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Licensed Unlicensed Requires Authentication Published by De Gruyter November 24, 2009

Binding of 92 kDa and 72 kDa Progelatinases to Insoluble Elastin Modulates Their Proteolytic Activation

  • Hervé Emonard and William Hornebeck
From the journal Biological Chemistry
https://doi.org/10.1515/bchm.1997.378.3-4.265
Published Online: 2009-11-24
Published in Print: 1997

Walter de Gruyter

From the journal
Biological Chemistry
Biological Chemistry
Volume 378 Issue 3-4
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Titelei
Sonstiges
Editorial
Review
Minireview
Review
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Titration and Mapping of the Active Site of Cysteine Proteinases from Porphyromonas gingivalis (Gingipains) Using Peptidyl Chloromethanes
Inhibition of the Interaction of Urokinase-Type Plasminogen Activator (uPA) with Its Receptor (uPAR) by Synthetic Peptides
Structural Investigation of Proteasome Inhibition
Short Communication
Molecular Basis of Proteolytic Activation of Sendai Virus Infection and the Defensive Compounds for Infection
Binding of 92 kDa and 72 kDa Progelatinases to Insoluble Elastin Modulates Their Proteolytic Activation
Purification and Primary Structure Determination of a Bowman-Birk Trypsin Inhibitor from Torresea cearensis Seeds
Horseshoe Grab Coagulogen Is an Invertebrate Protein with a Nerve Growth Factor-Like Domain
cDNA Cloning, Tissue Distribution, and Subcellular Localization of Horseshoe Crab Big Defensin
Isolation, Cloning, Sequence Analysis and X-Ray Structure of Dimethyl Sulfoxide/Trimethylamine N-Oxide Reductase from Rhodobactercapsulatus
Short Communication
Implications for the Catalytic Mechanism of the Vanadium-Containing Enzyme Chloroperoxidase from the Fungus Curvularia inaequalis by X-Ray Structures of the Native and Peroxide Form
Short Communication
Interaction of Salmonella Phage P22 with Its O-Antigen Receptor Studied by X-Ray Crystallography
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