Targeting protein serine/threonine phosphatases for drug development - Test2 - elhamkhani - TriplyDB

Targeting protein serine/threonine phosphatases for drug development

Targeting protein serine/threonine phosphatases for drug development

http://www.wikidata.org/entity/Q24658001

about

Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle Counteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein Phosphatases A Review: Molecular Aberrations within Hippo Signaling in Bone and Soft-Tissue Sarcomas Virulence-Associated Enzymes of Cryptococcus neoformans TGF-β cascade regulation by PPP1 and its interactors -impact on prostate cancer development and therapy A unique Kelch domain phosphatase in Plasmodium regulates ookinete morphology, motility and invasion Development of a Peptide that Selectively Activates Protein Phosphatase-1 in Living Cells The quest for an effective and safe personalized cell therapy using epigenetic tools The Basic Biology of PP2A in Hematologic Cells and Malignancies Mass spectrometric detection and characterization of atypical membrane-bound zinc-sensitive phosphatases modulating GABAA receptors Selectivity and potency of microcystin congeners against OATP1B1 and OATP1B3 expressing cancer cells Phosphatase Inhibitors Function as Novel, Broad Spectrum Botulinum Neurotoxin Antagonists in Mouse and Human Embryonic Stem Cell-Derived Motor Neuron-Based Assays Morphologic, Phylogenetic and Chemical Characterization of a Brackish Colonial Picocyanobacterium (Coelosphaeriaceae) with Bioactive Properties An ancient protein phosphatase, SHLP1, is critical to microneme development in Plasmodium ookinetes and parasite transmission Investigational inhibitors of PTP4A3 phosphatase as antineoplastic agents.Conformational isomers of calcineurin follow distinct dissociation pathways.Total synthesis and evaluation of phostriecin and key structural analogues Mathematical modelling of the MAP kinase pathway using proteomic datasets InAKTivation of insulin/IGF-1 signaling by dephosphorylation.Microcystin-LR (MCLR) induces a compensation of PP2A activity mediated by α4 protein in HEK293 cells.Phosphoproteomics analysis of a clinical Mycobacterium tuberculosis Beijing isolate: expanding the mycobacterial phosphoproteome catalog.The extended PP1 toolkit: designed to create specificity.Determinants for Substrate Specificity of Protein Phosphatase 2A.Viewing serine/threonine protein phosphatases through the eyes of drug designers Bisphenol-A affects male fertility via fertility-related proteins in spermatozoa.Aspects of eukaryotic-like signaling in Gram-positive cocci: a focus on virulence.Adaptation of HepG2 cells to a steady-state reduction in the content of protein phosphatase 6 (PP6) catalytic subunit Wip1 sensitizes p53-negative tumors to apoptosis by regulating the Bax/Bcl-xL ratio Efficient PKC inhibitor screening achieved using a quantitative CE-LIF assay.Label-free electrochemical impedance detection of kinase and phosphatase activities using carbon nanofiber nanoelectrode arrays.Protein phosphatase 2A has an essential role in the activation of gamma-irradiation-induced G2/M checkpoint response.Self-association of okadaic acid: structural and pharmacological significance Novel Ser/Thr protein phosphatases in cell death regulation Systemic Inhibition of CREB is Well-tolerated in vivo.Prostate cancer: the need for biomarkers and new therapeutic targets.The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.Small G proteins Rac1 and Ras regulate serine/threonine protein phosphatase 5 (PP5)·extracellular signal-regulated kinase (ERK) complexes involved in the feedback regulation of Raf1.Global analysis of serine/threonine and tyrosine protein phosphatase catalytic subunit genes in Neurospora crassa reveals interplay between phosphatases and the p38 mitogen-activated protein kinase.Bacterial serine/threonine protein kinases in host-pathogen interactions.

P2860

Q21131229-6619F2AC-A83B-488F-8CD3-66738D747348 Q24317158-C4148615-4911-475A-93AC-34F16257A77F Q26776182-8E583E74-9EFB-415A-9625-E6C8A109302B Q26782842-A0FD530D-33EC-4927-94D7-5B4DBE3BF604 Q26785005-FBFD91B2-9B93-42BD-83C8-9870BA619A65 Q26862838-C0E34AE7-3FAF-414B-B368-E6E48998E843 Q27319927-F44DC48A-316C-446A-8606-65AD59630DA4 Q27672858-A215BDD7-AD61-4D5C-A63A-8551B99F1E88 Q28079389-09C4330F-7E36-46CE-96B3-DD188ADD926E Q28088697-FD08583A-7374-4C41-946D-28E7F6C21242 Q28540055-59A8FD18-8BFB-42F6-BC62-BA422955DF7F Q28540711-BDD07812-E152-4629-9B6E-DC7B27FC4E22 Q28548051-CED48E84-3203-4955-B99D-8348DD543D16 Q28834033-EBA64907-A613-408A-8367-56F632A0EA6D Q30043288-BC783752-A8E7-456C-808E-2A1C859CF346 Q30457615-3A3D3761-AF9A-42D6-9861-71BF55D5E660 Q33995509-CB511F20-5D88-4967-9F2B-BF79B8699FA3 Q34300129-B8D4E016-74FB-4E47-AB16-953AF4D4247F Q34384343-4F9A0C00-6113-48FB-9CF1-3CE2392969DB Q35030359-171923CC-9A6F-4B9A-82FF-9AE657488515 Q35059243-B4E2DCE1-E0B3-47E6-9762-1160C1958A94 Q35067450-363846C8-DDBA-47F8-B3B0-63FAE745E300 Q35092072-8FA9FA73-E358-4C36-90CF-C9E451C5CBAD Q35095669-A8EAA700-D7C3-4BAF-906E-4C2A7ED43419 Q35146774-F2969936-5D8D-4A0C-8C80-A50BDC32EE5A Q35179308-227554F0-237E-489D-B037-CA9B090052EC Q35609664-03F443BC-B226-4CEE-B191-ABE3D55E7017 Q35798066-A0386CEE-9F41-4DCC-A682-CB490DFAABE1 Q35984061-C84BF0D7-F0A1-41EC-BC12-9C1269279D2F Q36174816-97CEE1D0-2A89-4EBB-9A82-EA8AB503EC12 Q36203630-7EDE6E98-324E-4CEB-AC29-E7EB365F9E66 Q36908131-F102E9C6-4768-4D78-A197-96B6ECFB0CDE Q37040052-5B1E2D0B-EE9A-4A5C-BA78-6C7DDA3B878A Q37256583-DA6C6C81-D64A-470C-B261-3F6A3F5EFA46 Q37303415-2F7150C5-595B-416C-A7BF-29C983A1BF54 Q37476043-F8E3271C-236B-416F-AF63-5A8FE2B7F457 Q37536572-71E0011A-02E1-428C-9560-E89C7A6526D9 Q37583522-A6296545-5C2A-4FAD-B2D3-8B51E735173A Q37597393-35B92923-DD4A-4B05-8DB4-3B9127082833 Q37683337-80E90ABB-B6E5-4666-86CE-A0699C36DD5B

P2860

Targeting protein serine/threonine phosphatases for drug development

http://www.wikidata.org/entity/Q24658001

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Targeting protein serine/threonine phosphatases for drug development

@ast

Targeting protein serine/threonine phosphatases for drug development

@en

Targeting protein serine/threonine phosphatases for drug development

@nl

type

label

Targeting protein serine/threonine phosphatases for drug development

@ast

Targeting protein serine/threonine phosphatases for drug development

@en

Targeting protein serine/threonine phosphatases for drug development

@nl

prefLabel

Targeting protein serine/threonine phosphatases for drug development

@ast

Targeting protein serine/threonine phosphatases for drug development

@en

Targeting protein serine/threonine phosphatases for drug development

@nl

P1433

Q24658001-E903C0B3-E869-47A9-B890-E3B091F53AE0

P1476

Q24658001-785A777A-42C9-4340-86DB-EF18E6E2C32B

P2093

Q24658001-691B9833-9CA0-4D5F-A152-79C0ABACA3C2

Q24658001-AA1065B9-08CC-4525-AF98-DBCAB9F2FB69

P2860

Q24658001-00BF99AE-95BB-417F-B367-9FFBD24B55DC

Q24658001-0306CB0B-874F-43E2-9115-941C75ED2F22

Q24658001-03AD9543-9758-4C3B-AB72-0559B3618B49

Q24658001-03C55A66-0778-4890-A213-F577DC20D706

Q24658001-055F51DA-E049-4710-896E-6E0BD79B8752

Q24658001-05BA7423-A844-4AD3-89CA-3E27CABD444F

Q24658001-06173689-4045-456F-8222-28D5208AC52B

Q24658001-0742B36F-3B19-465C-B183-19C1C21B9866

Q24658001-08FAC7D8-813E-4350-9E3B-5465EE90DA5C

Q24658001-09EFDFFB-B0C3-45B3-985C-B74006C036BF

P304

Q24658001-5AE96279-AFCC-4E5A-98E6-F6EE5FB308E7

P31

Q24658001-089D596B-6EB1-4CB6-B2EB-FDF5C912C67C

P3181

Q24658001-8E30FAEF-9188-4EE5-AF31-E2CF991F5A28

P356

Q24658001-7332FDD6-9016-47C5-BA08-A44189EFD796

P407

Q24658001-4637B037-2C17-4048-936E-9B0DDBA5EE4F

P433

Q24658001-8EBD42ED-EBF7-4513-87BD-0560D6724754

P478

Q24658001-F92BC406-9DAF-4284-9282-779671B8894F

P577

Q24658001-AC54DEE2-D165-407E-AAAA-19E8C8187BCA

P5875

Q24658001-BCF962AF-B0A7-4EE0-90C3-03E78FBC17CA

P698

Q24658001-124382F9-2943-4606-8F39-48C1DDC9555E

P932

Q24658001-FB1A9485-3E76-4877-BA8F-36E847D1BD85

P3181

P356

P1433

Molecular Pharmacology

P1476

Targeting protein serine/threonine phosphatases for drug development

@en

P2093

Brian E Wadzinski

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

Jamie L McConnell

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

P2860

Binding specificity of protein phosphatase 2A core enzyme for regulatory B subunits and T antigens

Protein phosphatase 2A interacts with and directly dephosphorylates RelA

A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5

B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK

A beta-arrestin 2 signaling complex mediates lithium action on behavior

Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex

Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1

Positive regulation of IkappaB kinase signaling by protein serine/threonine phosphatase 2A

A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB

A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus

P304

1249-61

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

P31

scholarly article

P3181

3182115

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

P356

10.1124/MOL.108.053140

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

P407

P433

6

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

P478

75

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

P577

2009-06-01T00:00:00Z

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

P5875

24213436

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

P698

19299564

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

P932

2684880

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