Linked Life Data

21045566

Source:http://linkedlifedata.com/resource/pubmed/id/21045566

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-11-30
pubmed:abstractText
Small heat shock proteins have been characterized in vitro as ATP-independent molecular chaperones that can prevent aggregation of un- or mis-folded proteins and assist in their refolding with the help of ATP-dependent chaperone machines (e.g., the Hsp70 proteins). Comparison of the functionality of the 10 human members of the small HSPB family in cell models now reveals that some members function entirely differently and independently from Hsp70 machines. One member, HSPB7, has strong activities to prevent toxicity of polyglutamine-containing proteins in cells and Drosophila, and seems to act by assisting the loading of misfolded proteins or small protein aggregates into autophagosomes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1554-8635
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
101-3
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Small heat shock proteins, protein degradation and protein aggregation diseases.
pubmed:affiliation
Department of Cell Biology, Section for Radiation and Stress Cell Biology, University Medical Center Groningen, Groningen, The Netherlands.
pubmed:publicationType
Journal Article