Literature DB >> 18651814

Studies on bacterial inclusion bodies.

Natalia S de Groot1, Alba Espargaró, Montserrat Morell, Salvador Ventura.   

Abstract

The field of protein misfolding and aggregation has become an extremely active area of research in recent years. Of particular interest is the deposition of polypeptides into inclusion bodies inside bacterial cells. One reason for this interest is that protein aggregation constitutes a major bottleneck in protein production and restricts the spectrum of protein-based drugs available for commercialization. Additionally, prokaryotic cells could provide a simple yet powerful system for studying the formation and prevention of toxic aggregates, such as those responsible for a number of degenerative diseases. Here, we review recent work that has challenged our understanding of the structure and physiology of inclusion bodies and provided us with a new view of intracellular protein deposition, which has important implications in microbiology, biomedicine and biotechnology.

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Year:  2008        PMID: 18651814     DOI: 10.2217/17460913.3.4.423

Source DB:  PubMed          Journal:  Future Microbiol        ISSN: 1746-0913            Impact factor:   3.165


  14 in total

Review 1.  Towards revealing the structure of bacterial inclusion bodies.

Authors:  Lei Wang
Journal:  Prion       Date:  2009-07-25       Impact factor: 3.931

Review 2.  Protein folding and aggregation in bacteria.

Authors:  Raimon Sabate; Natalia S de Groot; Salvador Ventura
Journal:  Cell Mol Life Sci       Date:  2010-04-01       Impact factor: 9.261

3.  Strategies for production of active eukaryotic proteins in bacterial expression system.

Authors:  Orawan Khow; Sunutcha Suntrarachun
Journal:  Asian Pac J Trop Biomed       Date:  2012-02

4.  Soluble expression of pullulanase from Bacillus acidopullulyticus in Escherichia coli by tightly controlling basal expression.

Authors:  Ana Chen; Yamei Li; Xiuxia Liu; Quan Long; Yankun Yang; Zhonghu Bai
Journal:  J Ind Microbiol Biotechnol       Date:  2014-10-14       Impact factor: 3.346

5.  Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability.

Authors:  Chunying Xu; Zhuoxin Yu; Masayori Inouye; Barbara Brodsky; Oleg Mirochnitchenko
Journal:  Biomacromolecules       Date:  2010-02-08       Impact factor: 6.988

6.  Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors.

Authors:  Anna Villar-Piqué; Alba Espargaró; Raimon Sabaté; Natalia S de Groot; Salvador Ventura
Journal:  Microb Cell Fact       Date:  2012-05-03       Impact factor: 5.328

Review 7.  Active protein aggregates produced in Escherichia coli.

Authors:  Spela Peternel; Radovan Komel
Journal:  Int J Mol Sci       Date:  2011-11-22       Impact factor: 5.923

8.  The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.

Authors:  Susanna Navarro; Patrizia Marinelli; Marta Diaz-Caballero; Salvador Ventura
Journal:  Microb Cell Fact       Date:  2015-07-11       Impact factor: 5.328

9.  Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion.

Authors:  Raimon Sabaté; Alba Espargaró; Sven J Saupe; Salvador Ventura
Journal:  Microb Cell Fact       Date:  2009-10-28       Impact factor: 5.328

10.  The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.

Authors:  Gaetano Invernizzi; Francesco A Aprile; Antonino Natalello; Andrea Ghisleni; Amanda Penco; Annalisa Relini; Silvia M Doglia; Paolo Tortora; Maria E Regonesi
Journal:  PLoS One       Date:  2012-12-14       Impact factor: 3.240

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