R
Rupert Timpl
Researcher at Max Planck Society
Publications - 410
Citations - 41322
Rupert Timpl is an academic researcher from Max Planck Society. The author has contributed to research in topics: Laminin & Basement membrane. The author has an hindex of 118, co-authored 410 publications receiving 40457 citations. Previous affiliations of Rupert Timpl include University of Liège & University of Innsbruck.
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A Network Model for the Organization of Type IV Collagen Molecules in Basement Membranes
TL;DR: Data indicate that the collagenous matrix of basement membranes consists of a regular network of type IV collagen molecules which is generated by two different interacting sites located at opposite ends of each molecule.
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Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix.
Jürgen Engel,Erich Odermatt,Andreas Engel,Joseph A. Madri,Heinz Furthmayr,Heilwig Rohde,Rupert Timpl +6 more
TL;DR: Electron microscopic images of the shapes and dimensions of laminin, of fragments of laminationin, and of fibronectin are consistent with the specific molecular weights and with the hydrodynamic properties determined in solution.
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The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival.
TL;DR: The survival of cultured chick sympathetic neurons and the outgrowth of neurites were stimulated by the basement membrane protein laminin coated onto polyornithine culture substrates, and the heparin‐binding domain of laminain is responsible for its effects on neurons.
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The J1 glycoprotein--a novel nervous system cell adhesion molecule of the L2/HNK-1 family.
TL;DR: Polyclonal antibodies are prepared to a prominent member of the L2/HNK-1 family and it is reported that these antibodies, designated J1 antibodies, react with astrocytes and oligodendroCytes and interfere with neurone–astrocyte adhesion, but not with neur one–neurone or astroCyte–astrospecific adhesion.
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Arg‐Gly‐Asp constrained within cyclic pentapoptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1
TL;DR: NMR studies of the two most active cyclic peptides showed for both an all‐trans conformation with a βII′ and γ turn that Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.