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(NAS Colloquium) Proteolytic Processing and Physiological Regulation (1999)
National Academy of Sciences (NAS)

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Colloqium on Proteolytic Processing and Physiological Regulation

NATIONAL ACADEMY OF SCIENCES

Colloquium Series

In 1991, the National Academy of Sciences inaugurated a series of scientific colloquia, five or six of which are scheduled each year under the guidance of the NAS Council’s Committee on Scientific Programs. Each colloquium addresses a scientific topic of broad and topical interest, cutting across two or more of the traditional disciplines. Typically two days long, colloquia are international in scope and bring together leading scientists in the field. Papers from colloquia are published in the Proceedings of the National Academy of Sciences (PNAS).

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Front Matter (R1-R7)
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)