Structure of ubiquitin refined at 1.8 Å resolution
- 1 April 1987
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 194 (3) , 531-544
- https://doi.org/10.1016/0022-2836(87)90679-6
Abstract
No abstract availableThis publication has 44 references indexed in Scilit:
- Cell Surface Molecule Associated with Lymphocyte Homing Is a Ubiquitinated Branched-Chain GlycoproteinScience, 1986
- Structure of α-chymotrypsin refined at 1.68 Å resolutionJournal of Molecular Biology, 1985
- OMITMAP: An electron density map suitable for the examination of errors in a macromolecular modelJournal of Applied Crystallography, 1984
- Refined crystal structure of carboxypeptidase a at 1·54 Å resolutionJournal of Molecular Biology, 1983
- Structure of thermolysin refined at 1.6 Å resolutionJournal of Molecular Biology, 1982
- Structural Studies on Two High‐Mobility‐Group Proteins from Calf Thymus, HMG‐14 and HMG‐20 (Ubiquitin), and Their Interaction with DNAEuropean Journal of Biochemistry, 1980
- Crystallization and preliminary X-ray investigation of ubiquitin, a non-histone chromosomal proteinJournal of Molecular Biology, 1979
- Complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cellsBiochemistry, 1975
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972
- Stereochemistry of polypeptide chain configurationsJournal of Molecular Biology, 1963