Linked Life Data

15930624

Source:http://linkedlifedata.com/resource/pubmed/id/15930624

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6
pubmed:dateCreated
2005-6-2
pubmed:abstractText
Initiation, propagation and regulatory processes of blood coagulation occur at the cell surface. During blood coagulation, many coagulation factors are anchored onto cell-surface membranes through their N-terminal carboxyglutamic acid-rich (Gla) domains found on such vitamin K-dependent blood coagulation factors as factors VII, IX, X, prothrombin, factors C and S. 10C12 is a conformation-specific calcium-dependent anti-factor IX antibody, which is directed at the calcium-stabilized Gla domain and interferes with factor IX-membrane interaction. In a variety of animal models, 10C12 has been demonstrated to be effective anticoagulant in attenuating thrombosis without severe bleeding. The crystallization of the Fab fragment of 10C12 and its complex with the Gla domain of human factor IX was not trivial. Here, the crystallization conditions and unusual aspects of this crystallization process are reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
701-3
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Crystallization of an anti-factor IX antibody and its complex.
pubmed:affiliation
State Key Laboratory of Structual Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't