Ontology highlight
ABSTRACT:
OTHER RELATED OMICS DATASETS IN: PRJNA369388
INSTRUMENT(S): LTQ Orbitrap, Q Exactive
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: Ignasi Forne
LAB HEAD: Prof. Dr. Dirk Eick
PROVIDER: PXD008270 | Pride | 2018-01-09
REPOSITORIES: Pride
Action | DRS | |||
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MS_rWTandYFFFmutants.xlsx | Xlsx | |||
Proteingroups_IF_20160919_NS.xlsx | Xlsx | |||
Ref547_NS_WTrec_150212.raw | Raw | |||
Ref547_NS_YF3_150212.raw | Raw | |||
Ref620_NS_WTrec_bead_160122.raw | Raw |
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Shah Nilay N Maqbool Muhammad Ahmad MA Yahia Yousra Y El Aabidine Amal Zine AZ Esnault Cyril C Forné Ignasi I Decker Tim-Michael TM Martin David D Schüller Roland R Krebs Stefan S Blum Helmut H Imhof Axel A Eick Dirk D Andrau Jean-Christophe JC
Molecular cell 20180101 1
The carboxy-terminal domain (CTD) of RNA polymerase (Pol) II is composed of a repetition of YSPTSPS heptads and functions as a loading platform for protein complexes that regulate transcription, splicing, and maturation of RNAs. Here, we studied mammalian CTD mutants to analyze the function of tyrosine1 residues in the transcription cycle. Mutation of 3/4 of the tyrosine residues (YFFF mutant) resulted in a massive read-through transcription phenotype in the antisense direction of promoters as w ...[more]