Solution Structure of Microtubule-associated Protein Light Chain 3 and Identification of Its Functional Subdomains
Open Access
- 1 July 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (26) , 24610-24617
- https://doi.org/10.1074/jbc.m413565200
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- HsAtg4B/HsApg4B/Autophagin-1 Cleaves the Carboxyl Termini of Three Human Atg8 Homologues and Delipidates Microtubule-associated Protein Light Chain 3- and GABAA Receptor-associated Protein-Phospholipid ConjugatesJournal of Biological Chemistry, 2004
- Human Apg3p/Aut1p Homologue Is an Authentic E2 Enzyme for Multiple Substrates, GATE-16, GABARAP, and MAP-LC3, and Facilitates the Conjugation of hApg12p to hApg5pJournal of Biological Chemistry, 2002
- Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiaePublished by Wiley ,2001
- 18 kDa microtubule‐associated protein: identification as a new light chain (LC‐3) of microtubule‐associated protein 1 (MAP‐1)Published by Wiley ,2001
- LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processingThe EMBO Journal, 2000
- Interpreting a Medium-resolution Model of Tubulin: Comparison of Zinc-sheet and Microtubule StructureJournal of Molecular Biology, 1996
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Isolation of autophagocytosis mutants of Saccharomyces cerevisiaeFEBS Letters, 1994
- MAP1B is encoded as a polyprotein that is processed to form a complex N-terminal microtubule-binding domainPublished by Elsevier ,1991