Cryoelectron Microscopy of Protein–Lipid Complexes of Human Myelin Basic Protein Charge Isomers Differing in Degree of Citrullination
- 1 February 2000
- journal article
- Published by Elsevier in Journal of Structural Biology
- Vol. 129 (1), 80-95
- https://doi.org/10.1006/jsbi.1999.4200
Abstract
No abstract availableKeywords
This publication has 75 references indexed in Scilit:
- Surfactant Protein A (SP-A) Forms a Novel Supraquaternary Structure in the Form of FibersBiochemical and Biophysical Research Communications, 1998
- Detection of Myelin Basic Protein Isoforms by Organic ConcentrationBiochemical and Biophysical Research Communications, 1997
- A New Generation of the IMAGIC Image Processing SystemJournal of Structural Biology, 1996
- Structural Similarities between Myelin and Hydrophobic Surfactant Associated Proteins: Protein Motifs for Interacting with BilayersJournal of Theoretical Biology, 1994
- Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2·2 Å resolutionJournal of Molecular Biology, 1991
- Myelin basic protein: Interaction with calmodulin and gangliosidesJournal of Neuroscience Research, 1990
- Similarity measures between imagesUltramicroscopy, 1987
- The encephalitogenic protein of myelin forms hexamers in which the polypeptides have a pleated‐sheet structureFEBS Letters, 1985
- NMR studies of myelin basic proteinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Sedimentation analysis of the self-association of bovine myelin basic proteinBiochemistry, 1980