Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site.
about
Structure of native protein C inhibitor provides insight into its multiple functionsMutation of the H-helix in antithrombin decreases heparin stimulation of protease inhibition.Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.Kinetic evidence that allosteric activation of antithrombin by heparin is mediated by two sequential conformational changes.Dynamic properties of the native free antithrombin from molecular dynamics simulations: computational evidence for solvent- exposed Arg393 side chain.
P2860
Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site.
description
2006 nî lūn-bûn
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2006年の論文
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name
Allosteric activation of antit ...... l in the heparin binding site.
@en
Allosteric activation of antit ...... l in the heparin binding site.
@nl
type
label
Allosteric activation of antit ...... l in the heparin binding site.
@en
Allosteric activation of antit ...... l in the heparin binding site.
@nl
prefLabel
Allosteric activation of antit ...... l in the heparin binding site.
@en
Allosteric activation of antit ...... l in the heparin binding site.
@nl
P2093
P2860
P1433
P1476
Allosteric activation of antit ...... l in the heparin binding site.
@en
P2093
James A Huntington
Jonathan Langdown
Trevor P Baglin
Wendy J Carter
P2860
P304
P356
10.1016/J.FEBSLET.2006.07.057
P407
P577
2006-07-26T00:00:00Z