Linked Life Data

17565234

Source:http://linkedlifedata.com/resource/pubmed/id/17565234

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-6-13
pubmed:abstractText
The hydrophobicity pattern distribution in the Aalpha-, Bbeta- and gamma-chains of human fibrinogen has been studied by a nonlinear method, recurrence quantification analysis, in the wild type and in a number of naturally occurring or simulated mutants. The aim was to find a structural basis for distinguishing between silent and pathological mutants. We were successful in the case of mutations on the Aalpha-chain, thanks to the peculiar features of this chain as compared to the other two. Relevant findings concerning the point mutants of the Aalpha-chain are the following: (a) the recurrence quantification analysis-based classification of such mutants is in good agreement with the clinical classification, and (b) the location of the mutated residue on the sequence plays a more relevant role than its hydrophobic features. Artificial point mutants in the terminal zone (600-866 residues) of the extended isoform of the Aalpha-chain cluster together with the natural hemorrhagic mutants of the first (1-207) residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1424-8832
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
417-27
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Simulated point mutations in the Aalpha-chain of human fibrinogen support a role of the alphaC domain in the stabilization of fibrin gel.
pubmed:affiliation
Department of Human Physiology and Pharmacology Vittorio Erspamer, University of Rome, La Sapienza, Rome, Italy.
pubmed:publicationType
Journal Article