K
Karlheinz Mann
Researcher at Max Planck Society
Publications - 174
Citations - 13260
Karlheinz Mann is an academic researcher from Max Planck Society. The author has contributed to research in topics: Peptide sequence & Laminin. The author has an hindex of 69, co-authored 174 publications receiving 12662 citations.
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Journal ArticleDOI
Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV.
Jay W. Fox,Ulrike Mayer,Roswitha Nischt,Monique Aumailley,Dieter P. Reinhardt,Hanna Wiedemann,Karlheinz Mann,Rupert Timpl,Thomas Krieg,Jürgen Engel +9 more
TL;DR: In this paper, the shape of the nidogen was shown to be a three globes of variable mass (31-56 kDa) connected by either a rod-like or a thin segment, indicating that the Nterminal domain of the more native, recombinant protein consists of two globules connected by a flexible segment.
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Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin.
TL;DR: It is demonstrated that proteolytic release of endostatin can occur through several pathways, which may lead to a switch from a matrix‐associated to a more soluble endocrine form.
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The eggshell: structure, composition and mineralization
Maxwell T. Hincke,Yves Nys,Joël Gautron,Karlheinz Mann,Alejandro B. Rodríguez-Navarro,Marc D. McKee +5 more
TL;DR: Eggshell microstructure and ultrastructure is reviewed, and the results of recent genomic, transcriptomic and proteomic analyses of the chicken eggshell matrix are reviewed to draw attention to areas of current uncertainty such as the potential role of amorphous calcium carbonate.
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Expression and Proteolysis of Vascular Endothelial Growth Factor is Increased in Chronic Wounds
Gereon Lauer,Stephan Sollberg,Melanie Cole,Ingo Flamme,Jörg Stürzebecher,Karlheinz Mann,Thomas Krieg,Sabine A. Eming +7 more
TL;DR: Data show that, although vascular endothelial growth factor expression is elevated in chronic wounds, increased proteolytic activity in this environment results in its degradation, which may contribute to an impaired wound healing response.
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A single EGF-like motif of laminin is responsible for high affinity nidogen binding.
Ulrike Mayer,Roswitha Nischt,Ernst Pöschl,Karlheinz Mann,K Fukuda,Martin Gerl,Y. Yamada,Rupert Timpl +7 more
TL;DR: Smaller fragments were prepared by the same recombinant procedure and showed that combinations of EGF‐like repeats 3–4 and 4–5 and the single repeat 4 but not repeats 3 or 5 possess full nidogen‐binding activity, identifying repeat 4 as the only binding structure.