Identification of amino acid residues lining the pore of a gap junction channel - Wikidata - wikimedia - TriplyDB

Identification of amino acid residues lining the pore of a gap junction channel

Identification of amino acid residues lining the pore of a gap junction channel

http://www.wikidata.org/entity/Q36323688

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The role of connexins in ear and skin physiology - functional insights from disease-associated mutations Asymmetric Configurations and N-terminal Rearrangements in Connexin26 Gap Junction Channels A fully atomistic model of the Cx32 connexon Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum Conductance of connexin hemichannels segregates with the first transmembrane segment.Cosegregation of permeability and single-channel conductance in chimeric connexins.Gap-junction channels dysfunction in deafness and hearing loss.Cardiac conduction is required to preserve cardiac chamber morphology.Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability.A transient diffusion model yields unitary gap junctional permeabilities from images of cell-to-cell fluorescent dye transfer between Xenopus oocytes.The permeability of gap junction channels to probes of different size is dependent on connexin composition and permeant-pore affinities.SCAM analysis of Panx1 suggests a peculiar pore structure Tryptophan scanning mutagenesis of the first transmembrane domain of the innexin Shaking-B(Lethal).Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule Tryptophan Scanning Reveals Dense Packing of Connexin Transmembrane Domains in Gap Junction Channels Composed of Connexin32 Pore-lining residues identified by single channel SCAM studies in Cx46 hemichannels.Voltage-dependent conformational changes in connexin channels Connexinopathies: a structural and functional glimpse Aberrant trafficking of a Leu89Pro connexin32 mutant associated with X-linked dominant Charcot-Marie-Tooth disease.Accessing gap-junction channel structure-function relationships through molecular modeling and simulations Single-channel SCAM identifies pore-lining residues in the first extracellular loop and first transmembrane domains of Cx46 hemichannels Connexin channel permeability to cytoplasmic molecules.Molecular modeling and mutagenesis of gap junction channels.Gap junction channel structure in the early 21st century: facts and fantasies Novel mutations in GJA1 cause oculodentodigital syndrome Antibodies targeting extracellular domain of connexins for studies of hemichannels The N-terminal half of the connexin protein contains the core elements of the pore and voltage gates.Site-directed mutagenesis reveals putative regions of protein interaction within the transmembrane domains of connexins Neurological manifestations of oculodentodigital dysplasia: a Cx43 channelopathy of the central nervous system?Conformational changes in a pore-forming region underlie voltage-dependent "loop gating" of an unapposed connexin hemichannel.Structure of the gap junction channel and its implications for its biological functions.A structural and functional comparison of gap junction channels composed of connexins and innexins Role of the N-terminus in permeability of chicken connexin45.6 gap junctional channels.Mutation of a conserved threonine in the third transmembrane helix of alpha- and beta-connexins creates a dominant-negative closed gap junction channel.Functional expression in Xenopus oocytes of gap-junctional hemichannels formed by a cysteine-less connexin 43.Diverse pattern of gap junction beta-2 and gap junction beta-4 genes mutations and lack of contribution of DFNB21, DFNB24, DFNB29, and DFNB42 loci in autosomal recessive nonsyndromic hearing loss patients in Hormozgan, Iran.Roles of Met-34, Cys-64, and Arg-75 in the assembly of human connexin 26. Implication for key amino acid residues for channel formation and function.Characterization of a novel water pocket inside the human Cx26 hemichannel structure.Gating on the outside.Charges dispersed over the permeation pathway determine the charge selectivity and conductance of a Cx32 chimeric hemichannel.

P2860

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P2860

Identification of amino acid residues lining the pore of a gap junction channel

http://www.wikidata.org/entity/Q36323688

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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2002年學術文章

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name

Identification of amino acid residues lining the pore of a gap junction channel

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Identification of amino acid residues lining the pore of a gap junction channel

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type

label

Identification of amino acid residues lining the pore of a gap junction channel

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Identification of amino acid residues lining the pore of a gap junction channel

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prefLabel

Identification of amino acid residues lining the pore of a gap junction channel

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Identification of amino acid residues lining the pore of a gap junction channel

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Journal of Cell Biology

P1476

Identification of amino acid residues lining the pore of a gap junction channel

@en

P2093

B J Nicholson

http://www.w3.org/2001/XMLSchema#string

E Kasperek

http://www.w3.org/2001/XMLSchema#string

F L Cao

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G Cymes

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I M Skerrett

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J Aronowitz

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J H Shin

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P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

Buried charged surface in proteins

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

Unique and redundant connexin contributions to lens development

Connexin46, a novel lens gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes

Human diseases: clues to cracking the connexin code?

Connexin genes in the mouse and human genome.

The molecular basis of selective permeability of connexins is complex and includes both size and charge.

Identification of a pore lining segment in gap junction hemichannels.

The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions.

P304

349-360

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scholarly article

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10.1083/JCB.200207060

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2

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159

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2173043

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