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F1000 Biology Reports
|
December 15, 2010
Mechanistic and functional versatility of radical SAM enzymes
Squire J Booker, Tyler L Grove
Current Opinion in Chemical Biology
|
October 16, 2007
Self-sacrifice in radical S-adenosylmethionine proteins
Squire J Booker, Robert M Cicchillo, Tyler L Grove
Biochemistry
|
May 23, 2018
Investigation of Solvent Hydron Exchange in the Reaction Catalyzed by the Antibiotic Resistance Protein Cfr
Matthew R Bauerle, Tyler L Grove, Squire J Booker
Nucleic Acids Research
|
July 9, 2018
Identification of a novel tRNA wobble uridine modifying activity in the biosynthesis of 5-methoxyuridine
Huijeong Ryu, Tyler L Grove, Steven C Almo, et al.
Journal of the American Chemical Society
|
September 16, 2011
Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation
Tyler L Grove, Matthew I Radle, Carsten Krebs, et al.
Current Opinion in Structural Biology
|
October 20, 2023
The new epoch of structural insights into radical SAM enzymology
Jake Lachowicz, James Lee, Alia Sagatova, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
September 20, 2013
X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry
Peter J Goldman, Tyler L Grove, Squire J Booker, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
August 9, 2013
A high-throughput screen for quorum-sensing inhibitors that target acyl-homoserine lactone synthases
Quin H Christensen, Tyler L Grove, Squire J Booker, et al.
Science (New York, N.Y.)
|
April 16, 2016
Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA
Erica L Schwalm, Tyler L Grove, Squire J Booker, et al.
Journal of the American Chemical Society
|
June 20, 2015
Electrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low-Potential Auxiliary Cluster
Stephanie J Maiocco, Tyler L Grove, Squire J Booker, et al.
Page
of 6
Search research articles
Search
Showing results (1-10 of 58) with videos related to
Sort By:
Page
of 6
F1000 Biology Reports
|
December 15, 2010
Mechanistic and functional versatility of radical SAM enzymes
Squire J Booker, Tyler L Grove
Current Opinion in Chemical Biology
|
October 16, 2007
Self-sacrifice in radical S-adenosylmethionine proteins
Squire J Booker, Robert M Cicchillo, Tyler L Grove
Biochemistry
|
May 23, 2018
Investigation of Solvent Hydron Exchange in the Reaction Catalyzed by the Antibiotic Resistance Protein Cfr
Matthew R Bauerle, Tyler L Grove, Squire J Booker
Nucleic Acids Research
|
July 9, 2018
Identification of a novel tRNA wobble uridine modifying activity in the biosynthesis of 5-methoxyuridine
Huijeong Ryu, Tyler L Grove, Steven C Almo, et al.
Journal of the American Chemical Society
|
September 16, 2011
Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation
Tyler L Grove, Matthew I Radle, Carsten Krebs, et al.
Current Opinion in Structural Biology
|
October 20, 2023
The new epoch of structural insights into radical SAM enzymology
Jake Lachowicz, James Lee, Alia Sagatova, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
September 20, 2013
X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry
Peter J Goldman, Tyler L Grove, Squire J Booker, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
August 9, 2013
A high-throughput screen for quorum-sensing inhibitors that target acyl-homoserine lactone synthases
Quin H Christensen, Tyler L Grove, Squire J Booker, et al.
Science (New York, N.Y.)
|
April 16, 2016
Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA
Erica L Schwalm, Tyler L Grove, Squire J Booker, et al.
Journal of the American Chemical Society
|
June 20, 2015
Electrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low-Potential Auxiliary Cluster
Stephanie J Maiocco, Tyler L Grove, Squire J Booker, et al.
Page
of 6