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Crystal structure of the kinesin motor domain reveals a structural similarity to myosinThe structural basis of the myosin ATPase activityStructural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction.Is myosin a "back door" enzyme?Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathyFunctionally similar vanadate-induced 8-azidoadenosine 5'-[alpha-(32)P]Diphosphate-trapped transition state intermediates of human P-glycoprotin are generated in the absence and presence of ATP hydrolysis.P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site.Chemical identification of serine 181 at the ATP-binding site of myosin as a residue esterified selectively by the fluorescent reagent 9-anthroylnitrile.
P2860
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P2860
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
name
Photochemical mapping of the active site of myosin.
@ast
Photochemical mapping of the active site of myosin.
@en
type
label
Photochemical mapping of the active site of myosin.
@ast
Photochemical mapping of the active site of myosin.
@en
prefLabel
Photochemical mapping of the active site of myosin.
@ast
Photochemical mapping of the active site of myosin.
@en
P2093
P356
P1476
Photochemical mapping of the active site of myosin.
@en
P2093
P304
55-60; discussion 60-1
P356
10.1098/RSTB.1992.0044
P407
P577
1992-04-01T00:00:00Z