Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation. - Wikidata - wikimedia - TriplyDB

Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation.

Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation.

http://www.wikidata.org/entity/Q37356550

about

Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins Prolyl isomerase Pin1 in cancer Understanding the role of PIN1 in hepatocellular carcinoma KSHV reactivation and novel implications of protein isomerization on lytic switch control Evaluation of MicroRNAs Regulating Anoikis Pathways and Its Therapeutic Potential The prolyl isomerase Pin1 acts synergistically with CDK2 to regulate the basal activity of estrogen receptor α in breast cancer Regulation of cardiac hypertrophic signaling by prolyl isomerase Pin1 Pin1: a molecular orchestrator in the heart.Physiological regulation of Akt activity and stability.Prolyl isomerase Pin1 regulates mouse embryonic fibroblast differentiation into adipose cells.Optimal homeostasis necessitates bistable control Active Pin1 is a key target of all-trans retinoic acid in acute promyelocytic leukemia and breast cancer β-catenin signaling controls metastasis in Braf-activated Pten-deficient melanomas Regulation of the microRNA 200b (miRNA-200b) by transcriptional regulators PEA3 and ELK-1 protein affects expression of Pin1 protein to control anoikis Differential regulation of cellular senescence and differentiation by prolyl isomerase Pin1 in cardiac progenitor cells Chemical or genetic Pin1 inhibition exerts potent anticancer activity against hepatocellular carcinoma by blocking multiple cancer-driving pathways.MicroRNA-140-5p inhibits hepatocellular carcinoma by directly targeting the unique isomerase Pin1 to block multiple cancer-driving pathways.Peptidyl-prolyl cis-trans isomerase Pin1 in ageing, cancer and Alzheimer disease.Akt/PKB: one kinase, many modifications.Prolyl isomerase Pin1 promotes survival in EGFR-mutant lung adenocarcinoma cells with an epithelial-mesenchymal transition phenotype.The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target.The role of Pin1 in the development and treatment of cancer.PIN1 in breast development and cancer: a clinical perspective.The cellular peptidyl-prolyl cis/trans isomerase Pin1 regulates reactivation of Kaposi's sarcoma-associated herpesvirus from latency Prolyl isomerase Pin1 and neurotrophins: a loop that may determine the fate of cells in cancer and neurodegeneration.Pin1 interacts with the Epstein-Barr virus DNA polymerase catalytic subunit and regulates viral DNA replication.Chronic AMD3100 antagonism of SDF-1alpha-CXCR4 exacerbates cardiac dysfunction and remodeling after myocardial infarction.3DBIONOTES v2.0: a web server for the automatic annotation of macromolecular structures.Sensitizing effect of juglone is mediated by down regulation of Notch1 signaling pathway in trastuzumab-resistant SKBR3 cells.Pin1 inhibition exerts potent activity against acute myeloid leukemia through blocking multiple cancer-driving pathways.Arsenic targets Pin1 and cooperates with retinoic acid to inhibit cancer-driving pathways and tumor-initiating cells

P2860

Q26825421-2A076F4C-5C1A-42A8-9DA9-917517B9122E Q27024695-A8C381B4-A09A-4DA6-B164-EA92A9C60F22 Q28073477-754CEE5A-A9AF-4ECE-A4CC-6B1C5CB9F7B8 Q28080937-675479EB-DE5E-419E-85C3-B1A3797E8C5A Q28084310-D90BB23C-2AE0-463F-8319-4AD86B34E45A Q28485944-B9C153BE-2E15-4A5F-B4F3-7453B4DE4F4B Q28572621-EE4C568F-8BE8-4763-ADC1-61E458004FF0 Q30365214-C46CAEB9-86DA-4881-9ECE-A1635E78ECD0 Q33680673-31983726-B098-4B74-9DFA-B610B0D1339C Q34193004-C820B27C-B735-412D-9C0E-CFE9208ED7E5 Q34270962-5655B37E-6998-42BC-94A6-8C4FA05EE40D Q35587470-D5F72E2A-7BFD-4E37-9274-B2CDFD4AEB68 Q35621787-F634C3DA-BE4D-44B0-8678-583E1776B721 Q37289320-AE831FF9-A00E-4DA0-834A-AA643FDEC709 Q37608398-D3247772-0396-48BF-AEF0-A77A2E2BAA96 Q37681728-0A8A689C-F30F-4458-9291-5F1326CA5036 Q37739814-E0CF7F6C-C463-48E2-B223-F631EFACDB09 Q37891181-B9B60C6D-7352-4824-A28A-F75BF72ABAF1 Q38495836-6D2E4E6D-17B4-4505-96E1-587E567C1B29 Q38804845-14E08A82-FD12-4F2B-A21B-3A23CB6001EE Q38852028-F8B8B73E-8EE7-403F-8592-1B077EF6518B Q38939954-49D2BA6D-8D5A-4953-B120-EA7DD6C5452E Q39005373-A92D8C50-57A3-4DCC-B327-2646AD454FA4 Q39068717-FAE8CEF8-4AFA-4DAA-808F-ED2F5B2941A3 Q39137665-7C15B390-E283-436B-A38D-9134BD5CC593 Q39230419-80B4914D-3B23-438C-B689-734F8BCF93D8 Q41266448-0A37AF1B-58CD-41EC-B38F-D84913B9D0E2 Q47317916-1456079A-CCA4-4EED-B822-0BD203C2FB02 Q48961614-BFE5D7BA-A7D8-4B96-B99F-D9A8BE7501A3 Q54917620-58335B9E-80E0-431D-B16B-A31DA053C5D7 Q58793896-FD28887D-ABC9-4F51-9256-EF42C388B819

P2860

Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation.

http://www.wikidata.org/entity/Q37356550

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 18 May 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Peptidyl-prolyl cis/trans isom ...... nd activation phosphorylation.

@en

Peptidyl-prolyl cis/trans isom ...... nd activation phosphorylation.

@nl

type

label

Peptidyl-prolyl cis/trans isom ...... nd activation phosphorylation.

@en

Peptidyl-prolyl cis/trans isom ...... nd activation phosphorylation.

@nl

prefLabel

Peptidyl-prolyl cis/trans isom ...... nd activation phosphorylation.

@en

Peptidyl-prolyl cis/trans isom ...... nd activation phosphorylation.

@nl

P1433

Q37356550-F92DDA9F-4858-4489-A3E9-3ACDD66DE051

P1476

Q37356550-69C92610-4ED6-4B68-B422-478CFC9EE5C9

P2093

Q37356550-080B0C4A-AA24-4A1F-814D-D8EBC4C016A3

Q37356550-134F3DFC-DF71-45AA-A6B0-B66F00DAD7CD

Q37356550-26096BD4-0770-406F-980D-50E74718EEF8

Q37356550-35286919-3E35-41B1-A5EA-E91D9C64FDA8

Q37356550-3C278C94-B6DF-489C-A80D-88CC92143865

Q37356550-6A06F35E-C9F2-4CE7-8D25-1E3A027535E6

Q37356550-A2CA7728-61E3-4306-86FF-D4AF482A3307

Q37356550-D1956B84-1B82-414C-BF88-E154F951FD52

Q37356550-D7842D35-4823-4F18-9D32-50DCCD8692A8

Q37356550-DEA19C12-597E-4C72-9EE0-7A0F1D26EE84

P2860

Q37356550-11825CDE-730D-46E8-92C6-5DC566884517

Q37356550-16EAA28A-52FC-4231-B4E6-5D1E7F9B0DD1

Q37356550-177005FC-22C5-411D-A445-5EDE5C18599E

Q37356550-1AD06A7D-5F8B-4421-9936-1059DCD65365

Q37356550-221B168C-24ED-4482-887F-10FB00278717

Q37356550-259B30D9-5FA6-49CC-BB67-196695F208C6

Q37356550-38D35DAB-3BBB-43E4-9818-56375D13B391

Q37356550-417C1639-366A-4879-B3B9-50E4E26179F7

Q37356550-48F98B45-822A-4C1B-B68F-9C5F5255DA8A

Q37356550-4C7DCDEC-9024-4006-98C4-F94BC3D53E0B

P2888

Q37356550-971063AA-9F14-4CFB-B0CB-0B4490B33B0A

P304

Q37356550-B9789AD0-2193-4E6D-9E0A-F06723FC41F7

P31

Q37356550-2DC9125E-C55B-48C9-91DA-1FC3D85E276F

P356

Q37356550-80BC8742-B6AB-450D-BDB7-CF11C55155EA

P407

Q37356550-6EA3A801-A04D-4461-A98E-7230837A1CCF

P433

Q37356550-AC36F296-D705-437F-8DD6-23CFE254A7AC

P478

Q37356550-A0CD8E74-6544-4F7E-9FAC-2B4B97D86812

P577

Q37356550-197CEC12-4367-4A5D-B91D-4466E43DF1B8

P5875

Q37356550-3DCA1471-3E06-43B2-9D9F-CC177C62EF7D

P698

Q37356550-BE18C3B1-1745-4794-8B9C-3BB6F268B67B

P921

Q37356550-3A0FECBF-5DC0-4187-936E-71A7DB7FDE0B

P932

Q37356550-F773BA64-B949-414E-B79D-B3826842208F

P356

P1433

P1476

Peptidyl-prolyl cis/trans isom ...... nd activation phosphorylation.

@en

P2093

C Dai

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

D Sarbassov

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

D Shi

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

D Yu

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

J-Y Yang

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

M-C Hung

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

N K Agarwal

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

X Zhou

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

Y Liao

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

Y Wei

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

P2860

Function of WW domains as phosphoserine- or phosphothreonine-binding modules

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms

Mechanism of activation of protein kinase B by insulin and IGF-1

Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling

AKT/PKB signaling: navigating downstream

A transforming mutation in the pleckstrin homology domain of AKT1 in cancer

Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic

AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation

The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults

P2888

P304

2436-2445

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

P31

scholarly article

P356

10.1038/ONC.2009.98

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

P407

P433

26

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

P478

28

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

P577

2009-05-18T00:00:00Z

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

P5875

24433537

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

P698

19448664

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

P921

phosphorylation

P932

2748248

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