The role of serine/threonine protein phosphatases in exocytosis - Wikidata - awgldk - TriplyDB

The role of serine/threonine protein phosphatases in exocytosis

The role of serine/threonine protein phosphatases in exocytosis

http://www.wikidata.org/entity/Q35128680

about

Beta-cell CaV channel regulation in physiology and pathophysiology.Anchored phosphatases modulate glucose homeostasis PP2B-mediated dephosphorylation of c-Jun C terminus regulates phorbol ester-induced c-Jun/Sp1 interaction in A431 cells.The role of intracellular signaling in insulin-mediated regulation of drug metabolizing enzyme gene and protein expression.The cannabinoid agonist WIN55212-2 decreases L-DOPA-induced PKA activation and dyskinetic behavior in 6-OHDA-treated rats Myosin phosphatase and RhoA-activated kinase modulate neurotransmitter release by regulating SNAP-25 of SNARE complex.Transcriptional profiling of native inner medullary collecting duct cells from rat kidney Lewy-like aggregation of α-synuclein reduces protein phosphatase 2A activity in vitro and in vivo.NMDA receptor-mediated extracellular adenosine accumulation is blocked by phosphatase 1/2A inhibitors.Interneuron activity controls endocannabinoid-mediated presynaptic plasticity through calcineurin.Inhibition of serine/threonine phosphatase enhances arachidonic acid-induced [Ca2+]i via protein kinase A.Evolutionary Cell Biology of Proteins from Protists to Humans and Plants.Antipsychotic drugs elevate mRNA levels of presynaptic proteins in the frontal cortex of the rat.Protein phosphatase 2B (PP2B, calcineurin) in Paramecium: partial characterization reveals that two members of the unusually large catalytic subunit family have distinct roles in calcium-dependent processes.Extracellular calcium chronically induced human osteoblasts effects: specific modulation of osteocalcin and collagen type XV.The Serine/Threonine-Protein Phosphatase 1 From Is Actively Involved in Suppressive Regulatory Roles on Immune Functions of Goat Peripheral Blood Mononuclear Cells Comparative 1D Blue-Native electrophoresis analysis of Plasmodium falciparum and human proteins associated with cytoadherence

P2860

Q27863802-973D406C-32FA-4F7A-81B3-41F0489BB587 Q28507313-8C1CA1F0-9093-4A87-87E2-81DA6D42BF98 Q35650808-1BCF0DF9-E228-40CC-B206-2A098B6BC6FD Q35688212-1AD7EE7C-F4C5-4841-86BB-3E0DCABB9C89 Q35740152-7774B649-8C68-494E-A41A-F06A28AD6477 Q36367152-B2AE9CFF-E173-4602-B36A-D90E046C7B52 Q36512949-62F2E05E-F12E-4A7E-87C0-E9D8FA39B5DF Q36603477-FD687597-3C48-46FE-9051-57159A6C4B67 Q36766306-03A9B883-4480-47F7-A93A-1D84EBE35996 Q36786835-83272AFB-BF1F-4C4C-949B-6AA0344D428F Q37086469-4CB0445E-2A70-4063-81BD-CC2B6A05B4E3 Q39441714-6B3834EC-9811-4936-9F82-1AC6080B325F Q42539139-65E05C80-01A3-4408-964F-468C32A2B980 Q42735129-6C1DF789-36FF-48FC-9598-014996958AB6 Q53209838-081C1D85-FA0E-47B8-8469-C50C94D470E8 Q57175797-64A9662A-0555-4D85-9695-82743C552582 Q58447207-6ED26213-0705-43FD-8327-FD7CBA6AA157

P2860

The role of serine/threonine protein phosphatases in exocytosis

http://www.wikidata.org/entity/Q35128680

description

2003 nî lūn-bûn

@nan

2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի օգոստոսին 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

The role of serine/threonine protein phosphatases in exocytosis

@ast

The role of serine/threonine protein phosphatases in exocytosis

@en

type

label

The role of serine/threonine protein phosphatases in exocytosis

@ast

The role of serine/threonine protein phosphatases in exocytosis

@en

prefLabel

The role of serine/threonine protein phosphatases in exocytosis

@ast

The role of serine/threonine protein phosphatases in exocytosis

@en

P1433

Q35128680-76BB823B-E652-4B4E-940E-8C1F2919BB0B

P1476

Q35128680-BFC2D694-CE6D-4460-9914-F3D492485224

P2093

Q35128680-5894618A-668C-4DFF-88E8-EEF62B1B6356

Q35128680-83CBAF14-EAEC-4A0C-9FD1-CF0C785FF45D

Q35128680-86DC8C0E-8857-453C-80F7-6CA8A210EB35

Q35128680-E49F4A9F-6E05-4928-BC14-9E8486EE02E0

P2860

Q35128680-01061C18-5765-4136-934F-DDF439BAC9FE

Q35128680-02076185-4699-4BB7-979E-37E0390CCA91

Q35128680-026175EF-F40A-4824-857D-77FBEAD40360

Q35128680-031E7128-F45C-454D-9783-F2D2B1CB7972

Q35128680-03EF4ED6-3662-4A71-8EF7-55B984FD6B58

Q35128680-043988CE-9FEA-4EC9-98FB-663EEEBCD0DE

Q35128680-05485403-0145-404A-82F9-D28D95129EE2

Q35128680-062B2F4C-48EA-4331-9344-7C8106B0AC2C

Q35128680-065C620A-8127-406A-B8C2-72400FED47C4

Q35128680-08A772F8-0076-42A5-A591-D72D4843500C

P304

Q35128680-EDEB1259-14D6-4B34-9C7F-C6DD76D5BCA1

P31

Q35128680-93EB10B6-BAEB-4CEE-ACEB-5310C95EC641

P356

Q35128680-ECFDB0A9-622F-416E-B59A-73C2BAEF1528

P407

Q35128680-C94D4FDE-24B6-47C0-A07B-03A70CB24E88

P433

Q35128680-1D79461A-3FB4-4AE1-A711-E3E55ED457CF

P478

Q35128680-757BA7E1-54BB-4E68-8C14-50706C23C56F

P50

Q35128680-CE537169-9B99-4DF6-BB84-480ADE0ED022

P577

Q35128680-824918E8-2DAC-402F-9665-01DDB3C89C8A

P698

Q35128680-23E81E31-155F-47A2-BEAA-89055036B6F6

P921

Q35128680-969B5655-AC64-457F-9A94-CC212B690087

P932

Q35128680-CB793768-EF59-4E66-9B8F-034509A5EA6B

P356

P1433

Biochemical Journal

P1476

The role of serine/threonine protein phosphatases in exocytosis

@en

P2093

Alistair T R Sim

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

John A P Rostas

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

Monique L Baldwin

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

Russell I Ludowyke

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

P2860

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

Rab6 is phosphorylated in thrombin-activated platelets by a protein kinase C-dependent mechanism: effects on GTP/GDP binding and cellular distribution

A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A

Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex

PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells

Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif

Type 2A protein phosphatase, the complex regulator of numerous signaling pathways

Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1.

Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells

The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family

P304

641-659

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

P31

scholarly article

P356

10.1042/BJ20030484

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

P407

P433

Pt 3

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

P478

373

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

P50

P577

2003-08-01T00:00:00Z

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

P698

12749763

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

P921

P932

1223558

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