID	5586923
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37081047
is cites work of	Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease Silencer of death domains (SODD) inhibits skeletal muscle and kidney enriched inositol 5-phosphatase (SKIP) and regulates phosphoinositide 3-kinase (PI3K)/Akt signaling to the actin cytoskeleton Quantitative proteomics analysis reveals BAG3 as a potential target to suppress severe acute respiratory syndrome coronavirus replication HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting. Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. BAG3-related myofibrillar myopathy in a Chinese family In silico study on Arabidopsis BAG gene expression in response to environmental stresses ER stress-induced cell death mechanisms Evidence for modulation of BAG3 by polyomavirus JC early protein. Autophagy inhibition promotes defective neosynthesized proteins storage in ALIS, and induces redirection toward proteasome processing and MHCI-restricted presentation. Hsp70 and its molecular role in nervous system diseases Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro Autophagic degradation of the inhibitory p53 isoform Δ133p53α as a regulatory mechanism for p53-mediated senescence. Bat3 promotes the membrane integration of tail-anchored proteins Apoptotic gene expression by human periodontal ligament cells following cyclic stretch A small molecule inhibitor of inducible heat shock protein 70. AtBAG7, an Arabidopsis Bcl-2-associated athanogene, resides in the endoplasmic reticulum and is involved in the unfolded protein response Regulation of survival gene hsp70. BAG6/BAT3: emerging roles in quality control for nascent polypeptides 2-phenylethynesulfonamide Prevents Induction of Pro-inflammatory Factors and Attenuates LPS-induced Liver Injury by Targeting NHE1-Hsp70 Complex in Mice The BAG homology domain of Snl1 cures yeast prion [URE3] through regulation of Hsp70 chaperones Bcl2-associated athanogene 3 interactome analysis reveals a new role in modulating proteasome activity. Heat shock protein 70 (hsp70) as an emerging drug target. Plant oxylipins: role of jasmonic acid during programmed cell death, defence and leaf senescence Cytoplasmic body component TRIM5{alpha} requires lipid-enriched microdomains for efficient HIV-1 restriction A nuclear glutathione cycle within the cell cycle Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. When supply does not meet demand-ER stress and plant programmed cell death A Role for the Chaperone Complex BAG3-HSPB8 in Actin Dynamics, Spindle Orientation and Proper Chromosome Segregation during Mitosis Downregulating sCLU enhances the sensitivity of hepatocellular carcinoma cells to gemcitabine by activating the intrinsic apoptosis pathway. Ethylene Antagonizes Salt-Induced Growth Retardation and Cell Death Process via Transcriptional Controlling of Ethylene-, BAG- and Senescence-Associated Genes in Arabidopsis Development of salinity tolerance in rice by constitutive-overexpression of genes involved in the regulation of programmed cell death Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants CaM/BAG5/Hsc70 signaling complex dynamically regulates leaf senescence GRP78 Interacting Partner Bag5 Responds to ER Stress and Protects Cardiomyocytes From ER Stress-Induced Apoptosis Novel characterization of the HSPA2-stabilizing protein BAG6 in human spermatozoa Tight regulation of the interaction between Brassica napus and Sclerotinia sclerotiorum at the microRNA level Transcriptome profiling of postharvest strawberry fruit in response to exogenous auxin and abscisic acid. LRRK2 Pathways Leading to Neurodegeneration

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