Zobrazeno 1 - 10
of 115
pro vyhledávání: '"Luis Reuss"'
Autor:
Luis Reuss, Calvin U. Cotton
Publikováno v:
Cellular and Molecular Physiology of Cell Volume Regulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9ebab8258782c6fee1314ca7afdfb240
https://doi.org/10.1201/9780367812140-3
https://doi.org/10.1201/9780367812140-3
Autor:
Rodolfo J. Arjona, Mauricio A. Retamal, Nicolás J. Arévalo, Rodrigo Moraga-Amaro, Cristóbal G. Rojas, Wendy González, Jimmy Stehberg, Luis Reuss, Constanza Alcaino, Jonathan G. Canan, Guillermo A. Altenberg, Viviana P. Orellana
Publikováno v:
Nitric oxide : biology and chemistry. 86
Under normal conditions, connexin (Cx) hemichannels have a low open probability, which can increase under pathological conditions. Since hemichannels are permeable to relatively large molecules, their exacerbated activity has been linked to cell dama
Autor:
Maria E. Zoghbi, Guillermo A. Altenberg, Vania Figueroa, Mariana C. Fiori, Juan C. Sáez, Luis Reuss
Publikováno v:
Journal of Biological Chemistry. 287:40826-40834
Indirect evidence suggests that connexin hemichannels are permeable to Ca(2+), but direct demonstration is lacking.Calcium moves into liposomes containing purified Cx26 in response to a concentration gradient.Cx26 hemichannels are permeable to Ca(2+)
Autor:
Carmen G. León-Paravic, Flavio Evangelista-Martínez, Mauricio A. Retamal, Guillermo A. Altenberg, Luis Reuss
Publikováno v:
Pflügers Archiv - European Journal of Physiology. 461:635-643
Connexins form hemichannels at undocked plasma membranes and gap-junction channels (GJCs) at intercellular contacting zones. Under physiological conditions, hemichannels have low open probabilities, but their activation under pathological conditions,
Publikováno v:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
Gap-junction hemichannels are composed of six protein subunits (connexins). Undocked hemichannels contribute to physiological autocrine/paracrine cell signaling, including release of signaling molecules, cell-volume regulation, and glucose uptake. In
Autor:
Srinivasan Krishnan, Mariana C. Fiori, Mauricio A. Retamal, D. Marien Cortes, Luis Reuss, Luis G. Cuello, Guillermo A. Altenberg
Publikováno v:
Bioscience Reports, Vol 35, Iss 2, p e00177 (2015)
Bioscience Reports
Bioscience Reports
Gap-junction channels (GJCs) communicate the cytoplasm of adjacent cells and are formed by head-to-head association of two hemichannels (HCs), one from each of the neighbouring cells. GJCs mediate electrical and chemical communication between cells,
Publikováno v:
Hearing Research. 220:87-94
Gap-junctional channels are large intercellular aqueous pores formed by head-to-head association of two gap-junctional hemichannels (connexin hexamers), one from each of the adjacent cells. The mechano-transduction of sound waves into electrical impu
Publikováno v:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
Marked increase in cell permeability ascribed to open connexin (Cx)43 hemichannels is induced by metabolic inhibition (MI) of cortical astrocytes in culture, but the molecular mechanisms are not established. Dephosphorylation and/or oxidation of Cx43
Autor:
Yongyue Chen, Sung Haeng Lee, Xiaoyong Bao, Guillermo A. Altenberg, Luis Reuss, Sung Chang Lee
Publikováno v:
Journal of Biological Chemistry. 280:8647-8650
Approximately 25% of all genome coding sequences correspond to membrane proteins, which perform varied and essential functions in cells. Eukaryotic integral membrane proteins are predominantly alpha-helical proteins that span the membrane several tim
Publikováno v:
American Journal of Physiology-Cell Physiology. 287:C1256-C1263
PKA-mediated phosphorylation of the regulatory (R) domain plays a major role in the activation of the human cystic fibrosis transmembrane conductance regulator (hCFTR). In contrast, the effect of PKC-mediated phosphorylation is controversial, smaller