Probing conformational and functional substates of calmodulin by high pressure FTIR spectroscopy: influence of Ca2+ binding and the hypervariable region of K-Ras4B.
about
Flexible-body motions of calmodulin and the farnesylated hypervariable region yield a high-affinity interaction enabling K-Ras4B membrane extraction.Phosphorylated Calmodulin Promotes PI3K Activation by Binding to the SH2 Domains.A high pressure study of calmodulin-ligand interactions using small-angle X-ray and elastic incoherent neutron scattering.
P2860
Probing conformational and functional substates of calmodulin by high pressure FTIR spectroscopy: influence of Ca2+ binding and the hypervariable region of K-Ras4B.
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
@wuu
2016年学术文章
@zh
2016年学术文章
@zh-cn
2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
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2016年學術文章
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2016年學術文章
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name
Probing conformational and fun ...... pervariable region of K-Ras4B.
@en
Probing conformational and fun ...... pervariable region of K-Ras4B.
@nl
type
label
Probing conformational and fun ...... pervariable region of K-Ras4B.
@en
Probing conformational and fun ...... pervariable region of K-Ras4B.
@nl
prefLabel
Probing conformational and fun ...... pervariable region of K-Ras4B.
@en
Probing conformational and fun ...... pervariable region of K-Ras4B.
@nl
P2860
P356
P1476
Probing conformational and fun ...... pervariable region of K-Ras4B.
@en
P2093
Nelli Erwin
Roland Winter
P2860
P304
30020-30028
P356
10.1039/C6CP06553H
P407
P577
2016-10-24T00:00:00Z