Quantifying Cathepsin S Activity in Antigen Presenting Cells Using a Novel Specific Substrate (original) (raw)
Receptor-Mediated Targeting of Cathepsins in Professional Antigen Presenting Cells
Bogdan Florea
Angewandte Chemie International Edition, 2009
View PDFchevron_right
Modulation of the Endosomal and Lysosomal Distribution of Cathepsins B, L and S in Human Monocytes/Macrophages
Ekkehard Weber, H. Kalbacher
Biological Chemistry, 2000
View PDFchevron_right
Specific role for cathepsin S in the generation of antigenic peptidesin vivo
Christoph Driessen
European Journal of Immunology, 2002
View PDFchevron_right
Human B lymphoblastoid cells contain distinct patterns of cathepsin activity in endocytic compartments and regulate MHC class II transport in a cathepsin S-independent manner
Ekkehard Weber
Journal of Leukocyte Biology, 2003
View PDFchevron_right
Emerging functional roles of cathepsin E
Nousheen Zaidi
Biochemical and Biophysical Research Communications, 2008
View PDFchevron_right
Proteolytic Activation of Human Cathepsin A
Nilima Kolli
Journal of Biological Chemistry, 2014
View PDFchevron_right
A new approach for distinguishing cathepsin E and D activity in antigen-processing organelles
Nousheen Zaidi
FEBS Journal, 2007
View PDFchevron_right
Cathepsin E: A mini review
Nousheen Zaidi
Biochemical and Biophysical Research Communications, 2008
View PDFchevron_right
Cathepsin S activity regulates antigen presentation and immunity
Richard Mitchell
Journal of Clinical Investigation, 1998
View PDFchevron_right
An activity-based probe for the determination of cysteine cathepsin protease activities in whole cells
Shankar Venkatraman
Analytical Biochemistry, 2004
View PDFchevron_right
Endocytosis targets exogenous material selectively to cathepsin S in live human dendritic cells, and cell- penetrating peptides mediate nonselective transport to cysteine cathepsins
Marianne Kraus
J Leukocyte Biol, 2007
View PDFchevron_right
Erratum to “An activity-based probe for the determination of cysteine cathepsin protease activities in whole cells
Shankar Venkatraman
Analytical Biochemistry, 2005
View PDFchevron_right
Endocytosis targets exogenous material selectively to cathepsin S in live human dendritic cells, while cell-penetrating peptides mediate nonselective transport to cysteine cathepsins
Ekkehard Weber
Journal of Leukocyte Biology, 2007
View PDFchevron_right
Recombinant cathepsin S propeptide attenuates cell invasion by inhibition of cathepsin L–like proteases in tumor microenvironment
Richard Buick
Molecular Cancer Therapeutics, 2008
View PDFchevron_right
Cysteine cathepsins: From structure, function and regulation to new frontiers
Boris Turk
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2012
View PDFchevron_right
Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
Paula Wolf
1996
View PDFchevron_right
Rat procathepsin B. Proteolytic processing to the mature form in vitro
John Mort
The Journal of Biological Chemistry, 1992
View PDFchevron_right
Activity and subcellular distribution of cathepsins in primary human monocytes
Ekkehard Weber
Journal of Leukocyte Biology, 2003
View PDFchevron_right
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
Luiz Juliano
European Journal of Biochemistry, 2000
View PDFchevron_right
Potency and Selectivity of the Cathepsin L Propeptide as an Inhibitor of Cysteine Proteases †
John Mort
Biochemistry, 1996
View PDFchevron_right
The Ins and Outs of Cathepsins: Physiological Function and Role in Disease Management
Ronit Shiri-sverdlov
Cells
View PDFchevron_right
Autocatalytic processing of procathepsin B is triggered by proenzyme activity
vito turk
2009
View PDFchevron_right
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase: Human cathepsin X
Igor Križaj
European Journal of Biochemistry, 2003
View PDFchevron_right
Cathepsins X and B Can Be Differentiated Through Their Respective Mono-and Dipeptidyl Carboxypeptidase Activities
E. Ziomek
Biochemistry, 2001
View PDFchevron_right