Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1
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Protein Allostery and Conformational Dynamics.Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases.The Exact Nuclear Overhauser Enhancement: Recent Advances.Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAblNeighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding.Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study.A Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1.
P2860
Q37232244-3760358A-2FCC-42DB-86EA-4F3F91DFB982Q37704650-C5B0D864-D562-46CE-BCB4-52AD220435F3Q38657706-6230E5F1-138E-4B76-85F9-AA695CDE1CD1Q39223642-76C152D9-8E1B-43ED-931A-6E327677566CQ39240086-F3AE26C8-1598-4AA2-B6A4-05EB45C4BC06Q42717863-B8C4C6FF-5934-4B69-B04B-55D7DCF57D08Q48183849-E7562EEE-335C-4ADF-B83F-1E5EA7B9F5CA
P2860
Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1
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2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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name
Negative Regulation of Peptidy ...... erdomain Contact in Human Pin1
@ast
Negative Regulation of Peptidy ...... erdomain Contact in Human Pin1
@en
type
label
Negative Regulation of Peptidy ...... erdomain Contact in Human Pin1
@ast
Negative Regulation of Peptidy ...... erdomain Contact in Human Pin1
@en
prefLabel
Negative Regulation of Peptidy ...... erdomain Contact in Human Pin1
@ast
Negative Regulation of Peptidy ...... erdomain Contact in Human Pin1
@en
P2093
P2860
P1433
P1476
Negative Regulation of Peptidy ...... erdomain Contact in Human Pin1
@en
P2093
Brendan J Mahoney
Jeffrey W Peng
John S Zintsmaster
Meiling Zhang
Xingsheng Wang
P2860
P304
P356
10.1016/J.STR.2015.08.019
P577
2015-10-15T00:00:00Z