Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Garbus, Ingrid | - |
| dc.creator | Roccamo, Ana Maria | - |
| dc.creator | Barrantes, Francisco Jose | - |
| dc.date | 2018-07-25T17:06:18Z | - |
| dc.date | 2018-07-25T17:06:18Z | - |
| dc.date | 2002-07 | - |
| dc.date | 2018-07-11T14:11:17Z | - |
| dc.date.accessioned | 2019-04-29T15:49:52Z | - |
| dc.date.available | 2019-04-29T15:49:52Z | - |
| dc.date.issued | 2002-07 | - |
| dc.identifier | Garbus, Ingrid; Roccamo, Ana Maria; Barrantes, Francisco Jose; Identification of threonine 422 in transmembrane domain αM4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone; Pergamon-Elsevier Science Ltd; Neuropharmacology; 43; 1; 7-2002; 65-73 | - |
| dc.identifier | 0028-3908 | - |
| dc.identifier | http://hdl.handle.net/11336/53088 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/303185 | - |
| dc.description | The modulatory effects exerted by the glucocorticoid hydrocortisone (HC) on the nicotinic acetylcholine receptor (AChR) were studied in mutants of the α subunit M4 transmembrane region. Based on the photoaffinity labeling of αM4 412 with the steroid promegestone this position was mutated to different residues to explore the properties of side-chain volume, hydrophobicity, and charge on AChR-steroid interactions. All mutants showed channel kinetics indistinguishable from those of the wild-type AChR, both in the absence and presence of HC (200 and 400 μM), in single-channel recordings at different acetylcholine (ACh) concentrations. An alanine-substituted quadruple mutant of four putative lipid-exposed residues in αM4 (L411, M415, C418 and T422) exhibited less inhibition by HC than that observed in wild-type AChR. When we dissected the quadruple mutant into four individual alanine-substituted receptors, we found that the T422 mutant AChR behaved like the quadruple mutant, whereas the other three were indistinguishable from the wild-type. We conclude that T422, a residue close to the extracellular-facing membrane hemilayer in αM4, has direct bearing on the changes in HC sensitivity and propose its involvement in the steroid-AChR interaction site. | - |
| dc.description | Fil: Garbus, Ingrid. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina | - |
| dc.description | Fil: Roccamo, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina | - |
| dc.description | Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina. Unesco; Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Pergamon-Elsevier Science Ltd | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0028390802000680 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/S0028-3908(02)00068-0 | - |
| dc.rights | info:eu-repo/semantics/restrictedAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.subject | CHOLINERGIC RECEPTOR | - |
| dc.subject | GLUCOCORTICOID | - |
| dc.subject | MUTATIONS | - |
| dc.subject | PATCH-CLAMP | - |
| dc.subject | STEROID | - |
| dc.subject | Otras Ciencias Biológicas | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Identification of threonine 422 in transmembrane domain αM4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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