Research Topics
Genomes and GenesSpecies | C L WillSummaryAffiliation: Philipps University Country: Germany Publications
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Detail Information
Publications
Protein functions in pre-mRNA splicingC L Will
Institut fur Molekularbiologie und Tumorforschung, Philipps Universitat Marburg, Emil Mannkopff Strasse 2, 35037, Marburg, Germany
Curr Opin Cell Biol 9:320-8. 1997..Finally, growing evidence suggests that proteins may contribute directly to the spliceosome's active sites...
The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that can be phosphorylated by the snRNP-associated protein kinaseS Fetzer
Institut fur Molekularbiologie und Tumorforschung, Marburg, Germany
RNA 3:344-55. 1997..Thus, the tri-snRNP-specific 27K protein could potentially be involved in SR protein-mediated protein/protein interactions and, additionally, its phosphorylation state could modulate pre-mRNA splicing...
The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28pS Teigelkamp
Institut fur Molekularbiologie und Tumorforschung, Philipps Universitat Marburg, Germany
RNA 3:1313-26. 1997....
The human U4/U6 snRNP contains 60 and 90kD proteins that are structurally homologous to the yeast splicing factors Prp4p and Prp3pJ Lauber
Institut fur Molekularbiologie und Tumorforschung, Marburg, Germany
RNA 3:926-41. 1997..Based on their structural similarity with essential splicing factors in yeast, the human U4/U6-60kD and 90kD proteins are likely also to play important roles in the mammalian splicing process...
In vitro reconstitution of mammalian U1 snRNPs active in splicing: the U1-C protein enhances the formation of early (E) spliceosomal complexesC L Will
Institut fur Molekularbiologie und Tumorforschung, Philipps Universitat Marburg, Germany
Nucleic Acids Res 24:4614-23. 1996..Studies with recombinant U1-C protein mutants indicated that the N-terminal domain of U1-C is necessary and sufficient for the stimulation of E complex formation...
Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factorsA Woppmann
Institut fur Molekularbiologie und Tumorforschung, Marburg, Germany
Nucleic Acids Res 21:2815-22. 1993..A potential general role for this enzyme in the phosphorylation of splicing factors and its consequences for pre-mRNA splicing regulation are discussed...
