S. Ahmed

发表

Autocatalytically fragmented light chain of botulinum a neurotoxin is enzymatically active.

Leonard A. Smith, P. McPhie, S. Ahmed, 2003, Biochemistry.

Structure-based design of peptide inhibitors of botulinum neurotoxin serotype A proteolytic activity

Leonard A. Smith, S. Ahmed, M. L. Ludivico, 2009 .

Composition and stability constants of iron- and copper-oxytetracycline chelates

S. Hassan, S. Ahmed, M. Amer, 1984 .

Medical Applications of Clostridia and Clostridial Toxins

G. Oyler, F. Lebeda, T. Kuboki, 2012, Journal of toxicology.

Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the beta 2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimurium.

K. Kirschner, E. W. Miles, S A Ahmed, 1986, Biochemistry.

Cleavage of SNAP25 and Its Shorter Versions by the Protease Domain of Serotype A Botulinum Neurotoxin

R. Mizanur, R. Stafford, S. Ahmed, 2014, PloS one.

Microspectrophotometric studies on single crystals of the tryptophan synthase alpha 2 beta 2 complex demonstrate formation of enzyme-substrate intermediates.

A. Mozzarelli, A. Peracchi, G. Rossi, 1989, The Journal of biological chemistry.

Mutation of an Active Site Residue of Tryptophan Synthase (β-Serine 377) Alters Cofactor Chemistry*

K. Jhee, E. W. Miles, P. McPhie, 1998, The Journal of Biological Chemistry.

The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.

H. Morita, E. W. Miles, S. Nagata, 1989, The Journal of biological chemistry.

Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits.

G. Zon, R. Bauerle, E. W. Miles, 1987, The Journal of biological chemistry.

Aliphatic alcohols stabilize an alternative conformation of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium.

E. W. Miles, S. Ahmed, 1994, The Journal of biological chemistry.

Identification of Residues Surrounding the Active Site of Type A Botulinum Neurotoxin Important for Substrate Recognition and Catalytic Activity

Leonard A. Smith, M. A. Olson, J. Gilsdorf, 2008, The protein journal.

Dissociation equilibria of the tryptophan synthase α2β2 complex in saline buffer and guanidine isothiocyanate, as studied by sedimentation equilibrium

D. Millar, A. Minton, E. W. Miles, 1997 .

Importance of Conserved and Variable C-terminal Residues for the Activity and Thermal Stability of the β Subunit of Tryptophan Synthase*

E. W. Miles, S. Rhee, S. Ahmed, 1997, The Journal of Biological Chemistry.

Mechanism of Activation of the Tryptophan Synthase α2β2 Complex

E. W. Miles, S. Ahmed, P. McPhie, 1996, The Journal of Biological Chemistry.

Monovalent Cations Partially Repair a Conformational Defect in a Mutant Tryptophan Synthase Complex (-E109A) (*)

S. Ruvinov, E. W. Miles, S. Ahmed, 1995, The Journal of Biological Chemistry.

Subunit Assembly in the Tryptophan Synthase α2β2 Complex

U. Banik, E. W. Miles, S. Ahmed, 1995, The Journal of Biological Chemistry.

Ligand-mediated Changes in the Tryptophan Synthase Indole Tunnel Probed by Nile Red Fluorescence with Wild Type, Mutant, and Chemically Modified Enzymes (*)

K. Parris, D. Sackett, Xiang-Jiao Yang, 1995, The Journal of Biological Chemistry.

The C Terminus of the Catalytic Domain of Type A Botulinum Neurotoxin May Facilitate Product Release from the Active Site*

Leonard A. Smith, S. Swaminathan, S. Bavari, 2013, The Journal of Biological Chemistry.

Tyrosine Phosphorylation of Botulinum Neurotoxin Protease Domains

Leonard A. Smith, G. Oyler, H. Hines, 2012, Front. Pharmacol..

Structure- and Substrate-based Inhibitor Design for Clostridium botulinum Neurotoxin Serotype A*

S. Swaminathan, D. Kumaran, M. L. Ludivico, 2008, Journal of Biological Chemistry.

Enzymatic Autocatalysis of Botulinum A Neurotoxin Light Chain

Leonard A. Smith, H. Hines, L. Smith, 2001, Journal of protein chemistry.

Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.

D. Davies, K. Parris, E. W. Miles, 1997, Biochemistry.

Development of a Coxiella burnetii culture method for high-throughput assay to identify host-directed therapeutics.

Cheryl N. Miller, R. Panchal, M. Hale, 2019, Journal of microbiological methods.

Extreme sensitivity of botulinum neurotoxin domains towards mild agitation.

Leonard A. Smith, S. Toth, S. Ahmed, 2009, Journal of pharmaceutical sciences.

Light Chain of Botulinum A Neurotoxin Expressed as an Inclusion Body from a Synthetic Gene Is Catalytically and Functionally Active

Leonard A. Smith, S. Ahmed, Ashraf Ahmed, 2000, Journal of protein chemistry.

A Thermally Induced Reversible Conformational Transition of the Tryptophan Synthase Subunit Probed by the Spectroscopic Properties of Pyridoxal Phosphate and by Enzymatic Activity (*)

E. W. Miles, S. Ahmed, P. McPhie, 1996, The Journal of Biological Chemistry.

Inhibition of the protease activity of the light chain of type A botulinum neurotoxin by aqueous extract from stinging nettle (Urtica dioica) leaf.

Leonard A. Smith, S. Ahmed, N. Gul, 2004, Basic & clinical pharmacology & toxicology.

Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

E. Padlan, D. Davies, E. W. Miles, 1988, The Journal of biological chemistry.

Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.

D. Davies, K. Parris, E. W. Miles, 1996, Biochemistry.

Basic Tetrapeptides as Potent Intracellular Inhibitors of Type A Botulinum Neurotoxin Protease Activity*

S. Swaminathan, G. Oyler, M. Hale, 2010, The Journal of Biological Chemistry.

Rapid product analysis and increased sensitivity for quantitative determinations of botulinum neurotoxin proteolytic activity.

Leonard A. Smith, S. Ahmed, James J. Schmidt, 2010, Analytical biochemistry.

Ex vivo inhibition of Clostridium botulinum neurotoxin types B, C, E, and F by small molecular weight inhibitors.

Leonard A. Smith, M. A. Olson, R. Mizanur, 2015, Toxicon : official journal of the International Society on Toxinology.

Microcrystals of tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium are catalytically active.

G. Thomas, E. W. Miles, S. Ahmed, 1987, Biochemistry.

Crystallization and preliminary X-ray crystallographic data of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium.

D. Davies, E. W. Miles, S. Ahmed, 1985, Journal of Biological Chemistry.

Light Chain Separated from the Rest of the Type A Botulinum Neurotoxin Molecule Is the Most Catalytically Active Form

Leonard A. Smith, S. Ahmed, N. Gul, 2010, PloS one.

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B.

Leonard A. Smith, S. Swaminathan, S. Jayaraman, 2005, Biochemical and biophysical research communications.

A Direct Spectropolarimetric Assay of Arabinose 5-phosphate Isomerase.

J. Bozue, R. Woodard, R. Panchal, 2021, Analytical biochemistry.

Mutations in the contact region between the alpha and beta subunits of tryptophan synthase alter subunit interaction and intersubunit communication.

K. Jhee, E. W. Miles, R. Rowlett, 1998, Biochemistry.

PCR mutagenesis and overexpression of tryptophan synthase from Salmonella typhimurium: on the roles of beta2 subunit Lys-382.

E. W. Miles, S. Ahmed, L. H. Yang, 1996, Protein expression and purification.

Peptide inhibitors of botulinum neurotoxin serotype A: design, inhibition, cocrystal structures, structure-activity relationship and pharmacophore modeling.

S. Swaminathan, D. Kumaran, G. Kumar, 2012, Acta crystallographica. Section D, Biological crystallography.

Substrate Binding Mode and Its Implication on Drug Design for Botulinum Neurotoxin A

Richa Rawat, S. Swaminathan, D. Kumaran, 2008, PLoS pathogens.

Beta-elimination of indole from L-tryptophan catalyzed by bacterial tryptophan synthase: a comparison between reactions catalyzed by tryptophanase and tryptophan synthase.

E. W. Miles, B. Martin, S. Ahmed, 1986, Biochemistry.

Tryptophan synthase from Escherichia coli and Salmonella typhimurium.

R. Bauerle, E. W. Miles, S. Ahmed, 1987, Methods in enzymology.