Tricellulin is a tight-junction protein necessary for hearing.
about
Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin familyAlterations of the CIB2 calcium- and integrin-binding protein cause Usher syndrome type 1J and nonsyndromic deafness DFNB48.Tight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functionsTargeted capture and next-generation sequencing identifies C9orf75, encoding taperin, as the mutated gene in nonsyndromic deafness DFNB79Behavior of tricellulin during destruction and formation of tight junctions under various extracellular calcium conditionsAutosomal recessive nonsyndromic deafness genes: a reviewTricellular Tight Junctions in the Inner EarDeletion of Tricellulin Causes Progressive Hearing Loss Associated with Degeneration of Cochlear Hair Cells.Comprehensive analysis via exome sequencing uncovers genetic etiology in autosomal recessive nonsyndromic deafness in a large multiethnic cohortThe Genetic Basis of Nonsyndromic Hearing Loss in Indian and Pakistani PopulationsThe Mammalian Blood-Testis Barrier: Its Biology and RegulationPhysiology and function of the tight junction.Delineation of the clinical, molecular and cellular aspects of novel JAM3 mutations underlying the autosomal recessive hemorrhagic destruction of the brain, subependymal calcification, and congenital cataractsTricellulin deficiency affects tight junction architecture and cochlear hair cells.Immunoglobulin-like domain containing receptor 1 mediates fat-stimulated cholecystokinin secretionA mutation in the Srrm4 gene causes alternative splicing defects and deafness in the Bronx waltzer mouseLipolysis-stimulated lipoprotein receptor: a novel membrane protein of tricellular tight junctionsDeficiency of angulin-2/ILDR1, a tricellular tight junction-associated membrane protein, causes deafness with cochlear hair cell degeneration in miceFinding new genes for non-syndromic hearing loss through an in silico prioritization studyJNK1/2-dependent phosphorylation of angulin-1/LSR is required for the exclusive localization of angulin-1/LSR and tricellulin at tricellular contacts in EpH4 epithelial sheetEpithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1The occludin and ZO-1 complex, defined by small angle X-ray scattering and NMR, has implications for modulating tight junction permeability.Association between segments of zonula occludens proteins: live-cell FRET and mass spectrometric analysis.ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton.ILDR1 null mice, a model of human deafness DFNB42, show structural aberrations of tricellular tight junctions and degeneration of auditory hair cells.Supporting cells eliminate dying sensory hair cells to maintain epithelial integrity in the avian inner ear.Inner ear supporting cells: rethinking the silent majority.Changes in the adult vertebrate auditory sensory epithelium after trauma.Linkage study and exome sequencing identify a BDP1 mutation associated with hereditary hearing lossTranscriptional changes in adhesion-related genes are site-specific during noise-induced cochlear pathogenesis.Acoustic overstimulation modifies Mcl-1 expression in cochlear sensory epithelial cells.Genomic duplication and overexpression of TJP2/ZO-2 leads to altered expression of apoptosis genes in progressive nonsyndromic hearing loss DFNA51.Function and expression pattern of nonsyndromic deafness genesPolychaetoid controls patterning by modulating adhesion in the Drosophila pupal retinaTricellulin forms a barrier to macromolecules in tricellular tight junctions without affecting ion permeability.Evidence for three loci modifying age-at-onset of Alzheimer's disease in early-onset PSEN2 families.A common variant in CLDN14 causes precipitous, prelingual sensorineural hearing loss in multiple families due to founder effect.Molecular basis of the core structure of tight junctions.The mouse blood-brain barrier transcriptome: a new resource for understanding the development and function of brain endothelial cellsBreaking barriers. New insights into airway epithelial barrier function in health and disease.
P2860
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P2860
Tricellulin is a tight-junction protein necessary for hearing.
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Tricellulin is a tight-junction protein necessary for hearing
@nl
Tricellulin is a tight-junction protein necessary for hearing.
@ast
Tricellulin is a tight-junction protein necessary for hearing.
@en
Tricellulin is a tight-junction protein necessary for hearing.
@en-gb
type
label
Tricellulin is a tight-junction protein necessary for hearing
@nl
Tricellulin is a tight-junction protein necessary for hearing.
@ast
Tricellulin is a tight-junction protein necessary for hearing.
@en
Tricellulin is a tight-junction protein necessary for hearing.
@en-gb
prefLabel
Tricellulin is a tight-junction protein necessary for hearing
@nl
Tricellulin is a tight-junction protein necessary for hearing.
@ast
Tricellulin is a tight-junction protein necessary for hearing.
@en
Tricellulin is a tight-junction protein necessary for hearing.
@en-gb
P2093
P2860
P921
P3181
P356
P1476
Tricellulin is a tight-junction protein necessary for hearing.
@en
P2093
Alan S Fanning
Andrew Forge
Ayala Lagziel
Inna A Belyantseva
James M Anderson
Khushnooda Ramzan
Parna Chattaraj
Penelope L Friedman
Saima Riazuddin
Shaheen N Khan
P2860
P304
P3181
P356
10.1086/510022
P407
P577
2006-10-31T00:00:00Z