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Heiner Niemann

Researcher at Hochschule Hannover

Publications -  52
Citations -  2969

Heiner Niemann is an academic researcher from Hochschule Hannover. The author has contributed to research in topics: Glycoprotein & Autophosphorylation. The author has an hindex of 24, co-authored 52 publications receiving 2903 citations. Previous affiliations of Heiner Niemann include University of Giessen & Centre national de la recherche scientifique.

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Journal ArticleDOI

Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity.

TL;DR: A dual role is assigned to SNAP-25 and it is suggested that its nine C-terminal amino acids are directly involved in coupling the calcium sensor to the final step in exocytosis.
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A Novel Tetanus Neurotoxin-insensitive Vesicle-associated Membrane Protein in SNARE Complexes of the Apical Plasma Membrane of Epithelial Cells

TL;DR: This study found that syntaxin 3, SNAP23, and a newly identified VAMP/brevin, tetanus neurotoxin (TeNT)-insensitive VAMP (TI-VAMP), are insensitive to clostridial NTs and are suggested to participate in exocytotic processes at the apical plasma membrane of epithelial cells and, more generally, domain-specificExocytosis in clostidial NT-resistant pathways.
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The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins.

TL;DR: The complete sequence of botulinum neurotoxin type A (BoNT/A; 1,296 amino acid residues, Mr = 149,425) and a partial sequence ofotoxin type E (273 amino acids residues) as deduced from the corresponding nucleotide sequences of the chromosomally located structural genes are established.
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Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins.

TL;DR: Overlapping peptides together covering the entire tetanus toxin molecule were synthesized in Escherichia coli and identified by monoclonal antibodies, indicating that the neurotoxins from C. tetani and C. botulinum are derived from a common ancestral gene.
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Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage.

TL;DR: It is demonstrated that cleavage of SNAP‐25 occurs between Arg198 and Ala199, depends on the presence of regions Asn93 to Glu145 and Ile156 to Met202, and requires about 1,000‐fold higher L chain concentrations in comparison with BoNT/A and BoNT /E.