The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
about
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityIdentification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alphaRibosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behaviormRNA:guanine-N7 cap methyltransferases: identification of novel members of the family, evolutionary analysis, homology modeling, and analysis of sequence-structure-function relationshipsAltered histone modifications in gliomasStructure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptidesInsights into histone code syntax from structural and biochemical studies of CARM1 methyltransferaseFunctional insights from structures of coactivator-associated arginine methyltransferase 1 domainsStructure and Function of a G-actin Sequestering Protein with a Vital Role in Malaria Oocyst Development inside the Mosquito VectorStructural basis for CARM1 inhibition by indole and pyrazole inhibitorsCrystal structure of the human PRMT5:MEP50 complexCrystal Structure of the Plant Epigenetic Protein Arginine Methyltransferase 10Structural insights into protein arginine symmetric dimethylation by PRMT5Crystal Structure of Arginine Methyltransferase 6 from Trypanosoma bruceiYeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2.Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p.Theoretical insights into catalytic mechanism of protein arginine methyltransferase 1Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient miceCharacterization of PRMT1 from Plasmodium falciparumPivotal and distinct role for Plasmodium actin capping protein alpha during blood infection of the malaria parasiteDisruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase.Enzymatic activity is required for the in vivo functions of CARM1.Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASFAdoMet-dependent methylation, DNA methyltransferases and base flipping.Histone-modifying complexes regulate gene expression pertinent to the differentiation of the protozoan parasite Toxoplasma gondiiRedox Control of Protein Arginine Methyltransferase 1 (PRMT1) Activity.Chemical biology of protein arginine modifications in epigenetic regulationPhosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1.Protein arginine methylation in Candida albicans: role in nuclear transport.Protein interfaces in signaling regulated by arginine methylation.Structural and sequence motifs of protein (histone) methylation enzymes.Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function.A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase.Protein arginine methyltransferases: from unicellular eukaryotes to humansThe enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulationChemical mechanisms of histone lysine and arginine modificationsType I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively.Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulationAutomethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity
P2860
Q24291936-AC7A29B9-891B-4A8D-9AA6-28AC415DFF77Q24298570-C642F70A-A90B-46D1-9943-15BE8A22C54DQ24306650-F578A618-71D4-4145-924A-4F3A77AA5073Q24314981-7C3CCAD0-DF1F-4D89-A46F-B3EF2A026525Q24801263-3A0C7F75-4AFD-412A-879D-E1D96298BEA6Q27027924-56E16CDB-25FE-418E-B120-97048835D023Q27641186-061C279C-461F-4F9E-8DB0-23DEF6C0E91CQ27648374-072CA120-80E9-4BE4-8F14-3F254E5A128BQ27648377-9B27F8BE-E21C-4BEB-B151-1F715D8BEB7EQ27659030-0E1DF557-15F8-43AA-BA24-0F94B73D441FQ27666983-D01A07A2-90F4-4306-9D12-0E87A37DBFA3Q27674576-22F189EE-E80A-4786-9337-5FBE6A046CD1Q27674910-C88C06D1-96EE-4B98-9334-20B81E6BE785Q27675998-3A9747A7-9150-4302-847C-30100EB42D5EQ27681586-617660E0-ECAE-4934-99C2-E39A5D477047Q27931761-AA3CB426-293F-4A0B-BD1F-58283C30D061Q27932390-01AE2E55-BDE4-44A1-88FA-C42BA29EEEF0Q28535458-084A0400-6C3D-47B7-A2AA-EACAFF88AF03Q28586486-780E5586-1473-4301-A717-52764DF7A1FFQ30043536-7D85203B-352C-4537-8446-6E42E2AC6562Q30043650-E08DA1A8-24B8-492E-90BD-33DDF9F1CC39Q31093400-9E242FC2-4059-4E42-9CA4-27DAF79D9CA5Q33569642-9701722B-53BD-488A-BF86-926F10FD5B02Q33877022-3275D27C-7A36-479C-BC6A-3491AB35872DQ33941847-22DA2CE5-B17A-4560-85AB-22107E740D88Q34150808-6AD16911-EEC2-4FAC-84DF-2AF823B43AC6Q35721676-DFB772AD-237D-454C-934F-4178D1EACE6FQ35722457-87466E79-5448-40F8-8F9F-D1D660442EADQ35927908-8311E185-8937-4860-905D-44868AEBC309Q35947027-9657B5C7-19C7-4099-B11A-8FAC04D9457DQ36043261-661607F3-B26D-4D36-9F2C-C57A79B2A3C1Q36115471-28A7429E-DB5D-420E-865D-AA7A8CB90B90Q36137995-5D3946B6-7809-4D09-87FD-266DD43A9845Q36646565-F2D147A4-B120-4434-BFF7-8883D50DDEA8Q36806235-777A6B07-26E7-44E9-8678-648A12E8ADA9Q36923058-2F2D23EF-F8A6-4CCE-BD0D-4B5F4882FFADQ37097824-DF9BC79C-BC04-4C83-A156-BC32F43322E3Q37136730-3CCA6C7C-2523-4C2D-980F-5122979017A3Q37155394-E8AA89C5-6E7D-46EE-A718-01A475ADB499Q37201210-735088A2-93D5-4ED4-A458-47D2B2F3445B
P2860
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@ast
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@en
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@nl
type
label
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@ast
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@en
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@nl
prefLabel
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@ast
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@en
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@nl
P2093
P356
P1476
The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
@en
P2093
A E McBride
D J Filman
M A Soriano
P A Silver
P304
P356
10.1038/82028
P577
2000-12-01T00:00:00Z