Search Results - "Machleidt, I"

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    Epoxysuccinyl peptide-derived affinity labels for cathepsin B by Schaschke, N, Assfalg-Machleidt, I, Laßleben, Th, Sommerhoff, C.P, Moroder, L, Machleidt, W

    Published in FEBS letters (29-09-2000)
    “…Extracellular cysteine proteases, in particular cathepsin B, have been implicated in a variety of pathological processes. Selectively targeting labels of this…”
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    Rapid enzymatic test for phenotypic HIV protease drug resistance by Hoffmann, Dieter, Assfalg-Machleidt, Irmgard, Nitschko, Hans, von der Helm, Klaus, Koszinowski, Ulrich, Machleidt, Werner

    Published in Biological chemistry (01-07-2003)
    “…A phenotypic resistance test based on recombinant expression of the active HIV protease in E. coli from patient blood samples was developed. The protease is…”
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    Cyclodextrins as templates for the presentation of protease inhibitors by Schaschke, N., Musiol, H.-J., Assfalg-Machleidt, I., Machleidt, W., Rudolph-Böhner, S., Moroder, L.

    Published in FEBS letters (12-08-1996)
    “…Mono(6-succinylamido-6-deoxy)-β-cyclodextrin was synthesized by classical carbohydrate chemistry and used as a template mono-functionalized with the linear,…”
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    Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions by Vogel, R, Assfalg-Machleidt, I, Esterl, A, Machleidt, W, Müller-Esterl, W

    Published in The Journal of biological chemistry (05-09-1988)
    “…Low molecular weight kininogen from human plasma was subjected to limited proteolysis with trypsin, chymotrypsin, elastase, and bromelain, and the resulting…”
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    Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors by Schaschke, Norbert, Assfalg-Machleidt, Irmgard, Machleidt, Werner, Moroder, Luis

    Published in FEBS letters (02-01-1998)
    “…Based on recent information about the anti-substrate binding mode of the propeptide portion of procathepsin B and the well established substrate-like binding…”
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    Inhibition of ATPase, GTPase and adenylate kinase activities of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator by genistein by Randak, C, Auerswald, E A, Assfalg-Machleidt, I, Reenstra, W W, Machleidt, W

    Published in Biochemical journal (15-05-1999)
    “…In the presence of ATP, genistein, like the ATP analogue adenosine 5'-[beta,gamma-imido]triphosphate (pp[NH]pA), increases cystic fibrosis transmembrane…”
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    Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: enhancing cell permeability by conjugation with penetratin by Gil-Parrado, Shirley, Assfalg-Machleidt, Irmgard, Fiorino, Ferdinando, Deluca, Dominga, Pfeiler, Dietmar, Schaschke, Norbert, Moroder, Luis, Machleidt, Werner

    Published in Biological chemistry (01-03-2003)
    “…The ubiquitous calpains, mu- and m-calpain, have been implicated in essential physiological processes and various pathologies. Cell-permeable specific…”
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    A novel type of bifunctional inhibitor directed against proteolytic activity and receptor/ligand interaction. Cystatin with a urokinase receptor binding site by Muehlenweg, B, Assfalg-Machleidt, I, Parrado, S G, Bürgle, M, Creutzburg, S, Schmitt, M, Auerswald, E A, Machleidt, W, Magdolen, V

    Published in The Journal of biological chemistry (27-10-2000)
    “…Cancer invasion and metastasis is a process requiring a coordinated series of (anti-)adhesive, migratory, and pericellular proteolytic events involving various…”
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    Enzymatically active cathepsin B dissociating from its inhibitor complexes is elevated in blood plasma of patients with septic shock and some malignant tumors by Assfalg-Machleidt, I, Jochum, M, Klaubert, W, Inthorn, D, Machleidt, W

    Published in Biological chemistry Hoppe-Seyler (01-05-1988)
    “…Using fluorogenic substrates and the specific inhibitor E-64, cysteine proteinase (CP) activity was measured in blood plasma of healthy controls (mean = 35.0…”
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    β-Cyclodextrin/epoxysuccinyl peptide conjugates : a new drug targeting system for tumor cells by SCHASCHKE, N, ASSFALG-MACHLEIDT, I, MACHLEIDT, W, LASSLEBEN, T, SOMMERHOFF, C. P, MORODER, L

    Published in Bioorganic & medicinal chemistry letters (03-04-2000)
    “…Beta-cyclodextrin is known to form inclusion complexes with hydrophobic drugs. Several tumor cell lines are known to secrete and/or contain membrane-associated…”
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    E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group by Schaschke, Norbert, Assfalg-Machleidt, Irmgard, Machleidt, Werner, Turk, Dushan, Moroder, Luis

    Published in Bioorganic & medicinal chemistry (01-09-1997)
    “…A series of trans-epoxysuccinyl-peptide derivatives based on the natural inhibitor E-64 were synthesized in the (2 R,3 R) and (2 S,3 S) configuration in order…”
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    Recombinant Q53E- and Q53N--chicken egg white cystatin variants inhibit papain, actinidin and cathepsin B by Genenger, G, Lenzen, S, Mentele, R, Assfalg-Machleidt, I, Auerswald, E A

    Published in Biomedica biochimica acta (1991)
    “…A cloned synthetic gene coding for (AEF S1M M29I M89L) chicken egg white cystatin was modified site-specifically at position Q53 by cassette mutagenesis. Two…”
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    A recombinant polypeptide model of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator functions as an active ATPase, GTPase and adenylate kinase by Randak, Christoph, Neth, Peter, Auerswald, Ennes A, Eckerskorn, Christoph, Assfalg-Machleidt, Irmgard, Machleidt, Werner

    Published in FEBS letters (30-06-1997)
    “…CFTR–NBF-2 expressed and purified in fusion with the maltose-binding protein was shown to catalyse the reaction ATP→ADP+P i by three different assays,…”
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    Proteolysis of defensive proteins in peritonitis exudate: pathobiochemical aspects and therapeutical approach by Billing, A, Fröhlich, D, Assfalg-Machleidt, I, Machleidt, W, Jochum, M

    Published in Biomedica biochimica acta (1991)
    “…Peritonitis exudate reveals strong proteolytic activity which is paralleled by deficient opsonic capacity and high concentrations of lysosomal proteinases…”
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    Novel bi- and trifunctional inhibitors of tumor-associated proteolytic systems by Krol, Janna, Sato, Sumito, Rettenberger, Peter, Assfalg-Machleidt, Irmgard, Schmitt, Manfred, Magdolen, Viktor, Magdolen, Ulla

    Published in Biological chemistry (01-07-2003)
    “…Serine proteases, cysteine proteases, and matrix metalloproteinases (MMPs) are involved in cancer cell invasion and metastasis. Recently, a recombinant…”
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