D
Dieter Brömme
Researcher at University of British Columbia
Publications - 202
Citations - 15654
Dieter Brömme is an academic researcher from University of British Columbia. The author has contributed to research in topics: Cathepsin & Cathepsin K. The author has an hindex of 67, co-authored 200 publications receiving 14652 citations. Previous affiliations of Dieter Brömme include Wilmington University & National Research Council.
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Journal ArticleDOI
Lysosomal Protease Pathways to Apoptosis: CLEAVAGE OF Bid, NOT PRO-CASPASES, IS THE MOST LIKELY ROUTE *
Veronika Stoka,Veronika Stoka,Boris Turk,Sharon L. Schendel,Tae-Hyoung Kim,Tina Cirman,Scott J. Snipas,Lisa M. Ellerby,Dale E. Bredesen,Hudson H. Freeze,Magnus Abrahamson,Dieter Brömme,Stanislaw Krajewski,John C. Reed,Xiao Ming Yin,Vito Turk,Guy S. Salvesen +16 more
TL;DR: Data suggest that Bid represents a sensor that allows cells to initiate apoptosis in response to widespread adventitious proteolysis, supported by the finding that cytosolic extracts from mice ablated in the bid gene are impaired in the ability to release cytochrome c in Response to lysosome extracts.
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Essential Role for Cathepsin S in MHC Class II–Associated Invariant Chain Processing and Peptide Loading
Richard J. Riese,Paula R. Wolf,Dieter Brömme,Lisa Natkin,Jose A Villadangos,Hidde L. Ploegh,Harold A. Chapman +6 more
TL;DR: Purified cathepsin S specifically digested li from alpha beta li trimers, generating alpha beta-CLIP complexes capable of binding exogenously added peptide in vitro, and the formation of SDS-stable complexes was markedly reduced.
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Vinyl sulfones as mechanism-based cysteine protease inhibitors.
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Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design.
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Molecular cloning, expression and potential functions of the human proteinase-activated receptor-2
Stephan K. Böhm,Wuyi Kong,Dieter Brömme,Steven P. Smeekens,David C. Anderson,Andrew J. Connolly,Mark L. Kahn,Nicholas A. Nelken,Shaun R. Coughlin,Donald G. Payan,Nigel W. Bunnett +10 more
TL;DR: Its expression by cells and tissues not normally exposed to pancreatic trypsin suggests that other proteases could serve as physiological activators and PAR-2 may serve as aTrypsin sensor in the gut.