M
Matthew P. DeLisa
Researcher at Cornell University
Publications - 203
Citations - 9530
Matthew P. DeLisa is an academic researcher from Cornell University. The author has contributed to research in topics: Glycosylation & Protein folding. The author has an hindex of 47, co-authored 188 publications receiving 8433 citations. Previous affiliations of Matthew P. DeLisa include University of Texas at Austin & University of California, Berkeley.
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Book
Bioprocess Engineering: Basic Concepts
TL;DR: The author explains how the biotechnology and bioprocess engineering profession has changed in the modern era, and some examples of this change can be found in the chapters on Bioreactors for Suspension and Immobilized Cultures.
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Engineering the spatial organization of metabolic enzymes: mimicking nature's synergy.
TL;DR: Several of nature's most notable multifunctional enzyme systems including the AROM complex and tryptophan synthase are discussed, each of which provides new fundamental insights into the structural organization of metabolic machinery within living cells.
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Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway.
TL;DR: It is demonstrated that in vivo only proteins that have attained the native conformation are exported by the Tat translocator, indicating that a folding quality-control mechanism is intrinsic to the export process.
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DNA Microarray-Based Identification of Genes Controlled by Autoinducer 2-Stimulated Quorum Sensing in Escherichia coli
TL;DR: This work investigated global changes in mRNA abundance elicited by the AI-2 signaling molecule through the use of a luxS mutant that was unable to synthesizeAI-2, and significant induction of ygeV, a putative sigma(54)-dependent transcriptional activator, and yhbH, a s Sigma(54) modulating protein, suggests sigma (54) may be involved in E. coli quorum sensing.
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Delivery of foreign antigens by engineered outer membrane vesicle vaccines
David J. Chen,Nikolaus Osterrieder,Nikolaus Osterrieder,Stephan M. Metzger,Elizabeth L. Buckles,Anne M. Doody,Matthew P. DeLisa,David Putnam +7 more
TL;DR: It is shown here that engineered Escherichia coli outer membrane vesicles (OMVs) are an easily purified vaccine-delivery system capable of greatly enhancing the immunogenicity of a low-immunogenicity protein antigen without added adjuvants.