The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes

Autores
Gutiérrez, Antonio M.; Echevarría, Miriam; Whittembury, Guillermo
Año de publicación
2006
Idioma
inglés
Tipo de recurso
reseña artículo
Estado
versión publicada
Descripción
We overview the critical steps leading to the demonstration that each ~28 kD protein monomer of the water channel (or pore)¹ pierce the lipid bilayer part of the cell membrane allowing the passage of ~ 10¹³ water molecules per second. The biophysical approach gives a functional and physical image of the water pore close to what has recently been obtained from the amino acid sequence, crystallography and other advances from the cloning era of trans-membrane water transport. Paracellular “wide” water channels of some leaky epithelia are not covered here [cf. Whittembury and Reuss, 1992; Whittembury and Hill, 2000].
Sociedad Argentina de Fisiología
Materia
Ciencias Médicas
Fisiología
Aquaporin
Water channels
Cell membrane
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/146979

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network_name_str SEDICI (UNLP)
spelling The old water channels are aquaporin proteins through which single files of water molecules cross cell membranesGutiérrez, Antonio M.Echevarría, MiriamWhittembury, GuillermoCiencias MédicasFisiologíaAquaporinWater channelsCell membraneWe overview the critical steps leading to the demonstration that each ~28 kD protein monomer of the water channel (or pore)¹ pierce the lipid bilayer part of the cell membrane allowing the passage of ~ 10¹³ water molecules per second. The biophysical approach gives a functional and physical image of the water pore close to what has recently been obtained from the amino acid sequence, crystallography and other advances from the cloning era of trans-membrane water transport. Paracellular “wide” water channels of some leaky epithelia are not covered here [cf. Whittembury and Reuss, 1992; Whittembury and Hill, 2000].Sociedad Argentina de Fisiología2006-05info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/146979enginfo:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/wp-content/uploads/2022/09/vol1_n10_may.pdfinfo:eu-repo/semantics/altIdentifier/issn/1669-5410info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:18:26Zoai:sedici.unlp.edu.ar:10915/146979Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:18:26.922SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
title The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
spellingShingle The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
Gutiérrez, Antonio M.
Ciencias Médicas
Fisiología
Aquaporin
Water channels
Cell membrane
title_short The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
title_full The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
title_fullStr The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
title_full_unstemmed The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
title_sort The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes
dc.creator.none.fl_str_mv Gutiérrez, Antonio M.
Echevarría, Miriam
Whittembury, Guillermo
author Gutiérrez, Antonio M.
author_facet Gutiérrez, Antonio M.
Echevarría, Miriam
Whittembury, Guillermo
author_role author
author2 Echevarría, Miriam
Whittembury, Guillermo
author2_role author
author
dc.subject.none.fl_str_mv Ciencias Médicas
Fisiología
Aquaporin
Water channels
Cell membrane
topic Ciencias Médicas
Fisiología
Aquaporin
Water channels
Cell membrane
dc.description.none.fl_txt_mv We overview the critical steps leading to the demonstration that each ~28 kD protein monomer of the water channel (or pore)¹ pierce the lipid bilayer part of the cell membrane allowing the passage of ~ 10¹³ water molecules per second. The biophysical approach gives a functional and physical image of the water pore close to what has recently been obtained from the amino acid sequence, crystallography and other advances from the cloning era of trans-membrane water transport. Paracellular “wide” water channels of some leaky epithelia are not covered here [cf. Whittembury and Reuss, 1992; Whittembury and Hill, 2000].
Sociedad Argentina de Fisiología
description We overview the critical steps leading to the demonstration that each ~28 kD protein monomer of the water channel (or pore)¹ pierce the lipid bilayer part of the cell membrane allowing the passage of ~ 10¹³ water molecules per second. The biophysical approach gives a functional and physical image of the water pore close to what has recently been obtained from the amino acid sequence, crystallography and other advances from the cloning era of trans-membrane water transport. Paracellular “wide” water channels of some leaky epithelia are not covered here [cf. Whittembury and Reuss, 1992; Whittembury and Hill, 2000].
publishDate 2006
dc.date.none.fl_str_mv 2006-05
dc.type.none.fl_str_mv info:eu-repo/semantics/review
info:eu-repo/semantics/publishedVersion
Revision
http://purl.org/coar/resource_type/c_dcae04bc
info:ar-repo/semantics/resenaArticulo
format review
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/146979
url http://sedici.unlp.edu.ar/handle/10915/146979
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/wp-content/uploads/2022/09/vol1_n10_may.pdf
info:eu-repo/semantics/altIdentifier/issn/1669-5410
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
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reponame_str SEDICI (UNLP)
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instname_str Universidad Nacional de La Plata
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institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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