Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor-Reference-Cited by-同舟云学术

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Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor

Published:2019-04 Issue:1 Volume:74 Page:143-157.e5
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Krupp Ferdinand,Said Nelly,Huang Yong-Heng,Loll Bernhard,Bürger Jörg,Mielke Thorsten,Spahn Christian M.T.,Wahl Markus C.

Funder

Chinese Scholarship Council

Deutsche Forschungsgemeinschaft

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference55 articles.

1. Towards automated crystallographic structure refinement with phenix.refine;Afonine;Acta Crystallogr. D Biol. Crystallogr.,2012

2. Regulation of transcript elongation;Belogurov;Annu. Rev. Microbiol.,2015

3. A NusE:NusG complex links transcription and translation;Burmann;Science,2010

4. Escherichia coli RNA polymerase mutations located near the upstream edge of an RNA:DNA hybrid and the beginning of the RNA-exit channel are defective for transcription antitermination by the N protein from lambdoid phage H-19B;Cheeran;J. Mol. Biol.,2005

5. The site of action of the antiterminator protein N from the lambdoid phage H-19B;Cheeran;J. Biol. Chem.,2007

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