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Bioorganic Chemistry
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January 17, 2012
Substrate specificity in thiamin diphosphate-dependent decarboxylases
Forest H Andrews, Michael J McLeish
The FEBS Journal
|
July 31, 2013
Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes
Forest H Andrews, Michael J McLeish
Nature Chemical Biology
|
August 19, 2016
Insights into newly discovered marks and readers of epigenetic information
Forest H Andrews, Brian D Strahl, Tatiana G Kutateladze
Biochemistry
|
June 24, 2014
Perturbation of the monomer-monomer interfaces of the benzoylformate decarboxylase tetramer
Forest H Andrews, Megan P Rogers, Lake N Paul, et al.
Transcription
|
March 3, 2016
The essential role of acetyllysine binding by the YEATS domain in transcriptional regulation
Forest H Andrews, Erin K Shanle, Brian D Strahl, et al.
ACS Chemical Biology
|
January 5, 2016
Regulation of Methyllysine Readers through Phosphorylation
Forest H Andrews, Jovylyn Gatchalian, Krzysztof Krajewski, et al.
Bioorganic & Medicinal Chemistry
|
July 12, 2017
Phosphonodifluoropyruvate is a mechanism-based inhibitor of phosphonopyruvate decarboxylase from Bacteroides fragilis
Katharina Pallitsch, Megan P Rogers, Forest H Andrews, et al.
Biochemistry
|
March 18, 2014
Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of signatures useful in mechanistic studies
Hetalben Patel, Natalia S Nemeria, Forest H Andrews, et al.
Journal of Molecular Biology
|
October 5, 2016
Structural Insight into Recognition of Methylated Histone H3K4 by Set3
Jovylyn Gatchalian, Muzaffar Ali, Forest H Andrews, et al.
Biochemistry
|
April 24, 2013
A bulky hydrophobic residue is not required to maintain the V-conformation of enzyme-bound thiamin diphosphate
Forest H Andrews, Alan R Tom, Peter R Gunderman, et al.
Page
of 3
Search research articles
Search
Showing results (1-10 of 21) with videos related to
Sort By:
Page
of 3
Bioorganic Chemistry
|
January 17, 2012
Substrate specificity in thiamin diphosphate-dependent decarboxylases
Forest H Andrews, Michael J McLeish
The FEBS Journal
|
July 31, 2013
Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes
Forest H Andrews, Michael J McLeish
Nature Chemical Biology
|
August 19, 2016
Insights into newly discovered marks and readers of epigenetic information
Forest H Andrews, Brian D Strahl, Tatiana G Kutateladze
Biochemistry
|
June 24, 2014
Perturbation of the monomer-monomer interfaces of the benzoylformate decarboxylase tetramer
Forest H Andrews, Megan P Rogers, Lake N Paul, et al.
Transcription
|
March 3, 2016
The essential role of acetyllysine binding by the YEATS domain in transcriptional regulation
Forest H Andrews, Erin K Shanle, Brian D Strahl, et al.
ACS Chemical Biology
|
January 5, 2016
Regulation of Methyllysine Readers through Phosphorylation
Forest H Andrews, Jovylyn Gatchalian, Krzysztof Krajewski, et al.
Bioorganic & Medicinal Chemistry
|
July 12, 2017
Phosphonodifluoropyruvate is a mechanism-based inhibitor of phosphonopyruvate decarboxylase from Bacteroides fragilis
Katharina Pallitsch, Megan P Rogers, Forest H Andrews, et al.
Biochemistry
|
March 18, 2014
Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of signatures useful in mechanistic studies
Hetalben Patel, Natalia S Nemeria, Forest H Andrews, et al.
Journal of Molecular Biology
|
October 5, 2016
Structural Insight into Recognition of Methylated Histone H3K4 by Set3
Jovylyn Gatchalian, Muzaffar Ali, Forest H Andrews, et al.
Biochemistry
|
April 24, 2013
A bulky hydrophobic residue is not required to maintain the V-conformation of enzyme-bound thiamin diphosphate
Forest H Andrews, Alan R Tom, Peter R Gunderman, et al.
Page
of 3