J
Jack D. Sadowsky
Researcher at University of Wisconsin-Madison
Publications - 17
Citations - 1245
Jack D. Sadowsky is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Protein structure & Peptide. The author has an hindex of 12, co-authored 16 publications receiving 1139 citations. Previous affiliations of Jack D. Sadowsky include University of California, San Francisco & California Institute of Technology.
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Journal ArticleDOI
Ring-closing metathesis of olefinic peptides: design, synthesis, and structural characterization of macrocyclic helical peptides.
Helen E. Blackwell,Jack D. Sadowsky,Rebecca J. Howard,Joshua N. Sampson,Jeffery A. Chao,Wayne E. Steinmetz,Daniel J. O'Leary,Robert H. Grubbs +7 more
TL;DR: The relative ease of introducing carbon-carbon bonds into peptide secondary structures by RCM and the predicted metabolic stability of these bonds renders olefin metathesis an exceptional methodology for the synthesis of rigidified peptide architectures.
Journal ArticleDOI
(alpha/beta+alpha)-Peptide antagonists of BH3 Domain/Bcl-x(L) recognition: Toward general strategies for foldamer-based inhibition of protein-protein interactions
Jack D. Sadowsky,W. Douglas Fairlie,Erik B. Hadley,Hee Seung Lee,Naoki Umezawa,Zaneta Nikolovska-Coleska,Shaomeng Wang,David C.S. Huang,York Tomita,Samuel H. Gellman +9 more
TL;DR: The identification and analysis of helical peptide-based foldamers that bind to a specific cleft on the anti-apoptotic protein Bcl-xL by mimicking an alpha-helical BH3 domain are described and it is shown that the most potent (alpha/beta + alpha)-peptide can induce cytochrome C release from mitochondria, an early step in apoptosis, in cell lysates.
Journal ArticleDOI
Chimeric (α/β + α)-Peptide Ligands for the BH3-Recognition Cleft of Bcl-xL: Critical Role of the Molecular Scaffold in Protein Surface Recognition
Jack D. Sadowsky,Margaret A. Schmitt,Hee-Seung Lee,Naoki Umezawa,Shaomeng Wang,York Tomita,Samuel H. Gellman +6 more
TL;DR: The results suggest that combining different types of foldamer backbones will be an effective and general strategy for creating high-affinity and specific ligands for protein surface sites.
Journal ArticleDOI
High-Resolution Structural Characterization of a Helical α/β-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-xL
Erinna F. Lee,Jack D. Sadowsky,Brian J. Smith,Peter E. Czabotar,Kimberly J. Peterson-Kaufman,Peter M. Colman,Samuel H. Gellman,W. Douglas Fairlie +7 more
TL;DR: The first high-resolution structure of a foldamer bound to a protein target is described and additional contacts in the foldamer/Bcl-x(L) complex involving beta-amino acid residues appear to contribute to binding affinity.
Journal ArticleDOI
Turning a protein kinase on or off from a single allosteric site via disulfide trapping
Jack D. Sadowsky,Mark A. Burlingame,Dennis W. Wolan,Christopher L. McClendon,Matthew P. Jacobson,James A. Wells +5 more
TL;DR: These studies show that disulfide trapping is useful for characterizing allosteric sites on kinases and that a singleAllosteric site on a protein kinase can be exploited for both activation and inhibition by small molecules.