Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
about
Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerizationFunctional states of homooligomers: insights from the evolution of glycosyltransferases.Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric statesComposite structural motifs of binding sites for delineating biological functions of proteins.Robust and accurate prediction of protein self-interactions from amino acids sequence using evolutionary information.SPAR: a random forest-based predictor for self-interacting proteins with fine-grained domain information.Computational methods using weighed-extreme learning machine to predict protein self-interactions with protein evolutionary information.Conformationally constrained sequence designs to bias monomer-dimer equilibriums in TASP systems.
P2860
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P2860
Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Alteration of oligomeric state ...... rolase with the same scaffold.
@en
Alteration of oligomeric state ...... rolase with the same scaffold.
@nl
type
label
Alteration of oligomeric state ...... rolase with the same scaffold.
@en
Alteration of oligomeric state ...... rolase with the same scaffold.
@nl
prefLabel
Alteration of oligomeric state ...... rolase with the same scaffold.
@en
Alteration of oligomeric state ...... rolase with the same scaffold.
@nl
P2093
P2860
P356
P1433
P1476
Alteration of oligomeric state ...... rolase with the same scaffold.
@en
P2093
Akinori Kidera
Motonori Ota
Ryotaro Koike
P2860
P304
P356
10.1002/PRO.218
P577
2009-10-01T00:00:00Z