The Crystal Structure of the Ligand Binding Module of Axonin-1/TAG-1 Suggests a Zipper Mechanism for Neural Cell Adhesion
- 1 May 2000
- Vol. 101 (4) , 425-433
- https://doi.org/10.1016/s0092-8674(00)80852-1
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1Proceedings of the National Academy of Sciences, 1998
- THE MOLECULAR STRUCTURE OF CELL ADHESION MOLECULESAnnual Review of Biochemistry, 1997
- [27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methodsPublished by Elsevier ,1997
- Mass spectrometric characterisation of primary structure, sequence heterogeneity, and intramolecular disulfide loops of the cell adhesion protein axonin-1 from chickenEuropean Journal of Mass Spectrometry, 1997
- Cell adhesion molecules NgCAM and axonin-1 form heterodimers in the neuronal membrane and cooperate in neurite outgrowth promotion.The Journal of cell biology, 1996
- Structure/function relationships of axon-associated adhesion receptors of the immunoglobulin superfamilyCurrent Opinion in Neurobiology, 1996
- Functional analysis of posttranslational cleavage products of the neuron-glia cell adhesion molecule, Ng-CAM.The Journal of cell biology, 1995
- TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrinsNeuron, 1994
- Renaturation, Purification and Characterization of Recombinant Fab-Fragments Produced in Escherichia coliNature Biotechnology, 1991
- The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activityCell, 1990