WordNet

be a contributing factor; "make things factor into a companys profitability"
any of the numbers (or symbols) that form a product when multiplied together
an independent variable in statistics
anything that contributes causally to a result; "a number of factors determined the outcome"
consider as relevant when making a decision; "You must factor in the recent developments" (同)factor in, factor out
resolve into factors; "a quantum computer can factor the number 15" (同)factor in, factor out
an event known to have happened or something known to have existed; "your fears have no basis in fact"; "how much of the story is fact and how much fiction is hard to tell"
a concept whose truth can be proved; "scientific hypotheses are not facts"
a piece of information about circumstances that exist or events that have occurred; "first you must collect all the facts of the case"
a statement or assertion of verified information about something that is the case or has happened; "he supported his argument with an impressive array of facts"

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1. 血友病患者における第VIIIおよび第IX因子阻害物質 factor viii and factor ix inhibitors in patients with hemophilia
2. 第VIII因子および第IX因子の生物学と正常な機能 biology and normal function of factor viii and factor ix
3. 静脈血栓症の原因の概要 overview of the causes of venous thrombosis
4. 後天性の凝固因子阻害物質 acquired inhibitors of coagulation
5. 血友病の治療 treatment of hemophilia

Structural insights into the interaction of blood coagulation co-factor VIIIa with factor IXa: A computational protein-protein docking and molecular dynamics refinement study.

Venkateswarlu D.
Biochemical and biophysical research communications.Biochem Biophys Res Commun.2014 Sep 26;452(3):408-14. doi: 10.1016/j.bbrc.2014.08.078. Epub 2014 Aug 23.
Coagulation factor X (FX) zymogen activation by factor IXa (FIXa) enzyme plays a critical role in the middle-phase of coagulation cascade. The activation process is catalytically inert and requires FIXa binding and complex formation with co-factor VIIIa (FVIIIa). In order to understand the structura
PMID 25157807

Enhanced factor VIIIa stability of A2 domain interface variants results from an increased apparent affinity for the A2 subunit. Results from an increased apparent affinity for the A2 subunit.

Monaghan M1, Wakabayashi H2, Griffiths A, Wintermute J, Fay PJ.
Thrombosis and haemostasis.Thromb Haemost.2014 Sep 2;112(3):495-502. doi: 10.1160/TH14-01-0086. Epub 2014 Jun 5.
Factor (F)VIIIa, a heterotrimer comprised of A1, A2, and A3C1C2 subunits, is labile due to the tendency of the A2 subunit to dissociate from the A1/A3C1C2 dimer. As dissociation of the A2 subunit inactivates FVIIIa activity, retention of A2 defines FVIIIa stability and thus, FXase activity. Earlier
PMID 24899227

Role of hydrophobic mutations on the binding affinity and stability of blood coagulation factor VIIIa: a computational molecular dynamics and free-energy analysis.

Venkateswarlu D.
Biochemical and biophysical research communications.Biochem Biophys Res Commun.2014 Jul 18;450(1):735-40. doi: 10.1016/j.bbrc.2014.06.043. Epub 2014 Jun 18.
Factor VIIIa is a non-covalently bound hetero-trimer among A1, A2 and A3-C1-C2 domains and an essential co-factor for factor IXa enzyme during proteolytic activation of factor X zymogen. The relatively weak interactions between A2 and the interface A1/A3 domains dampen the functional stability of FV
PMID 24952158