[PDF][PDF] Structure of mammalian RNA polymerase II elongation complex bound by α-amanitin and study of mammalian transcription termination and 3'end processing
X Liu - 2019 - ediss.uni-goettingen.de
Dissertation Page 1 Structure of mammalian RNA polymerase II elongation complex bound by
α-amanitin and study of mammalian transcription termination and 3’ end processing Dissertation …
α-amanitin and study of mammalian transcription termination and 3’ end processing Dissertation …
[HTML][HTML] α-Amanitin blocks translocation by human RNA polymerase II
XQ Gong, YA Nedialkov, ZF Burton - Journal of Biological Chemistry, 2004 - ASBMB
Our laboratory has developed methods for transient state kinetic analysis of human RNA
polymerase II elongation. In these studies, multiple conformations of the RNA polymerase II …
polymerase II elongation. In these studies, multiple conformations of the RNA polymerase II …
Abundance of the largest subunit of RNA polymerase II in the nucleus is regulated by nucleo-cytoplasmic shuttling
N Custódio, M Antoniou, M Carmo-Fonseca - Experimental cell research, 2006 - Elsevier
Eukaryotic RNA polymerase II is a complex enzyme composed of 12 distinct subunits that is
present in cells in low abundance. Transcription of mRNA by RNA polymerase II involves a …
present in cells in low abundance. Transcription of mRNA by RNA polymerase II involves a …
[HTML][HTML] Action of α-amanitin during pyrophosphorolysis and elongation by RNA polymerase II
DR Chafin, H Guo, DH Price - Journal of Biological Chemistry, 1995 - ASBMB
Using defined elongation complexes formed on dC-tailed templates with Drosophila RNA
polymerase II, we have examined elongation, pyrophosphorolysis, and DmS-II-mediated …
polymerase II, we have examined elongation, pyrophosphorolysis, and DmS-II-mediated …
Structural basis of transcription: α-amanitin–RNA polymerase II cocrystal at 2.8 Å resolution
DA Bushnell, P Cramer… - Proceedings of the …, 2002 - National Acad Sciences
Structural basis of transcription: α-Amanitin–RNA polymerase II cocrystal at 2.8 Å resolution |
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[HTML][HTML] Cryo-EM structure of a mammalian RNA polymerase II elongation complex inhibited by α-amanitin
RNA polymerase II (Pol II) is the central enzyme that transcribes eukaryotic protein-coding
genes to produce mRNA. The mushroom toxin α-amanitin binds Pol II and inhibits …
genes to produce mRNA. The mushroom toxin α-amanitin binds Pol II and inhibits …
Isolation and functional analysis of RNA polymerase II elongation complexes
B Cheng, DH Price - Methods, 2009 - Elsevier
The elongation phase of transcription by RNA polymerase II (RNAP II) is tightly controlled by
a large number of transcription elongation factors. Here we describe experimental …
a large number of transcription elongation factors. Here we describe experimental …
Elongation by RNA polymerase II: structure–function relationship
A Gnatt - Biochimica et Biophysica Acta (BBA)-Gene Structure …, 2002 - Elsevier
RNA polymerase II is the eukaryotic enzyme that transcribes all the mRNA in the cell.
Complex mechanisms of transcription and its regulation underlie basic functions including …
Complex mechanisms of transcription and its regulation underlie basic functions including …
Yeast and human RNA polymerase II elongation complexes: evidence for functional differences and postinitiation recruitment of factors
TS Pardee, MA Ghazy, AS Ponticelli - Eukaryotic Cell, 2003 - Am Soc Microbiol
Immobilized DNA templates, glycerol gradient centrifugation, and native gel analysis were
utilized to isolate and compare functional RNA polymerase II (RNAPII) elongation …
utilized to isolate and compare functional RNA polymerase II (RNAPII) elongation …
[引用][C] The α-amanitin-binding subunits of eukaryotic RNA polymerase II
E BATEMAN, B NICHOLSON - 1981 - portlandpress.com
Eukaryotic DNA-dependent RNA polymerases are multimeric enzymes consisting of 1&15
polypeptides (Roeder, 1976). Information about the role of subunits in transcription of …
polypeptides (Roeder, 1976). Information about the role of subunits in transcription of …