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Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic acid (SADTA) via two mechanisms (at pH 7.0).
Dali Liu
(Contributor)
Edvin V. Pozharski
(Contributor)
Bryan W. Lepore
(Contributor)
Mengmeng Fu
(Contributor)
Richard B Silverman
(Contributor)
Gregory A. Petsko
(Contributor)
Dagmar Ringe
(Contributor)
Northwestern University
Chemistry
Dataset
Overview
Research Output
(1)
Research output
Research Output per year
2007
2007
2007
1
Article
Research Output per year
Research Output per year
1 results
Publication Year, Title
(descending)
Publication Year, Title
(ascending)
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2007
Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "A tale of two mechanisms"
Liu, D., Pozharski, E., Lepore, B. W., Fu, M.,
Silverman, R. B.
, Petsko, G. A. & Ringe, D.,
Sep 18 2007
,
In:
Biochemistry.
46
,
37
,
p. 10517-10527
11 p.
Research output
:
Contribution to journal
›
Article
›
peer-review
Amino
100%
Escherichia Coli
100%
Aspartate Aminotransferase
100%
L-aspartate
100%
2-thiophenecarboxylic Acid
100%
14
Scopus citations