Colloquium on Proteolytic Processing and Physiological Regulation / [edited by Hans Neurath and Charles S. Craik].

Includes bibliographical references.

Print version record.

COLLOQUIUM ON PROTEOLYTIC PROCESSING AND PHYSIOLOGICAL REGULATION -- NATIONAL ACADEMY OF SCIENCES -- Proteolytic Processing and Physiological Regulation -- A COLLOQUIUM SPONSORED BY THE NATIONAL ACADEMY OF SCIENCES -- FEBRUARY 20�21, 1999 -- Saturday, February 20, 1999 -- Sunday, February 21, 1999 -- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA -- Contents -- National Academy of Sciences Colloquia -- BOUND REPRINTS AVAILABLE -- Proteolytic enzymes, past and future -- Caspase activation: The induced-proximity model

Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursorsConversion of Gastric Aspartic Protease Zymogens -- Conversion of Proplasmepsin II -- Autocatalytic Excision of Picornaviral 3C Proteases -- The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study -- MATERIALS AND METHODS -- RESULTS AND DISCUSSION -- The structure of the human βII-tryptase tetramer: Fo(u)r better or worse -- CONCLUSION

Sonic hedgehog protein signals not as a hydrolytic enzyme but as an apparent ligand for PatchedMATERIALS AND METHODS -- RESULTS -- DISCUSSION -- Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral� -- Picornaviral 3C Proteases -- Inhibitors of 3C Protease and the Issue of Serotypic Diversity Among Rhinoviruses -- Irreversible Michael Acceptors as Inhibitors of 3C Protease -- Michael-Acceptor Inhibitors of 3C Protease: Structure-Activity Studies

AG7088, a 3C Protease Inhibitor with Potent Antiviral Activity Against Multiple Human Rhinovirus SerotypesKinetic stability as a mechanism for protease longevity -- Cysteine protease inhibitors as chemotherapy: Lessons from a parasite target -- METHODS -- RESULTS -- DISCUSSION -- How the protease thrombin talks to cells -- How Does a Protease Talk to a Cell? -- Irreversible Activation, Disposable Receptors, and Intracellular Reserves -- A Protease-Activated Receptor Family -- PARs and Platelet Activation

A Role for Thrombin Signaling in Embryonic Development and Other Processes?Summary -- VanX, a bacterial D-alanyl-D-alanine dipeptidase: Resistance, immunity, or survival function? -- Chaperone rings in protein folding and degradation -- Architecture-Function Considerations -- Substrate Protein Recognition -- Action of ATP -- Commitment of Substrate -- Prospects for Further Mechanistic Understanding -- A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood -- Two-Step Proteolytic Release of SREBPs

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