Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion - Test2 - elhamkhani - TriplyDB

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

http://www.wikidata.org/entity/Q24536290

about

CDK1 promotes cell proliferation and survival via phosphorylation and inhibition of FOXO1 transcription factor ERF nuclear shuttling, a continuous monitor of Erk activity that links it to cell cycle progression Glycogen synthase kinase-3 regulates IGFBP-1 gene transcription through the thymine-rich insulin response element Redox regulation of FoxO transcription factors Akt signaling dynamics in individual cells.Neutrophil activation by fMLP regulates FOXO (forkhead) transcription factors by multiple pathways, one of which includes the binding of FOXO to the survival factor Mcl-1 FoxO6 transcriptional activity is regulated by Thr26 and Ser184, independent of nucleo-cytoplasmic shuttling The FoxO code Both the N-terminal loop and wing W2 of the forkhead domain of transcription factor Foxo4 are important for DNA binding FoxO6, a novel member of the FoxO class of transcription factors with distinct shuttling dynamics FOXO transcription factors at the interface between longevity and tumor suppression PP2A regulates the pro-apoptotic activity of FOXO1.Identification and analysis of evolutionary selection pressures acting at the molecular level in five forkhead subfamilies.Green tea polyphenol epigallocatechin gallate reduces endothelin-1 expression and secretion in vascular endothelial cells: roles for AMP-activated protein kinase, Akt, and FOXO1 FOXO transcription factors: their clinical significance and regulation.Modelling the response of FOXO transcription factors to multiple post-translational modifications made by ageing-related signalling pathways Phosphorylation and acetylation modifications of FOXO3a: Independently or synergistically?Regulation of FOXO1 by TAK1-Nemo-like kinase pathway Protein phosphatase 2A reactivates FOXO3a through a dynamic interplay with 14-3-3 and AKT.Insulin signaling, resistance, and the metabolic syndrome: insights from mouse models into disease mechanisms.The FoxO family in cardiac function and dysfunction.PDK1 recruitment to the SHPS-1 signaling complex enhances insulin-like growth factor-i-stimulated AKT activation and vascular smooth muscle cell survival.The double-stranded RNA-dependent protein kinase differentially regulates insulin receptor substrates 1 and 2 in HepG2 cells FOXO1: a potential target for human diseases FoxO, autophagy, and cardiac remodeling.Mitochondrial longevity pathways A farnesylated G-protein suppresses Akt phosphorylation in INS 832/13 cells and normal rat islets: regulation by pertussis toxin and PGE₂.The many forks in FOXO's road.Insulin and LiCl synergistically rescue myogenic differentiation of FoxO1 over-expressed myoblasts Decisions on life and death: FOXO Forkhead transcription factors are in command when PKB/Akt is off duty.Deciphering the role of forkhead transcription factors in cancer therapy Hepatic insulin signalling is dispensable for suppression of glucose output by insulin in vivo.Nuclear transport and cancer: from mechanism to intervention.The ins and outs of FoxO shuttling: mechanisms of FoxO translocation and transcriptional regulation.Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.Computational identification and modeling of crosstalk between phosphorylation, O-β-glycosylation and methylation of FoxO3 and implications for cancer therapeutics.Surf the post-translational modification network of p53 regulation FoxO1 inhibits sterol regulatory element-binding protein-1c (SREBP-1c) gene expression via transcription factors Sp1 and SREBP-1c.The oncogenic fusion protein Pax3-FKHR has a greater post-translational stability relative to Pax3 during early myogenesis.Arsenic trioxide-induced growth arrest of breast cancer MCF-7 cells involving FOXO3a and IκB kinase β expression and localization.

P2860

Q24321230-68001056-6204-4243-8F72-A4458EBEB501 Q24629604-27500609-913D-424D-8596-1BB567486E67 Q24793511-339E142B-36F8-4FFF-ACE9-3C5698D2891C Q26799843-8AD144F4-216B-461A-88E1-C5A47EB9A738 Q27340143-917691B6-F1B4-4639-B0B9-310FBC4A61F0 Q28205486-5D3188FF-B9BA-42A6-9192-3DBCF7CAE2CB Q28258996-DAC93D46-4EE8-49BB-96FF-8CBEBA2C5CE6 Q28275268-50711E5C-9A74-4D9D-B9E7-B9725DA83730 Q28284616-1CC8D5ED-4072-4D92-83CC-D56E8648148B Q28504819-A73214CD-FD17-4FC9-8CAA-CE90C4959B48 Q29620472-07EE64B9-26EB-4909-B1BD-2C9870BE5CBE Q30440004-3BB42255-200E-46B8-AA58-EA9BA724C0CE Q33371818-4DCD00B0-CBE4-4AD0-AD66-C123B78224CA Q33577496-710CBE8D-986D-4DC5-8A59-20AF56CA8C2C Q33594004-3F70C143-ED67-4908-992F-959FAEFA9398 Q33612153-35EBE300-68A7-4D3A-9008-4B098E83CE90 Q33685068-4B53B39B-E495-4372-954C-059BA2466280 Q33707056-A5A45287-7FC3-4227-B613-398E1396737E Q33721192-7A0E95A8-B002-48B2-B694-85A690982D79 Q33865096-6EB71C25-236D-4020-9877-C5C8A8949808 Q34013124-993D5955-C1A5-4D41-9378-9A8061E3A266 Q34121608-9B72D853-CC9E-4A93-AC09-6BEC92D49ED5 Q34163416-F10D432C-2958-41B0-AD0A-7803769465E7 Q34173809-A4836A01-2958-465B-8C30-8B8D97D5D821 Q34362813-B68CD773-1067-429C-9177-28888A7D4998 Q34767374-96878A5F-4102-4953-938B-D342046AA04C Q34884341-6FD72B69-0D7E-4376-8CA2-89996D9CBFBA Q35079447-DF75426B-B725-41FE-B432-B1E02F5F3979 Q35097402-78D0BAAE-1909-48B1-9F21-72CB212A32B1 Q35139549-CB5011AE-65DD-4D8B-A2F8-A6420C76326F Q35146638-56033EA2-17E2-4FCB-AED7-65CE92B0DE64 Q35601144-4B7DBE31-04C9-4421-9547-BCFBE1AB34DA Q35633427-2611673C-826A-4AE5-9466-4FA14143BF12 Q35684376-450E1579-7CB2-49DB-B306-3D3B480C833E Q35787179-3327A247-AD41-4061-AC92-FE05DD7B3B0D Q35865318-486E9BB4-152D-4C9D-917A-1784CFCD7170 Q35967111-5E4D358C-5A29-4E8E-A912-592073468C3F Q36016844-D7FDF933-BB95-4036-A93D-94FA655C3A9E Q36095563-42477EDC-4522-4DF6-A792-5D9DE11AE6AC Q36305178-1FDF7C1A-A521-46DD-8A3C-26B4D49E3F10

P2860

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

http://www.wikidata.org/entity/Q24536290

description

2002 nî lūn-bûn

@nan

2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@ast

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@en

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@nl

type

label

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@ast

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@en

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@nl

prefLabel

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@ast

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@en

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@nl

P1433

Q24536290-37DA4390-5E32-4D92-BF8F-DA61B518F964

P1476

Q24536290-B3E24FC5-90CE-4869-9ECB-52FA8E415DDF

P2093

Q24536290-0E5C5660-EACC-494E-9B90-6D75E495D371

Q24536290-782B6D6D-6407-4D56-B436-49C262BEF27E

Q24536290-791226A3-BCEB-409A-9D63-3AFB9C365CC9

Q24536290-AC64AFC7-4770-48AC-8FCD-4865EC9AE45E

Q24536290-CD721468-B131-4DF2-AC25-19CFC9494D3B

Q24536290-CE027EA8-1E5C-4752-BD70-9CE0B8D72058

P2860

Q24536290-0494B473-13F2-47E6-971E-07DF5FD0D357

Q24536290-07451156-FAD4-4A71-9468-19ED9790613A

Q24536290-093D9F12-03C6-44F8-B98A-7E1D5A869ADE

Q24536290-0A542714-6360-4473-9E05-209899DC388A

Q24536290-0B1C1812-8AE5-47AB-A72A-4DF988D4DBE5

Q24536290-0D71DDBB-1487-4032-B405-0C89665F09C5

Q24536290-23D27673-2C17-46D3-9248-CF0A57A62BC7

Q24536290-27C5AB67-F07F-4DE0-B336-8AA143A335F7

Q24536290-2AF60192-7DB3-4886-A7A1-A34A53F0EDAF

Q24536290-2F37E308-9E38-4C1A-B21E-AF8DDAE78A7B

P304

Q24536290-6D32EAF8-A6B5-4D54-B4DC-25AF52B0ED9C

P31

Q24536290-E96126CF-1E84-466C-9770-7EF28F3940C4

P3181

Q24536290-DD5FDA93-BCC4-4DEB-B4DC-5126BAE1E732

P356

Q24536290-916F3A0E-40F3-4A08-8024-A958EE2C88D9

P407

Q24536290-4E4E2F9D-B7DC-4E86-A561-7113719B6F98

P433

Q24536290-E65FE3D4-7465-4926-B08C-81763AE3F9B8

P478

Q24536290-B5623326-3771-416C-9B36-387E5E2B6C81

P50

Q24536290-68B2780E-B62E-43D5-BD42-75ED54D60558

P577

Q24536290-6ABFF52A-4B7C-4578-B581-019DB6A3546E

P5875

Q24536290-3C2D90A0-A3AE-4DDB-A909-924F105C932C

P698

Q24536290-F78D30AA-2808-46A5-91DF-7FCE4B55AEFE

P921

Q24536290-8B67D8DE-437A-4091-A054-6422C7535203

P932

Q24536290-9069E41D-6AD5-41F3-8496-37966DC44C93

P3181

P356

P1433

The EMBO Journal

P1476

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

@en

P2093

Alan R Prescott

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

Mark Peggie

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

Michayla R Williams

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

Philip Cohen

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

Terry G Unterman

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

Yvonne L Woods

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

P2860

Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

Direct control of the Forkhead transcription factor AFX by protein kinase B

Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targetting

The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site

The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase

Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3

Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX.

RanBP3 influences interactions between CRM1 and its nuclear protein export substrates.

The PI3K-PDK1 connection: more than just a road to PKB

Regulation of the Forkhead transcription factor AFX by Ral-dependent phosphorylation of threonines 447 and 451

P304

2263-2271

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

P31

scholarly article

P3181

4149076

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

P356

10.1093/EMBOJ/21.9.2263

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

P407

P433

9

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

P478

21

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

P50

P577

2002-05-01T00:00:00Z

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

P5875

11388220

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

P698

11980723

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

P921

phosphorylation

P932

125977

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