Linked Life Data

19286366

Source:http://linkedlifedata.com/resource/pubmed/id/19286366

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-4-22
pubmed:abstractText
The p53 tumour suppressor protein has presented a challenge for structural biology for more than two decades. The complete p53 molecule has eluded numerous attempts to determine its structure, presumably owing to the intrinsic conformational flexibility that is essential to the protein's function. Recent data obtained by X-ray crystallography, NMR spectroscopy and electron microscopy provide new insight into the quaternary architecture of the whole molecule and new strategies for examining how these structures correlate with the cell and molecular biology of the 'Guardian of the Genome'.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1879-033X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-202
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Structural biology of the p53 tumour suppressor.
pubmed:affiliation
Wolfson Institute for Biomedical Research, University College London, Gower Street, London, UK.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't