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Jeffery Constance J.
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http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_10/101021bi035688h/authorship/3
http://hub.abes.fr/oup/periodical/proeng/1999/volume_12/issue_10/101093protein1210863/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_5/101021bi991604m/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_26/101021bi002916o/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_6/101021bi0018483/authorship/1
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The Escherichia coli aspartate receptor: sequence specificity of a transmembrane helix studied by hydrophobic-biased random mutagenesis
Inhibition of Type I and Type II Phosphomannose Isomerases by the ReactionIntermediate Analogue 5-Phospho-d-Arabinonohydroxamic Acid Supports aCatalytic Role for the Metal Cofactor
Crystal Structure of Rabbit Phosphoglucose Isomerase Complexed with Its Substrated-Fructose 6-Phosphate
Crystal Structure of Rabbit Phosphoglucose Isomerase, a Glycolytic Enzyme ThatMoonlights as Neuroleukin, Autocrine Motility Factor, and DifferentiationMediator,
Crystal Structure of Rabbit Phosphoglucose Isomerase Complexed with5-Phospho-d-Arabinonate Identifies the Role of Glu357 in Catalysis
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