Structure-function analysis of the bestrophin family of anion channels - Test2 - elhamkhani - TriplyDB

Structure-function analysis of the bestrophin family of anion channels

Structure-function analysis of the bestrophin family of anion channels

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Bestrophin-1 enables Ca2+-activated Cl- conductance in epithelia Missense mutations in a retinal pigment epithelium protein, bestrophin-1, cause retinitis pigmentosa BEST1 expression in the retinal pigment epithelium is modulated by OTX family members Molecular and functional analyses of two new calcium-activated chloride channel family members from mouse eye and intestine Chloride channels as drug targets.Anoctamin/TMEM16 family members are Ca2+-activated Cl- channels Dysregulation of human bestrophin-1 by ceramide-induced dephosphorylation Functional roles of bestrophins in ocular epithelia Bestrophin-2 is a candidate calcium-activated chloride channel involved in olfactory transduction The bestrophin- and TMEM16A-associated Ca(2+)- activated Cl(–) channels in vascular smooth muscles A C-terminally truncated mouse Best3 splice variant targets and alters the ion balance in lysosome-endosome hybrids and the endoplasmic reticulum.Human disease-causing mutations disrupt an N-C-terminal interaction and channel function of bestrophin 1 VMD2 promoter requires two proximal E-box sites for its activity in vivo and is regulated by the MITF-TFE family Molecular physiology of bestrophins: multifunctional membrane proteins linked to best disease and other retinopathies A short motif in the C-terminus of mouse bestrophin 3 [corrected] inhibits its activation as a Cl channel The light peak of the electroretinogram is dependent on voltage-gated calcium channels and antagonized by bestrophin (best-1)Bestrophin Cl- channels are highly permeable to HCO3-Molecular evolution and functional divergence of the bestrophin protein family Effects of alternative splicing on the function of bestrophin-1 calcium-activated chloride channels The best disease-linked Cl- channel hBest1 regulates Ca V 1 (L-type) Ca2+ channels via src-homology-binding domains.Biallelic mutation of BEST1 causes a distinct retinopathy in humans SLO-2 isoforms with unique Ca(2+) - and voltage-dependence characteristics confer sensitivity to hypoxia in C. elegans.Stoichiometry and specific assembly of Best ion channels Gene expression profiling in gills of the great spider crab Hyas araneus in response to ocean acidification and warming.Mouse bestrophin-2 is a bona fide Cl(-) channel: identification of a residue important in anion binding and conduction.Determinants of anion permeation in the second transmembrane domain of the mouse bestrophin-2 chloride channel.The role of bestrophin in airway epithelial ion transport.Drosophila bestrophin-1 chloride current is dually regulated by calcium and cell volume.Lineage-specific expression of bestrophin-2 and bestrophin-4 in human intestinal epithelial cells Activation of bestrophin Cl- channels is regulated by C-terminal domains.Regulation of bestrophins by Ca2+: a theoretical and experimental study.Mechanism of olfactory masking in the sensory cilia.Functional and clinical data of Best vitelliform macular dystrophy patients with mutations in the BEST1 gene.Bestrophin-2 is involved in the generation of intraocular pressure.Hydrodynamic properties of porcine bestrophin-1 in Triton X-100.A model of best vitelliform macular dystrophy in rats Chloride channels: often enigmatic, rarely predictable.Tmem16A encodes the Ca2+-activated Cl- channel in mouse submandibular salivary gland acinar cells Bestrophins and retinopathies.Role of the Ca2+ -activated Cl- channels bestrophin and anoctamin in epithelial cells.

P2860

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P2860

Structure-function analysis of the bestrophin family of anion channels

http://www.wikidata.org/entity/Q24633985

description

2003 nî lūn-bûn

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2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Structure-function analysis of the bestrophin family of anion channels

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Journal of Biological Chemistry

P1476

Structure-function analysis of the bestrophin family of anion channels

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Hugh Cahill

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Hui Sun

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John Williams

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King-Wai Yau

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

Takashi Tsunenari

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P2860

VMD2 mutations in vitelliform macular dystrophy (Best disease) and other maculopathies

The voltage-gated potassium channels and their relatives

Bestrophin, the product of the Best vitelliform macular dystrophy gene (VMD2), localizes to the basolateral plasma membrane of the retinal pigment epithelium

Molecular genetics of human color vision: the genes encoding blue, green, and red pigments

Identification of the gene responsible for Best macular dystrophy

The vitelliform macular dystrophy protein defines a new family of chloride channels.

A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing

ClC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells

A simple method for displaying the hydropathic character of a protein

X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity

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41114-25

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scholarly article

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1007865

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10.1074/JBC.M306150200

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42

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278

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Philip M Smallwood

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2003-10-17T00:00:00Z

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12907679

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P932

2885917

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