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

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Format:
Book
Conference/Event
Author/Creator:
Proceedings of the National Academy of Sciences, Corporate Author.
Contributor:
National Academy of Sciences (U.S.)
Neurath, Hans, 1909-2002.
Craik, Charles S.
Conference Name:
Colloquium on Proteolytic Processing and Physiological Regulation (1999 : Irvine, Calif.)
Series:
National Academy of Sciences colloquium series.
National Academy of Sciences colloquium series
Language:
English
Subjects (All):
Proteolytic enzymes.
Cell physiology.
Physical Description:
1 online resource (107 p.)
Edition:
1st ed.
Place of Publication:
Washington, D.C. : National Academy of Sciences, 1999.
Language Note:
English
Contents:
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 precursors
Conversion 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 Patched
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 Serotypes
Kinetic stability as a mechanism for protease longevity
Cysteine protease inhibitors as chemotherapy: Lessons from a parasite target
METHODS
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
SREBP Cleavage-Activating Protein (SCAP)
SCAP as a Sterol Sensor
Candidate Gene for Site-2 Protease
Candidate Gene for Site-1 Protease
Unresolved Questions
Cellular mechanisms of β-amyloid production and secretion
Reverse biochemistry: Use of macromolecular protease inhibitors to dissect complex biological processes and identify a…
Notes:
"Reprinted from the Proceedings of the National Academy of Sciences of the United States of America, volume 96, pp. 10962-11061, September 28, 1999, and includes articles based on the National Academy of Sciences' Colloquium on Proteolytic Processing and Physiological Regulation, held at the Arnold and Mabel Beckman Center in Irvine, California, February 20-21, 1999"--P. [2] of cover.
Includes bibliographical references.
ISBN:
1-280-20990-9
9786610209903
0-309-56942-7
OCLC:
70774062

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