Measles Virus Forms Inclusion Bodies with Properties of Liquid Organelles (original) (raw)

Upon Infection the Cellular WD Repeat-containing Protein 5 (WDR5) Localizes to Cytoplasmic Inclusion Bodies and Enhances Measles Virus Replication

Roberto Cattaneo

Journal of virology, 2017

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Structural disorder within the replicative complex of measles virus: Functional implications

Sonia Longhi

Virology, 2006

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Sequence of events in measles virus replication: role of phosphoprotein-nucleocapsid interactions

Sonia Longhi

Journal of virology, 2014

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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

Kenth Hallberg

Journal of Biological Chemistry, 2003

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Intrinsic disorder in measles virus nucleocapsids

Stefano Longhi

Proceedings of the National Academy of Sciences, 2011

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Measles virus M and F proteins associate with detergent-resistant membrane fractions and promote formation of virus-like particles

Georg Krohne

Journal of General Virology, 2007

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Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus

Sonia Longhi

The Journal of biological chemistry, 2012

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Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum

Roberto Cattaneo

Journal of Biological Chemistry, 2001

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Measles Virus Assembly within Membrane Rafts

Serge Manié

Journal of Virology, 2000

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Measles virus induces persistent infection by autoregulation of viral replication

Chieko Kai

Scientific reports, 2016

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Structural and mechanistic studies of measles virus illuminate paramyxovirus entry

Richard Plemper, Ronald Iorio

PLoS pathogens, 2011

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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

Kenth Hallberg

Journal of Biological Chemistry, 2003

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

Gavin Wilkinson

Journal of General Virology, 1993

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The Measles Virus Nucleocapsid Protein Tail Domain Is Dispensable for Viral Polymerase Recruitment and Activity

Richard Plemper

Journal of Biological Chemistry, 2013

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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

herve darbon

Protein Science, 2005

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Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions

Juha Huiskonen

Proceedings of the National Academy of Sciences, 2011

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Phosphorylation of Measles Virus Nucleoprotein Affects Viral Growth by Changing Gene Expression and Genomic RNA Stability

Chieko Kai

Journal of Virology, 2013

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Strength of Envelope Protein Interaction Modulates Cytopathicity of Measles Virus

Roberto Cattaneo

Journal of Virology, 2002

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Long Untranslated Regions of the Measles Virus M and F Genes Control Virus Replication and Cytopathogenicity

Shinji Ohno

Journal of Virology, 2005

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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

Sonia Longhi

Virus Research, 2004

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Substitution of Two Residues in the Measles Virus Nucleoprotein Results in an Impaired Self-Association

Sonia Longhi

Virology, 2002

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Measles Virus Phosphoprotein Gene Products: Conformational Flexibility of the P/V Protein Amino-Terminal Domain and C Protein Infectivity Factor Function

Patricia Devaux

Journal of Virology, 2004

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Measles virus glycoprotein complexes preassemble intracellularly and relax during transport to the cell surface in preparation for fusion

Richard Plemper

Journal of virology, 2015

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Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence

Roberto Cattaneo

Journal of virology, 1998

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Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm

Erling Norrby, Roberto Cattaneo

Virology, 1991

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IgA targeting on the α-molecular recognition element (α-MoRE) of viral phosphoprotein inhibits measles virus replication by interrupting formation and function of P-N complex intracellularly

Jingyi Yang

Antiviral Research, 2018

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Complex Dynamic Development of Poliovirus Membranous Replication Complexes

Vinod Nair

Journal of Virology, 2011

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The feet of the measles virus polymerase bind the viral nucleocapsid protein at a single site

Richard Kingston

Protein science : a publication of the Protein Society, 2010

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Reovirus Forms Neo-Organelles for Progeny Particle Assembly within Reorganized Cell Membranes

Bernardo Mainou

mBio, 2014

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Infective substructures of measles virus from acutely and persistently infected cells

Shmuel Rozenblatt

Journal of Virology, 1979

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Inefficient Measles Virus Budding in Murine L.CD46 Fibroblasts

Serge Manié

Virology, 1999

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Probing the Spatial Organization of Measles Virus Fusion Complexes

Richard Plemper

Journal of Virology, 2009

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CD46-MEDIATED Measles-Virus Entry - a First Key to Host-Range Specificity

Patricia Devaux

Trends in Microbiology, 1995

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The C Protein Is Recruited to Measles Virus Ribonucleocapsids by the Phosphoprotein

Roberto Cattaneo

Journal of Virology, 2019

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Measles Virus Matrix Protein Inhibits Host Cell Transcription

Reena Ghildyal

PLOS ONE, 2016

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