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Aspartate transcarbamylase from Escherichia coli: activity and regulation.
Department of Chemistry, Harvard University, Cambridge, MA.
PMID: 8154326 [PubMed - indexed for MEDLINE]
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Cited by 25 PubMed Central articles
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Overexpression, purification, crystallization and preliminary structural studies of catabolic ornithine transcarbamylase from Lactobacillus hilgardii.
de Las Rivas B, Rodríguez H, Angulo I, Muñoz R, Mancheño JM.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1; 63(Pt 7):563-7. Epub 2007 Jun 11.
[Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007]
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A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase.
Velyvis A, Yang YR, Schachman HK, Kay LE.
Proc Natl Acad Sci U S A. 2007 May 22; 104(21):8815-20. Epub 2007 May 14.
[Proc Natl Acad Sci U S A. 2007]
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Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.
Fetler L, Kantrowitz ER, Vachette P.
Proc Natl Acad Sci U S A. 2007 Jan 9; 104(2):495-500. Epub 2007 Jan 3.
[Proc Natl Acad Sci U S A. 2007]
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