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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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Journal ArticleDOI

Expression of the human urokinase-type plasminogen activator receptor in E. coli and Chinese hamster ovary cells: purification of the recombinant proteins and generation of polyclonal antibodies in chicken.

Viktor Magdolen, +11 more
- 01 Jan 1995 - 
TL;DR: A set of different polyclonal uPAR antibodies has been generated in order to investigate the role of uPAR in tumor spreading in more detail and the reaction patterns of these antibodies were analyzed by Western blot analyses and flow cytofluorometry.
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Murine protein which binds preferentially to oligo-C-rich single-stranded nucleic acids

Martin Goller, +5 more
- 25 May 1994 - 
TL;DR: Two single-stranded nucleic acid binding proteins mCBP and mCTBP were identified by means of their binding to a potential recombination hotspot in LTRs of mouse retro-transposons.
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PorH, a new channel-forming protein present in the cell wall of Corynebacterium efficiens and Corynebacterium callunae.

Peter Hünten, +3 more
- 01 Jul 2005 - 
TL;DR: The structure of PorH in the cell wall of the corynebacteria is discussed and the properties of the pore-forming proteins, extracted by organic solvents, were studied.
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Isolation of Two Interleukin‐6 Response Element Binding Proteins from Acute Phase Rat Liversa

Jürgen A. E. Ripperger, +9 more
- 17 Dec 2006 - 
TL;DR: It is suggested, that APRF/Stat3 and p91/Stat1 are not the only factors mediating the effects of IL-6 on class 2 acute phase genes, and the 92 kD Stat factor binding at the IL- 6 RE probably also functions as a transcription factor in the cytokine-induced activation of the alpha 2M gene.
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OmpW of Caulobacter crescentus Functions as an Outer Membrane Channel for Cations.

Roland Benz, +9 more
- 25 Nov 2015 - 
TL;DR: It is reported that high channel-forming activity was observed with crude outer membrane extracts of C. crescentus in lipid bilayer experiments, indicating that the outer membrane of Crescentus contained an ion-permeable channel with a single-channel conductance of about 120 pS in 1M KCl.