Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
about
Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virusCrystal Structure of the Nipah Virus Phosphoprotein Tetramerization DomainCoiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative exampleExploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy.Structural disorder within paramyxoviral nucleoproteinsDetecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteinsPlasticity 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.Molecular dynamics simulation in virus research.Characterization of a viral phosphoprotein binding site on the surface of the respiratory syncytial nucleoprotein.Critical phosphoprotein elements that regulate polymerase architecture and function in vesicular stomatitis virusMultiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.Functional correlations of respiratory syncytial virus proteins to intrinsic disorder.Fuzziness endows viral motif-mimicry.Partially disordered structure in intravirus coat protein of potyvirus potato virus A.Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling.An amino acid of human parainfluenza virus type 3 nucleoprotein is critical for template function and cytoplasmic inclusion body formation.Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy.The glutamic residue at position 402 in the C-terminus of Newcastle disease virus nucleoprotein is critical for the virus.Interfacial Properties of NTAIL, an Intrinsically Disordered Protein.Structure of the paramyxovirus PIV5 nucleoprotein in complex with an amino-terminal peptide of the phosphoprotein.SimLabel: a graphical user interface to simulate continuous wave EPR spectra from site-directed spin labeling experiments.The Unstructured Paramyxovirus Nucleocapsid Protein Tail Domain Modulates Viral Pathogenesis through Regulation of Transcriptase Activity.Initiation, extension, and termination of RNA synthesis by a paramyxovirus polymerase.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function
P2860
Q21131369-E15461C2-9B84-45CD-A7E9-0CEA6740FEFCQ27680451-46A2E768-6D0E-4A72-8E3D-EA44E21658FAQ27690688-44583AC4-0EDD-4BAE-A0B9-565CEC717744Q27692089-FA5FAC6E-FEEE-4CAE-80B9-488648CCFB14Q28080740-1E4C72CE-841A-4510-8F6A-ECDE21BD1AACQ34189305-3FBB6C54-C9CC-4476-A8DD-6C77D3B6C16DQ35874419-2DB6003A-8D5E-47C9-BA8E-788CF23A2DE9Q35902551-4D2E0312-BEF4-4443-8459-D102BFA0F9CAQ36104304-094BF8C5-BFC7-4DA1-90EB-C5BBB5977606Q36171959-854C277B-97E9-49B5-92D4-410C1672C506Q36221929-2F026174-6BB7-4491-81BA-018D7070AFD9Q37218609-A768F963-2DA2-4055-9A81-09A71C435F93Q37624303-A17CC0A7-AAD8-4467-8775-43FE722FDAC1Q38732930-28D65DB3-3A07-41F0-815D-31BD54BED211Q40721101-A42F2236-3860-4F6F-B189-8F7258CCFF06Q41469393-7C792108-3786-4894-9CC4-C94DC38356DAQ42028176-9E5198DA-8F96-407D-A40E-FD5C6E68537DQ42176887-6C18521E-DC13-4739-B1DA-A41C40096116Q42270304-5D81E546-8DBD-40A2-BC66-5203B05E49D7Q43638249-4B08B249-D28D-41EB-8B73-E48AF7D805ADQ47096139-DA20F8B2-B7FB-4D1A-A4B5-794A1E31AE92Q47270597-94CB53C8-90FB-48E0-B76C-537457625F0CQ47296321-6A9F2965-ACBC-42D5-9554-E615801438DBQ48360604-598D6562-D1A4-47E5-A166-F853FF8FB1DEQ50043355-955C21AD-AFE9-4068-ACEF-B86C20851934Q50099241-E5016400-9143-4EAE-9D7C-D77D4730A630Q50922689-D11096D1-72AC-46D1-8016-FF6D25DB834BQ54348285-2F12FD5E-1FDC-48C3-9095-F187C7983EA7Q58722689-7AB5D3F4-E3E5-4439-8E48-7C06F945D586
P2860
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
@en
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
@nl
type
label
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
@en
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
@nl
altLabel
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins
@en
prefLabel
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
@en
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
@nl
P2860
P356
P1433
P1476
Structural disorder within paramyxovirus nucleoproteins and phosphoproteins.
@en
P2093
Johnny Habchi
Sonia Longhi
P2860
P356
10.1039/C1MB05204G
P407
P577
2011-08-01T00:00:00Z