Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1997-5-14
pubmed:databankReference
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D17582, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D64000, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/H10859, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L09547, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L16533, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L18867, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L34677, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L35272, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M29364, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M31045, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M32229, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M67479, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M76451, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M92325, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/T18272, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U02604, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U09874, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U13949, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U16134, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20646, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U39719, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U43536, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U46549, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X73140, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X75328, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X77160, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X95276, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/Z25810, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/Z29026, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/Z38058
pubmed:abstractText
The HSP100/Clp proteins are a newly discovered family with a great diversity of functions, such as increased tolerance to high temperatures, promotion of proteolysis of specific cellular substrates and regulation of transcription. HSP100/Clp proteins are also synthesized in a variety of specific patterns and, in eukaryotes, are localized to different subcellular compartments. Recent data suggest that a common ability to disassemble higher-order protein structures and aggregates unifies the molecular functions of this diverse family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/ClpB protein, Leishmania, http://linkedlifedata.com/resource/pubmed/chemical/ClpX protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase Clp, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HsP104 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0968-0004
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
289-96
pubmed:dateRevised
2009-9-3
pubmed:meshHeading
pubmed-meshheading:8772382-Adenosine Triphosphatases, pubmed-meshheading:8772382-Amino Acid Sequence, pubmed-meshheading:8772382-Animals, pubmed-meshheading:8772382-Bacteriophage mu, pubmed-meshheading:8772382-Endopeptidase Clp, pubmed-meshheading:8772382-Escherichia coli Proteins, pubmed-meshheading:8772382-Heat-Shock Proteins, pubmed-meshheading:8772382-Humans, pubmed-meshheading:8772382-Mice, pubmed-meshheading:8772382-Models, Biological, pubmed-meshheading:8772382-Molecular Chaperones, pubmed-meshheading:8772382-Molecular Sequence Data, pubmed-meshheading:8772382-Protein Conformation, pubmed-meshheading:8772382-Protozoan Proteins, pubmed-meshheading:8772382-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8772382-Serine Endopeptidases, pubmed-meshheading:8772382-Stress, Physiological
pubmed:year
1996
pubmed:articleTitle
HSP100/Clp proteins: a common mechanism explains diverse functions.
pubmed:affiliation
Howard Hughes Medical Institute, Chicago, IL, USA.
pubmed:publicationType
Journal Article, Review