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l-amino acid oxidases (LAAOs) are flavoenzymes that catalyze the oxidative deamination of l-amino acids to the corresponding α-keto acids, ammonia, and hydrogen peroxide. Here, we show the overexpression, purification, and the characterization of LAAO4 from the fungus Hebeloma cylindrosporum in the.
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Fischer von Mollard, G., Nothwehr, S.F., Stevens, T.H. (1997) The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. J. J. Cell Biol. 137 1511-1524
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The exocytosis of cytotoxic proteins stored in lytic granules of activated CTL is a key event during killing of target cells. Membrane fusion events that are mediated by soluble N-ethylmaleimide-sensitive-factor attachment protein receptor (SNARE) proteins are crucial, as demonstrated by patients with familial hemophagocytic lymphohistocytosis type 4 who have mutations in the SNARE protein.
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Dressel R, Elsner L, Novota P, Kanwar N, Fischer von Mollard G. The exocytosis of lytic granules is impaired in Vti1b- or Vamp8-deficient CTL leading to a reduced cytotoxic activity following antigen-specific activation. J Immunol. 2010; 185:1005-1014. doi: 10.4049/jimmunol.1000770. [Google Scholar]
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Yeast Strains. Temperature-sensitive (ts) 1 alleles in VTI1 were introduced into yeast strains BJ3505 and DKY6281 by transformation and loop in-loop out of plasmids containing the vti1 ts alleles and a URA3 marker at the VTI1 locus (Fischer von Mollard et al., 1997).Ura + transformants were selected and Ura − clones which were generated in a second selection with 5-fluoroorotic acid were.
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Dressel R., Elsner L., Novota P., Kanwar N., Fischer von Mollard G. The exocytosis of lytic granules is impaired in Vti1b- or Vamp8-deficient CTL leading to a reduced cytotoxic activity following antigen-specific activation. J. Immunol. 2010; 185:1005-1014. [Google Scholar]
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The v-SNARE Vti1p interacts both genetically and biochemically with Pep12p (Fischer von Mollard et al., 1997). It was thus proposed that Vti1p and Pep12p form a SNARE complex that is involved in docking and fusion of TGN-derived transport vesicles with the PVC. It has recently been reported that a subset of proteins,.
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Fischer von Mollard G 1 , Stahl B, Li C, Südhof TC, Jahn R. Author information. Affiliations. 1. Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06510. (1 author) ORCIDs linked to this article. Jahn R | 0000-0003-1542-3498.
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Fischer von Mollard G. and Stevens,T.H. (1999) The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole. Mol. Biol. Cell, 10, 1719-1732. [PMC free article] [Google Scholar] Fischer von Mollard G., Nothwehr,S.F. and Stevens,T.H. (1997) The yeast v-SNARE Vti1p mediates two vesicle transport.
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As shown * G. Fischer von Mollard, B. Stahl, A. Khokhlatchev, T. C. Sudhof, and R. Jahn, manuscript in preparation. in Fig. 2, most of Rab3C copurified in parallel with Rab3A and synaptophysin (p38), two established marker proteins of synaptic vesicles (for review, see Jahn and Sudhof (1993)), with the highest concentration found in the purified synaptic vesicle fraction (compare levels in the.
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Fischer von Mollard G, 0000-0003-3236-1401; Applied Microbiology and Biotechnology, 16 Dec 2016, 101(7): 2853-2864 DOI: 10.1007/s00253-016-8054-y PMID: 27986991 . Share this article Share with email Share with twitter Share with linkedin Share with facebook. Abstract .
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Thomas Jany 1 , Alexander Moreth, Claudia Gruschka, Andy Sischka, Andre Spiering, Mareike Dieding, Ying Wang, Susan Haji Samo, Anja Stammler, Hartmut Bögge, Gabriele Fischer von Mollard, Dario Anselmetti, Thorsten Glaser
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ORCID record for Gabriele Fischer von Mollard. ORCID provides an identifier for individuals to use with their name as they engage in research, scholarship, and innovation activities.
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Gabriele Fischer von Mollard & Reinhard Jahn. Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas, 75235, USA.
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The current address of Dr. G. Fischer von Mollard is the Institute of Mo- lecular Biology, University of Oregon, Eugene, OR 97403. 1. Abbreviations used in this paper: BoNT/C1, botulinum neurotoxin C1; CCV, clathrin-coated vesicles; GST, glutathione-s-transferase; hm, heavy membrane fraction; lm, light membrane fraction; NSF, N-ethylmaleimide.
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Katharina Hahn 1 , Katrin Neumeister 1 , Andreas Mix 2 , Tilman Kottke 3 , Harald Gröger 4 , Gabriele Fischer von Mollard 5 Affiliations 1 Biochemie III, Fakultät für Chemie, Universität Bielefeld, Universitätsstrasse 25, 33615, Bielefeld, Germany.
