Colloquium on Proteolytic Processing and Physiological Regulation /

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Autores Corporativos: National Academy of Sciences Colloquium "Proteolytic Processing and Physiological Regulation" Irvine, Calif., National Academy of Sciences (U.S.)
Otros Autores: Neurath, Hans, 1910-, Craik, Charles S.
Formato: Electrónico Congresos, conferencias eBook
Idioma:Inglés
Publicado: Washington, D.C. : National Academy of Sciences, 1999.
Colección:Proceedings of the National Academy of Sciences of the United States of America ; v. 96, no. 20.
Temas:
Proteolytic enzymes > Congresses.
Enzymes protéolytiques > Congrès.
SCIENCE > Life Sciences > Biochemistry.
Proteolytic enzymes.
Conference papers and proceedings.
Acceso en línea:Texto completo
Tabla de Contenidos:
  • 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 20â€?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 antiviralâ€?
  • 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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