about
Restoration of full-length SMN promoted by adenoviral vectors expressing RNA antisense oligonucleotides embedded in U7 snRNAsThe SR protein familyThe role of U2AF35 and U2AF65 in enhancer-dependent splicingExtended base pair complementarity between U1 snRNA and the 5' splice site does not inhibit splicing in higher eukaryotes, but rather increases 5' splice site recognitionLinking splicing to Pol II transcription stabilizes pre-mRNAs and influences splicing patternsA systematic analysis of the factors that determine the strength of pre-mRNA splicing enhancers.Retention of spliceosomal components along ligated exons ensures efficient removal of multiple intronsThe architecture of pre-mRNAs affects mechanisms of splice-site pairing.Structural and functional conservation of the Drosophila doublesex splicing enhancer repeat elements.G Run-mediated recognition of proteolipid protein and DM20 5' splice sites by U1 small nuclear RNA is regulated by context and proximity to the splice site.Combinatorial control of exon recognition.The TCF C-clamp DNA binding domain expands the Wnt transcriptome via alternative target recognition.Genomic splice-site analysis reveals frequent alternative splicing close to the dominant splice site.Efficient internal exon recognition depends on near equal contributions from the 3' and 5' splice sites.Splicing predictions reliably classify different types of alternative splicing.The splicing regulators Tra and Tra2 are unusually potent activators of pre-mRNA splicing.The Silent Sway of Splicing by Synonymous SubstitutionsPreparation of splicing competent nuclear extracts.Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms.Enhancer-dependent 5'-splice site control of fruitless pre-mRNA splicing.Spliceosome assembly pathways for different types of alternative splicing converge during commitment to splice site pairing in the A complex.Splice-site pairing is an intrinsically high fidelity process.Coupling between alternative polyadenylation and alternative splicing is limited to terminal intronsSpliceosomes walk the line: splicing errors and their impact on cellular function.Thermodynamic dissection of the substrate-ribozyme interaction in the hammerhead ribozyme.Release of SR Proteins from CLK1 by SRPK1: A Symbiotic Kinase System for Phosphorylation Control of Pre-mRNA Splicing.Embracing the complexity of pre-mRNA splicing.In vitro assay of pre-mRNA splicing in mammalian nuclear extract.Extensive regulation of NAGNAG alternative splicing: new tricks for the spliceosome?Kinetic analysis of in vitro pre-mRNA splicing in HeLa nuclear extract.Inhibition of the hammerhead ribozyme by neomycin.Preparation of Splicing Competent Nuclear Extract from Mammalian Cells and In Vitro Pre-mRNA Splicing Assay.Isolation of Newly Transcribed RNA Using the Metabolic Label 4-Thiouridine.Molecular Mechanisms for CFIm-Mediated Regulation of mRNA Alternative Polyadenylation.The function of multisite splicing enhancers.Dangerous play--splitting the message may leave you empty handed.The internal equilibrium of the hammerhead ribozyme reactionSR proteins are 'locators' of the RNA splicing machineryUltra-deep sequencing reveals pre-mRNA splicing as a sequence driven high-fidelity processPancreatic pericytes originate from the embryonic pancreatic mesenchyme
P50
Q21142695-265437E0-E95D-4EE6-8F82-DDE3B584FCDEQ21183897-F1F92DD2-16D1-4DBA-AB70-5BA4E59D1A2AQ24540026-2204D5C0-5520-4391-BD69-FBF968802155Q24812684-6FF06F40-A8FB-4C07-9755-5D9B2C615085Q33241167-861198DA-5885-4A61-A872-EA597DD20873Q33890073-AE6CE609-CAB8-47EE-A7F0-360EA909FE6EQ34075915-53FFDF70-5159-4F77-BB22-519DF1D1D429Q34132523-773F1F9E-D133-4A65-BBFF-1F9A1C913151Q34361105-A1248284-7F17-41EF-B58A-63E6172B8630Q34575659-AE0CB49F-1620-4771-8AD2-58886909C866Q34585102-E17F6EBD-3697-4460-B8E4-7CB4C923856EQ34711963-2C35487F-C6AB-46D8-AE6D-F41A3EF7B38AQ35172222-B202594A-39EB-4A63-864B-B558C0899448Q35468251-2C1939F5-66D6-4677-8785-6EC1A9F7E61FQ35534944-540727FE-9331-4326-9E7C-E7D2916513F1Q35537142-7974AEA2-CA96-4F3C-950D-8DCAD40E9B97Q35794628-584F1CFB-DBAF-4940-AEDA-86CE53FB5D87Q35849740-B3845B7F-C618-4147-B876-E85352EDA1F6Q36481243-0085BA30-4EBF-45C3-8600-FC221D61B58CQ36661325-795F6F70-C715-49E4-91EC-9715DB353D9EQ37099916-7E62F7D3-231A-4677-91FC-246C35763E73Q37100836-0901F77A-87DD-4C56-9BE9-43ABA59710BDQ37130394-6A528604-A5FB-4B19-8014-5082F4F9A769Q37549292-1E9B3153-D6BF-4D1D-A8FC-D31410658998Q38330854-2156DC32-0E77-457A-A45C-82062AA1FB1CQ41845300-A2A362BF-AB35-48A4-A107-F3BDE7858C74Q41909890-71E5B139-8474-471F-88C8-0DB2FFBD5B28Q42026538-2C57E0AA-50C9-480D-BDF7-8CECF76A0925Q42132653-6A267655-2833-4C93-BB6F-BDEB8A489E00Q43037725-C4444415-0303-4804-972E-344552EA5D0FQ43205493-96182195-F114-435C-9D5B-CAD2626786F8Q45050760-987B581D-91F6-4F7F-A4B1-C4D4274A016CQ46371240-2B95D07D-10AC-48C4-AF39-9822ECC8034FQ47256963-0BCCB1B6-0CCA-41C8-8C3E-7FE0F7D2CDE6Q47858556-4D270DA6-A9F6-4C67-B96D-650F64BE8C77Q54721726-A31C192F-377B-4C6D-A4D6-D43FDA141E55Q72528345-14F8A3F9-8A4C-4BE4-A4F7-2C31AB9F971EQ77796058-15D0F2FF-E0D3-47B2-AAEF-118B5C64B4CEQ90458196-42202CCA-2FB8-4391-BE28-0C442BCDCBBEQ91640773-DE3369E6-9008-4785-A02A-3EDAAD9B23BB
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Klemens J Hertel
@ast
Klemens J Hertel
@en
Klemens J Hertel
@es
Klemens J Hertel
@nl
type
label
Klemens J Hertel
@ast
Klemens J Hertel
@en
Klemens J Hertel
@es
Klemens J Hertel
@nl
prefLabel
Klemens J Hertel
@ast
Klemens J Hertel
@en
Klemens J Hertel
@es
Klemens J Hertel
@nl
P106
P31
P496
0000-0002-7560-9529