Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-4-17
pubmed:abstractText
During the past two years, a large amount of biochemical, biophysical and low- to high-resolution structural data have provided mechanistic insights into the machinery of protein folding and unfolding. It has emerged that dual functionality in terms of folding and unfolding might exist for some systems. The majority of folding/unfolding machines adopt oligomeric ring structures in a cooperative fashion and utilise the conformational changes induced by ATP binding/hydrolysis for their specific functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin 10, http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin 60, http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin Containing TCP-1, http://linkedlifedata.com/resource/pubmed/chemical/Chaperonins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/N-Ethylmaleimide-Sensitive Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/dnaK protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/prefoldin
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0959-440X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
231-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Machinery of protein folding and unfolding.
pubmed:affiliation
Centre for Structural Biology, Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Flowers Building, South Kensington, SW7 2AZ, London, UK. xiaodong.zhang@ic.ac.uk
pubmed:publicationType
Journal Article, Review