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Marc Tessier-Lavigne

Researcher at Stanford University

Publications -  328
Citations -  65255

Marc Tessier-Lavigne is an academic researcher from Stanford University. The author has contributed to research in topics: Axon guidance & Netrin. The author has an hindex of 131, co-authored 319 publications receiving 61481 citations. Previous affiliations of Marc Tessier-Lavigne include University of California & Columbia University.

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Journal ArticleDOI

The Molecular Biology of Axon Guidance

TL;DR: Evidence is accumulating that these mechanisms act simultaneously and in a coordinated manner to direct pathfinding and that they are mediated by mechanistically and evolutionarily conserved ligand-receptor systems.
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Netrins are diffusible chemotropic factors for commissural axons in the embryonic spinal cord.

TL;DR: It is shown that netrin-1 is a chemotropic factor expressed by floor plate cells and suggested that the two netrin proteins guide commissural axons in the developing spinal cord.
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Netrin-1 is required for commissural axon guidance in the developing vertebrate nervous system

TL;DR: Results establish netrin-1 as a guidance cue that likely collaborates with other diffusible cues to guide axons in vivo and evidence is provided for a distinct trochlear axon chemorepellent produced by floor plate cells.
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The netrins define a family of axon outgrowth-promoting proteins homologous to C. elegans UNC-6

TL;DR: In this article, the authors have purified from embryonic chick brain two proteins, Netrin-1 and netrin-2, that each possess commissural axon outgrowth-promoting activity and also identified a distinct activity that potentiates their effects.
Journal ArticleDOI

Slit Proteins Bind Robo Receptors and Have an Evolutionarily Conserved Role in Repulsive Axon Guidance

TL;DR: The characterization of three mammalian Slit homologs are described and it is shown that the Drosophila Slit protein and at least one of the mammals Slit proteins, Slit2, are proteolytically processed and show specific, high-affinity binding to Robo proteins.