pH-dependent association of factor VIII chains: enhancement of affinity at physiological pH by Cu2+.
about
The tertiary structure and domain organization of coagulation factor VIIIStructural investigation of zymogenic and activated forms of human blood coagulation factor VIII: a computational molecular dynamics studyIncreasing hydrophobicity or disulfide bridging at the factor VIII A1 and C2 domain interface enhances procofactor stability.Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface.Modification of interdomain interfaces within the A3C1C2 subunit of factor VIII affects its stability and activityCombining mutations of charged residues at the A2 domain interface enhances factor VIII stability over single point mutations
P2860
pH-dependent association of factor VIII chains: enhancement of affinity at physiological pH by Cu2+.
description
2006 nî lūn-bûn
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
@zh-hk
2006年論文
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2006年論文
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2006年论文
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2006年论文
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name
pH-dependent association of fa ...... y at physiological pH by Cu2+.
@en
pH-dependent association of fa ...... y at physiological pH by Cu2+.
@nl
type
label
pH-dependent association of fa ...... y at physiological pH by Cu2+.
@en
pH-dependent association of fa ...... y at physiological pH by Cu2+.
@nl
prefLabel
pH-dependent association of fa ...... y at physiological pH by Cu2+.
@en
pH-dependent association of fa ...... y at physiological pH by Cu2+.
@nl
P2093
P2860
P1476
pH-dependent association of fa ...... y at physiological pH by Cu2+.
@en
P2093
Charles Ansong
Fatbardha Varfaj
Hironao Wakabayashi
Keiji Nogami
Philip J Fay
Stephen Miles
P2860
P304
P356
10.1016/J.BBAPAP.2006.04.004
P577
2006-04-22T00:00:00Z