Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Gisela D. Cymes"'
Publikováno v:
Proc Natl Acad Sci U S A
Although it has long been proposed that membrane proteins may contain tightly bound lipids, their identity, the structure of their binding sites, and their functional and structural relevance have remained elusive. To some extent, this is because tig
Autor:
Claudio Grosman, Gisela D. Cymes
Publikováno v:
Proc Natl Acad Sci U S A
One of the most fundamental questions in the field of Cys-loop receptors (pentameric ligand-gated ion channels, pLGICs) is how the affinity for neurotransmitters and the conductive/nonconductive state of the transmembrane pore are correlated despite
Autor:
Emad Tajkhorshid, Claudio Grosman, Zhiyu Zhao, Gisela D. Cymes, Zhening Zhang, Pramod Kumar, Yuhang Wang
Publikováno v:
Proc Natl Acad Sci U S A
The lipid dependence of the nicotinic acetylcholine receptor from the Torpedo electric organ has long been recognized, and one of the most consistent experimental observations is that, when reconstituted in membranes formed by zwitterionic phospholip
Publikováno v:
The Journal of General Physiology
Members of the pentameric ligand-gated ion channel family have been crystallized in different conformations, including one in which the transmembrane pore is surprisingly wide. Gonzalez-Gutierrez et al. show that the open-channel conformation of anim
Autor:
Gisela D. Cymes, Claudio Grosman
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 113(45)
Among neurotransmitter-gated ion channels, the superfamily of pentameric ligand-gated ion channels (pLGICs) is unique in that its members display opposite permeant-ion charge selectivities despite sharing the same structural fold. Although much effor
Autor:
Claudio Grosman, Gisela D. Cymes
Publikováno v:
Nature chemical biology
In ion channels, “rings” of ionized side chains that decorate the walls of the permeation pathway often lower the energetic barrier to ion conduction. Using single-channel electrophysiological recordings, we studied the poorly understood ring of
Autor:
Claudio Grosman, Gisela D. Cymes
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:3485-3493
As a step toward gaining a better understanding of the physicochemical bases of pK(a)-value shifts in ion channels, we have previously proposed a method for estimating the proton affinities of systematically engineered ionizable side chains from the
Autor:
Claudio Grosman, Gisela D. Cymes
Publikováno v:
Nature
Among ion channels, only the nicotinic-receptor superfamily has evolved to generate both cation- and anion-selective members. Although other, structurally unrelated, neurotransmitter-gated cation channels exist, no other type of neurotransmitter-gate
Publikováno v:
The Journal of General Physiology
The slow-channel congenital myasthenic syndrome (SCCMS) is a disorder of the neuromuscular junction caused by gain-of-function mutations to the muscle nicotinic acetylcholine (ACh) receptor (AChR). Although it is clear that the slower deactivation ti
Autor:
Gisela D. Cymes, Carlota Wolfenstein-Todel, Juan J. Caridad, Fabián M. Atlasovich, M. Mercedes Iglesias
Publikováno v:
International Journal of Peptide and Protein Research. 44:31-35
The reactivity of arginine residues in ovine prolactin was studied by reaction with 1,2-cyclohexanedione. Kinetic analysis of the data showed a good fit with two simultaneous pseudo-first-order equations with apparent velocity constants of 0.28 and 1