About: Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable

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description	artículu científicu espublizáu en 2000 (ast) vědecký článek publikovaný v roce 2000 (cs) наукова стаття, опублікована в липні 2000 (uk) 2000 թվականի հուլիսին հրատարակված գիտական հոդված (hy) 2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في يوليو 2000) (ar) article scientifique publié en 2000 (fr) vedecký článok (publikovaný 2000/07/01) (sk) wetenschappelijk artikel (gepubliceerd op 2000/07/01) (nl) scientific journal article (en) im Juli 2000 veröffentlichter wissenschaftlicher Artikel (de) মলিকুলার অ্যাণ্ড সেলুলার বায়োলজি নামক বৈজ্ঞানিক পত্রিকায় প্রকাশিত নিবন্ধ (bn)
publication date	wds:Q28585102-D9DCC0E7-5DC1-4F38-A407-44445FBCFB34
publication date	2000-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28585102-43963996-5D19-49AE-A2D3-B7D5396BA340
language of work or name	English
cites work	wds:Q28585102-101535E3-4295-4765-B40A-C1AB5BE2A8E2 wds:Q28585102-38581A58-A72F-4A71-84E9-4B71F24107AC wds:Q28585102-3AFFF798-A336-45F3-BA66-CE64144DAB67 wds:Q28585102-3BC1B359-E014-45E7-955B-B01051213F9D wds:Q28585102-3BDC3215-9859-407A-BB24-0428345E15D0 wds:Q28585102-3D1C809B-A0D4-427D-A97B-B687E6EEF352 wds:Q28585102-3F0D5375-C5F5-41B9-A75C-7FAC0A6356EF wds:Q28585102-4624EEB0-A080-427C-AF63-87F011FF0DAA wds:Q28585102-4CA2063E-58D0-4F67-9020-F5435F433576 wds:Q28585102-4F597B77-4D14-4731-8238-B90593556E65 wds:Q28585102-54B52364-BD66-48E3-9671-88E82C2BB749 wds:Q28585102-673E0B1B-F58B-46F9-9A97-9F52185079DA wds:Q28585102-67E5C8ED-BEAC-4D09-AAC2-4777FECEEABF wds:Q28585102-682B6B95-7208-4986-97D9-7B57B566FEDF wds:Q28585102-69152D23-0D10-46F1-BC27-257E8D6F9BAE wds:Q28585102-6C0FCCDB-3227-416F-8CBE-00FA00AFAA7C wds:Q28585102-7C36C756-FB08-48B5-BDFB-E3073B3230F4 wds:Q28585102-7C4149C3-5C65-4DA4-8FE9-83A4F9443AC8 wds:Q28585102-9669DB29-12A0-453A-A700-CA7248F71ED6 wds:Q28585102-A50F13F2-7BC6-49C6-B807-AED90A6D13DD wds:Q28585102-B065EBC0-A8E8-4940-B768-72CAFB735AF8 wds:Q28585102-BB59A418-2A12-4DED-8EBD-8F4BB7FF0DA9 wds:Q28585102-C068AEFA-3953-437F-89B0-E9DC8D274559 wds:Q28585102-CB08C696-4EB5-4D14-9F2F-A39E9E9C2906 wds:Q28585102-CEF9ABE9-E98F-4A22-9D53-86E7CDC46960 wds:Q28585102-D28667B8-1C85-4277-8A88-50314D42AE5E wds:Q28585102-E4EC5503-C3EB-4818-B3F4-5926C14CC040 wds:Q28585102-E6B09D2C-9555-4C12-A081-03C1F94AEA78 wds:Q28585102-EFDBD096-5955-460B-9F76-85BD92EA48C3 wds:Q28585102-F26FBF2F-FCD4-4BEE-93BC-8EED06CFFF31 wds:Q28585102-F3C5BAAC-3FB2-47EC-8A66-844D0FC00F27 wds:Q28585102-F6C92733-A1F0-4548-A85A-699967485DA6 wds:Q28585102-F83CE89B-8030-4437-9041-DA7C50626A6D
cites work	"A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2) Death before birth: clues from gene knockouts and mutations A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine Fluorescence-activated sorting of totipotent embryonic stem cells expressing developmentally regulated lacZ fusion genes Maps from two interspecific backcross DNA panels available as a community genetic mapping resource The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase Regulation of transcription by a protein methyltransferase Gapped BLAST and PSI-BLAST: a new generation of protein database search programs A murine homolog of the yeast RNA1 gene is required for postimplantation development. In vivo and in vitro arginine methylation of RNA-binding proteins Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23. The distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells Nerve growth factor-specific regulation of protein methylation during neuronal differentiation of PC12 cells. RNA and protein interactions modulated by protein arginine methylation. Arginine methylation facilitates the nuclear export of hnRNP proteins Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3'-end formation. Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins. Effect of enzymic methylation of heterogeneous ribonucleoprotein particle A1 on its nucleic-acid binding and controlled proteolysis Transcription of H-2 and Qa genes in embryonic and adult mice Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12. hnRNP C is required for postimplantation mouse development but Is dispensable for cell viability Protein methylation during the development of rat brain Methylation of high molecular weight fibroblast growth factor-2 determines post-translational increases in molecular weight and affects its intracellular distribution Transcriptional specificity of the pluripotent embryonic stem cell. Retrovirus gene traps Effects of sinefungin and 5′-deoxy-5′-S-isobutyl-adenosine on lipopolysaccharide-induced proliferation and protein N-methylation of arginyl residues in murine splenic lymphocytes
author name string	wds:Q28585102-30EB37A2-FF74-43DE-97D7-91CC4D9BB7BB wds:Q28585102-45411EAF-13B3-413B-BE67-C4A0515A55EC wds:Q28585102-664B9462-AECF-4800-AEDE-7B91C693A1B6 wds:Q28585102-9CF555AF-E9F8-40DE-8452-2481A592A80B
author name string	H E Ruley C A Scherer M J Roshon M R Pawlak
rdfs:label	Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (en) Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (nl) Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (ast)
skos:prefLabel	Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (en) Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (nl) Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (ast)
name	Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (en) Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (nl) Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable (ast)

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