MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases.
about
MAP kinase phosphatasesMKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle proteinScaffold role of a mitogen-activated protein kinase phosphatase, SKRP1, for the JNK signaling pathwayThe NLR adaptor ASC/PYCARD regulates DUSP10, mitogen-activated protein kinase (MAPK), and chemokine induction independent of the inflammasomeA distinct interaction mode revealed by the crystal structure of the kinase p38α with the MAPK binding domain of the phosphatase MKP5JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein, regulates duration of JNK activity.Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38.Multiple molecular targets of resveratrol: Anti-carcinogenic mechanismsSensitivity and fidelity of DNA microarray improved with integration of Amplified Differential Gene Expression (ADGE)Regulatory Roles of MAPK Phosphatases in CancerpCAP-based peptide substrates: the new tool in the box of tyrosine phosphatase assaysA novel dual specificity phosphatase SKRP1 interacts with the MAPK kinase MKK7 and inactivates the JNK MAPK pathway. Implication for the precise regulation of the particular MAPK pathwayConvergent functional genomics of oligodendrocyte differentiation identifies multiple autoinhibitory signaling circuitsA non-redundant role for MKP5 in limiting ROS production and preventing LPS-induced vascular injuryRegulation of innate and adaptive immune responses by MAP kinase phosphatase 5A novel mitogen-activated protein kinase phosphatase is an important negative regulator of lipopolysaccharide-mediated c-Jun N-terminal kinase activation in mouse macrophage cell lines.DUSP10 regulates intestinal epithelial cell growth and colorectal tumorigenesis.Oxidative stress-induced JNK activation contributes to proinflammatory phenotype of aging diabetic mesangial cells.ROS signaling by NOX4 drives fibroblast-to-myofibroblast differentiation in the diseased prostatic stromaRole of MLK3 in the regulation of mitogen-activated protein kinase signaling cascades.Synergistic induction of tissue factor by coagulation factor Xa and TNF: evidence for involvement of negative regulatory signaling cascadesA Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs.Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress.The JNK-interacting protein-1 scaffold protein targets MAPK phosphatase-7 to dephosphorylate JNK.RACK1 mediates activation of JNK by protein kinase C [corrected].The noncatalytic amino terminus of mitogen-activated protein kinase phosphatase 1 directs nuclear targeting and serum response element transcriptional regulation.Regulation of stress-activated protein kinase signaling pathways by protein phosphatases.mTORC2 modulates feedback regulation of p38 MAPK activity via DUSP10/MKP5 to confer differential responses to PP242 in glioblastomaInsulin growth factor-binding protein 2 is a candidate biomarker for PTEN status and PI3K/Akt pathway activation in glioblastoma and prostate cancer.Regulation of Adipose Tissue Inflammation and Insulin Resistance by MAPK Phosphatase 5.Histone deacetylase 7 functions as a key regulator of genes involved in both positive and negative selection of thymocytesMap kinase phosphatase 5 protects against sepsis-induced acute lung injury.Ubiquitin chains in the ladder of MAPK signaling.Resistance to apoptosis, increased growth potential, and altered gene expression in cells that survived genotoxic hexavalent chromium [Cr(VI)] exposure.The hepatitis E virus open reading frame 3 protein activates ERK through binding and inhibition of the MAPK phosphataseImproved regenerative myogenesis and muscular dystrophy in mice lacking Mkp5.Label transfer reagents to probe p38 MAPK binding partnersType 2 cGMP-dependent protein kinase regulates homeostasis by blocking c-Jun N-terminal kinase in the colon epithelium.Role for Prdx1 as a specific sensor in redox-regulated senescence in breast cancer.Histone deacetylase inhibitor impairs plasminogen activator inhibitor-1 expression via inhibiting TNF-α-activated MAPK/AP-1 signaling cascade.
P2860
Q21999790-95F19CF2-5159-4F90-A2B6-C8085B315BA9Q24291539-7CCB47FF-701C-426A-98BA-187F4D2C5573Q24294660-EAF84748-4F70-4D0D-822A-6D281D7AA845Q24299627-5B17B9C5-0010-4C0F-BAD2-75476649ED3CQ24306508-89FED7E5-A1F6-4341-8B60-F98A01655AB3Q24534871-50CCB24F-C312-4B07-82B8-C336FB42C92DQ24537701-A7A0FFA9-0D45-4F3B-B138-B0B9BD4D2596Q24648759-0C096485-1189-4A98-8A71-84AAC742984EQ24793538-5F7AB55B-B0E4-4810-9945-6466565D8804Q26751025-F68D2B6A-5517-4894-9B29-6139F5328E1FQ26830090-BE59BB30-836E-456A-BD57-E19FDC74A04AQ28215085-D1F4ECDE-E2E7-4BC5-BF30-25037BDBF34DQ28572241-6D252B25-E5BE-482A-9327-72F66DC1F79BQ28592281-05FBCC63-8A66-4F61-A791-E4967896D063Q28594911-06724B34-1909-42C2-9B33-88F8B262D7FBQ30723911-DF4D2B7C-B05F-47B2-8ACD-31CEE332D652Q31813071-FEA872F6-882B-4EEA-93D6-29787C9C29F9Q33570113-7F2CD5A9-262D-4C92-8F7A-4E6120EA0920Q33636981-9FBF1FAA-5D16-43BD-8F12-2B4B40E3B4E9Q33758352-B2A3D933-C2CF-48E8-8906-217EE31FB052Q33922885-B9895C67-5263-4276-AE49-6D9D2BE82E89Q33947411-68D36F44-4D18-4489-B6B3-5399555F9F18Q33967914-16F7594E-667E-4D27-98E6-8CD8BEC67DB2Q34170029-242F317D-E1EA-4EAF-99D2-DC05EEEACD7EQ34191543-C764FC09-6714-4E0C-BB5A-0299016AF72DQ34419558-00C5488D-381B-463D-8573-2E7BBFC37C61Q34539377-F5E41D9C-F46A-42FA-8CF2-447476A30724Q34786646-FE2341BF-066A-4AE9-AC9C-3FB6D377EF34Q35720774-71F45873-C341-4B9B-B07E-957B9D239C1DQ35721642-837A1607-21F2-458E-870C-EB029BB4F35AQ35949614-C8E40C9E-B0F6-4CB2-94CA-DE3259D36832Q35994496-790DEB20-F882-4618-B05C-8797234C8C98Q36108376-24D4EB03-44F0-47B3-87BA-4592D950D6BAQ36147392-9C818F7A-84B5-4702-8732-F4527D8244E3Q36739811-5AFD74C1-73DB-460E-8305-8B7D1355231EQ36793413-0585192D-1553-4136-9E72-0A23C56BBB1BQ37146385-9E6017A5-3592-417C-9F2B-FD65DEADAD53Q37578804-5CA7D15D-3BBB-47AB-9A52-2220265E637DQ37605870-5172507B-8C4A-4F3C-BC65-D9A4ED17AF9DQ37636118-C7541B89-7A70-4799-AE74-5DB50A9705E1
P2860
MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին 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
MKP5, a new member of the MAP ...... ates stress-activated kinases.
@ast
MKP5, a new member of the MAP ...... ates stress-activated kinases.
@en
type
label
MKP5, a new member of the MAP ...... ates stress-activated kinases.
@ast
MKP5, a new member of the MAP ...... ates stress-activated kinases.
@en
prefLabel
MKP5, a new member of the MAP ...... ates stress-activated kinases.
@ast
MKP5, a new member of the MAP ...... ates stress-activated kinases.
@en
P2093
P2860
P356
P1433
P1476
MKP5, a new member of the MAP ...... ates stress-activated kinases.
@en
P2093
A Theodosiou
C Gillieron
S Arkinstall
P2860
P2888
P304
P356
10.1038/SJ.ONC.1203185
P407
P577
1999-11-01T00:00:00Z
P6179
1026105952