Causes of evolutionary rate variation among protein sites

Autores
Echave, Julián; Spielman, Stephanie J.; Wilke, Claus O.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It has long been recognized that certain sites within a protein, such as sites in the protein core or catalytic residues in enzymes, are evolutionarily more conserved than other sites. However, our understanding of rate variation among sites remains surprisingly limited. Recent progress to address this includes the development of a wide array of reliable methods to estimate site-specific substitution rates from sequence alignments. In addition, several molecular traits have been identified that correlate with site-specific mutation rates, and novel mechanistic biophysical models have been proposed to explain the observed correlations. Nonetheless, current models explain, at best, approximately 60% of the observed variance, highlighting the limitations of current methods and models and the need for new research directions.
Fil: Echave, Julián. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Spielman, Stephanie J.. University of Texas at Austin; Estados Unidos
Fil: Wilke, Claus O.. University of Texas at Austin; Estados Unidos
Materia
Protein
Evolution
Biophysical
Model
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/43699

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spelling Causes of evolutionary rate variation among protein sitesEchave, JuliánSpielman, Stephanie J.Wilke, Claus O.ProteinEvolutionBiophysicalModelhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1It has long been recognized that certain sites within a protein, such as sites in the protein core or catalytic residues in enzymes, are evolutionarily more conserved than other sites. However, our understanding of rate variation among sites remains surprisingly limited. Recent progress to address this includes the development of a wide array of reliable methods to estimate site-specific substitution rates from sequence alignments. In addition, several molecular traits have been identified that correlate with site-specific mutation rates, and novel mechanistic biophysical models have been proposed to explain the observed correlations. Nonetheless, current models explain, at best, approximately 60% of the observed variance, highlighting the limitations of current methods and models and the need for new research directions.Fil: Echave, Julián. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Spielman, Stephanie J.. University of Texas at Austin; Estados UnidosFil: Wilke, Claus O.. University of Texas at Austin; Estados UnidosNature Publishing Group2016-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/43699Echave, Julián; Spielman, Stephanie J.; Wilke, Claus O.; Causes of evolutionary rate variation among protein sites; Nature Publishing Group; Nature Reviews Genetics; 17; 2; 1-2016; 109-1211471-0056CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1038/nrg.2015.18info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/nrg.2015.18info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:51:25Zoai:ri.conicet.gov.ar:11336/43699instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:51:25.515CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Causes of evolutionary rate variation among protein sites
title Causes of evolutionary rate variation among protein sites
spellingShingle Causes of evolutionary rate variation among protein sites
Echave, Julián
Protein
Evolution
Biophysical
Model
title_short Causes of evolutionary rate variation among protein sites
title_full Causes of evolutionary rate variation among protein sites
title_fullStr Causes of evolutionary rate variation among protein sites
title_full_unstemmed Causes of evolutionary rate variation among protein sites
title_sort Causes of evolutionary rate variation among protein sites
dc.creator.none.fl_str_mv Echave, Julián
Spielman, Stephanie J.
Wilke, Claus O.
author Echave, Julián
author_facet Echave, Julián
Spielman, Stephanie J.
Wilke, Claus O.
author_role author
author2 Spielman, Stephanie J.
Wilke, Claus O.
author2_role author
author
dc.subject.none.fl_str_mv Protein
Evolution
Biophysical
Model
topic Protein
Evolution
Biophysical
Model
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv It has long been recognized that certain sites within a protein, such as sites in the protein core or catalytic residues in enzymes, are evolutionarily more conserved than other sites. However, our understanding of rate variation among sites remains surprisingly limited. Recent progress to address this includes the development of a wide array of reliable methods to estimate site-specific substitution rates from sequence alignments. In addition, several molecular traits have been identified that correlate with site-specific mutation rates, and novel mechanistic biophysical models have been proposed to explain the observed correlations. Nonetheless, current models explain, at best, approximately 60% of the observed variance, highlighting the limitations of current methods and models and the need for new research directions.
Fil: Echave, Julián. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Spielman, Stephanie J.. University of Texas at Austin; Estados Unidos
Fil: Wilke, Claus O.. University of Texas at Austin; Estados Unidos
description It has long been recognized that certain sites within a protein, such as sites in the protein core or catalytic residues in enzymes, are evolutionarily more conserved than other sites. However, our understanding of rate variation among sites remains surprisingly limited. Recent progress to address this includes the development of a wide array of reliable methods to estimate site-specific substitution rates from sequence alignments. In addition, several molecular traits have been identified that correlate with site-specific mutation rates, and novel mechanistic biophysical models have been proposed to explain the observed correlations. Nonetheless, current models explain, at best, approximately 60% of the observed variance, highlighting the limitations of current methods and models and the need for new research directions.
publishDate 2016
dc.date.none.fl_str_mv 2016-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/43699
Echave, Julián; Spielman, Stephanie J.; Wilke, Claus O.; Causes of evolutionary rate variation among protein sites; Nature Publishing Group; Nature Reviews Genetics; 17; 2; 1-2016; 109-121
1471-0056
CONICET Digital
CONICET
url http://hdl.handle.net/11336/43699
identifier_str_mv Echave, Julián; Spielman, Stephanie J.; Wilke, Claus O.; Causes of evolutionary rate variation among protein sites; Nature Publishing Group; Nature Reviews Genetics; 17; 2; 1-2016; 109-121
1471-0056
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1038/nrg.2015.18
info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/nrg.2015.18
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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