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Department of Life Sciences
Robert O.J. Weinzierl has not added Biography.
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A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription.
Molecular cell Sep, 2002 | Pubmed ID: 12408830
A fully recombinant system for activator-dependent archaeal transcription.
The Journal of biological chemistry Dec, 2004 | Pubmed ID: 15485836
Direct modulation of RNA polymerase core functions by basal transcription factors.
Molecular and cellular biology Sep, 2005 | Pubmed ID: 16135821
Modulation of RNA polymerase core functions by basal transcription factor TFB/TFIIB.
Biochemical Society symposium , 2006 | Pubmed ID: 16626286
The RNA polymerase factory: a robotic in vitro assembly platform for high-throughput production of recombinant protein complexes.
Nucleic acids research Jan, 2008 | Pubmed ID: 18025041
Bridge helix and trigger loop perturbations generate superactive RNA polymerases.
Journal of biology , 2008 | Pubmed ID: 19055851
Nanomechanical constraints acting on the catalytic site of cellular RNA polymerases.
Biochemical Society transactions Apr, 2010 | Pubmed ID: 20298196
The linker domain of basal transcription factor TFIIB controls distinct recruitment and transcription stimulation functions.
Nucleic acids research Jan, 2011 | Pubmed ID: 20851833
The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain.
BMC biology , 2010 | Pubmed ID: 21034443
Cation-Ï€ interactions induce kinking of a molecular hinge in the RNA polymerase bridge-helix domain.
Biochemical Society transactions Jan, 2011 | Pubmed ID: 21265743
Activity map of the Escherichia coli RNA polymerase bridge helix.
The Journal of biological chemistry Apr, 2011 | Pubmed ID: 21357417
Revealing the functions of TFIIB.
Transcription Nov-Dec, 2011 | Pubmed ID: 22223047
The Bridge Helix of RNA polymerase acts as a central nanomechanical switchboard for coordinating catalysis and substrate movement.
Archaea (Vancouver, B.C.) , 2011 | Pubmed ID: 22312317
Imperial College London
Simone C. Wiesler1,
Robert O.J. Weinzierl1
1Department of Life Sciences, Imperial College London
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