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The human U4/U6 snRNP contains 60 and 90kD proteins that are structurally homologous to the yeast splicing factors Prp4p and Prp3p.
Lauber J, Plessel G, Prehn S, Will CL, Fabrizio P, Gröning K, Lane WS, Lührmann R. Lauber J, et al. Among authors: luhrmann r. RNA. 1997 Aug;3(8):926-41. RNA. 1997. PMID: 9257651 Free PMC article.
Immunoaffinity-purified human 25S [U4/U6.U5] tri-snRNPs harbor a set of polypeptides, termed the tri-snRNP proteins, that are not present in Mono Q-purified 20S U5 snRNPs or 10S U4/U6 snRNPs and that are important for tri-snRNP complex formation (Behrens SE, Luhrmann R …
Immunoaffinity-purified human 25S [U4/U6.U5] tri-snRNPs harbor a set of polypeptides, termed the tri-snRNP proteins, that are not present in …
The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p.
Teigelkamp S, Mundt C, Achsel T, Will CL, Lührmann R. Teigelkamp S, et al. Among authors: luhrmann r. RNA. 1997 Nov;3(11):1313-26. RNA. 1997. PMID: 9409622 Free PMC article.
Through UV-crosslinking experiments, we previously provided evidence suggesting that a U5 snRNP protein with a molecular weight in the 100-kDa range is an ATP-binding protein (Laggerbauer B, Lauber J, Luhrmann R, 1996, Nucleic Acid Res 24:868-875). Separation of HeL …
Through UV-crosslinking experiments, we previously provided evidence suggesting that a U5 snRNP protein with a molecular weight in the 100-k …
357 results