S
Sittinan Chanarat
Researcher at Max Planck Society
Publications - 12
Citations - 309
Sittinan Chanarat is an academic researcher from Max Planck Society. The author has contributed to research in topics: Gene & RNA splicing. The author has an hindex of 6, co-authored 7 publications receiving 245 citations. Previous affiliations of Sittinan Chanarat include Ludwig Maximilian University of Munich.
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The Prp19 complex is a novel transcription elongation factor required for TREX occupancy at transcribed genes
TL;DR: The Prp19 splicing complex is identified as a novel transcription elongation factor that is essential for TREX occupancy at transcribed genes and that thus provides a novel link between transcription and messenger ribonucleoprotein (mRNP) formation.
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Splicing and beyond: the many faces of the Prp19 complex.
TL;DR: The different functions of NTC/Prp19C are discussed focusing on the novel and emerging ones as well as open questions.
Journal ArticleDOI
Transgenic overexpression of the alpha-synuclein interacting protein synphilin-1 leads to behavioral and neuropathological alterations in mice.
Silke Nuber,Thomas Franck,Hartwig Wolburg,Ulrike Schumann,Nicolas Casadei,Kristina Fischer,Carsten Calaminus,Bernd J. Pichler,Sittinan Chanarat,Peter Teismann,Jörg B. Schulz,Andreas R. Luft,Jiirgen Tomiuk,Johannes Wilbertz,Antje Bornemann,Rejko Krüger,Olaf Riess +16 more
TL;DR: A pathological role of overexpressed synphilin-1 in vivo will help to further elucidate the mechanisms of protein aggregation and neuronal cell death in Parkinson’s disease.
Error-Prone Splicing Controlled by the Ubiquitin Relative Hub1
TL;DR: It is shown that the ubiquitin-like protein Hub1 binds to the DEAD-box helicase Prp5, a key regulator of early spliceosome assembly, and stimulates its ATPase activity thereby enhancing splicing and relaxing fidelity.
Journal ArticleDOI
Error-Prone Splicing Controlled by the Ubiquitin Relative Hub1
TL;DR: In this paper, the ubiquitin-like protein Hub1 was shown to activate the DEAD-box helicase Prp5, a key regulator of early spliceosome assembly, and stimulate its ATPase activity thereby enhancing splicing and relaxing fidelity.