| dc.creator | Gutiérrez, Antonio M. | |
| dc.creator | Echevarría, Miriam | |
| dc.creator | Whittembury, Guillermo | |
| dc.date | 2006-05 | |
| dc.date | 2022-12-07T13:38:59Z | |
| dc.date.accessioned | 2023-07-15T09:03:23Z | |
| dc.date.available | 2023-07-15T09:03:23Z | |
| dc.identifier | http://sedici.unlp.edu.ar/handle/10915/146979 | |
| dc.identifier | https://pmr.safisiol.org.ar/wp-content/uploads/2022/09/vol1_n10_may.pdf | |
| dc.identifier | issn:1669-5410 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/7486653 | |
| dc.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]. | |
| dc.description | Sociedad Argentina de Fisiología | |
| dc.format | application/pdf | |
| dc.language | en | |
| dc.rights | http://creativecommons.org/licenses/by/4.0/ | |
| dc.rights | Creative Commons Attribution 4.0 International (CC BY 4.0) | |
| dc.subject | Ciencias Médicas | |
| dc.subject | Fisiología | |
| dc.subject | Aquaporin | |
| dc.subject | Water channels | |
| dc.subject | Cell membrane | |
| dc.title | The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes | |
| dc.type | Articulo | |
| dc.type | Revision | |
