about
Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodiesDetection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transferA mutation linked to retinitis pigmentosa in HPRP31 causes protein instability and impairs its interactions with spliceosomal snRNPs.Chromatin position in human HepG2 cells: although being non-random, significantly changed in daughter cells.In vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies.The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing.Histone deacetylase activity modulates alternative splicing.In vivo kinetics of Cajal body componentsNuclear LSm8 affects number of cytoplasmic processing bodies via controlling cellular distribution of Like-Sm proteins.The Cajal body: a meeting place for spliceosomal snRNPs in the nuclear maze.In vivo detection of RNA-binding protein interactions with cognate RNA sequences by fluorescence resonance energy transfer.Where splicing joins chromatin.Spliceosomal small nuclear ribonucleoprotein particles repeatedly cycle through Cajal bodies.Cajal bodies and snRNPs - friends with benefits.Nuclear bodies: news insights into structure and function.The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells.Enhancement of U4/U6 small nuclear ribonucleoprotein particle association in Cajal bodies predicted by mathematical modeling.CRE promoter sites modulate alternative splicing via p300-mediated histone acetylationsnRNP proteins in health and disease.Non-isotopic mapping of ribosomal RNA synthesis and processing in the nucleolus.Nuclear organization studied with the help of a hypotonic shift: its use permits hydrophilic molecules to enter into living cells.Retinitis pigmentosa mutations of SNRNP200 enhance cryptic splice-site recognition.In situ fluorescence visualization of bromouridine incorporated into newly transcribed nucleolar RNAPre-ribosomal RNA is processed in permeabilised cells at the site of transcriptionDIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs
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description
researcher
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wetenschapper
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հետազոտող
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name
David Stanek
@ast
David Stanek
@en
David Stanek
@es
David Stanek
@nl
David Stanek
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type
label
David Stanek
@ast
David Stanek
@en
David Stanek
@es
David Stanek
@nl
David Stanek
@sl
prefLabel
David Stanek
@ast
David Stanek
@en
David Stanek
@es
David Stanek
@nl
David Stanek
@sl
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P21
P31
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0000-0002-5865-175X