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Friedrich Lottspeich

Researcher at Max Planck Society

Publications -  449
Citations -  31053

Friedrich Lottspeich is an academic researcher from Max Planck Society. The author has contributed to research in topics: Peptide sequence & Amino acid. The author has an hindex of 94, co-authored 449 publications receiving 30250 citations. Previous affiliations of Friedrich Lottspeich include Technische Universität Darmstadt & University of Marburg.

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Ferritin - A mediator of apoptosis?

TL;DR: It is demonstrated that acidic isoferritins with homology to immunomodulatory ferritin isoforms are released from hepatocytes in vitro, and are able to stimulate upregulation of p53 and mediate apoptosis involving Fas (CD95) signalling as well as addressing the intrinsic mitochondrial proapoptotic pathway.
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Glutamate dehydrogenase, the marker protein of Plasmodium falciparum--cloning, expression and characterization of the malarial enzyme.

TL;DR: The gene of an NADP+-specific glutamate dehydrogenase was cloned from Plasmodium falciparum, the causative agent of tropical malaria, and western-blot analysis of stage-specific parasites shows that glutamate dehydrogensase is present in all intraerythrocytic stages.
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Proteomic, functional and motif‐based analysis of C‐terminal Src kinase‐interacting proteins

TL;DR: The newly identified potential interacting partners of Csk provided new insights into its functional diversity in regulation of numerous cellular events, in addition to controlling the SFK activity.
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Human low-molecular-mass kininogen. Amino-acid sequence of the light chain; homology with other protein sequences.

TL;DR: The complete amino acid sequence of the human low-molecular-mass kininogen light chain has been determined and it is indicated that the amino-terminal part of it is species-specific and the carboxy- terminal part is function-specific.
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Catabolic ornithine transcarbamylase of Halobacterium halobium (salinarium): purification, characterization, sequence determination, and evolution.

TL;DR: The halobacterial cOT case is found in a group with the anabolic OTCases of Bacillus subtilis, P. aeruginosa, and Mycobacterium bovis, and the halophilic enzyme exhibits Michaelis-Menten kinetics with both carbamylphosphate and ornithine as substrates with Km values of 0.4 and 8 mM, respectively.