Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis

Intrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival proteins of the B-cell lymphoma-2 (Bcl-2) family. Members of this family are either intrinsically disordered or contain intrinsically disordered regions/domains that are critical to their function. Alternate splic...

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Detalles Bibliográficos
Autores principales: Rautureau, Gilles J. P., Day, Catherine L., Hinds, Mark G.
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2010
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2871139/
https://www.ncbi.nlm.nih.gov/pubmed/20480043
http://dx.doi.org/10.3390/ijms11041808
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author Rautureau, Gilles J. P.
Day, Catherine L.
Hinds, Mark G.
author_facet Rautureau, Gilles J. P.
Day, Catherine L.
Hinds, Mark G.
author_sort Rautureau, Gilles J. P.
collection PubMed
description Intrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival proteins of the B-cell lymphoma-2 (Bcl-2) family. Members of this family are either intrinsically disordered or contain intrinsically disordered regions/domains that are critical to their function. Alternate splicing and post-translational modifications can determine the extent of these disordered regions and are critical for regulating Bcl-2 proteins. Conformational plasticity and structural transitions characterize the interactions within the Bcl-2 family, with conserved sequence motifs on both binding partners required for their molecular recognition.
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spelling pubmed-28711392010-05-17 Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis Rautureau, Gilles J. P. Day, Catherine L. Hinds, Mark G. Int J Mol Sci Review Intrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival proteins of the B-cell lymphoma-2 (Bcl-2) family. Members of this family are either intrinsically disordered or contain intrinsically disordered regions/domains that are critical to their function. Alternate splicing and post-translational modifications can determine the extent of these disordered regions and are critical for regulating Bcl-2 proteins. Conformational plasticity and structural transitions characterize the interactions within the Bcl-2 family, with conserved sequence motifs on both binding partners required for their molecular recognition. Molecular Diversity Preservation International (MDPI) 2010-04-16 /pmc/articles/PMC2871139/ /pubmed/20480043 http://dx.doi.org/10.3390/ijms11041808 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Rautureau, Gilles J. P.
Day, Catherine L.
Hinds, Mark G.
Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_full Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_fullStr Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_full_unstemmed Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_short Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
title_sort intrinsically disordered proteins in bcl-2 regulated apoptosis
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2871139/
https://www.ncbi.nlm.nih.gov/pubmed/20480043
http://dx.doi.org/10.3390/ijms11041808
work_keys_str_mv AT rautureaugillesjp intrinsicallydisorderedproteinsinbcl2regulatedapoptosis
AT daycatherinel intrinsicallydisorderedproteinsinbcl2regulatedapoptosis
AT hindsmarkg intrinsicallydisorderedproteinsinbcl2regulatedapoptosis

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