Protein aggregation as bacterial inclusion bodies is reversible
Open Access
- 26 January 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 489 (1), 29-33
- https://doi.org/10.1016/s0014-5793(01)02073-7
Abstract
Inclusion bodies are refractile, intracellular protein aggregates usually observed in bacteria upon targeted gene overexpression. Since their occurrence has a major economical impact in protein produ...Keywords
This publication has 39 references indexed in Scilit:
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999
- Posttranslational Quality Control: Folding, Refolding, and Degrading ProteinsScience, 1999
- Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble formsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- Formation of Fibrous Aggregates from a Non-native Intermediate: The Isolated P22 Tailspike β-Helix DomainPublished by Elsevier ,1999
- Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteriaFEMS Microbiology Letters, 1998
- Insertional Mutagenesis in the Tailspike Protein of Bacteriophage P22Biochemical and Biophysical Research Communications, 1998
- Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodiesProtein Science, 1997
- Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein FoldingJournal of Molecular Biology, 1996
- Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chainsProtein Science, 1995
- High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase DFEBS Letters, 1991