Multiple conformations of the nucleotide site of Kinesin family motors in the triphosphate state
about
Plant Kinesin-Like Calmodulin Binding Protein Employs Its Regulatory Domain for DimerizationExamining kinesin processivity within a general gating framework.The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.EPR spectra and molecular dynamics agree that the nucleotide pocket of myosin V is closed and that it opens on binding actin.
P2860
Multiple conformations of the nucleotide site of Kinesin family motors in the triphosphate state
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Multiple conformations of the ...... tors in the triphosphate state
@en
Multiple conformations of the ...... tors in the triphosphate state
@nl
type
label
Multiple conformations of the ...... tors in the triphosphate state
@en
Multiple conformations of the ...... tors in the triphosphate state
@nl
prefLabel
Multiple conformations of the ...... tors in the triphosphate state
@en
Multiple conformations of the ...... tors in the triphosphate state
@nl
P2093
P2860
P1476
Multiple conformations of the ...... tors in the triphosphate state
@en
P2093
Adam Larson
Edward Pate
Nariman Naber
Roger Cooke
Sarah Rice
P2860
P304
P356
10.1016/J.JMB.2011.01.001
P407
P577
2011-01-26T00:00:00Z