Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution (Q27643183)

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Nicolas Tarbouriech

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Peter Timmins

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Wilhelm P Burmeister

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Rob W H Ruigrok

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Dominique Marion

The 5′ terminal structure of the methylated mRNA synthesized in vitro by vesicular stomatitis virus

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language of work or name

English

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publication date

20 February 2004

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published in

Virology

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volume

319

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issue

2

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page(s)

201-11

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cites work

1 reference

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Domains of the measles virus N protein required for binding to P protein and self-assembly

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Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics

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Accurate measurement of small spin-spin couplings in partially aligned molecules using a novel J-mismatch compensated spin-state-selection filter.

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Backbone Dynamics and Structural Characterization of the Partially Folded A State of Ubiquitin by 1H, 13C, and 15N Nuclear Magnetic Resonance Spectroscopy

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The CCP4 suite: programs for protein crystallography

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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An acidic activation-like domain of the Sendai virus P protein is required for RNA synthesis and encapsidation

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Paramyxovirus phosphoproteins form homotrimers as determined by an epitope dilution assay, via predicted coiled coils

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

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Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr

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De novo determination of protein structure by NMR using orientational and long-range order restraints

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Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids

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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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Improved methods for building protein models in electron density maps and the location of errors in these models

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The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins

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The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein

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NMR structure of the bovine prion protein

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Assignment of the 1H, 15N and 13C resonances of the nucleocapsid-binding domain of the Sendai virus phosphoprotein.

7 January 2021

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Identification of nucleocapsid protein residues required for Sendai virus nucleocapsid formation and genome replication

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Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy

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Refinement of local and long-range structural order in theophylline-binding RNA using (13)C-(1)H residual dipolar couplings and restrained molecular dynamics

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Deletion analysis defines a carboxyl-proximal region of Sendai virus P protein that binds to the polymerase L protein

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On the domain structure and the polymerization state of the sendai virus P protein

7 January 2021

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Tetrameric coiled coil domain of Sendai virus phosphoprotein

7 January 2021

1 reference

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The C-terminal 88 amino acids of the Sendai virus P protein have multiple functions separable by mutation

7 January 2021

1 reference

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

7 January 2021

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Dissection of individual functions of the Sendai virus phosphoprotein in transcription

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/J.VIROL.2003.10.029

inferred from DOI database lookup

7 January 2021

based on heuristic

The Sendai virus nucleocapsid exists in at least four different helical states

1 reference

https://api.crossref.org/works/10.1016/J.VIROL.2003.10.029

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VIROL.2003.10.029

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Fatcat ID

release_4d2az26d5jazxhmrtkjzbxw4dm

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/4d2az26d5jazxhmrtkjzbxw4dm