Structure, function, and regulation of cellular tight junctions.
about
Claudin multigene family encoding four-transmembrane domain protein components of tight junction strandsBehavior of tricellulin during destruction and formation of tight junctions under various extracellular calcium conditionsThe tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctionsGEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectorsA small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cellsOccludin: a novel integral membrane protein localizing at tight junctionsWIF-B cells: an in vitro model for studies of hepatocyte polarityInterspecies diversity of the occludin sequence: cDNA cloning of human, mouse, dog, and rat-kangaroo homologuesDirect association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctionsInvolvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filamentsExpression of occludin, tight-junction-associated protein, in human digestive tractDirect binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudinsClaudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludinEndothelial claudin: claudin-5/TMVCF constitutes tight junction strands in endothelial cellsManner of interaction of heterogeneous claudin species within and between tight junction strandsTight junctions in inflammatory bowel diseases and inflammatory bowel disease associated colorectal cancerGlucocorticoids and endothelial cell barrier functionTight junctions in human pancreatic duct epithelial cellsSize-selective loosening of the blood-brain barrier in claudin-5-deficient miceIntestinal barrier function: molecular regulation and disease pathogenesisTranscriptional regulators of claudins in epithelial tight junctionsNormal establishment of epithelial tight junctions in mice and cultured cells lacking expression of ZO-3, a tight-junction MAGUK proteinClaudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient miceAmastin Knockdown in Leishmania braziliensis Affects Parasite-Macrophage Interaction and Results in Impaired Viability of Intracellular AmastigotesProminin, a novel microvilli-specific polytopic membrane protein of the apical surface of epithelial cells, is targeted to plasmalemmal protrusions of non-epithelial cellsAdult neurogenesis: ultrastructure of a neurogenic niche and neurovascular relationshipsCOOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos.Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion.Transcriptional changes in adhesion-related genes are site-specific during noise-induced cochlear pathogenesis.Acoustic overstimulation modifies Mcl-1 expression in cochlear sensory epithelial cells.Dynamic behavior of paired claudin strands within apposing plasma membranes.Displayed correlation between gene expression profiles and submicroscopic alterations in response to cetuximab, gefitinib and EGF in human colon cancer cell lines.Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctionsPores in the wall: claudins constitute tight junction strands containing aqueous pores.Medicinal chemical properties of successful central nervous system drugsTestosterone regulates tight junction proteins and influences prostatic autoimmune responsesClostridium difficile toxins disrupt epithelial barrier function by altering membrane microdomain localization of tight junction proteins.Transcriptional control of tight junction proteins via a protein kinase C signal pathway in human telomerase reverse transcriptase-transfected human pancreatic duct epithelial cells.Deafness in occludin-deficient mice with dislocation of tricellulin and progressive apoptosis of the hair cells.Zonula occludens toxin modulates tight junctions through protein kinase C-dependent actin reorganization, in vitro
P2860
Q22008687-3E1F6734-D6DE-45F0-8B23-C91327DA3A5FQ24301050-586C30CD-C6A8-447C-A639-6FDA5D7077FCQ24316928-4C2AEE57-281B-4031-B38F-853EDA0D98EEQ24319756-D1797268-11B5-4912-B91F-22DFDA427C76Q24336878-AEC15C47-4F63-4C21-BB31-0D7AA1B53B9BQ24657666-C4458C96-7B05-4653-AD2F-317394085788Q24657706-D17E839F-27D9-4AE7-945E-2CC7C4B6704AQ24671949-D0847529-3801-4A65-B795-26EA5EB3A48DQ24672971-567CDF0C-9078-46C8-8064-114E1E714E3CQ24678389-B808FBBE-A666-4B69-B536-C17A35674EA5Q24678630-27525502-1011-45CD-9175-1D742BDDAAA4Q24682136-DE4F63E6-5C65-4163-B42A-01EAC1388864Q24682664-4DFA52EE-01DD-48D5-B6B8-1F30810D55A5Q24682677-DA4DED95-EC6C-404B-90DF-42D773858FD5Q24683327-FE5FCEDD-8D9B-4D52-846E-D47A2FE3DE2FQ26752750-A527D39D-05C4-44C9-893D-2638653656EBQ26853743-EEFC3CFB-EB35-484D-81BD-AF41EAA5816AQ27012318-E60FCBBA-EC17-4423-BC08-5AB442F5F83AQ28203769-9028081C-F55D-486F-B4DD-46CD84811508Q28250081-278BD556-AE41-4EA0-AD19-CB00444227C6Q28261649-76FD1627-E5B5-4052-A36E-395FB56E3F66Q28508837-2B279366-50AC-466E-892E-E1FCC72BA128Q28513737-434932EA-48B3-43C3-AC0F-7988B5540728Q28551397-2CC05C1B-04B1-4AFB-83A3-80DB404E9B4FQ28585056-9E33EEC9-CCB7-430B-A3DE-85E819E0D622Q28728277-3527827D-DC6F-445F-8A74-9CF94298F654Q29041617-F54867E3-1D2A-4160-ACB5-ABA3C7B36EF0Q30449794-2FA211C8-8C0E-4195-B552-58B4CDFF0673Q30458738-0B0932DC-AAE8-40F5-9C23-63FA87C58625Q30459919-1652F988-35E0-45E8-BA64-A0EE45001DB0Q30477728-EC300274-0EF6-4759-9DD4-EEDC8E15074CQ33358967-DFAA086E-E12F-4B13-8367-04AEA552B187Q33853393-D14A93CE-8468-4BF5-AAF9-73D51A2EBE97Q33881242-19E50A09-EF48-415B-946D-748A9C8043A9Q33946968-3F69F206-EAA7-4A63-B994-40EB176C7D96Q33962057-53AB750D-B0BC-4B06-A95A-1979E6D1D941Q34006206-3A5D5971-CF53-4F00-941D-055B124BDF9BQ34033442-820DE33F-A7D8-4E7C-82D7-4010761D7DFDQ34048824-4568F5BE-E202-4CAB-BE83-FE3E486D5F46Q34058314-E770904E-C010-4424-B1BC-C847C8BAE47C
P2860
Structure, function, and regulation of cellular tight junctions.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Structure, function, and regulation of cellular tight junctions.
@ast
Structure, function, and regulation of cellular tight junctions.
@en
type
label
Structure, function, and regulation of cellular tight junctions.
@ast
Structure, function, and regulation of cellular tight junctions.
@en
prefLabel
Structure, function, and regulation of cellular tight junctions.
@ast
Structure, function, and regulation of cellular tight junctions.
@en
P1476
Structure, function, and regulation of cellular tight junctions.
@en
P2093
Schneeberger EE
P304
P356
10.1152/AJPLUNG.1992.262.6.L647
P407
P433
P577
1992-06-01T00:00:00Z