Towards understanding the crosstalk between protein post-translational modifications: Homo- and heterotypic PTM pair distances on protein surfaces are not random.
about
Docking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP)-Insights into a noncanonical and fuzzy interaction.Co-occurring protein phosphorylation are functionally associated.Dissecting Structure-Encoded Determinants of Allosteric Cross-Talk between Post-Translational Modification Sites in the Hsp90 Chaperones.Estimating the Distribution of Protein Post-Translational Modification States by Mass Spectrometry
P2860
Towards understanding the crosstalk between protein post-translational modifications: Homo- and heterotypic PTM pair distances on protein surfaces are not random.
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2016 nî lūn-bûn
@nan
2016 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
Towards understanding the cros ...... otein surfaces are not random.
@ast
Towards understanding the cros ...... otein surfaces are not random.
@en
type
label
Towards understanding the cros ...... otein surfaces are not random.
@ast
Towards understanding the cros ...... otein surfaces are not random.
@en
prefLabel
Towards understanding the cros ...... otein surfaces are not random.
@ast
Towards understanding the cros ...... otein surfaces are not random.
@en
P2860
P356
P1433
P1476
Towards understanding the cros ...... otein surfaces are not random.
@en
P2093
Dirk Walther
Paula Korkuć
P2860
P356
10.1002/PROT.25200
P407
P577
2016-11-01T00:00:00Z