Phosphorylation of MafA is essential for its transcriptional and biological properties
about
MafA is a glucose-regulated and pancreatic beta-cell-specific transcriptional activator for the insulin geneIdentification of beta-cell-specific insulin gene transcription factor RIPE3b1 as mammalian MafA.The minimal transactivation domain of the basic motif-leucine zipper transcription factor NRL interacts with TATA-binding proteinCytoprotection "gone astray": Nrf2 and its role in cancerRegulation of alphaA-crystallin via Pax6, c-Maf, CREB and a broad domain of lens-specific chromatinMembers of the large Maf transcription family regulate insulin gene transcription in islet beta cellsPhosphorylation within the MafA N terminus regulates C-terminal dimerization and DNA binding.Regulation of MafA expression in pancreatic beta-cells in db/db mice with diabetes.TAT-mediated transduction of MafA protein in utero results in enhanced pancreatic insulin expression and changes in islet morphologySumoylation of bZIP transcription factor NRL modulates target gene expression during photoreceptor differentiation.Generation of insulin-producing cells from the mouse liver using β cell-related gene transfer including Mafa and Mafb.A small molecule differentiation inducer increases insulin production by pancreatic β cellsRegulation of gene expression by Pax6 in ocular cells: a case of tissue-preferred expression of crystallins in lens.MafA stability in pancreatic beta cells is regulated by glucose and is dependent on its constitutive phosphorylation at multiple sites by glycogen synthase kinase 3.Genetic and epigenetic mechanisms of gene regulation during lens development.Large Maf Transcription Factors: Cousins of AP-1 Proteins and Important Regulators of Cellular Differentiation.A-raf and B-raf are dispensable for normal endochondral bone development, and parathyroid hormone-related peptide suppresses extracellular signal-regulated kinase activation in hypertrophic chondrocytesMAP kinases and the control of nuclear events.Chromatin-bound mitogen-activated protein kinases transmit dynamic signals in transcription complexes in beta-cells.Preventing p38 MAPK-mediated MafA degradation ameliorates β-cell dysfunction under oxidative stress.Inactivation of specific β cell transcription factors in type 2 diabetes.Deficiency of programmed cell death 4 results in increased IL-10 expression by macrophages and thereby attenuates atherosclerosis in hyperlipidemic mice.Inhibition of human insulin gene transcription and MafA transcriptional activity by the dual leucine zipper kinasep38 MAPK is a major regulator of MafA protein stability under oxidative stress.Involvement of Per-Arnt-Sim Kinase and extracellular-regulated kinases-1/2 in palmitate inhibition of insulin gene expression in pancreatic beta-cells.Mutations associated with retinopathies alter mitogen-activated protein kinase-induced phosphorylation of neural retina leucine-zipper.Sumoylation regulates the transcriptional activity of MafA in pancreatic beta cells.Role of c-Maf in Chondrocyte Differentiation: A Review.Proper activation of MafA is required for optimal differentiation and maturation of pancreatic β-cellsShielding Engineered Islets With Mesenchymal Stem Cells Enhance Survival Under Hypoxia.c-Maf, the gammaD-crystallin Maf-responsive element and growth factor regulation.CD13/APN transcription is regulated by the proto-oncogene c-Maf via an atypical response element.Regulation of insulin gene expression by overlapping DNA-binding elements.Human telomerase reverse transcriptase immortalizes bovine lens epithelial cells and suppresses differentiation through regulation of the ERK signaling pathway.Functional interactions between alternatively spliced forms of Pax6 in crystallin gene regulation and in haploinsufficiency.The stability and transactivation potential of the mammalian MafA transcription factor are regulated by serine 65 phosphorylation.A Comprehensive Survey of the Roles of Highly Disordered Proteins in Type 2 Diabetes.The stability of the lens-specific Maf protein is regulated by fibroblast growth factor (FGF)/ERK signaling in lens fiber differentiation.MafA has strong cell transforming ability but is a weak transactivator.MafA transcription factor is phosphorylated by p38 MAP kinase.
P2860
Q24309331-C981DF52-A118-4612-AE11-67201AE9E903Q24531243-CB01EDDF-EE56-4438-AAD5-B85F4C65C21BQ28278683-CCB174F7-F2C7-4B93-A839-654F190E1F57Q28393784-AAC085FC-4B70-4A73-A018-4C3159D7F6B9Q28507941-21322946-5EC8-4E46-ADAD-231439EEE760Q28510639-F06918B8-54FA-420E-9D1E-5FA698E65E74Q33800071-CA515C35-0D55-4BA5-9689-5F41AAD72CB5Q33930262-5437B751-8644-46AF-9383-56A4CCD5F215Q33998880-04C46831-72EB-427F-A994-C6F7B532A871Q34055928-5663E3B4-6F29-4980-8ADF-33973378AB40Q35420665-9FDA3692-2E7D-4545-9DB4-7B1ACCE9EB2FQ35651147-81312047-C45A-4374-B7C1-65CB1F949B6FQ35959737-B5F280E7-EAE1-4E6F-8FFB-6BFB7AAD98F4Q36176619-E6541DF9-E8B6-4E96-8D6D-58A8A389B30BQ36262540-90A684EA-5199-427B-AE89-9CC2706742E6Q36296242-D1CEE632-D0D7-4FC4-8351-76BF10D37BA6Q36421146-3F303CA5-DEEC-4527-B392-0252C067064EQ36819401-96AA13A6-C1C9-4535-82D4-81501D245DCEQ36869826-CEDF6D54-C7B2-497C-BE13-BE1A578A3214Q36998047-FF30EA57-318D-497A-8F61-EF7160DD0FCCQ37052883-4FDA84CB-B158-425C-AB00-E5809F92E40DQ37101142-F06F6B79-2AF6-455B-B61F-709326D7BE21Q37221457-6E370E1D-F0D2-400E-B727-F9DCFFB08AEFQ37283631-3E30AE2D-C903-44A6-A30E-A3779EA2E35CQ37317469-C291F04D-64FB-4913-8064-4556518E770CQ37425407-D6CE81B3-9EAB-4F97-B944-10FF356CFC0BQ38358697-439233E1-D960-4C0B-830B-AC974E7B09E6Q38526198-5718E087-039E-4596-B78F-8156545DD234Q38676902-5F6E247A-70B6-4528-814C-5932E3786032Q39015256-068ABA53-2AEA-4A8A-B09B-427359464A27Q39530824-45AB3971-C19C-403C-AB84-2EA2B41CAC8CQ40075882-AFE762B2-8F61-467A-9B05-A28F100AD29FQ40392325-FA7263DF-3F02-4439-AB9E-EBE0ECC871BAQ40431338-EA1C45BD-FDAA-4021-A8F2-41AF5F24F19AQ40578478-783258B1-6A72-477C-B51D-106925F73892Q43213325-3338A466-9FE8-4F93-BB27-1D1A5C54B921Q43283307-5E0E967A-152E-49DB-9E10-051DE98D7F3EQ44189971-355F48A8-FA87-450D-A0C2-61271EADDC36Q44582762-3FC73137-3172-4527-B64E-0C267B96EDBBQ46553269-AEE19D2F-6D5B-4039-A1C7-0F5A30F3F455
P2860
Phosphorylation of MafA is essential for its transcriptional and biological properties
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Phosphorylation of MafA is essential for its transcriptional and biological properties
@ast
Phosphorylation of MafA is essential for its transcriptional and biological properties
@en
Phosphorylation of MafA is essential for its transcriptional and biological properties
@nl
type
label
Phosphorylation of MafA is essential for its transcriptional and biological properties
@ast
Phosphorylation of MafA is essential for its transcriptional and biological properties
@en
Phosphorylation of MafA is essential for its transcriptional and biological properties
@nl
prefLabel
Phosphorylation of MafA is essential for its transcriptional and biological properties
@ast
Phosphorylation of MafA is essential for its transcriptional and biological properties
@en
Phosphorylation of MafA is essential for its transcriptional and biological properties
@nl
P2093
P2860
P50
P1476
Phosphorylation of MafA is essential for its transcriptional and biological properties
@en
P2093
Felder-Schmittbuhl MP
P2860
P304
P356
10.1128/MCB.21.14.4441-4452.2001
P407
P577
2001-07-01T00:00:00Z