Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site.
about
Host-Pathogen Interactions in Measles Virus Replication and Anti-Viral ImmunityStructural disorder within paramyxoviral nucleoproteinsRIG-I self-oligomerization is either dispensable or very transient for signal transduction.Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.
P2860
Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site.
description
2012 nî lūn-bûn
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name
Interaction between the C-term ...... lex implying one binding site.
@en
type
label
Interaction between the C-term ...... lex implying one binding site.
@en
prefLabel
Interaction between the C-term ...... lex implying one binding site.
@en
P2093
P2860
P356
P1433
P1476
Interaction between the C-term ...... lex implying one binding site.
@en
P2093
Anthony Doizy
David Blocquel
Johnny Habchi
Michael Oglesbee
Sonia Longhi
Stéphanie Costanzo
P2860
P304
P356
10.1002/PRO.2138
P577
2012-09-17T00:00:00Z