about
RBM4 down-regulates PTB and antagonizes its activity in muscle cell-specific alternative splicingHomologues of the Caenorhabditis elegans Fox-1 protein are neuronal splicing regulators in mammalsA common variant in MTHFD1L is associated with neural tube defects and mRNA splicing efficiencyNext-generation SELEX identifies sequence and structural determinants of splicing factor binding in human pre-mRNA sequenceMicroRNAs regulate the expression of the alternative splicing factor nPTB during muscle developmentThe hepatitis B virus PRE contains a splicing regulatory element.Characterization of multimeric complexes formed by the human PTB1 protein on RNA.The domains of polypyrimidine tract binding protein have distinct RNA structural preferencesGenome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skippingDe novo prediction of PTBP1 binding and splicing targets reveals unexpected features of its RNA recognition and function.RNA looping by PTB: Evidence using FRET and NMR spectroscopy for a role in splicing repressionELAV multimerizes on conserved AU4-6 motifs important for ewg splicing regulation.Drosophila polypyrimidine tract-binding protein is necessary for spermatid individualization.A biophysical model for identifying splicing regulatory elements and their interactions.Regulation of the mutually exclusive exons 8a and 8 in the CaV1.2 calcium channel transcript by polypyrimidine tract-binding protein.The polypyrimidine tract binding protein (PTB) represses splicing of exon 6B from the beta-tropomyosin pre-mRNA by directly interfering with the binding of the U2AF65 subunitHNRNP G and HTRA2-BETA1 regulate estrogen receptor alpha expression with potential impact on endometrial cancer.Activation and repression functions of an SR splicing regulator depend on exonic versus intronic-binding positionPSD-95 is post-transcriptionally repressed during early neural development by PTBP1 and PTBP2.A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons.A correlation with exon expression approach to identify cis-regulatory elements for tissue-specific alternative splicing.Mutually exclusive splicing regulates the Nav 1.6 sodium channel function through a combinatorial mechanism that involves three distinct splicing regulatory elements and their ligandsNeuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2.YB-1 binds to CAUC motifs and stimulates exon inclusion by enhancing the recruitment of U2AF to weak polypyrimidine tractsThe splicing regulator PTBP1 controls the activity of the transcription factor Pbx1 during neuronal differentiation.Polypyrimidine tract binding protein 1 protects mRNAs from recognition by the nonsense-mediated mRNA decay pathway.Discontinuous native protein gel electrophoresis: pros and cons.VEGF-A splicing: the key to anti-angiogenic therapeutics?Arginine-rich motifs are not required for hepatitis delta virus RNA binding activity of the hepatitis delta antigen.Tannic acid facilitates expression of the polypyrimidine tract binding protein and alleviates deleterious inclusion of CHRNA1 exon P3A due to an hnRNP H-disrupting mutation in congenital myasthenic syndromeMultiple roles for polypyrimidine tract binding (PTB) proteins in trypanosome RNA metabolismFunctional mapping of the interaction between TDP-43 and hnRNP A2 in vivoLarge-scale remodeling of a repressed exon ribonucleoprotein to an exon definition complex active for splicing.U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression.Functional diversity of the hnRNPs: past, present and perspectives.Defining the roles and interactions of PTB.Nuclear matrix protein Matrin3 regulates alternative splicing and forms overlapping regulatory networks with PTB.Position-dependent alternative splicing activity revealed by global profiling of alternative splicing events regulated by PTB.Polypyrimidine tract binding protein (PTB) associates with intronic and exonic domains to squelch nuclear export of unspliced RNA.Polypyrimidine tract binding protein blocks the 5' splice site-dependent assembly of U2AF and the prespliceosomal E complex.
P2860
Q24300358-A2A2E12A-75D9-4FE9-8380-337530E271D5Q24537300-B05181F0-F081-4F03-AE94-0703CC014ECFQ24646784-71CCBCEF-BA84-4212-AB02-42038E0B6B16Q24654214-7CF1699C-2573-4494-A380-0CFF8E0D66C8Q24670766-A103BCE6-10B8-4534-908A-986E1C96ADFDQ25255938-65E164B5-EF1E-47B7-88B3-695BA9189B7FQ27473021-E9B75023-86C1-4A64-9161-4BC81762D0D5Q27490218-03CEFDDC-84BD-4DDB-BCAE-B5F8EBE16790Q28269954-7188A48F-9B97-4267-9F55-E3C7F62F8FA8Q31151038-68AB1382-39C0-4E3A-8C7C-0B86E43BC671Q33733006-3AF7A667-F391-4B33-8582-09BA00D75C27Q33925028-09D40C38-BC06-4EA6-AD83-6239431A8610Q34005173-D3D17256-FDE6-4721-9D3C-ADFDA8933853Q34575772-4CEBC477-33C8-4118-B476-ACA7386286AEQ34695458-F1DC453B-C249-4300-94AD-642C2E86B125Q35131606-8D9AB043-3067-453B-A65F-B9C19945F1D1Q35164945-7799DDB7-300D-4108-8458-8009795E7960Q35633621-E70A31D3-0C90-45DD-AEED-5A9AF9F1E406Q35783819-9B1DC54F-D2CC-44F6-B1A0-60985E2AAD81Q35855671-A2E9ECD8-9206-416A-8FEE-356074154843Q35945401-8BD46964-04B3-4F60-B569-D770B29C1F1BQ36106891-87E37B3A-7641-49AD-807E-C522F6DF81E7Q36174640-4EE53867-7E23-4D46-806D-C642A1F16B1AQ36280625-0ABB7429-8CAD-4AA9-8866-91A757053E6CQ36585875-975444E5-8FC6-487D-9269-01D4F0DD5B19Q36609961-6EC28FBA-EF35-46A8-A701-E56866AC3375Q36841865-4667A25E-740E-4F45-A997-C4931532E58CQ37035757-A3E5C429-A8B0-486C-9447-804E51C73996Q37036730-0B84A56E-5897-4B60-833B-885E0969C3FFQ37128363-2451696B-5395-439D-ACD7-05B16AB823C8Q37142075-F54E8E90-572A-4DAA-817A-65A4D8DD82D9Q37259106-552E872E-1777-4403-AD51-62D74AABFE82Q37437764-B9B3BFE7-2E55-4C1B-97BF-DE8868334C08Q37597322-13504EBC-0C77-4CEC-8396-BCB3364EA74CQ37783316-EC0E70FC-8875-4502-9F72-116197CB9F11Q38027965-4AFCDEF9-58E8-47D0-BFE1-245C5EF2A2C4Q38301627-FC29C103-64EA-402E-8D7C-8A8F7B30621DQ38341668-5232E5E6-805F-448C-B28E-DE8316773A00Q39075069-A5B5D5BF-0945-42D2-8A81-EA38CCCFF4ACQ39101565-6B3D9BBC-FA20-45F8-BA21-FD0D589B3620
P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Exon repression by polypyrimidine tract binding protein
@ast
Exon repression by polypyrimidine tract binding protein
@en
Exon repression by polypyrimidine tract binding protein
@nl
type
label
Exon repression by polypyrimidine tract binding protein
@ast
Exon repression by polypyrimidine tract binding protein
@en
Exon repression by polypyrimidine tract binding protein
@nl
prefLabel
Exon repression by polypyrimidine tract binding protein
@ast
Exon repression by polypyrimidine tract binding protein
@en
Exon repression by polypyrimidine tract binding protein
@nl
P2093
P2860
P356
P1433
P1476
Exon repression by polypyrimidine tract binding protein
@en
P2093
Batoul Amir-Ahmady
Douglas L Black
Martin L Phillips
Paul L Boutz
Vadim Markovtsov
P2860
P304
P356
10.1261/RNA.2250405
P407
P577
2005-05-01T00:00:00Z