James E. Strickler
Yale University
16 Papers
199 Citations
James E. Strickler is an academic researcher from Yale University. The author has contributed to research in topics: Proteolytic enzymes & Trypanosoma brucei. The author has an hindex of 10, co-authored 16 publications.
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Papers
SUMO Fusion Technology for Enhanced Protein Expression and Purification in Prokaryotes and Eukaryotes
TL;DR: Efficient removal of the SUMO tag by SUMO protease in vitro facilitates the generation of target protein with a native N-terminus and can be used as a powerful biotechnology tool for enhanced functional protein expression in prokaryotes and eukaryotes.
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Application of high-performance liquid chromatographic peptide purification to protein microsequencing by solid-phase Edman degradation.
TL;DR: Peptide purification via high-performance liquid chromatography (HPLC) and solid-phase sequencing were integrated to form a system allowing the determination of complete sequence information on a microscale without the use of radiolabels or modified phenylisothiocyanate.
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Trypanosoma brucei brucei: isolation of the major surface coat glycoprotein by lectin affinity chromatography.
TL;DR: The preparation after lectin chromatography is stable, showing no degradation after standing 72 hr at 4 C, and the purification is 16- and 17.3-fold at each step out of a theoretical 18-fold possible purification.
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Identification and partial characterization of plasma membrane polypeptides of Trypanosoma brucei.
TL;DR: A plasma membrane-enriched vesicle fraction has been prepared from Trypanosoma brucei by sonication and differential centrifugation on sucrose gradients and several high molecular weight surface glycopeptides have been selectively investigated and partially characterized by a combination of metabolic labeling with [3H]mannose, lactoperoxidase-catalyzed surface iodination, and affinity chromatography on Con A-Sepharose.
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Bioluminescence Assay Platform for Selective and Sensitive Detection of Ub/Ubl Proteases
TL;DR: Conjugation of aminoluciferin to a full-length Ub (Ub-AML) yields a substrate that has a wide dynamic range, yet displays detection limits for DUBs 100- to 1000-fold lower than observed with DUB-Glo™, providing an alternative drug discovery platform for Ub/Ubl isopeptidases.
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