Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR
about
Structure of the Nucleoprotein Binding Domain of Mokola Virus PhosphoproteinStructural 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.Probing 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.Characterization of the interactions between the nucleoprotein and the phosphoprotein of HenipavirusDividing to unveil protein microheterogeneities: traveling wave ion mobility studyElectron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.The 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.Roles of intrinsic disorder in protein-nucleic acid interactions.Newly identified minor phosphorylation site threonine-279 of measles virus nucleoprotein is a prerequisite for nucleocapsid formation.Phosphorylation of measles virus nucleoprotein affects viral growth by changing gene expression and genomic RNA stability.The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein.Nipah and Hendra Virus Nucleoproteins Inhibit Nuclear Accumulation of Signal Transducer and Activator of Transcription 1 (STAT1) and STAT2 by Interfering with Their Complex Formation.The feet of the measles virus polymerase bind the viral nucleocapsid protein at a single site.Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain.Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site.Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling.Dynamics of the intrinsically disordered C-terminal domain of the nipah virus nucleoprotein and interaction with the x domain of the phosphoprotein as unveiled by NMR spectroscopy.Phosphorylation of measles virus phosphoprotein at S86 and/or S151 downregulates viral transcriptional activity.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.
P2860
Q27658139-3B9FD615-8F12-4CB5-97FC-A2266DB9E2BCQ33640276-3E0114E5-0813-4E54-8D74-9499A5D62E89Q33767753-13D87CAA-7D8C-402E-BA42-B9D394E27599Q34098982-00D21B5C-E881-4712-8B34-ED7B3AA387F8Q34144831-900FF801-EB16-426F-8F26-A09746FB2E40Q34787399-392A9F9E-A18A-42EF-86CD-0EE8E13196CCQ35250293-A018C81A-373B-499E-AC89-451B0D48B501Q35518621-A683B1E6-CDF4-4109-B7A6-10613543E884Q35874419-4D52E03C-F892-46E6-ACE8-CF186865FEB2Q36218409-D2D92A90-701C-4D23-830E-4C3EBD031918Q37624303-4E2BFB7E-0E8F-4DEF-BEF7-C818CAB18AC4Q37847124-AE9CD8EA-3CB6-4342-892E-827869E55440Q37909067-F5047C38-88ED-4953-AF46-6A0F9C7CACF1Q37923321-CF96D674-123C-4A90-8874-D527608EA0C6Q39066362-8363AC62-13F0-4F96-948A-41A927700976Q39106893-B7A3E1AB-C24E-40E1-BD89-8E3F025FC3E1Q39816466-238F08A2-7C1C-4273-86D2-86364715C2D2Q40072967-8F73990E-2FF7-4DD6-9023-E37706595DB9Q40455192-5132509E-4CEA-4E1D-BFC7-10FF25C3C95FQ40839713-0BA65027-C101-4E8F-900D-3C545C4E7527Q41814829-8605FCA5-6591-4A5E-A561-80BF73036E32Q42176887-9AF59AF0-3A7B-4160-8DBD-B8056EE1DC75Q42177256-E85DC49C-D518-41A2-AEE5-EBE6179DA792Q45354561-C9D9AA91-8657-4642-8921-8CEFCB60C15BQ50922689-645EE2C9-FA51-4F67-AE4C-ABC0E4FF70F0
P2860
Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
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
name
Interaction between the C-term ...... sles virus investigated by NMR
@ast
Interaction between the C-term ...... sles virus investigated by NMR
@en
Interaction between the C-term ...... sles virus investigated by NMR
@nl
type
label
Interaction between the C-term ...... sles virus investigated by NMR
@ast
Interaction between the C-term ...... sles virus investigated by NMR
@en
Interaction between the C-term ...... sles virus investigated by NMR
@nl
prefLabel
Interaction between the C-term ...... sles virus investigated by NMR
@ast
Interaction between the C-term ...... sles virus investigated by NMR
@en
Interaction between the C-term ...... sles virus investigated by NMR
@nl
P2093
P2860
P1433
P1476
Interaction between the C-term ...... sles virus investigated by NMR
@en
P2093
Cedric Bernard
Hervé Darbon
Sonia Longhi
Stéphane Gely
P2860
P304
P356
10.1016/J.FEBSLET.2009.03.004
P407
P577
2009-04-02T00:00:00Z