Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock. - Wikidata - wikimedia - TriplyDB

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

http://www.wikidata.org/entity/Q34278664

about

RanBP2 modulates Cox11 and hexokinase I activities and haploinsufficiency of RanBP2 causes deficits in glucose metabolism PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus Hyperosmotic stress-induced ATF-2 activation through Polo-like kinase 3 in human corneal epithelial cells CCM1 and CCM2 protein interactions in cell signaling: implications for cerebral cavernous malformations pathogenesis CHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic response Role of the JIP4 scaffold protein in the regulation of mitogen-activated protein kinase signaling pathways Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38 Mutations within the programmed cell death 10 gene cause cerebral cavernous malformations Identification of protein interactions involved in cellular signaling Brx mediates the response of lymphocytes to osmotic stress through the activation of NFAT5 MKP-1 inhibits high NaCl-induced activation of p38 but does not inhibit the activation of TonEBP/OREBP: opposite roles of p38alpha and p38delta How do kinases contribute to tonicity-dependent regulation of the transcription factor NFAT5?Dynamic regulation of aquaporin-4 water channels in neurological disorders Cerebral cavernous malformation is a vascular disease associated with activated RhoA signaling Vascular anomalies: from genetics toward models for therapeutic trials Micro-CT Imaging Reveals Mekk3 Heterozygosity Prevents Cerebral Cavernous Malformations in Ccm2-Deficient Mice The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association.A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling complex involved in α1-adrenergic receptor-induced p38 activation Rho kinase inhibition rescues the endothelial cell cerebral cavernous malformation phenotype.Trophoblast stem cell maintenance by fibroblast growth factor 4 requires MEKK4 activation of Jun N-terminal kinase PAK is regulated by PI3K, PIX, CDC42, and PP2Calpha and mediates focal adhesion turnover in the hyperosmotic stress-induced p38 pathway Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2) interaction with Krev interaction trapped 1 (KRIT1) by disease-associated mutations KLF4 is a key determinant in the development and progression of cerebral cavernous malformations.Phosphorylation sites in the cerebral cavernous malformations complex Hyperosmotic stress signaling to the nucleus disrupts the Ran gradient and the production of RanGTP Laser-scanning velocimetry: a confocal microscopy method for quantitative measurement of cardiovascular performance in zebrafish embryos and larvae Hydroxyurea exposure triggers tissue-specific activation of p38 mitogen-activated protein kinase signaling and the DNA damage response in organogenesis-stage mouse embryos.Loss of Arp2/3 induces an NF-κB-dependent, nonautonomous effect on chemotactic signaling Coordination of satellite cell activation and self-renewal by Par-complex-dependent asymmetric activation of p38α/β MAPK Computational model explains high activity and rapid cycling of Rho GTPases within protein complexes Mouse preimplantation embryo responses to culture medium osmolarity include increased expression of CCM2 and p38 MAPK activation The neogenin intracellular domain regulates gene transcription via nuclear translocation.Cerebral cavernous malformation: new molecular and clinical insights.Recent insights into cerebral cavernous malformations: a complex jigsaw puzzle under construction.Safeguarding entry into mitosis: the antephase checkpoint.Biology of vascular malformations of the brain.Rac1 mediates NaCl-induced superoxide generation in the thick ascending limb.Role of cytoskeletal proteins in cerebral cavernous malformation signaling pathways: a proteomic analysis.

P2860

Q21145250-F602C6C3-9A40-4E11-AFCE-6D382F986881 Q24300270-E12F1D4A-3575-4457-9D84-C50DA5164C05 Q24307063-D50CD58E-434B-46A1-BAF2-E56D67BC0790 Q24307842-6A9F2F3D-5A83-4F70-93A3-5544D899716C Q24309334-C9DF8E2A-6A21-4313-A396-DD153DCB3C91 Q24336920-A7435D0D-298D-40CA-9BBB-519E4184FAA9 Q24519085-2C413B2C-1448-4B41-874B-E7D49B5BB8DE Q24528106-5F0BEA93-23B2-4F9B-A487-9B040A718B1E Q24530747-A2294D91-BCD6-4EA9-BD15-668883EAC210 Q24601574-436FD9BE-5668-4ECD-8DBE-7A090C394E57 Q24634561-6C0193C8-F24F-4A6A-B15D-8E0CB750F2CA Q24657455-2B8AC95F-C197-4159-825A-757B23177182 Q26770757-13690376-BC66-48E2-B379-36491F4B808A Q26777349-7E2C5E09-6EAE-40BE-9EB3-ABF342B72C53 Q26849566-571054A7-494C-45DA-9F3A-7873EF96EBBC Q27025402-CD7961F6-698B-4CDD-8605-095199F7AE87 Q27329910-D446819E-8AF8-4268-A13F-BE5940D30843 Q27437628-657FA1AD-CB6E-4B48-9795-E6E7D13382A9 Q27939643-BF9C6F3F-5DB9-42A8-BD98-06397B67D052 Q28115053-B2F79420-3F38-410C-8A5C-9070A90EC8CD Q28274176-90FACA33-788E-491E-AD3F-DF873724583F Q28505246-76D12F8B-3E56-4A5D-8E9D-CFE79D1B6E22 Q28582141-A8FA9E46-3A32-47B9-977F-7A8F55B3BB3E Q28650470-00EEEABA-E605-4AF0-B8E7-8498C16D609D Q30278010-1F88CF54-16B2-4D06-9BDB-EBB92A151D44 Q30423675-112D3114-E783-4EA4-A82D-5B3C37DF2DC0 Q30444083-79DE7689-6CE5-4446-AFBB-4A34B26B96BF Q30479978-F85AB7D4-8672-4026-AD04-C080CF92F635 Q30540055-D03360CA-3515-4DD2-B1EC-4F0F1A367279 Q30560511-3272D30F-D9AF-42DA-BE31-98932E88703B Q30582181-2D1D1452-807C-48E8-9FB3-30C27138B87B Q33265219-BD696D5D-E3B9-487C-A76D-C37FBB53B9EB Q33268789-A22E8317-34D4-464B-A870-67F863C5E6E5 Q33327050-E4F6B1BC-9785-4119-BD04-1AA3DB840E5E Q33342264-13F4BAAE-3686-46D2-BDC8-79182663D961 Q33348515-3D7822C6-F30D-4AA8-821A-7C6DC97B8A03 Q33558235-B6C17F8B-A795-4158-A6D5-5D39453E6BBE Q33606813-5C2EA77E-A9D9-48BB-87C3-6403A2F13B0B Q33655668-C64BBEB0-F39F-47D6-8526-23E235CCBB4D Q33707224-57B5CA71-4A8E-458D-9BC3-64060091FF84

P2860

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

http://www.wikidata.org/entity/Q34278664

description

2003 nî lūn-bûn

@nan

2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@ast

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@en

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@nl

type

label

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@ast

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@en

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@nl

prefLabel

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@ast

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@en

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.

@nl

P1433

Q34278664-CC1B9D73-1F61-4BA8-A798-47A501845B55

P1476

Q34278664-4F626F23-179C-4975-88DE-9555A96E3682

P2093

Q34278664-0772823D-4A0D-46E6-9D16-1E9922A831A4

Q34278664-1BE5465B-373C-4616-809D-B306C4F0046F

Q34278664-4360320B-776E-4C5E-84E8-4693F3F567F9

Q34278664-7D58A0BD-E6ED-451D-A391-E8D0407F5494

Q34278664-8FBA855F-E9FD-4179-88E8-31D96CAF71BE

Q34278664-CD2CA2E0-0408-4CA5-B8F2-2ABB8286E248

Q34278664-E1EF2542-C0B5-4E79-8576-DF401691943C

Q34278664-F7F984B4-C814-439B-9956-79CFAE8C67FF

P2888

Q34278664-19827D3D-B837-447E-AFB1-2A561313D006

P304

Q34278664-E9FF171E-14D5-473F-83E4-27D9B4244DBF

P31

Q34278664-31B70D3D-730E-45FD-987A-A1B3B484F10F

P356

Q34278664-A54A6A0D-3C58-404C-ABF5-7BBD009DB6CC

P433

Q34278664-D2B8B7C6-E255-4251-B9E3-64CB190BF184

P478

Q34278664-FAECE3A3-B2D0-47B9-AFDD-6B22DEC96131

P50

Q34278664-47C85303-1069-4906-A0DE-2A5629112041

P577

Q34278664-1B8B2D87-AF82-4D6A-A3A6-426711EA85EE

P5875

Q34278664-5894CA5E-19C7-43BD-83F2-2C942928AC35

P6179

Q34278664-AB1036C2-F576-4A2F-9779-85D57DC0BBE8

P698

Q34278664-D114BE41-41F3-482D-882D-5814F52122C8

P356

P1433

Nature Cell Biology

P1476

Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock

@en

P2093

Amy N Abell

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

Bruce D Cuevas

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

Eric A Horne

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

Gary L Johnson

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

Katherine E Lobel-Rice

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

Mark T Uhlik

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

Nancy L Johnson

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

Weiyong Sun

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

P2888

P304

1104-1110

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

P31

scholarly article

P356

10.1038/NCB1071

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

P433

12

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

P478

5

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

P50

Mark L Dell'Acqua

P577

2003-11-23T00:00:00Z

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

P5875

8993194

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

P6179

1031905902

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

P698

14634666

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