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Highlight: 3rd General IPS Meeting/International Conference on Protease inhibitors
Published/Copyright:
June 1, 2005
Published Online: 2005-06-01
Published in Print: 2004-06-07
Copyright © 2004 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Highlight: 3rd General IPS Meeting/International Conference on Protease inhibitors
- Colon cancer: genomics and apoptotic events
- Interaction of calpastatin with calpain: a review
- Cathepsin L and Arg/Lys aminopeptidase: a distinct prohormone processing pathway for the biosynthesis of peptide neurotransmitters and hormones
- Searching for the most effective screening system to identify cell-active inhibitors of β-secretase
- Accumulation of mini-plasmin in the cerebral capillaries causes vascular invasion of the murine brain by a pneumotropic influenza A virus: implications for influenza-associated encephalopathy
- Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors
- Human cathepsin F: expression in baculovirus system, characterization and inhibition by protein inhibitors
- Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages
- Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation
- Growth phase-dependent production of a cell wall-associated elastinolytic cysteine proteinase by Staphylococcus epidermidis
- Evidence for an interaction between leptin, T cell costimulatory antigens CD28, CTLA-4 and CD26 (dipeptidyl peptidase IV) in BCG-induced immune responses of leptin- and leptin receptor-deficient mice
- Characterisation of a highly specific, endogenous inhibitor of cysteine protease from Staphylococcus epidermidis, a new member of the staphostatin family
- Identification of cysteine protease inhibitors that belong to cystatin family 1 in the cellular slime mold Dictyostelium discoideum
- High molecular weight kininogen as substrate for cathepsin B
- 'Dipeptidyl peptidase-IV activity and/or structure homologs' (DASH) in growth-modulated glioma cell lines
- The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A
- Metalloproteases with EGF, CUB, and thrombospondin-1 domains function in molting of Caenorhabditis elegans