Electron microscopy and image analysis reveal common principles of organization in two large protein complexes: groEL-Type proteins and proteasomes
- 1 May 1990
- journal article
- research article
- Published by Elsevier in Journal of Structural Biology
- Vol. 103 (3), 197-203
- https://doi.org/10.1016/1047-8477(90)90037-d
Abstract
No abstract availableThis publication has 48 references indexed in Scilit:
- Identification of two unknown reading frames in Synechococcus 6301 as homologues of the 10k and 65k antigen genes ofMyobacterium tuberculosisand related heat shock genes inE.coliandCoxiella burnetiiNucleic Acids Research, 1989
- The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteriaFEBS Letters, 1989
- Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondriaNature, 1989
- Electron microscopy and image analysis of the multicatalytic proteinaseFEBS Letters, 1988
- Transient association of newly synthesized unfolded proteins with the heat-shock GroEL proteinNature, 1988
- A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptidesNature, 1988
- 70K heat shock related proteins stimulate protein translocation into microsomesNature, 1988
- Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome)Nature, 1988
- A 20S particle ubiquitous from yeast to humanJournal of Molecular Evolution, 1987
- Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscleBiochemical Journal, 1985