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TRIM22: A Diverse and Dynamic Antiviral Protein

The tripartite motif (TRIM) family of proteins is an evolutionarily ancient group of proteins with homologues identified in both invertebrate and vertebrate species. Human TRIM22 is one such protein that has a dynamic evolutionary history that includes gene expansion, gene loss, and strong signature...

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Detalles Bibliográficos
Autores principales: Hattlmann, Clayton J., Kelly, Jenna N., Barr, Stephen D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356915/
https://www.ncbi.nlm.nih.gov/pubmed/22649727
http://dx.doi.org/10.1155/2012/153415
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author Hattlmann, Clayton J.
Kelly, Jenna N.
Barr, Stephen D.
author_facet Hattlmann, Clayton J.
Kelly, Jenna N.
Barr, Stephen D.
author_sort Hattlmann, Clayton J.
collection PubMed
description The tripartite motif (TRIM) family of proteins is an evolutionarily ancient group of proteins with homologues identified in both invertebrate and vertebrate species. Human TRIM22 is one such protein that has a dynamic evolutionary history that includes gene expansion, gene loss, and strong signatures of positive selection. To date, TRIM22 has been shown to restrict the replication of a number of viruses, including encephalomyocarditis virus (EMCV), hepatitis B virus (HBV), and human immunodeficiency virus type 1 (HIV-1). In addition, TRIM22 has also been implicated in cellular differentiation and proliferation and may play a role in certain cancers and autoimmune diseases. This comprehensive paper summarizes our current understanding of TRIM22 structure and function.
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spelling pubmed-33569152012-05-30 TRIM22: A Diverse and Dynamic Antiviral Protein Hattlmann, Clayton J. Kelly, Jenna N. Barr, Stephen D. Mol Biol Int Review Article The tripartite motif (TRIM) family of proteins is an evolutionarily ancient group of proteins with homologues identified in both invertebrate and vertebrate species. Human TRIM22 is one such protein that has a dynamic evolutionary history that includes gene expansion, gene loss, and strong signatures of positive selection. To date, TRIM22 has been shown to restrict the replication of a number of viruses, including encephalomyocarditis virus (EMCV), hepatitis B virus (HBV), and human immunodeficiency virus type 1 (HIV-1). In addition, TRIM22 has also been implicated in cellular differentiation and proliferation and may play a role in certain cancers and autoimmune diseases. This comprehensive paper summarizes our current understanding of TRIM22 structure and function. Hindawi Publishing Corporation 2012 2012-05-08 /pmc/articles/PMC3356915/ /pubmed/22649727 http://dx.doi.org/10.1155/2012/153415 Text en Copyright © 2012 Clayton J. Hattlmann et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Hattlmann, Clayton J.
Kelly, Jenna N.
Barr, Stephen D.
TRIM22: A Diverse and Dynamic Antiviral Protein
title TRIM22: A Diverse and Dynamic Antiviral Protein
title_full TRIM22: A Diverse and Dynamic Antiviral Protein
title_fullStr TRIM22: A Diverse and Dynamic Antiviral Protein
title_full_unstemmed TRIM22: A Diverse and Dynamic Antiviral Protein
title_short TRIM22: A Diverse and Dynamic Antiviral Protein
title_sort trim22: a diverse and dynamic antiviral protein
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356915/
https://www.ncbi.nlm.nih.gov/pubmed/22649727
http://dx.doi.org/10.1155/2012/153415
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