about
Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1A novel splicing regulator shares a nuclear import pathway with SR proteinsIdentification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein KPost-transcriptional regulation of thioredoxin by the stress inducible heterogenous ribonucleoprotein A18.LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAsRNPC1, an RNA-binding protein and a target of the p53 family, is required for maintaining the stability of the basal and stress-induced p21 transcriptN(6)-methyladenosine-dependent RNA structural switches regulate RNA-protein interactionshnRNP G elicits tumor-suppressive activity in part by upregulating the expression of TxnipRegulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7Nuclear actin is associated with a specific subset of hnRNP A/B-type proteinsProtein arginine methylation during lytic adenovirus infectionNuclear transit of human zipcode-binding protein IMP1Protein kinase A enhances, whereas glycogen synthase kinase-3 beta inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein D in a hierarchical fashionNovel DNA-binding properties of the RNA-binding protein TIAR.SMN interacts with a novel family of hnRNP and spliceosomal proteinsMagoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex.Regulation of alternative splicing by the ATP-dependent DEAD-box RNA helicase p72.Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAsThe Ct-RAE1 protein interacts with Balbiani ring RNP particles at the nuclear pore.Regulation of alternative splicing by SRrp86 through coactivation and repression of specific SR proteins.Novel functional role of CA repeats and hnRNP L in RNA stability.The hnRNPs F and H2 bind to similar sequences to influence gene expressionA sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIISCooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding proteinMCG10, a novel p53 target gene that encodes a KH domain RNA-binding protein, is capable of inducing apoptosis and cell cycle arrest in G(2)-MNucleocytoplasmic shuttling of polypyrimidine tract-binding protein is uncoupled from RNA exportTARDBP mutation analysis in TDP-43 proteinopathies and deciphering the toxicity of mutant TDP-43DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent mannerA mammalian germ cell-specific RNA-binding protein interacts with ubiquitously expressed proteins involved in splice site selectionPseudosubstrate regulation of the SCF(beta-TrCP) ubiquitin ligase by hnRNP-USplicing in action: assessing disease causing sequence changesProtein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding proteinSwitched alternative splicing of oncogene CoAA during embryonal carcinoma stem cell differentiationRoles of hnRNP A1, SR proteins, and p68 helicase in c-H-ras alternative splicing regulationRaver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteinsThe ASRG database: identification and survey of Arabidopsis thaliana genes involved in pre-mRNA splicingIdentification of RNA Binding Proteins Associated with Dengue Virus RNA in Infected Cells Reveals Temporally Distinct Host Factor RequirementsRNA-binding protein hnRNPLL as a critical regulator of lymphocyte homeostasis and differentiation
P2860
Q24291422-341BA21C-5FDC-467D-B7B9-D2E74A76FF28Q24291581-440D156D-D62B-474B-8D4A-10E95E26F3D4Q24297455-E0B473F5-BF48-4E08-A7CD-E4C0FE4DDEB1Q24298086-0E992A57-AB96-4A5E-965D-7D001AE3C7BBQ24304883-DEB47C26-71C5-431E-9A68-2BEC5CBC5B0AQ24306489-B6C36ED7-27B5-4E3B-B7BE-CCEA2905A1F0Q24306502-8BC450C2-C884-4162-B43C-3DD7147D1F33Q24307571-C7AB899B-85A7-4EE2-9475-282415F687D8Q24320088-835DFF6B-083D-475B-9345-F5C9B004EDAFQ24320117-71371978-261C-4AFC-9429-2A6B5A570538Q24337326-AB81AAA5-42A1-4152-8EE2-AD19DEFF4A76Q24527516-85B9E529-7A68-4F17-B3EA-FECE53F7776BQ24528126-74EECA74-BF56-4D90-B3B3-8AB365773AF7Q24530552-297523CF-C4AE-4C9C-9957-EBB7654F7B11Q24534031-4E682BAA-B461-481F-80DD-B8273A3F4ED5Q24534847-80EB9BE7-4945-4FDB-9739-9AC3213D0802Q24535803-4FE2FA47-4389-4BCE-8239-CDF84D39AFBEQ24535973-DC346FB8-8B1C-4990-987E-3168970BB18BQ24537705-CD26E6DF-F7C5-409D-B9A0-227AE492FC5DQ24539187-2A9980BF-F8A7-40E1-9C86-07CB004A0609Q24539824-DBC9CBEB-256E-4521-95A5-D0EE9EF76A2DQ24540103-23B5ACDB-AA06-4D0A-AC55-7D986092ACDFQ24540205-117D0678-E693-42F0-A790-FB00FF2A4222Q24541421-8EEDA8FE-4ACC-44B6-A1FE-A9A2BD72B318Q24545366-D1090D7C-DDE3-4809-A026-7309E85C0AEEQ24551190-106D7D2A-6BAF-4BAF-B8C8-7F99E870E860Q24552865-69168F4C-EE0E-4294-B011-4A85FF4E7566Q24555111-EAD84453-7EDF-47B5-8B48-051FC1FAF827Q24594172-DC0C76D6-710D-44D3-AF8A-4E0697C6C5D5Q24634159-864255B4-02A8-46D3-9063-FEC7CF1ADF62Q24670000-E48B0F31-B254-43AD-94E6-84F1350C8692Q24672630-55A13414-4E17-4591-8244-06470730E684Q24674554-B6CC282C-492E-4654-8D47-C3078CFF299AQ24678906-C52A7A59-A77C-4BB0-9B37-2F35446082E1Q24682844-234170EA-5EBA-4438-BE3F-803971AB077FQ24684890-A34BA15A-EFB4-4ABC-88FD-7A61C5A51B3CQ24685280-1B67946E-4F30-4921-90DB-266C87850A70Q24791274-3CFE5C2A-3327-46B5-A5BD-DEB694E240FCQ26694068-5C2BAC64-C0A9-4CA7-A4F5-52F697FF8441Q26773043-2B26AB49-890F-43A5-A565-235AA1812F20
P2860
description
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1999
@ast
im Juni 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: June 1999)
@en
wetenschappelijk artikel (gepubliceerd in 1999-06)
@nl
наукова стаття, опублікована в червні 1999
@uk
مقالة علمية (نشرت في يونيو 1999)
@ar
name
hnRNP complexes: composition, structure, and function
@ast
hnRNP complexes: composition, structure, and function
@en
type
label
hnRNP complexes: composition, structure, and function
@ast
hnRNP complexes: composition, structure, and function
@en
prefLabel
hnRNP complexes: composition, structure, and function
@ast
hnRNP complexes: composition, structure, and function
@en
P3181
P1476
hnRNP complexes: composition, structure, and function
@en
P2093
P304
P3181
P356
10.1016/S0955-0674(99)80051-9
P407
P577
1999-06-01T00:00:00Z