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dc.date.accessioned | 2022-12-07T13:38:59Z | |
dc.date.available | 2022-12-07T13:38:59Z | |
dc.date.issued | 2006-05 | |
dc.identifier.uri | http://sedici.unlp.edu.ar/handle/10915/146979 | |
dc.description.abstract | 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]. | en |
dc.language | en | es |
dc.subject | Fisiología | es |
dc.subject | Aquaporin | es |
dc.subject | Water channels | es |
dc.subject | Cell membrane | es |
dc.title | The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes | en |
dc.type | Articulo | es |
sedici.identifier.uri | https://pmr.safisiol.org.ar/wp-content/uploads/2022/09/vol1_n10_may.pdf | es |
sedici.identifier.issn | 1669-5410 | es |
sedici.creator.person | Gutiérrez, Antonio M. | es |
sedici.creator.person | Echevarría, Miriam | es |
sedici.creator.person | Whittembury, Guillermo | es |
sedici.subject.materias | Ciencias Médicas | es |
sedici.description.fulltext | true | es |
mods.originInfo.place | Sociedad Argentina de Fisiología | es |
sedici.subtype | Revision | es |
sedici.rights.license | Creative Commons Attribution 4.0 International (CC BY 4.0) | |
sedici.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
sedici.description.peerReview | peer-review | es |
sedici.relation.journalTitle | Physiological Mini Reviews (PMR) | es |
sedici.relation.journalVolumeAndIssue | vol. 1, no. 10 | es |