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SopE and SopE2 from Salmonella typhimurium Activate Different Sets of RhoGTPases of the Host Cell*
- A. Friebel, H. Ilchmann, M. Aepfelbacher, K. Ehrbar, W. Machleidt, W. Hardt
- BiologyThe Journal of Biological Chemistry
- 7 September 2001
It is concluded that the translocated effector proteins SopE and SopE2 allow S. typhimurium to specifically activate different sets of RhoGTPase signaling cascades.
Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin.
Ionomycin-activated Calpain Triggers Apoptosis
- S. Gil-Parrado, A. Fernández-Montalván, W. Machleidt
- Biology, ChemistryThe Journal of Biological Chemistry
- 26 July 2002
It is concluded that ionomycin-induced calpain activation promotes decrease of Bcl-2 proteins thereby triggering the intrinsic apoptotic pathway.
Inhibition of ATPase, GTPase and adenylate kinase activities of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator by genistein.
- C. Randak, E. Auerswald, I. Assfalg-Machleidt, W. Reenstra, W. Machleidt
- BiologyThe Biochemical journal
These observations provide the first direct biochemical evidence that genistein interacts with CFTR, thus inhibiting NBF-2 activity, and suggest a similar mechanism forgenistein-dependent stimulation of CFTR chloride currents.
Isolation and Characterization of Two Forms of an Acidic Bromelain Stem Proteinase
- T. Harrach, K. Eckert, H. Maurer, I. Machleidt, W. Machleidt, R. Nuck
- Chemistry, MedicineJournal of protein chemistry
- 19 February 1998
Two forms of an acidic bromelain proteinase isolated from crude bromELain, an extract from pineapple stem, were found by a two-step FPLC purification procedure and can be considered as two forms of a single enzyme.
Amino-acid sequence of a coelenterate toxin: toxin II from Anemonia sulcata.
- G. Wunderer, H. Fritz, E. Wachter, W. Machleidt
- Biology, ChemistryEuropean journal of biochemistry
- 1 September 1976
Toxin II from Anemonia sulcata, the main component of the sea anemone venom, consists of 47 amino acid residues which are interconnected by three disulfide bridges and might constitute a new class of polypeptide toxins.
Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: kinetic studies with natural and recombinant variants of cystatins and stefins.
- W. Machleidt, U. Thiele, I. Assfalg-Machleidt, D. Förger, E. Auerswald
- Biology, ChemistryBiomedica biochimica acta
Natural and recombinant variants of the cysteine proteinase inhibitors chicken cystatin and human stefin B were characterized by determination of their inhibition constants for papain, actinidin and…
The acid‐stable proteinase inhibitor of human mucous secretions (HUSI‐I, antileukoprotease)
Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver.
Surface Cathepsin B Protects Cytotoxic Lymphocytes from Self-destruction after Degranulation
- K. N. Balaji, N. Schaschke, W. Machleidt, M. Catálfamo, P. Henkart
- Biology, ChemistryThe Journal of experimental medicine
- 19 August 2002
It is shown that CTL and NK cells die within a few hours if they are triggered to degranulate in the presence of nontoxic thiol cathepsin protease inhibitors, which supports a model in which granule-derived surface cathePSin B provides self-protection for degranulating cytotoxic lymphocytes.