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Author Details

Ingeborg Feil
Howard Hughes Medical Institute, University of Washington
1994
15
12
Andrej Sali (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
16021622Structural analysis of a set of proteins resulting from a bacterial genomics project.Proteins2005
16211523New York-Structural GenomiX Research Consortium (NYSGXRC): a large scale center for the protein structure initiative.J Struct Funct Genomics2005
15507431A novel mode of Gleevec binding is revealed by the structure of spleen tyrosine kinase.J Biol Chem2004
11278766A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity.J Biol Chem2001
9767427Role of GM1 binding in the mucosal immunogenicity and adjuvant activity of the Escherichia coli heat-labile enterotoxin and its B subunit.Immunology1998
9876933Stepwise transplantation of an active site loop between heat-labile enterotoxins LT-II and LT-I and characterization of the obtained hybrid toxins.Protein Eng1998
9565364Mutational analysis of the role of ADP-ribosylation activity and GM1-binding activity in the adjuvant properties of the Escherichia coli heat-labile enterotoxin towards intranasally administered keyhole limpet hemocyanin.Eur J Immunol1998
9384564Structural foundation for the design of receptor antagonists targeting Escherichia coli heat-labile enterotoxin.Structure1997
9153075Modified substrate specificity of L-hydroxyisocaproate dehydrogenase derived from structure-based protein engineering.Protein Eng1997
9416616Crystal structure of heat-labile enterotoxin from Escherichia coli with increased thermostability introduced by an engineered disulfide bond in the A subunit.Protein Sci1997
8793878Protein engineering studies of A-chain loop 47-56 of Escherichia coli heat-labile enterotoxin point to a prominent role of this loop for cytotoxicity.Mol Microbiol1996
8945598Mutants of the Escherichia coli heat-labile enterotoxin with reduced ADP-ribosylation activity or no activity retain the immunogenic properties of the native holotoxin.Infect Immun1996
7578111Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Leishmania mexicana: implications for structure-based drug design and a new position for the inorganic phosphate binding site.Biochemistry1995
7849584Protein crystallography and infectious diseases.Protein Sci1994
8055963Deletion variants of L-hydroxyisocaproate dehydrogenase. Probing substrate specificity.Eur J Biochem1994
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Lilly Research Laboratories
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Argonne National Laboratory
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