Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
about
"You Shall Not Pass"-tight junctions of the blood brain barrierThe small GTPase Rab13 regulates assembly of functional tight junctions in epithelial cells.hScrib interacts with ZO-2 at the cell-cell junctions of epithelial cellsJRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludinClaudin-5 controls intercellular barriers of human dermal microvascular but not human umbilical vein endothelial cellsDensity-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cellsRab13 regulates PKA signaling during tight junction assemblyTyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stressLink of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2Association of ARVCF with zonula occludens (ZO)-1 and ZO-2: binding to PDZ-domain proteins and cell-cell adhesion regulate plasma membrane and nuclear localization of ARVCFDistinct domains of paracingulin are involved in its targeting to the actin cytoskeleton and regulation of apical junction assemblyAlterations of the apical junctional complex and actin cytoskeleton and their role in colorectal cancer progressionThe actin cytoskeleton as a barrier to virus infection of polarized epithelial cellsThe reversible increase in tight junction permeability induced by capsaicin is mediated via cofilin-actin cytoskeletal dynamics and decreased level of occludinReshaping the Cone-Mosaic in a Rat Model of Retinitis Pigmentosa: Modulatory Role of ZO-1 Expression in DL-Alpha-Aminoadipic Acid ReshapingStructural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domainDomain Swapping within PDZ2 Is Responsible for Dimerization of ZO ProteinsStructure of the second PDZ domain from human zonula occludens 2Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeletonIn vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysisThe tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-BThe carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctionsIdentification of an essential endogenous regulator of blood-brain barrier integrity, and its pathological and therapeutic implicationsTight-junction protein zonula occludens 2 is a target of phosphorylation by protein kinase CRegulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeabilityProgressive Hearing Loss in Mice Carrying a Mutation in Usp53.Normal establishment of epithelial tight junctions in mice and cultured cells lacking expression of ZO-3, a tight-junction MAGUK proteinMolecular characterization of angiomotin/JEAP family proteins: interaction with MUPP1/Patj and their endogenous propertiesEarly lead exposure increases the leakage of the blood-cerebrospinal fluid barrier, in vitroEffects of cardiopulmonary bypass on tight junction protein expressions in intestinal mucosa of ratsConnexin 43 interacts with zona occludens-1 and -2 proteins in a cell cycle stage-specific mannerCalcium dobesilate inhibits the alterations in tight junction proteins and leukocyte adhesion to retinal endothelial cells induced by diabetesJACOP, a novel plaque protein localizing at the apical junctional complex with sequence similarity to cingulinExpression and distribution of ZO-3, a tight junction MAGUK protein, in mouse tissuesEpithelial junctions and Rho family GTPases: the zonular signalosome.Occludin OCEL-domain interactions are required for maintenance and regulation of the tight junction barrier to macromolecular flux.Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1Association between segments of zonula occludens proteins: live-cell FRET and mass spectrometric analysis.Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling network of striated muscle.hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions.
P2860
Q21129349-334B5652-0A36-411D-98D5-3393D6685BAFQ24299510-A639D641-B444-4C0F-ADEF-341E38CF8059Q24306134-BFD7FDD9-FF27-46A2-9BB1-B657A828CAA3Q24306920-792A609E-CF8D-4F47-909B-A40AAC61A231Q24307651-8BE2D2BA-ED54-4598-B8E6-0236A1ECE886Q24310946-A2800F90-432E-48B2-A9E7-E1B57C7EA0CDQ24337319-7E486964-8799-4B62-A095-850E4497F2B8Q24534909-DD71C12E-C79D-4330-B77E-22060E194059Q24535830-BF80CEB3-2948-4FE7-806B-A9B5DA067085Q24559951-2A53BBB4-F7BB-47D2-93A8-F6323FB09649Q24631674-A6C750A4-0C54-4B52-B5C6-669093522BFEQ26785540-6090D578-DA3F-40DE-919C-7116322A1594Q27015995-CE01D176-5554-40D6-BF37-DB9E72F36B1BQ27302299-098D9ACD-C863-4A74-9B22-09412B49EDD7Q27317130-3F5928B4-0FB2-4635-B848-56FEE7BE4F85Q27646892-C58C5754-4EBD-4E91-8A37-EC3D282E6E4BQ27648746-AE10D56B-32CD-44C7-9276-280318951C2BQ27654546-4906643F-FB36-497E-88CA-E97405E1F620Q28139599-5A461DFD-313F-4E34-A5F4-E25445110293Q28205182-2ECEED6E-4253-4A5B-BA8C-FCA662D9D17CQ28211466-57010743-5FEF-480E-9DF3-7373A7EB8A80Q28218429-96F57EC6-7B48-49BB-BC9C-7F4D932E65E6Q28282373-D1FEEDF1-7D95-4E5E-ABAE-86926123149EQ28364570-986A7678-0CD3-4037-93A1-E1A8416C11F3Q28365900-E5CD5B46-B587-4044-B5A0-AE956EE16905Q28506642-F02DC6AC-D5BA-42E2-A723-457BE057077BQ28508837-3E3C1497-B880-4E2F-8FED-0BF08DD6D5E6Q28510848-32E76E0D-65DC-4443-8983-AD46C0C30E02Q28565677-7D2226C0-77F4-42BB-B4B6-18B736FF68A0Q28576271-F05DDB38-F7AB-44DD-9503-6A78A02EB852Q28582860-D32F9218-D7EE-4D99-BD8B-3DC990C653A4Q28584295-0977022E-D37F-4173-9587-EEDFE92E47B8Q28591650-8088AF3E-6DC4-4765-BCD9-D987A50800EBQ28593224-FB4B428B-E06D-461B-B646-84F8ACD03636Q30009261-E263D335-BC98-43EB-9921-636D673BB169Q30009590-7436DE9E-3B98-4989-9136-E7F761DBEB1CQ30009921-0F1E7EAC-F841-4CAE-BEDB-9B17004B1390Q30010079-4BACE25F-3661-4207-8327-D11E00C9B8ACQ30010222-C0FA3D0E-FB93-4019-98AD-941A1F315871Q30168747-C53B5619-7E7F-434F-AC43-5D9FA752999E
P2860
Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Protein interactions at the ti ...... t complexes with ZO-2 and ZO-3
@en
Protein interactions at the ti ...... t complexes with ZO-2 and ZO-3
@nl
type
label
Protein interactions at the ti ...... t complexes with ZO-2 and ZO-3
@en
Protein interactions at the ti ...... t complexes with ZO-2 and ZO-3
@nl
prefLabel
Protein interactions at the ti ...... t complexes with ZO-2 and ZO-3
@en
Protein interactions at the ti ...... t complexes with ZO-2 and ZO-3
@nl
P2093
P3181
P356
P1476
Protein interactions at the ti ...... t complexes with ZO-2 and ZO-3
@en
P2093
B R Stevenson
E S Wittchen
P304
P3181
P356
10.1074/JBC.274.49.35179
P407
P577
1999-12-03T00:00:00Z