CARM1 regulates proliferation of PC12 cells by methylating HuD - Test2 - elhamkhani - TriplyDB

CARM1 regulates proliferation of PC12 cells by methylating HuD

CARM1 regulates proliferation of PC12 cells by methylating HuD

http://www.wikidata.org/entity/Q28567419

about

The molecular mechanism of translational control via the communication between the microRNA pathway and RNA-binding proteins The methyltransferases PRMT4/CARM1 and PRMT5 control differentially myogenesis in zebrafish Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase Structural basis for CARM1 inhibition by indole and pyrazole inhibitors UBXD4, a UBX-containing protein, regulates the cell surface number and stability of alpha3-containing nicotinic acetylcholine receptors The survival of motor neuron (SMN) protein interacts with the mRNA-binding protein HuD and regulates localization of poly(A) mRNA in primary motor neuron axons.Protein kinase C stimulates HuD-mediated mRNA stability and protein expression of neurotrophic factors and enhances dendritic maturation of hippocampal neurons in culture Biochemical control of CARM1 enzymatic activity by phosphorylation Coactivator-Associated Arginine Methyltransferase-1 Function in Alveolar Epithelial Senescence and Elastase-Induced Emphysema Susceptibility CARM1 is required for proper control of proliferation and differentiation of pulmonary epithelial cells Influence of sequential guanidinium methylation on the energetics of the guanidinium...guanine dimer and guanidinium...guanine...cytosine trimer: implications for the control of protein...DNA interactions by arginine methyltransferases.miR-375 inhibits differentiation of neurites by lowering HuD levels.Characterization of 3'-untranslated region of the mouse GDNF gene Emerging roles for ribonucleoprotein modification and remodeling in controlling RNA fate Cell cycle regulation by the PRMT6 arginine methyltransferase through repression of cyclin-dependent kinase inhibitors.Identification of small-molecule enhancers of arginine methylation catalyzed by coactivator-associated arginine methyltransferase 1.Automethylation of CARM1 allows coupling of transcription and mRNA splicing Loss of CARM1 is linked to reduced HuR function in replicative senescence.Selective inhibitors of protein methyltransferases The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation Arginine methylation of RNA-binding proteins regulates cell function and differentiation Spinal muscular atrophy: the role of SMN in axonal mRNA regulation.PARAQUAT TOLERANCE3 Is an E3 Ligase That Switches off Activated Oxidative Response by Targeting Histone-Modifying PROTEIN METHYLTRANSFERASE4b.Novel CARM1-Interacting Protein, DZIP3, Is a Transcriptional Coactivator of Estrogen Receptor-α Expression and sub-cellular localization of an epigenetic regulator, co-activator arginine methyltransferase 1 (CARM1), is associated with specific breast cancer subtypes and ethnicity.Signaling pathways that control mRNA turnover.Small Molecule Inhibitors of Protein Arginine Methyltransferases.Diverse molecular functions of Hu proteins.A TR-FRET-based functional assay for screening activators of CARM1 Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation The Role of Protein Arginine Methylation in mRNP Dynamics Inhibitors of Protein Methyltransferases and Demethylases.A novel role for CARM1 in promoting nonsense-mediated mRNA decay: potential implications for spinal muscular atrophy.Mouse Prickle1 and Prickle2 are expressed in postmitotic neurons and promote neurite outgrowth.Crosstalk between histone modifications indicates that inhibition of arginine methyltransferase CARM1 activity reverses HIV latency.Discovery of a Potent, Selective, and Cell-Active Dual Inhibitor of Protein Arginine Methyltransferase 4 and Protein Arginine Methyltransferase 6.Inhibition of coactivator-associated arginine methyltransferase 1 modulates dendritic arborization and spine maturation of cultured hippocampal neurons.GAP43 overexpression and enhanced neurite outgrowth in mucopolysaccharidosis type IIIB cortical neuron cultures.Regulation of differentiation potential of human mesenchymal stem cells by intracytoplasmic delivery of coactivator-associated arginine methyltransferase 1 protein using cell-penetrating peptide.

P2860

81586af207f642c6f5feb25ef6c30b87bda4f95e b0abd77128d21b1d7132a11fa9b825147e61e1b3

P248

Q26798135-2A949A59-4DF9-4E31-B029-1B20B5CC67F7 Q27318301-84010CB7-0C69-49CD-BDC3-D0EA45DB9D1B Q27648374-ABD10F23-1310-44E1-A5B2-63087144C321 Q27666983-8A792407-1EC4-46CB-948E-C8CEBF8EE71A Q28507709-511410F6-D097-4507-87F4-CFEE81161098 Q28570605-3A00015D-74E5-4693-84EF-EFE40B2A3C1A Q28575286-4360DB36-4217-49AF-872C-ECAF836D92AD Q28590505-2425C9B4-6822-4F7B-A46B-41FBF5C5B550 Q33756658-8E1B2A4E-789B-4A41-83C0-67699B8B528D Q33899490-2986328C-25F7-4593-9D7F-9F0734E31439 Q34090472-BA14EC68-252A-47BD-AB52-FCE22DA951B5 Q34119806-2541EF6D-1191-4B2D-AC1B-274E572BC530 Q34128599-182F1937-CCE1-408B-A57A-0FD44DC75B5C Q34350089-E035901F-A004-4999-8B1A-4408AC752591 Q34390742-569E10CE-E1D0-4044-8FD9-3FF797BD8A4B Q34456824-BADE65C9-4F5D-4F62-9F90-F0911C3A86DC Q34779467-8AECC28D-84D9-4EA8-8A87-9D4E34E62241 Q34803610-5B9FFF1E-CB3A-4CD4-BBB7-D69D1A7274B4 Q35135783-3FCB0AAF-221B-46ED-BC72-F0D03927EEAB Q35641696-808013F6-1442-449B-A329-67E61682E68B Q35775944-DF166336-2992-4618-815C-3747F1CFF108 Q35990221-B8AA7670-4501-4D5A-BAD8-121CEA884054 Q36145924-DBD6E91B-8D6F-4CFD-9F66-A298EAD727FF Q36331785-BE8E16D8-093C-4E5C-9A9E-31DFEC66EF03 Q36874135-0C4A43B6-9F29-41DC-8EA3-32CA5C26481E Q36988764-D39981AF-15B2-421C-9637-D851C811FA5A Q37056442-76F0774B-54E8-4E37-B9FF-4D06084A003F Q37200596-70F543A9-6876-420C-B5DA-AFA625B6CECA Q37310314-7F542886-C50B-4CD0-B92B-9B98FF299216 Q38122142-B1B01B72-5275-4069-B9C9-04F262B0070A Q38291795-E07D7EBF-B35B-4D82-AAA8-286FC9A30974 Q38737543-51A6877A-590F-443F-9B67-B8C972F4EDC9 Q38740496-79F9AFFE-6A93-4CAE-9613-0A0B22F29904 Q38812591-8AFCB48E-6213-4779-B659-3E11DEF33C31 Q40080457-3F9D8E16-4F46-4FD8-BE5A-DA41AEA9306B Q40150928-58A18ECE-9372-4FB1-8343-4262934DC926 Q42383290-F160E682-6D5B-4901-B589-A2A92E12E124 Q45054089-336EF957-ACC9-49A8-9173-3498E16A9DAB Q48493230-6A496825-8BFF-42A9-B855-1C36509E2D86 Q51539345-E3DE2B4B-CBA2-4E1E-B652-B9CE3F9FC581

P2860

CARM1 regulates proliferation of PC12 cells by methylating HuD

http://www.wikidata.org/entity/Q28567419

description

2006 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի մարտին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 2006

@ast

im März 2006 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2006/03/01)

@sk

vědecký článek publikovaný v roce 2006

@cs

wetenschappelijk artikel (gepubliceerd op 2006/03/01)

@nl

наукова стаття, опублікована в березні 2006

@uk

مقالة علمية (نشرت في مارس 2006)

@ar

name

CARM1 regulates proliferation of PC12 cells by methylating HuD

@ast

CARM1 regulates proliferation of PC12 cells by methylating HuD

@en

CARM1 regulates proliferation of PC12 cells by methylating HuD

@nl

type

label

CARM1 regulates proliferation of PC12 cells by methylating HuD

@ast

CARM1 regulates proliferation of PC12 cells by methylating HuD

@en

CARM1 regulates proliferation of PC12 cells by methylating HuD

@nl

prefLabel

CARM1 regulates proliferation of PC12 cells by methylating HuD

@ast

CARM1 regulates proliferation of PC12 cells by methylating HuD

@en

CARM1 regulates proliferation of PC12 cells by methylating HuD

@nl

P1433

Q28567419-E37F997D-3DD7-4873-BEEF-0E23ADA56BD8

P1476

Q28567419-63FAFEC6-0E04-4675-A3EE-47CB3C7F5D9A

P2093

Q28567419-235307EE-7945-497C-BE4E-D3AE188D5EA6

Q28567419-2F54EAE5-26A3-4835-8814-D2FAD102A131

Q28567419-2FC61979-DEDE-4828-A55F-FB8A3E466D4B

Q28567419-61DDB9BD-0824-4E96-B340-42EEB0AF3BCB

Q28567419-68D6409F-8F9F-40BE-9355-2DF85030B40D

Q28567419-80711A66-081A-4F53-AB96-6549AD46E9CB

Q28567419-8B01D463-4BC8-4D0C-84B1-9FF5053BF1B9

Q28567419-8D4CFE2D-192D-4F9E-B7EE-46811E7730C5

Q28567419-8EE1118A-A796-4A06-94F4-F382B4029B7C

Q28567419-B81B720E-DA85-478B-9160-C5383AAE90C6

P2860

Q28567419-03403B6F-E212-4C0C-A77A-BB0458C6AF95

Q28567419-03B7D28A-CAC2-4385-965B-F2E47C2BD222

Q28567419-087865AC-86DC-433E-BC95-D2DACB8293C2

Q28567419-0A31513F-31F4-4117-9F37-02B4AD1F8CE7

Q28567419-0DA053D7-A802-4887-BC00-3A29C469B1C6

Q28567419-0ED9FEE6-B679-4EB7-8778-5907B88E0CC9

Q28567419-10048C1F-A21E-4F3F-817C-1439632D95DD

Q28567419-19520B4B-5902-489A-9FCA-27F2C11DD02B

Q28567419-19CFD516-B3CE-4E05-8CB8-8A0D18D41983

Q28567419-1A68CF85-9D2A-4A4F-B734-9EE2E1D2E104

P304

Q28567419-D201BC16-A964-4FDC-9CFA-F459D52036C2

P31

Q28567419-32C436EE-EB0E-45D0-A46A-E62509A6EB93

P3181

Q28567419-52F299CD-4C0E-4220-A348-37C96820EE93

P356

Q28567419-ED3E1F89-9DA6-4709-BAAD-4B3B69AFB37E

P407

Q28567419-53C70A0A-200F-4BBE-B3A9-94ECD1004012

P433

Q28567419-A973F420-B623-4E9D-AC16-490174E3C960

P478

Q28567419-0BEC139D-CED1-44CD-9418-C0E343CB9AD2

P577

Q28567419-837DCEAE-CC6F-4212-A49D-15A7B30ABD97

P698

Q28567419-812D3BEB-8FA4-4944-89AD-B54D472B935B

P932

Q28567419-3B649FFA-953C-4053-8A03-9F1FA4E47B8A

P3181

P356

MCB.26.6.2273-2285.2006

P1433

Molecular and Cellular Biology

P1476

CARM1 regulates proliferation of PC12 cells by methylating HuD

@en

P2093

Dong Ling Chu

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

Hideki Yoshikawa

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

Hiroyuki Tanaka

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

Kohji Yachi

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

Masaya Tohyama

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

Shingo Miyata

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

Tateki Kubo

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

Tatsuji Fujiwara

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

Yasutake Mori

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

Yoshihisa Koyama

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

P2860

HuD RNA recognition motifs play distinct roles in the formation of a stable complex with AU-rich RNA

Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1

The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity

Histone deimination antagonizes arginine methylation

HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal

PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm

Arginine methylation of RNA helicase a determines its subcellular localization

PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

P304

2273–2285

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

P31

scholarly article

P3181

3325779

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

P356

10.1128/MCB.26.6.2273-2285.2006

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

P407

P433

6

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

P478

26

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

P577

2006-03-01T00:00:00Z

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

P698

16508003

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

P932

1430293

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