S
Subramanyam Swaminathan
Researcher at Brookhaven National Laboratory
Publications - 99
Citations - 3771
Subramanyam Swaminathan is an academic researcher from Brookhaven National Laboratory. The author has contributed to research in topics: Clostridium botulinum & Active site. The author has an hindex of 31, co-authored 99 publications receiving 3561 citations. Previous affiliations of Subramanyam Swaminathan include Stony Brook University.
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Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B.
TL;DR: The structures of BoNT/B and its complex with sialyllactose provide a detailed description of the active site and a model for interactions between the toxin and its cell surface receptor, and the latter may provide valuable information for recombinant vaccine development.
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Structural genomics: beyond the human genome project.
Stephen K. Burley,Stephen K. Burley,Steven C. Almo,Jeffrey B. Bonanno,Jeffrey B. Bonanno,Malcolm Capel,Mark R. Chance,Terry Gaasterland,Dawei Lin,Andrej Sali,F. William Studier,Subramanyam Swaminathan +11 more
TL;DR: A program of high-throughput X-ray crystallography aimed at developing a comprehensive mechanistic understanding of normal and abnormal human and microbial physiology at the molecular level is about to embark on.
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Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution.
TL;DR: The crystal structure of brewers' yeast pyruvate decarboxylase, a thiamin diphosphate dependent alpha-keto acid decarboxesyase, has been determined to 2.4-A resolution and Amino acids important in cofactor binding and likely to participate in catalysis and substrate activation are identified.
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Mechanism of action of a flavin-containing monooxygenase
TL;DR: It is proposed that FMOs exist in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, readying them to act on substrates to eliminate nonnutritional and insoluble compounds.
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Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation.
Desigan Kumaran,Subramaniam Eswaramoorthy,William Furey,Jorge Navaza,M. Sax,Subramanyam Swaminathan +5 more
TL;DR: It is suggested that the translocation domain in other BoNTs follows a two-step process to attain translocation-competent conformation as in BoNT E, and this is a probable reason for its faster toxic rate compared to BoNT A.