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Frank J. Lebeda

Researcher at United States Department of the Army

Publications -  34
Citations -  895

Frank J. Lebeda is an academic researcher from United States Department of the Army. The author has contributed to research in topics: Clostridium botulinum & Neurotoxin. The author has an hindex of 15, co-authored 33 publications receiving 815 citations.

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IC50-to-Ki: a web-based tool for converting IC50 to Ki values for inhibitors of enzyme activity and ligand binding

TL;DR: A new web-server tool estimates Ki values from experimentally determined IC50 values for inhibitors of enzymes and of binding reactions between macromolecules and ligands to enable end users to help gauge the quality of the underlying assumptions used in these calculations.
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The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring beta-trefoil fold in the progenitor toxin complex.

TL;DR: The crystal structure of serotype A HA33 (HA33/A) at 1.5 A resolution is reported that contains a unique domain organization and a carbohydrate recognition site and suggests that most of the toxin complex consists of a reoccurring beta-trefoil fold.
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Prediction of a conserved, neutralizing epitope in ribosome-inactivating proteins

TL;DR: The secondary structures, side-chain solvent accessibilities, and superpositioned crystal structures of the A-chain of ricin and four other plant rRNA N-glycosidases (ribosome-inactivating proteins, RIPs) were examined and it is suggested that this exposed region represents a logical starting point for experiments designed to locate neutralizing epitopes in these RIPs.
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Identifying the principal protective antigenic determinants of type A botulinum neurotoxin.

TL;DR: It should be possible to develop small peptides that could be useful in the design of future vaccines against these neurotoxins, based on analyses of the X-ray crystal structure of the tetanus neurotoxin Hc fragment.
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Secondary structural predictions for the clostridial neurotoxins

TL;DR: The neural net program, PHD, predicted that the secondary structures of the neurotoxins were indeed conserved in both single and multiple sequence modes of analysis, and predicted that a conserved state (variable loops) also exists in non‐aligned regions.