Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
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Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virusOrganization, Function, and Therapeutic Targeting of the Morbillivirus RNA-Dependent RNA Polymerase ComplexStructure of the Nucleocapsid-Binding Domain from the Mumps Virus Polymerase; an Example of Protein Folding Induced by CrystallizationInteraction between the C-terminal domains of N and P proteins of measles virus investigated by NMRStructure of the Nucleoprotein Binding Domain of Mokola Virus PhosphoproteinStructure of the Dimerization Domain of the Rabies Virus PhosphoproteinStructure of the Tetramerization Domain of Measles Virus PhosphoproteinStructure of the C-Terminal Domain of Lettuce Necrotic Yellows Virus PhosphoproteinProtein domain definition should allow for conditional disorderSolution and Crystallographic Structures of the Central Region of the Phosphoprotein from Human MetapneumovirusCoiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative exampleStructural disorder within paramyxoviral nucleoproteinsStructural basis for the attachment of a paramyxoviral polymerase to its template.Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.Conformational analysis of the partially disordered measles virus N(TAIL)-XD complex by SDSL EPR spectroscopy.Peste des petits ruminants virus infection of small ruminants: a comprehensive review.Expression of measles virus nucleoprotein induces apoptosis and modulates diverse functional proteins in cultured mammalian cellsProbing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteinesOne-step generation of error-prone PCR libraries using Gateway® technology.Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteinsA single codon in the nucleocapsid protein C terminus contributes to in vitro and in vivo fitness of Edmonston measles virus.Characterization of the interactions between the nucleoprotein and the phosphoprotein of HenipavirusIntrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Intrinsic disorder in measles virus nucleocapsids.Dividing to unveil protein microheterogeneities: traveling wave ion mobility studyPlasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.Crystal Structure of the Measles Virus Nucleoprotein Core in Complex with an N-Terminal Region of Phosphoprotein.Viral proteomics.Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.Measles virus phosphoprotein gene products: conformational flexibility of the P/V protein amino-terminal domain and C protein infectivity factor functionThe structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy.Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins.The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.
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P2860
Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Crystal structure of the measl ...... al domain of the nucleoprotein
@ast
Crystal structure of the measl ...... al domain of the nucleoprotein
@en
Crystal structure of the measl ...... al domain of the nucleoprotein
@nl
type
label
Crystal structure of the measl ...... al domain of the nucleoprotein
@ast
Crystal structure of the measl ...... al domain of the nucleoprotein
@en
Crystal structure of the measl ...... al domain of the nucleoprotein
@nl
prefLabel
Crystal structure of the measl ...... al domain of the nucleoprotein
@ast
Crystal structure of the measl ...... al domain of the nucleoprotein
@en
Crystal structure of the measl ...... al domain of the nucleoprotein
@nl
P2093
P2860
P50
P3181
P356
P1476
Crystal structure of the measl ...... al domain of the nucleoprotein
@en
P2093
Kenth Johansson
Sonia Longhi
Valerie Campanacci
P2860
P304
P3181
P356
10.1074/JBC.M308745200
P407
P577
2003-11-07T00:00:00Z