Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells. - Wikidata - wikimedia - TriplyDB

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

http://www.wikidata.org/entity/Q36559702

about

Anthrax lethal toxin downregulates claudin-5 expression in human endothelial tight junctions Tight junction between endothelial cells: the interaction between nanoparticles and blood vessels From mechanical force to RhoA activation Methamphetamine effects on blood-brain barrier structure and function Poly(ADP-ribose) polymerase-1 inhibition in brain endothelium protects the blood-brain barrier under physiologic and neuroinflammatory conditions.Residues in a Highly Conserved Claudin-1 Motif Are Required for Hepatitis C Virus Entry and Mediate the Formation of Cell-Cell Contacts Rho kinase as a target for cerebral vascular disorders The blood-testis barrier and its implications for male contraception The occludin and ZO-1 complex, defined by small angle X-ray scattering and NMR, has implications for modulating tight junction permeability.Inhibition of glycogen synthase kinase 3beta (GSK3beta) decreases inflammatory responses in brain endothelial cells Cerebral cavernous malformations proteins inhibit Rho kinase to stabilize vascular integrity.Molecular insights and therapeutic targets for blood-brain barrier disruption in ischemic stroke: critical role of matrix metalloproteinases and tissue-type plasminogen activator Placenta growth factor-1 exerts time-dependent stabilization of adherens junctions following VEGF-induced vascular permeability.Treatment with a rho kinase inhibitor improves survival from graft-versus-host disease in mice after MHC-haploidentical hematopoietic cell transplantation.CD8 T cell-initiated vascular endothelial growth factor expression promotes central nervous system vascular permeability under neuroinflammatory conditions.Fasudil regulates T cell responses through polarization of BV-2 cells in mice experimental autoimmune encephalomyelitis.Targeting the shift from M1 to M2 macrophages in experimental autoimmune encephalomyelitis mice treated with fasudil.Claudins and the modulation of tight junction permeability.Caffeine protects against disruptions of the blood-brain barrier in animal models of Alzheimer's and Parkinson's diseases.Breaking down the barrier: the effects of HIV-1 on the blood-brain barrier.Claudins: control of barrier function and regulation in response to oxidant stress.ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation.Angiopoietin-1 Regulates Brain Endothelial Permeability through PTPN-2 Mediated Tyrosine Dephosphorylation of Occludin Phenotypes of trypsin- and collagenase-prepared bovine corneal endothelial cells in the presence of a selective Rho kinase inhibitor, Y-27632.Occludin oligomeric assemblies at tight junctions of the blood-brain barrier are altered by hypoxia and reoxygenation stress.Engaging neuroscience to advance translational research in brain barrier biology.Role of reactive oxygen and nitrogen species in the vascular responses to inflammation.Protein kinase cβ phosphorylates occludin regulating tight junction trafficking in vascular endothelial growth factor-induced permeability in vivo.The dual action of poly(ADP-ribose) polymerase -1 (PARP-1) inhibition in HIV-1 infection: HIV-1 LTR inhibition and diminution in Rho GTPase activity Multiple roles for the Na,K-ATPase subunits, Atp1a1 and Fxyd1, during brain ventricle development Shear-dependent attenuation of cellular ROS levels can suppress proinflammatory cytokine injury to human brain microvascular endothelial barrier properties.Glycogen synthase kinase 3β inhibition prevents monocyte migration across brain endothelial cells via Rac1-GTPase suppression and down-regulation of active integrin conformation.Changes in the phosphorylation of claudins during the course of experimental colitis The tension mounts: stress fibers as force-generating mechanotransducers HIV-1, methamphetamine and astrocyte glutamate regulation: combined excitotoxic implications for neuro-AIDS.Persistent neuroinflammatory effects of serial exposure to stress and methamphetamine on the blood-brain barrier.Matrix metalloproteinases and blood-brain barrier disruption in acute ischemic stroke.ROCK activity regulates functional tight junction assembly during blastocyst formation in porcine parthenogenetic embryos.Junctional proteins of the blood-brain barrier: New insights into function and dysfunction.Biology of claudins.

P2860

Q24339455-3008A498-B311-4AEF-806D-DCA1469C5369 Q26747571-284EE37A-ABB3-46AD-963D-3C8D5CA453B1 Q26824081-B10A4C18-56B1-473F-B27A-3991CAF88472 Q26825795-BF41843D-9D14-4D9E-BCC2-075B2EF773DF Q27321704-0EEB78E5-E2F7-4FE5-97A4-B0E7AC46E2F1 Q27488396-63F24289-FE88-4439-BBA5-F5BC2BD3D1BF Q28081507-1D44879D-A628-4FD1-9462-2D5FB053A507 Q28395237-494ADC94-4188-4619-9396-F2F404B84800 Q30010066-9BA337A7-6A03-42CB-9FE1-EACD515ED023 Q33597201-ACDEAA23-0F96-4CB4-A857-DFB2E2F07732 Q33794968-1F72DBA4-4C69-4E7D-91B2-1AB21958581C Q33823616-165596DC-A7EE-4B98-88A3-E4DF1C097ED7 Q33862606-7CE22229-6E19-4858-A2CD-BFF9D9B3A37D Q33918485-8371AE2D-08F6-4813-A443-57B46F98F4B8 Q33957132-1ADB66E1-B657-4332-A755-75195FBFE3F8 Q34451923-7FD06442-1F34-4C5F-9716-D592D34524FF Q34589502-BDE8702D-9795-4CF7-916D-6ABFF6F15655 Q34650517-10FDB132-EF89-4C4D-B2CF-223EF355DAE4 Q34905120-4342174F-3641-4BA5-B7FA-6BE1C9E4466B Q35114694-D21ADC67-08CA-4F81-8085-7C279AC1B34B Q35130231-74977AAD-4979-4643-974B-552175EC2FDE Q35184431-38D7D1A4-16B4-4BBB-AFBE-9BE2E85CF5CD Q35668323-6E081E38-5DF1-49C8-85AC-3A39D9933E0D Q35683985-6140C9E8-C2D9-49E9-9312-25121F423C22 Q35855676-9D1A8F76-CEEB-4EEE-A322-A42B7D541616 Q35909313-93940509-7425-44A5-A1BD-8D940DD87F67 Q35948515-22FDCFAD-2CC4-4169-95E6-080BFF7C8D8B Q35976653-CC927B54-F78E-4A28-900F-841190034C9E Q35992296-7E83AD52-76E2-46C1-AF44-1CFDBDE57725 Q36110119-4B547128-42ED-407C-A0F1-D0A5189875DB Q36267412-E3A74690-8B50-43A1-8257-54BF86CF684E Q36295454-7F001412-8C49-41F6-A45E-0C1669CC71AB Q36375073-49613175-549F-4AF4-847F-C320C94BFF20 Q36525640-D74FCD58-7D85-4699-8128-64DC7B86A147 Q36634233-F23875F2-E86F-4BE2-9493-7F32CB996D91 Q36730363-489D842B-B252-43C5-A714-DCEB4CF4792B Q36736442-D0AD0E1A-8FED-4A41-A647-ECD7CD2F13C2 Q36794215-DA784395-4C89-42CC-BBC3-98EC0369350F Q36812374-20D82758-4E21-4E54-8B35-0715B9B92A07 Q36956748-AC816960-219B-4E17-9181-0925CB9F2572

P2860

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

http://www.wikidata.org/entity/Q36559702

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

@ast

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

@en

type

label

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

@ast

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

@en

prefLabel

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

@ast

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells.

@en

P1433

Q36559702-A90421ED-6388-470D-8347-F9F5883C378C

P1476

Q36559702-754A4749-2443-4779-B9A5-1B5681A30642

P2093

Q36559702-26ED1467-C1E9-40BB-83FA-7366DEE7DD3E

Q36559702-734ACC70-D90F-4AD9-B19F-AFF39F91EA07

Q36559702-8F1A0AFC-92BD-47E0-A606-F1397A9DB94E

Q36559702-AABBA69C-E1E5-4025-BE4F-7AD33EBA650D

Q36559702-C89C922A-7683-49BD-A171-9AB0F82A1EED

Q36559702-E50ECDAC-1434-490A-A2B4-87A05AEC2A19

Q36559702-EB52C00B-779F-44EB-97CB-F9FA8893C87C

P2860

Q36559702-02917836-8B5C-466B-868B-B806035D21D1

Q36559702-0B6BFB70-4C40-4878-8AB6-95B5D6687623

Q36559702-0C3109F1-732B-4B24-835D-9AD0E665909A

Q36559702-16F579C5-36C6-4FE5-A31A-5E0995D85B47

Q36559702-19DDFD97-2330-40D2-B896-E9460ADFEBED

Q36559702-1C11EEFB-5439-4989-9C70-A598D1420164

Q36559702-248B46C8-6C6C-44D1-A08E-9C9379A278E7

Q36559702-28A713D9-F060-4FA3-AD2F-DF7A8FB32544

Q36559702-2FC54C9D-2565-4B99-9934-0431699D4F47

Q36559702-39D0181F-DB46-4C05-946F-3899735827C3

P304

Q36559702-A474A35B-5557-41F2-8EDD-3EF2687307FD

P31

Q36559702-C082005A-07BC-41D2-82DA-5B474DCD3F46

P356

Q36559702-AAFCAE83-DFF7-487D-BF13-5BC2CF516259

P407

Q36559702-8946234A-B2F0-4FA1-96EE-523DA202ABCD

P433

Q36559702-2073270E-1E5D-439D-9F6C-39BF4D8FB223

P478

Q36559702-F167F2C6-D42F-42F6-A169-5F736CADED88

P50

Q36559702-27D19C1A-87F2-4B10-AED8-EB18F8FC6B3D

P577

Q36559702-6446A381-7AD5-4DC9-8F00-11C3FAE50E64

P5875

Q36559702-4A4E4937-E99C-446B-9E8D-E7ACBC9D157A

P698

Q36559702-9ACF5792-7A1B-434E-ACE3-5F7EA145A412

P921

Q36559702-319E4627-0592-47EE-BECC-640810B4ABF2

Q36559702-8DCD0868-1BE8-4CDA-BA54-675C67D281CE

P932

Q36559702-BEA68201-C839-4269-A812-ED713E32D03E

P356

AJPATH.2008.070076

P1433

The American Journal of Pathology

P1476

Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells

@en

P2093

Kozo Kaibuchi

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

Masaru Yamamoto

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

Ronald L Cerny

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

Servio H Ramirez

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

Shinji Sato

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

Tomomi Kiyota

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

Yuri Persidsky

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

P2860

Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands

Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions

Tight junctions of the blood-brain barrier: development, composition and regulation

Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)

Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells

Occludin: a novel integral membrane protein localizing at tight junctions

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice

Protein kinase C regulates the phosphorylation and cellular localization of occludin

Identification of a putative target for Rho as the serine-threonine kinase protein kinase N

P304

521-533

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

P31

scholarly article

P356

10.2353/AJPATH.2008.070076

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

P407

P433

2

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

P478

172

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

P50

P577

2008-01-10T00:00:00Z

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

P5875

5662347

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

P698

18187566

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

P921

phosphorylation

P932

2312373

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