Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs
about
sameAs
An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAsRegulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signalsThe stem-loop structure at the 3' end of histone mRNA is necessary and sufficient for regulation of histone mRNA stabilityUnusual structure, evolutionary conservation of non-coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene familyHistone H3 mutations--a special role for H3.3 in tumorigenesis?Identification of G1-regulated genes in normally cycling human cellsSLBP is associated with histone mRNA on polyribosomes as a component of the histone mRNPA subset of replication-dependent histone mRNAs are expressed as polyadenylated RNAs in terminally differentiated tissuesFormation of mRNA 3' ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesisIdentification of genes periodically expressed in the human cell cycle and their expression in tumorsRole for a YY1-binding element in replication-dependent mouse histone gene expression.A genomic clone encoding a novel proliferation-dependent histone H2A.1 mRNA enriched in the poly(A)+ fraction.A histone H1 protein in sea urchins is encoded by a poly(A)+ mRNA.A signal regulating mouse histone H4 mRNA levels in a mammalian cell cycle mutant and sequences controlling RNA 3' processing are both contained within the same 80-bp fragment.ERV3 and related sequences in humans: structure and RNA expression.The mRNP remodeling mediated by UPF1 promotes rapid degradation of replication-dependent histone mRNA.Different 3'-end processing produces two independently regulated mRNAs from a single H1 histone gene.Coupling of replication type histone mRNA levels to DNA synthesis requires the stem-loop sequence at the 3' end of the mRNA.Nuclear export of metazoan replication-dependent histone mRNAs is dependent on RNA length and is mediated by TAP.eIF4AIII enhances translation of nuclear cap-binding complex-bound mRNAs by promoting disruption of secondary structures in 5'UTR.Identification of a second conserved element within the coding sequence of a mouse H3 histone gene that interacts with nuclear factors and is necessary for normal expressionPolyadenylate polymerase (PAP) and 3' end pre-mRNA processing: function, assays, and association with disease.The coding sequences of mouse H2A and H3 histone genes contains a conserved seven nucleotide element that interacts with nuclear factors and is necessary for normal expression.Variable effects of the conserved RNA hairpin element upon 3' end processing of histone pre-mRNA in vitro.Replication-dependent histone gene expression is related to Cajal body (CB) association but does not require sustained CB contact.Induction of H3.3 replacement histone mRNAs during the precommitment period of murine erythroleukemia cell differentiationA chimeric mouse histone H4 gene containing either an intron or poly(A) addition signal behaves like a basal histone.Dynamic regulation of histone modifications in Xenopus oocytes through histone exchange.Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progressionExpression of a mouse replacement histone H3.3 gene with a highly conserved 3' noncoding region during SV40- and polyoma-induced Go to S-phase transition.Involvement of the 5'-leader sequence in coupling the stability of a human H3 histone mRNA with DNA replicationCytoplasmic synthesis of globin RNA in differentiated murine erythroleukemia cells: possible involvement of RNA-dependent RNA polymeraseCell cycle-dependent expression of a stable episomal human histone gene in a mouse cellExtreme sequence conservation characterizes the rabbit H3.3A histone cDNAA comprehensive compilation and alignment of histones and histone genes.Histone genes of Volvox carteri: DNA sequence and organization of two H3-H4 gene lociCharacterization of a cDNA clone coding for a sea urchin histone H2A variant related to the H2A.F/Z histone protein in vertebrates.Compilation analysis of histones and histone genes.Drosophila has a single copy of the gene encoding a highly conserved histone H2A variant of the H2A.F/Z type
P2860
Q22066003-36557B89-CAF1-456D-B125-40AF1989B98FQ24313451-88EEB7BA-DC19-4F00-9969-969039107427Q24336698-EBD6DD71-A9B1-4634-9F2D-814DE3E7D2B4Q24612966-46F2EC9F-90CC-44DC-8FF8-884FF66E2C62Q24628813-555A8365-39AA-45BA-9C00-D756D1F00DA1Q26865965-D7393D94-4986-4B2F-92B7-327FE1186AFAQ28474350-DD04F401-2724-40E7-9164-27C6955311FAQ28585828-C7588A8A-5B92-4A23-B10E-0BFC6EAE0EC3Q28596144-1C03E2DC-AC7D-4626-8D1A-9692D53E5D32Q28609911-2CF4B9FC-1968-4BE4-9E80-A6D1D9618F4BQ29619131-BB13FFC5-FC05-496E-8E48-AF586C5A9BF6Q31973939-B52BF7F4-5E60-4101-BDF9-528CDB8088B3Q33497876-A7F9E19B-A2C4-4895-8F0F-0A6023F1A7A0Q33579932-7586F1A0-28F3-4E4B-AFC1-C700C82C050BQ33881020-D7AB47CE-2C03-4414-BE78-9C79F61D12D4Q33883965-91E188C9-46BE-47C1-8EE2-ED9170F0F032Q34044351-E0D06808-F71C-4FD2-9588-961F76A95D25Q34303579-8E8F0A17-76A5-440B-9944-B853865304B5Q34343180-25FAEAFC-1C04-42BF-87D3-9498AFD5CA69Q34366173-0638E15C-1D49-46F1-9C80-4657615BF13EQ34442451-6ECEE3FF-5BD1-43C8-899C-BC3F9B0DADB3Q34588807-6E63099B-98FE-4A32-BFA4-39E78975EAE3Q34743681-991D31B5-CF1D-4193-92EF-8C79359BD972Q34766821-5F89ECAE-B439-43AC-8698-1D36445F17F4Q34978310-1ABB5622-75DF-4266-A167-C99BD8F377B5Q34986765-6FDCABF0-F6AA-459A-B3C5-D86EFB13FFACQ34988043-98250E10-B7D3-40D4-B405-AAB4489BB799Q35057177-DDD34A85-70A6-443A-BF81-9CC04058FEB9Q35071278-6030A33F-4100-4032-9E4F-C58FB170D78AQ35076429-6DEE7A62-175F-49F1-869F-A7B32C10B58FQ35222215-554A4372-AB0C-4E93-B6CD-3B084521DE7FQ35590350-D6CF18EC-8D33-4B5E-9698-DEF0055642FFQ35591900-772E10FE-8C53-48C2-8019-97D51F187F8BQ35598711-DA003617-BF2F-4278-BB66-027AC2CD1E91Q35841588-02E3B2FE-EA51-4E8C-A524-ABC490E5AD87Q35945323-0AA24BB7-1A66-4E58-A4EE-94964CC0DD3CQ36003121-F555CEFE-E148-4B19-852D-74BDC24F240BQ36129575-089C1481-1108-4B7D-BB86-98D967BFA218Q36144809-9C8567DB-CECE-462A-B6D6-54B8C0EFA2FEQ36433823-F611AF89-0BCE-4CD1-B253-D18D31D0C26F
P2860
Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs
description
1985 nî lūn-bûn
@nan
1985 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
name
Structure of a human histone c ...... encode polyadenylylated mRNAs
@ast
Structure of a human histone c ...... encode polyadenylylated mRNAs
@en
Structure of a human histone c ...... encode polyadenylylated mRNAs
@nl
type
label
Structure of a human histone c ...... encode polyadenylylated mRNAs
@ast
Structure of a human histone c ...... encode polyadenylylated mRNAs
@en
Structure of a human histone c ...... encode polyadenylylated mRNAs
@nl
prefLabel
Structure of a human histone c ...... encode polyadenylylated mRNAs
@ast
Structure of a human histone c ...... encode polyadenylylated mRNAs
@en
Structure of a human histone c ...... encode polyadenylylated mRNAs
@nl
P2860
P3181
P356
P1476
Structure of a human histone c ...... encode polyadenylylated mRNAs
@en
P2860
P304
P3181
P356
10.1073/PNAS.82.9.2834
P407
P577
1985-05-01T00:00:00Z