Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction

Pin 1 is an enzyme that specifically catalyzes the cis–trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by...

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Detalles Bibliográficos
Autores principales: Kojima, Yoshitsugu, Ryo, Akihide
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2010
Materias:
Microbiology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3125566/
https://www.ncbi.nlm.nih.gov/pubmed/21738521
http://dx.doi.org/10.3389/fmicb.2010.00107
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author Kojima, Yoshitsugu
Ryo, Akihide
author_facet Kojima, Yoshitsugu
Ryo, Akihide
author_sort Kojima, Yoshitsugu
collection PubMed
description Pin 1 is an enzyme that specifically catalyzes the cis–trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by a host factor Pin1. Pin1 is now positioned as an important modulator of the molecular crosstalk between virus and host cells and could be a unique target for anti-virus therapy. This new type of post-translational modification by Pin1 might be involved in the regulation of other viral proteins.
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spelling pubmed-31255662011-07-07 Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction Kojima, Yoshitsugu Ryo, Akihide Front Microbiol Microbiology Pin 1 is an enzyme that specifically catalyzes the cis–trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by a host factor Pin1. Pin1 is now positioned as an important modulator of the molecular crosstalk between virus and host cells and could be a unique target for anti-virus therapy. This new type of post-translational modification by Pin1 might be involved in the regulation of other viral proteins. Frontiers Research Foundation 2010-09-09 /pmc/articles/PMC3125566/ /pubmed/21738521 http://dx.doi.org/10.3389/fmicb.2010.00107 Text en Copyright© 2010 Kojima and Ryo. http://www.frontiersin.org/licenseagreement This is an open-access article subject to an exclusive license agreement between the authors and the Frontiers Research Foundation, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are credited.
spellingShingle Microbiology
Kojima, Yoshitsugu
Ryo, Akihide
Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction
title Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction
title_full Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction
title_fullStr Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction
title_full_unstemmed Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction
title_short Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction
title_sort pinning down viral proteins: a new prototype for virus–host cell interaction
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3125566/
https://www.ncbi.nlm.nih.gov/pubmed/21738521
http://dx.doi.org/10.3389/fmicb.2010.00107
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