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Biochemistry|April 26, 1994
Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactoseM N Vyas, N K Vyas, F A QuiochoScience (New York, N.Y.)|December 10, 1993
Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structuresW E Meador, A R Means, F A QuiochoScience (New York, N.Y.)|May 31, 1991
Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutationsD K Wilson, F B Rudolph, F A QuiochoThe Journal of Biological Chemistry|June 15, 1986
Crystallization and x-ray diffraction studies of a phosphate-binding protein involved in active transport in Escherichia coliB D Kubena, H Luecke, H Rosenberg, et al.Biochemistry|February 20, 1996
Modulation of a salt link does not affect binding of phosphate to its specific active transport receptorN Yao, P S Ledvina, A Choudhary, et al.The Journal of Biological Chemistry|March 15, 1991
Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose. Structural and Functional SimilarityN K Vyas, M N Vyas, F A QuiochoThe Journal of Biological Chemistry|March 15, 1991
The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxisJ C Spurlino, G Y Lu, F A QuiochoBiochemistry|October 12, 1993
Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding proteinA J Sharff, L E Rodseth, F A QuiochoThe Journal of Biological Chemistry|January 21, 1994
The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding proteinZ Chang, A Choudhary, R Lathigra, et al.The Journal of Biological Chemistry|December 25, 1981
L-Arabinose-binding protein-sugar complex at 2.4 A resolution. Stereochemistry and evidence for a structural changeM E Newcomer, G L Gilliland, F A QuiochoPageof 13