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Table representation of search results timeline featuring number of search results per year.
Year | Number of Results |
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1996 | 1 |
1998 | 1 |
1999 | 1 |
2001 | 1 |
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2011 | 1 |
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In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae.
J Biol Chem. 2011 Nov 25;286(47):40734-42. doi: 10.1074/jbc.M111.274068. Epub 2011 Oct 7.
J Biol Chem. 2011.
PMID: 21984832
Free PMC article.
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Olsen LR, Vetting MW, Roderick SL.
Olsen LR, et al.
Protein Sci. 2007 Jun;16(6):1230-5. doi: 10.1110/ps.072779707. Epub 2007 May 1.
Protein Sci. 2007.
PMID: 17473010
Free PMC article.
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Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
Olsen LR, Roderick SL.
Olsen LR, et al.
Biochemistry. 2001 Feb 20;40(7):1913-21. doi: 10.1021/bi002503n.
Biochemistry. 2001.
PMID: 11329257
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Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y.
Brown K, et al.
EMBO J. 1999 Aug 2;18(15):4096-107. doi: 10.1093/emboj/18.15.4096.
EMBO J. 1999.
PMID: 10428949
Free PMC article.
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Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes.
Pompeo F, van Heijenoort J, Mengin-Lecreulx D.
Pompeo F, et al.
J Bacteriol. 1998 Sep;180(18):4799-803. doi: 10.1128/JB.180.18.4799-4803.1998.
J Bacteriol. 1998.
PMID: 9733680
Free PMC article.
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Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.
Gehring AM, Lees WJ, Mindiola DJ, Walsh CT, Brown ED.
Gehring AM, et al.
Biochemistry. 1996 Jan 16;35(2):579-85. doi: 10.1021/bi952275a.
Biochemistry. 1996.
PMID: 8555230
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