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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/43699
Ver los metadatos del registro completo
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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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1844613581273825280 |
score |
13.070432 |