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Front Matter i-vii
Proteolytic enzymes, past and future 10962-10963
Caspase activation: The induced-proximity model 10964-10967
Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursors 10968-10975
The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study 10976-10983
The structure of the human ßII-tryptase tetramer: Fo(u)r better or worse 10984-10991
Sonic hedgehog protein signals not as a hydrolic enzyme but as an apparent ligand for Patched 10992-10999
Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes 11000-11007
Kinetic stability as a mechanism for protease longevity 11008-11014
Cysteine protease inhibitors as chemotherapy: Lessons from a parasite target 11015-11022
How the protease thrombin talks to cells 11023-11027
VanX, a bacterial D-alanyl-D-alanine dipeptidase: Resistance, immunity, or survival function? 11028-11032
Chaperone rings in protein folding and degradation 11033-11040
A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood 11041-11048
Cellular mechanisms of ß-amyloid production and secretion 11049-11053
Reverse biochemistry: Use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue 11054-11061

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(NAS Colloquium) Proteolytic Processing and Physiological Regulation (1999)

Chapter: How the protease thrombin talks to cells

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(NAS Colloquium) Proteolytic Processing and Physiological Regulation (1999)

Chapter: How the protease thrombin talks to cells