S. Ahmed

发表

Medical Applications of Clostridia and Clostridial Toxins

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

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.

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.

Mechanism of Activation of the Tryptophan Synthase α2β2 Complex

E. W. Miles, S. Ahmed, P. McPhie, 1996, 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.

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.

Crystallographic and kinetic studies of the tryptophan synthase α2β2 complex with a mutation in β subunit lysine-87 that binds pyridoxal phosphate

D. Davies, K. Parris, U. Banik, 1994 .

Exploring the Tryptophan Synthase α2β2 Multienzyme Complex by X-Ray Crystallography and Site-Directed Mutagensis

A. M. Kayastha, E. W. Miles, S. Ahmed, 1991 .

Iron oxides mapping from E0-1 hyperion data

P. K. Gupta, S. Ahmed, S. Kiran Raj, 2015, Journal of the Geological Society of India.

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.

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.

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.

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.

Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids.

C. Matthews, T. Stackhouse, E. W. Miles, 1988, Biochemistry.

Tyrosine Phosphorylation of Botulinum Neurotoxin Protease Domains

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

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.

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.

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

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

Evidence for a vesicle-mediated maintenance of store-operated calcium channels in a human embryonic kidney cell line.

R. Steinhardt, J. Alderton, L. Smith, 2000, Cell calcium.

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

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

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.

Enzymatic Autocatalysis of Botulinum A Neurotoxin Light Chain

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

Subunit assembly in the tryptophan synthase alpha 2 beta 2 complex. Stabilization by pyridoxal phosphate aldimine intermediates.

U. Banik, E. W. Miles, S. Ahmed, 1995, The Journal of biological chemistry.

Mechanism of alpha-amino-epsilon-caprolactam racemase reaction.

H. Tanaka, K. Soda, N. Esaki, 1986, 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.

Expression, purification, and efficacy of the type A botulinum neurotoxin catalytic domain fused to two translocation domain variants.

L. Smith, T. Smith, S. Ahmed, 2003, Toxicon : official journal of the International Society on Toxinology.

Inhibition of catalytic activities of botulinum neurotoxin light chains of serotypes A, B and E by acetate, sulfate and calcium.

S. Swaminathan, R. Mizanur, S. Ahmed, 2012, International journal of biochemistry and molecular biology.

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.

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.