The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties. - Wikidata - wikimedia - TriplyDB

The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties.

The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties.

http://www.wikidata.org/entity/Q30159513

about

"You Shall Not Pass"-tight junctions of the blood brain barrier Ischemic injury to kidney induces glomerular podocyte effacement and dissociation of slit diaphragm proteins Neph1 and ZO-1 Brain endothelial cell-cell junctions: how to "open" the blood brain barrier Physiology and pathophysiology of the blood-brain barrier: P-glycoprotein and occludin trafficking as therapeutic targets to optimize central nervous system drug delivery Domain Swapping within PDZ2 Is Responsible for Dimerization of ZO Proteins Insights into Regulated Ligand Binding Sites from the Structure of ZO-1 Src Homology 3-Guanylate Kinase Module The Src Homology 3 Domain Is Required for Junctional Adhesion Molecule Binding to the Third PDZ Domain of the Scaffolding Protein ZO-1 SUMOylation of claudin-2 Alcohol increases the permeability of airway epithelial tight junctions in Beas-2B and NHBE cells Glibenclamide reduces inflammation, vasogenic edema, and caspase-3 activation after subarachnoid hemorrhage Clustering of CARMA1 through SH3-GUK domain interactions is required for its activation of NF-κB signalling.Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1 The 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.Involvement of the interaction of afadin with ZO-1 in the formation of tight junctions in Madin-Darby canine kidney cells ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton.Junctional music that the nucleus hears: cell-cell contact signaling and the modulation of gene activity.ZO-1- and ZO-2-dependent integration of myosin-2 to epithelial zonula adherens.Molecular basis of the core structure of tight junctions.ZO proteins redundantly regulate the transcription factor DbpA/ZONAB The hinge region of the scaffolding protein of cell contacts, zonula occludens protein 1, regulates interacting with various signaling proteins.The active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation Su(dx) E3 ubiquitin ligase-dependent and -independent functions of polychaetoid, the Drosophila ZO-1 homologue Molecular mechanisms of microvascular failure in central nervous system injury--synergistic roles of NKCC1 and SUR1/TRPM4.Occludin S408 phosphorylation regulates tight junction protein interactions and barrier function Occludin localizes to centrosomes and modifies mitotic entry.Zonula occludens-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia.The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state.Junctional proteins of the blood-brain barrier: New insights into function and dysfunction.Tight junction modulation of the blood brain barrier: CNS delivery of small molecules JunD represses transcription and translation of the tight junction protein zona occludens-1 modulating intestinal epithelial barrier function.Adherens and tight junctions: structure, function and connections to the actin cytoskeleton.Tight junctions on the move: molecular mechanisms for epithelial barrier regulation.Tight junction proteins: from barrier to tumorigenesis.ZO-1 recruitment to α-catenin--a novel mechanism for coupling the assembly of tight junctions to adherens junctions Epithelial junctions and polarity: complexes and kinases.Caveolae-mediated internalization of occludin and claudin-5 during CCL2-induced tight junction remodeling in brain endothelial cells.Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions.Hydrogen sulfide attenuates neurodegeneration and neurovascular dysfunction induced by intracerebral-administered homocysteine in mice.The dual role of zonula occludens (ZO) proteins.

P2860

Q21129349-C40465E4-111A-4C29-8A52-243595FE83EC Q24645152-A2DCFEF4-CD24-4513-8B55-B3766B3F92E0 Q24654117-08F5ABCA-7027-4395-A088-A3ADC57A3EC2 Q26861408-61CF325A-D114-405C-93CF-36C60E084E6B Q27648746-48C36739-9631-4781-8AAA-745A3402E1E5 Q27660107-12B69462-0333-460C-A787-10A1562BF2BC Q27675242-2BE866D5-8A04-4105-9D23-16DFC90A0BEE Q28269524-4BC949A8-FC7D-4BB4-9740-19B08C76EEC5 Q28395326-8587CD09-DBC9-4592-932D-C30C23C62C89 Q28941185-904FD39E-9039-41F3-A037-B4D03392C59E Q30009245-4F470B5B-6DB9-47DD-A332-B8655E65C6B2 Q30009921-0CAF1836-146D-46E4-9AFA-353BBB57E67E Q30010066-0A3BF2A5-E3FF-4D3F-ADB5-384684923479 Q30010079-5B8EAF37-5B4A-42D9-88CB-CAF3400C2249 Q30157022-6498CA09-21B4-48B5-8E57-F7DE611C4073 Q30157199-16A144E9-5B6B-4F30-B6C9-65E524969F3E Q30384261-55C55233-F2DB-4671-BD5F-1610BF0E5A03 Q30483283-1A7DE903-80C7-478B-B2D2-CDCC2F3F7353 Q33685399-B7181A3A-DD9D-4E95-8ECD-94BF21ABA795 Q34070506-2424E2C3-22CC-4B65-9E62-436EA5C821D3 Q34174733-A6B7E445-71D2-4826-A122-2124F0E46DA6 Q34421772-3C6D1970-ADBA-41FB-AB1D-31302644F0BA Q34483154-32BB0CD5-DFDD-4E45-935D-58AD00ED7DEB Q34548221-3DA96101-B53F-4BEA-ADB9-F0F81B31A3AF Q34918139-94D07AB1-E7F0-4CCF-97E4-2904C33B3433 Q35182998-86E06DBD-DE51-4987-A1BA-C2F7F10FE373 Q35756679-5E3C0483-C180-41F3-84D1-C99740797E22 Q36660697-5DB5657E-EC78-4306-9B0F-4C4D54552EED Q36812374-6155B96C-6CC7-4010-9EB8-679C5AA13C6E Q36812411-A4F4B757-1146-419C-9FD6-E88E56DBD945 Q36854925-A38DA82F-1295-4CC4-9F53-DBF0E3D0666A Q36940193-4915AD39-E81F-4E33-A504-25957347B8B3 Q36950607-F132829A-7D5A-4A99-AE45-45AD0E397B5D Q37118065-AB6FDC79-30D3-4E60-BE19-ED3C2BA6CDBF Q37132493-5B67585A-B45F-45CE-AE5A-8197E5E05A3F Q37241585-FB96DB4C-6418-4199-90DD-309FBB187E18 Q37253945-AD5426A8-44EE-49E5-8FF3-007BC2225A29 Q37524262-9152ACC3-C6E3-4C4B-8377-D691F45FCB1D Q37527202-E7585921-3F15-4050-952B-C3384F17FA35 Q37708020-C14C31F8-1243-4DAF-9EA8-B0CEA5157E6B

P2860

The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties.

http://www.wikidata.org/entity/Q30159513

description

2006 nî lūn-bûn

@nan

2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի դեկտեմբերին 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

The unique-5 and -6 motifs of ...... on and scaffolding properties.

@ast

The unique-5 and -6 motifs of ...... on and scaffolding properties.

@en

type

label

The unique-5 and -6 motifs of ...... on and scaffolding properties.

@ast

The unique-5 and -6 motifs of ...... on and scaffolding properties.

@en

prefLabel

The unique-5 and -6 motifs of ...... on and scaffolding properties.

@ast

The unique-5 and -6 motifs of ...... on and scaffolding properties.

@en

P1433

Q30159513-5D67E939-09C8-4118-A6EF-3D7439065DC6

P1476

Q30159513-0DD8F259-9990-43EB-95E9-9F60797E5737

P2093

Q30159513-2B511A3B-A5B0-4A00-9D34-EA6558D82886

Q30159513-98FA4F18-9C25-4239-96D8-BD2D38525EE0

Q30159513-BA60B4AD-5246-4DEC-97B8-2F8D135CCC2F

Q30159513-C373AFE2-D318-4624-BEC7-C561C97CB339

Q30159513-E010DC7F-0A2A-4464-A63B-54C09787305E

Q30159513-FC11F6EB-0F31-4B07-A195-86290EB77390

P2860

Q30159513-05A37F8C-9CD1-48C1-BCAC-F255FF94DDFD

Q30159513-072F1E6F-9E76-4DA5-90FE-68D80B2BEFCD

Q30159513-095F666F-D5B9-439B-A13E-65C5A98D32DE

Q30159513-1BF046B6-8769-4915-B00F-8E759330900D

Q30159513-1C7809DF-90B5-4E19-A6C9-D8A83313DB3E

Q30159513-25537CB3-A05F-4175-8C6A-E2C912155024

Q30159513-25F1DA2E-1A19-4F17-8358-2A4CF185B3FC

Q30159513-300AC1C7-CA73-434C-B87E-FA3C84159BDA

Q30159513-35B1151F-9B8E-40AB-AC8A-9A6FB3A7E530

Q30159513-3844DD51-6F84-49D4-AE2A-8CD0B43C8E46

P304

Q30159513-43586FB8-9CE1-4F33-B531-0B8AB6FBCD28

P31

Q30159513-9EA46B11-1113-4AFF-AC24-027A19B85FCB

P356

Q30159513-4EF557D2-1237-4136-938D-0781083F58AE

P433

Q30159513-6851AC1E-0E91-4520-9C8F-FCA7F197C10A

P478

Q30159513-4247C71F-4F99-4AC6-BDF9-4D258440C205

P577

Q30159513-FA52126B-4457-45F0-9A5B-ABBFC9DD21D3

P698

Q30159513-3CDCA136-2C1C-4A0E-8B05-9EBDBE488203

P932

Q30159513-E4C9A208-53D0-4DF5-9D01-B6D85457AD25

P356

MBC.E06-08-0764

P1433

Molecular Biology of the Cell

P1476

The unique-5 and -6 motifs of ...... on and scaffolding properties.

@en

P2093

Alan S Fanning

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

Brent P Little

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

Christoph Rahner

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

Darkhan Utepbergenov

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

James M Anderson

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

Zenta Walther

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

P2860

Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A

Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain

A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia

p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP

Intramolecular interactions regulate SAP97 binding to GKAP

Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins

Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95

Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites

Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton

Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein

P304

721-731

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

P31

scholarly article

P356

10.1091/MBC.E06-08-0764

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

P433

3

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

P478

18

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

P577

2006-12-20T00:00:00Z

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

P698

17182847

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

P932

1805089

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