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Journal of Immunology (Baltimore, Md. : 1950)|April 1, 1981
Inhibition of human natural cytotoxicity by macromolecular antiproteasesD Hudig, T Haverty, C Fulcher, et al.
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|June 3, 1999
Calreticulin, a component of the endoplasmic reticulum and of cytotoxic lymphocyte granules, regulates perforin-mediated lysis in the hemolytic model systemS A Fraser, M Michalak, W H Welch, et al.
Biochemical and Biophysical Research Communications|December 31, 1987
Lymphocyte granule-mediated cytolysis requires serine protease activityD Hudig, N J Gregg, C M Kam, et al.
International Immunopharmacology|May 23, 2001
Dipeptide vinyl sulfones suitable for intracellular inhibition of dipeptidyl peptidase IG E Korver, C M Kam, J C Powers, et al.
Molecular Immunology|August 1, 1989
Selective isocoumarin serine protease inhibitors block RNK-16 lymphocyte granule-mediated cytolysisD Hudig, N J Allison, C M Kam, et al.
Bioconjugate Chemistry|September 1, 1994
Fluorescent derivatives of diphenyl [1-(N-peptidylamino)alkyl]phosphonate esters: synthesis and use in the inhibition and cellular localization of serine proteasesA S Abuelyaman, D Hudig, S L Woodard, et al.
Nature Structural Biology|June 1, 1994
Conversion of the substrate specificity of mouse proteinase granzyme BA Caputo, M N James, J C Powers, et al.
The Journal of Biological Chemistry|August 25, 1993
Activation of recombinant murine cytotoxic cell proteinase-1 requires deletion of an amino-terminal dipeptideA Caputo, R S Garner, U Winkler, et al.
Protein Expression and Purification|October 1, 1993
Rapid purification of cationic granule proteases: application to human granzymesW L Hanna, X Zhang, J Turbov, et al.
Biochimica Et Biophysica Acta|December 15, 1988
Localization, implications for function, and gene expression of chymotrypsin-like proteinases of cytotoxic RNK-16 lymphocytesS J Zunino, N J Allison, C M Kam, et al.
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