The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases. - Wikidata - wikimedia - TriplyDB

The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases.

The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases.

http://www.wikidata.org/entity/Q44039955

about

Modulation of neuronal signal transduction and memory formation by synaptic zinc Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases Metal-dependent protein phosphatase 1A functions as an extracellular signal-regulated kinase phosphatase Diacylglycerol kinase-zeta localization in skeletal muscle is regulated by phosphorylation and interaction with syntrophins Activation of Erk and JNK MAPK pathways by acute swim stress in rat brain regions Ultrasensitization: switch-like regulation of cellular signaling by transcriptional induction pCAP-based peptide substrates: the new tool in the box of tyrosine phosphatase assays LB100, a small molecule inhibitor of PP2A with potent chemo- and radio-sensitizing potential The relationship between the MMP system, adrenoceptors and phosphoprotein phosphatases Crystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold for Structure-based Drug Design of Serine/Threonine Phosphatase Inhibitors Mitogen-activated Protein Kinase (MAPK) Phosphatase 3-mediated Cross-talk between MAPKs ERK2 and p38 Structural Insight into Caenorhabditis elegans Sex-determining Protein FEM-2 Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1 Rapid alteration of protein phosphorylation during postmortem: implication in the study of protein phosphorylation Segregation and crosstalk of D1 receptor-mediated activation of ERK in striatal medium spiny neurons upon acute administration of psychostimulants DUSP6 (MKP3) null mice show enhanced ERK1/2 phosphorylation at baseline and increased myocyte proliferation in the heart affecting disease susceptibility Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2.Topological analysis of MAPK cascade for kinetic ErbB signaling.Regulation of a protein phosphatase cascade allows convergent dopamine and glutamate signals to activate ERK in the striatum PP2A inhibition from LB100 therapy enhances daunorubicin cytotoxicity in secondary acute myeloid leukemia via miR-181b-1 upregulation.Induction of nitric oxide synthase in Anopheles stephensi by Plasmodium falciparum: mechanism of signaling and the role of parasite glycosylphosphatidylinositols.Epidermal growth factor receptor mutation in combination with expression of MIG6 alters gefitinib sensitivity.Serine 129 phosphorylation reduces the ability of alpha-synuclein to regulate tyrosine hydroxylase and protein phosphatase 2A in vitro and in vivo.Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling.Protein phosphatase-dependent circadian regulation of intermediate-term associative memory.Molecular determinants of substrate recognition in hematopoietic protein-tyrosine phosphatase.Interconnected network motifs control podocyte morphology and kidney function.MAP kinase modules: the excursion model and the steps that count.Specificity profiling of dual specificity phosphatase vaccinia VH1-related (VHR) reveals two distinct substrate binding modes Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3.Dynamic regulation of extracellular signal-regulated kinase (ERK) by protein phosphatase 2A regulatory subunit B56γ1 in nuclei induces cell migration.The role of specific mitogen-activated protein kinase signaling cascades in the regulation of steroidogenesis Solution NMR insights into docking interactions involving inactive ERK2 A cholesterol-regulated PP2A/HePTP complex with dual specificity ERK1/2 phosphatase activity.Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states.Identification of inhibitors that target dual-specificity phosphatase 5 provide new insights into the binding requirements for the two phosphate pockets Inhibition of hematopoietic protein tyrosine phosphatase augments and prolongs ERK1/2 and p38 activation Glutaminolysis Was Induced by TGF-β1 through PP2Ac Regulated Raf-MEK-ERK Signaling in Endothelial Cells.Resistance to apoptosis, increased growth potential, and altered gene expression in cells that survived genotoxic hexavalent chromium [Cr(VI)] exposure.

P2860

Q21090473-9F2D3B00-8B69-4FFD-B415-F1CD3AEFFE5A Q24316361-FC864C73-3622-4F50-917F-F6EC6195DCC8 Q24337870-BA6704C4-925C-4664-8C87-F201730EEC93 Q24644928-50435AE9-5FA5-4E16-9C1F-C37BE501B590 Q24791140-131B88A1-7DFF-4446-A93F-7ABDDE0A4894 Q24811827-76FC0ED6-02CA-4984-9DCE-4CF3AE7A1FBB Q26830090-C7901B07-1A88-4F17-B5AC-814A7CC40038 Q26865711-DD1BAD74-D099-4EBD-94B7-2631C2547B45 Q27003263-02F67AFE-0D88-46AC-BB94-182CDA992599 Q27652817-50342D90-A306-4494-9FBF-FB50B82BB6EB Q27667368-4C3F0CE1-E813-440D-ADC7-B0B71C58D5F0 Q27678591-F8D18AE4-97CB-4C66-AAA4-BEBC048BD804 Q27695708-38277AD4-1035-41E2-BDEA-F6D25FBD12F6 Q28271104-2380D830-7D8C-45BB-A201-AF9566F4483E Q28392483-AC09CFD7-E0A1-47BA-98BA-DC7633960AE9 Q28395155-850AA08C-020B-4D45-BF65-4AF71F653EE4 Q28511686-C24A3DED-3589-47F4-B19F-17E8226F7615 Q30952448-3DF3D9ED-F2D0-43CB-8A5E-070E6B7353C4 Q33323383-853ED4D8-87BC-4925-8F0F-0D03D8ED3995 Q33723743-7869E066-BEF5-4C5E-A540-549D85AA4982 Q33767159-E2CF5885-49ED-4C81-BA2A-E30A177B449F Q33769102-F0437118-60E6-457D-ABB4-FB4E45F295D7 Q33824203-31521A9A-A730-4A2F-B842-6F50B44539F0 Q33885205-4A29AB56-0657-420A-8CAE-E06571342F47 Q34289063-368D7B51-5D22-4951-B013-680F3018283F Q34331443-D26E3F49-6578-4D9A-93F8-DFA233637B21 Q34355962-CC8139B3-D07A-45BA-A8E8-FA0D71EC2CCC Q34455351-6C4F6040-4CB4-4CD2-8515-8D80489312F0 Q34467087-14F5A2EF-D80C-4573-A9FF-96ADCCCBF6C5 Q34549319-1DDB71A2-AD33-4381-B3EA-233544826D42 Q34600125-979D0B3F-004C-4EB7-95C5-41AA2C37FE56 Q34737646-59C86752-A835-491F-A64F-4AFEB55E4AA3 Q35001465-405894EB-FA3E-44D2-A9BF-8CAAD69BCB72 Q35012791-93A34E39-E010-4988-84DA-CB60C0DA268D Q35032640-26FB41C9-0833-4EF6-829D-15E0ABA5DAFC Q35674496-04658859-9F68-4EF3-8143-027831E78F5F Q35749625-1ECC9C1B-C1F5-473B-8E38-38D040D23E13 Q35784471-C326EF0B-1CBC-4596-9DC2-4717380D1138 Q36128637-5174D8DB-D349-4328-A74A-9D2635AD7473 Q36147392-757A0479-6E66-4B5A-8E64-3EF621860745

P2860

The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases.

http://www.wikidata.org/entity/Q44039955

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

2002年學術文章

@zh-hant

name

The specificity of extracellul ...... ation by protein phosphatases.

@en

The specificity of extracellul ...... ation by protein phosphatases.

@nl

type

label

The specificity of extracellul ...... ation by protein phosphatases.

@en

The specificity of extracellul ...... ation by protein phosphatases.

@nl

prefLabel

The specificity of extracellul ...... ation by protein phosphatases.

@en

The specificity of extracellul ...... ation by protein phosphatases.

@nl

P1433

Q44039955-48581779-741C-423F-B8C3-A9D963E0B32F

P1476

Q44039955-4B8D686E-1EED-4F83-9029-D386EDEBD0AF

P2093

Q44039955-06975F19-3732-4D50-88F0-A205DD61889C

Q44039955-0E377990-BC34-46B4-AED6-ECBDEE0A44CC

Q44039955-308489D1-C2AB-47DA-8971-B8E3AE14E571

Q44039955-6FBCC054-C16E-4AE7-B3D7-A890DA2D5043

Q44039955-7009DDB8-DC14-4868-BD70-5A6CB9ACF319

P2860

Q44039955-01738F08-2DBA-4388-B8EE-DE923C488E8E

Q44039955-0A784466-08F7-4C0B-924E-C17BB379F316

Q44039955-1E709007-F3DA-42CA-92E6-92EE54BE7BB6

Q44039955-3C8932FA-BD2F-41E8-B691-4BA6D1C345D2

Q44039955-3FAC62E8-4369-4759-91EF-ED9E6634336F

Q44039955-3FD4A940-C44A-47C8-A6F6-20C138D6929D

Q44039955-40AB4CA2-369A-46C6-AE82-06BA4F4C364D

Q44039955-47981678-B54E-45EE-95D0-F41E592C1F1C

Q44039955-47BE6BCB-4A9F-4A8D-ADBA-2348F3523953

Q44039955-4CC55828-275B-4491-855D-E5A310284D98

P304

Q44039955-3C6A8167-23A9-4399-984E-2A4BEF4BDBBA

P31

Q44039955-9A35B8F6-4A1F-43E6-AAD8-B1B9A2D8182F

P356

Q44039955-C6A077F6-94F2-49D3-BC4A-3AC289E05E4F

P407

Q44039955-20DCFB8C-4ECA-46D2-9489-BC2703B75292

P433

Q44039955-C80F166E-30B2-4A67-A2D3-1685B78745C8

P478

Q44039955-6F7E5230-9EEE-4235-A22F-BC6708606C87

P577

Q44039955-C02DBDFB-1D3D-43C6-B239-360331CC23E8

P698

Q44039955-57E3A52C-736D-4649-8D87-09AA3F60B4D1

P356

P1433

Journal of Biological Chemistry

P1476

The specificity of extracellul ...... ation by protein phosphatases.

@en

P2093

Bo Zhou

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

David L Brautigan

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

Yu Zhao

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

Zhi-Xin Wang

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

Zhong-Yin Zhang

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

P2860

Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5

Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm

Structural basis of plasticity in protein tyrosine phosphatase 1B substrate recognition

Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation

The purification and characterization of a human dual-specific protein tyrosine phosphatase

Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways.

PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.

Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevisiae.

P304

31818-31825

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

P31

scholarly article

P356

10.1074/JBC.M203969200

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

P407

P433

35

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

P478

277

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

P577

2002-06-24T00:00:00Z

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

P698

12082107

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