M
Melitta Schachner
Researcher at Rutgers University
Publications - 878
Citations - 70217
Melitta Schachner is an academic researcher from Rutgers University. The author has contributed to research in topics: Neural cell adhesion molecule & Neurite. The author has an hindex of 135, co-authored 861 publications receiving 67304 citations. Previous affiliations of Melitta Schachner include Eppendorf (Germany) & École Polytechnique Fédérale de Lausanne.
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Monoclonal antibodies (O1 to O4) to oligodendrocyte cell surfaces: An immunocytological study in the central nervous system
TL;DR: In this article, four monoclonal antibodies are characterized from a fusion of mouse myeloma P3-NS1/1-Ag4-1 with spleen cells from BALB/c mice immunized with white matter from bovine corpus callosum.
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Neural recognition molecules of the immunoglobulin superfamily: signaling transducers of axon guidance and neuronal migration
TL;DR: This work focuses on the best-studied subclasses, the neural cell adhesion molecule NCAM and the L1 family of adhesion molecules, which share important structural and functional features and are instructive for elucidating the mechanisms by which other recognition molecules may guide cell interactions during development or modify their function as a result of injury, learning and memory.
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Immunocytological and biochemical characterization of a new neuronal cell surface component (L1 antigen) which is involved in cell adhesion.
TL;DR: During cerebellar development L1 antigen is detectable on tetanus toxin‐positive cells as early as embryonic day 13 after 3 days in culture and in the adult cerebellum, where it is predominantly localized in the molecular layer and around Purkinje cells.
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Neural cell adhesion molecules and myelin-associated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1.
J. Kruse,R. Mailhammer,H Wernecke,Andreas Faissner,Iris E. C. Sommer,Christo Goridis,Melitta Schachner +6 more
TL;DR: It is shown here that a carbohydrate moiety recognized by L2 and HNK-1 monoclonal antibodies, is present in mouse N-CAM and LI, which points to a previously undetected molecular diversity which may have functional implications for modulating cell adhesion during development.
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Neural adhesion molecule L1 as a member of the immunoglobulin superfamily with binding domains similar to fibronectin.
TL;DR: It is shown here that in addition to sharing carbohydrate epitopes with N-CAM and MAG, L1 is also a member of the immunoglobulin superfamily, which contains six C2 domains and also shares three type III domains with the extracellular matrix adhesion molecule fibronectin.