S
Sunbin Liu
Researcher at Free University of Berlin
Publications - 12
Citations - 829
Sunbin Liu is an academic researcher from Free University of Berlin. The author has contributed to research in topics: snRNP & Spliceosome. The author has an hindex of 9, co-authored 12 publications receiving 784 citations. Previous affiliations of Sunbin Liu include Max Planck Society.
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Journal ArticleDOI
Protein 61K, encoded by a gene (PRPF31) linked to autosomal dominant retinitis pigmentosa, is required for U4/U6·U5 tri-snRNP formation and pre-mRNA splicing
TL;DR: These studies suggest that disruptions in tri‐snRNP formation and function resulting from mutations in the 61K protein may contribute to the manifestation of this disease.
Journal ArticleDOI
The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP.
TL;DR: Interactions between tri-snRNP proteins are investigated using the yeast two-hybrid assay and in vitro binding assays, and distinct protein domains that are critical for the connectivity of this protein network in the human tri- SnRNP are identified.
Journal ArticleDOI
Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa.
Vladimir Pena,Sunbin Liu,Janusz M. Bujnicki,Janusz M. Bujnicki,Reinhard Lührmann,Markus C. Wahl +5 more
TL;DR: It is concluded that the expanded Prp8 Jab1/MPN domain represents a pseudoenzyme converted into a protein-protein interaction platform and that dysfunction of this platform underlies Retinitis pigmentosa.
Journal ArticleDOI
Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
Sunbin Liu,Ping Li,Olexandr Dybkov,Stephanie Nottrott,Klaus Hartmuth,Reinhard Lührmann,Teresa Carlomagno,Markus C. Wahl +7 more
TL;DR: Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation and suggest the Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces.
Journal ArticleDOI
The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation
Bernhard Laggerbauer,Sunbin Liu,Evgeny M. Makarov,Hans-Peter Vornlocher,Olga V. Makarova,Dierk Ingelfinger,Tilmann Achsel,Reinhard Lührmann +7 more
TL;DR: The characterized 52-kDa protein associated with the human U5 snRNP, designated U5-52K, is identical to the CD2BP2 and interacts with the cytoplasmic portion of the human T-cell surface protein CD2, suggesting it might function in tri-snRNP assembly.