(Q44746385)

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The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner

scientific article published in February 2004

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scholarly article

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Europe PubMed Central

5 December 2017

The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner (English)

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Europe PubMed Central

5 December 2017

protein folding

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Jean-Marie Bourhis

1

object named as

Jean-Marie Bourhis

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Véronique Receveur-Bréchot

3

object named as

Véronique Receveur-Bréchot

0 references

6

object named as

Bruno Canard

1 reference

Europe PubMed Central

5 December 2017

7

object named as

Sonia Longhi

1 reference

Europe PubMed Central

5 December 2017

Kenth Johansson

2

object named as

Kenth Johansson

1 reference

Europe PubMed Central

5 December 2017

Véronique Receveur-Bréchot

3

object named as

Véronique Receveur-Bréchot

1 reference

Europe PubMed Central

5 December 2017

author name string

Christopher J Oldfield

4

1 reference

Europe PubMed Central

5 December 2017

Keith A Dunker

5

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Europe PubMed Central

5 December 2017

publication date

1 February 2004

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Europe PubMed Central

5 December 2017

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Europe PubMed Central

5 December 2017

99

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Europe PubMed Central

5 December 2017

157-167

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Europe PubMed Central

5 December 2017

2

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Europe PubMed Central

5 December 2017

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

1 reference

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Significant differences in nucleocapsid morphology within the Paramyxoviridae

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High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product

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Evolutionary rate heterogeneity in proteins with long disordered regions.

1 reference

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The carboxy-terminal domain of Sendai virus nucleocapsid protein is involved in complex formation between phosphoprotein and nucleocapsid-like particles

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Expression of measles virus nucleoprotein in Escherichia coli: use of deletion mutants to locate the antigenic sites

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Nucleocapsid incorporation into parainfluenza virus is regulated by specific interaction with matrix protein

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Determinants of the polyproline II helix from modeling studies

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JPred: a consensus secondary structure prediction server

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Reexamination of the Sendai virus P protein domains required for RNA synthesis: a possible supplemental role for the P protein

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FlgM gains structure in living cells

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Structural and functional analysis of sendai virus nucleocapsid protein NP with monoclonal antibodies

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Intrinsically disordered protein

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The protein trinity--linking function and disorder.

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Coupling of folding and binding for unstructured proteins

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The helical hydrophobic moment: a measure of the amphiphilicity of a helix

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Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures

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Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate.

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Antigenic analysis of African measles virus field isolates: identification and localisation of one conserved and two variable epitope sites on the NP protein

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Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself

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Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration

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The relationship of conformational changes in the sendai virus nucleocapsid to proteolytic cleavage of the NP polypeptide

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Transcriptional activator-coactivator recognition: nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding

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Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm

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From proteases to proteomics

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Substitution of two residues in the measles virus nucleoprotein results in an impaired self-association

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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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Structural disorder and modular organization in Paramyxovirinae N and P.

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Urea-induced conformational changes in cold- and heat-denatured states of a protein, Streptomyces subtilisin inhibitor

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Measles virus (MV) nucleoprotein binds to a novel cell surface receptor distinct from FcgammaRII via its C-terminal domain: role in MV-induced immunosuppression

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Protein interaction domains of the measles virus nucleocapsid protein (NP).

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Loopy proteins appear conserved in evolution.

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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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Mechanism of measles virus-induced suppression of inflammatory immune responses.

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Host cell proteins required for measles virus reproduction

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Helix propensities are identical in proteins and peptides

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A highly conserved region of the Sendai virus nucleocapsid protein contributes to the NP-NP binding domain

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

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Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright

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Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering

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Measles virus nucleocapsid protein binds to FcgammaRII and inhibits human B cell antibody production

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Sequence complexity of disordered protein

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Separate domains of Sendai virus P protein are required for binding to viral nucleocapsids

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Antibodies to paramyxovirus nucleoproteins define regions important for immunogenicity and nucleocapsid assembly

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The assembly of the measles virus nucleoprotein into nucleocapsid-like particles is modulated by the phosphoprotein

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Poly(pro)II helices in globular proteins: identification and circular dichroic analysis

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Intrinsically unstructured proteins

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Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule.

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Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.

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Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein

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A role for the Sendai virus P protein trimer in RNA synthesis

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10.1016/J.VIRUSRES.2003.11.007

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Europe PubMed Central

5 December 2017

1 reference

Europe PubMed Central

5 December 2017

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