Cooperative fluctuations point to the dimerization interface of p53 core domain.
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Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family membersProbing potential binding modes of the p53 tetramer to DNA based on the symmetries encoded in p53 response elements.Comparative Study of Elastic Network Model and Protein Contact Network for Protein Complexes: The Hemoglobin Case.Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis.
P2860
Cooperative fluctuations point to the dimerization interface of p53 core domain.
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2006 nî lūn-bûn
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2006年の論文
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Cooperative fluctuations point to the dimerization interface of p53 core domain.
@en
type
label
Cooperative fluctuations point to the dimerization interface of p53 core domain.
@en
prefLabel
Cooperative fluctuations point to the dimerization interface of p53 core domain.
@en
P2093
P2860
P1433
P1476
Cooperative fluctuations point to the dimerization interface of p53 core domain.
@en
P2093
Nigar Kantarci
Pemra Doruker
Turkan Haliloglu
P2860
P304
P356
10.1529/BIOPHYSJ.106.077800
P407
P577
2006-07-01T00:00:00Z