Binding of bovine factor Va to phosphatidylcholine membranes.
about
The role of hydrophobic interactions in positioning of peripheral proteins in membranesModulation of prothrombinase assembly and activity by phosphatidylethanolamineRoles of factor Va heavy and light chains in protein and lipid rearrangements associated with the formation of a bovine factor Va-membrane complex.Properties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusionFunctional and structural characterization of factor Xa dimer in solution.Hemagglutinin fusion peptide mutants in model membranes: structural properties, membrane physical properties, and PEG-mediated fusionThe thrombin-sensitive region of protein S mediates phospholipid-dependent interaction with factor Xa.Wild-type and mutant hemagglutinin fusion peptides alter bilayer structure as well as kinetics and activation thermodynamics of stalk and pore formation differently: mechanistic implications.Glucosylceramide, a neutral glycosphingolipid anticoagulant cofactor, enhances the interaction of human- and bovine-activated protein C with negatively charged phospholipid vesicles.Factor Va residues 311-325 represent an activated protein C binding region.
P2860
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P2860
Binding of bovine factor Va to phosphatidylcholine membranes.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Binding of bovine factor Va to phosphatidylcholine membranes.
@en
type
label
Binding of bovine factor Va to phosphatidylcholine membranes.
@en
prefLabel
Binding of bovine factor Va to phosphatidylcholine membranes.
@en
P2860
P1433
P1476
Binding of bovine factor Va to phosphatidylcholine membranes.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(96)79863-6
P407
P577
1996-06-01T00:00:00Z