1,671
Views
56
CrossRef citations to date
0
Altmetric
Review

Towards revealing the structure of bacterial inclusion bodies

Pages 139-145 | Received 02 Apr 2009, Accepted 25 Aug 2009, Published online: 01 Jul 2009

Keep up to date with the latest research on this topic with citation updates for this article.

Read on this site (4)

Kajal Kachhawaha, Santanu Singh, Khyati Joshi, Priyanka Nain & Sumit K. Singh. (2023) Bioprocessing of recombinant proteins from Escherichia coli inclusion bodies: insights from structure-function relationship for novel applications. Preparative Biochemistry & Biotechnology 53:7, pages 728-752.
Read now
Cornelia Walther, Martin Kellner, Matthias Berkemeyer, Cécile Brocard & Astrid Dürauer. (2017) Integrated process development—a robust, rapid method for inclusion body harvesting and processing at the microscale level. Preparative Biochemistry & Biotechnology 47:9, pages 874-880.
Read now
Anastasia V. Grizel, Aleksandr A. Rubel & Yury O. Chernoff. (2016) Strain conformation controls the specificity of cross-species prion transmission in the yeast model. Prion 10:4, pages 269-282.
Read now
Caroline Piercey Åkesson, Charles McL. Press, Michael A. Tranulis, Martin Jeffrey, Mona Aleksandersen, Thor Landsverk & Arild Espenes. (2012) Phenotypic characterization of cells participating in transport of prion protein aggregates across the intestinal mucosa of sheep. Prion 6:3, pages 261-275.
Read now

Articles from other publishers (52)

Julya Sorokina, Irina Sokolova, Mariya Majorina, Anastasia Ungur, Vasiliy Troitskiy, Amir Tukhvatulin, Bogdan Melnik & Yury Belyi. (2023) Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase of Clostridioides difficile. Biomolecules 13:6, pages 1012.
Crossref
Ricardo Baltà-Foix, Caterina Serrano-Adrover, Adrià López-Cano, Laia Gifre-Renom, Alejandro Sanchez-Chardi, Anna Arís & Elena Garcia-Fruitós. (2023) Lactiplantibacillus plantarum: a new example of inclusion body producing bacteria. Microbial Cell Factories 22:1.
Crossref
Gizem Ölçücü, Ulrich Krauss, Karl-Erich Jaeger & Jörg Pietruszka. (2023) Carrier‐Free Enzyme Immobilizates for Flow Chemistry. Chemie Ingenieur Technik 95:4, pages 531-542.
Crossref
Sarah Kamel, Julia Schollmeyer, Anke Kurreck & Peter Neubauer. 2023. Inclusion Bodies. Inclusion Bodies 121 138 .
Julian Kopp & Oliver Spadiut. 2023. Inclusion Bodies. Inclusion Bodies 1 13 .
Tamara F. Solov'eva, Svetlana I. Bakholdina, Valentina A. Khomenko, Evgeniy V. Sidorin, Natalya Yu. Kim, Olga D. Novikova, Valery L. Shnyrov, Anna M. Stenkova, Vyacheslav I. Eremeev, Evgenia P. Bystritskaya & Marina P. Isaeva. (2022) Expression of membrane beta-barrel protein in E. coli at low temperatures: Structure of Yersinia pseudotuberculosis OmpF porin inclusion bodies. Biochimica et Biophysica Acta (BBA) - Biomembranes 1864:9, pages 183971.
Crossref
Ricardo Baltà-Foix, Ramon Roca-Pinilla, Adria López-Cano, Laia Gifre-Renom, Anna Arís & Elena Garcia-Fruitós. 2022. Microbial Production of High-Value Products. Microbial Production of High-Value Products 289 308 .
Neus Ferrer-Miralles, Paolo Saccardo, José Luis Corchero & Elena Garcia-Fruitós. 2022. Insoluble Proteins. Insoluble Proteins 1 31 .
Sarah Kamel, Miriam C. Walczak, Felix Kaspar, Sarah Westarp, Peter Neubauer & Anke Kurreck. (2021) Thermostable adenosine 5′-monophosphate phosphorylase from Thermococcus kodakarensis forms catalytically active inclusion bodies. Scientific Reports 11:1.
Crossref
Gizem Ölçücü, Oliver Klaus, Karl-Erich Jaeger, Thomas Drepper & Ulrich Krauss. (2021) Emerging Solutions for in Vivo Biocatalyst Immobilization: Tailor-Made Catalysts for Industrial Biocatalysis . ACS Sustainable Chemistry & Engineering 9:27, pages 8919-8945.
Crossref
Svetlana I. Bakholdina, Anna M. Stenkova, Evgenia P. Bystritskaya, Evgeniy V. Sidorin, Natalya Yu. Kim, Ekaterina S. Menchinskaya, Tatiana Yu. Gorpenchenko, Dmitry L. Aminin, Nikita A. Shved & Tamara F. Solov’eva. (2021) Studies on the Structure and Properties of Membrane Phospholipase A1 Inclusion Bodies Formed at Low Growth Temperatures Using GFP Fusion Strategy. Molecules 26:13, pages 3936.
Crossref
Xiaojuan Liu, Xihui Xie, Hong Du, Edmond Sanganyado, Wanna Wang, Muhammad Aslam, Jichen Chen, Weizhou Chen & Honghao Liang. (2021) Bioinformatic analysis and genetic engineering approaches for recombinant biopharmaceutical glycoproteins production in microalgae. Algal Research 55, pages 102276.
Crossref
Fatemeh Mohammadi, Zeinab Takalloo, Hossein Rahmani, Mohammad Ali Nasiri Khalili, Khosro Khajeh, Gholamhossein Riazi & Reza H. Sajedi. (2021) Interplay of isoform 1N4R tau protein and amyloid-β peptide fragment 25–35 in reducing and non-reducing conditions. The Journal of Biochemistry 169:1, pages 119-134.
Crossref
Himanshu Malani, Deepak Kumar & Anurag S Rathore. (2020) Effect of chemically defined growth medium components on characteristics of bacterial inclusion bodies. Journal of Chemical Technology & Biotechnology 95:6, pages 1640-1648.
Crossref
Anupam Singh, Vaibhav Upadhyay, Akansha Singh & Amulya K. Panda. (2020) Structure-Function Relationship of Inclusion Bodies of a Multimeric Protein. Frontiers in Microbiology 11.
Crossref
Karl F.J. Metzger, Wolfgang Padutsch, Alexander Pekarsky, Julian Kopp, Alexei M. Voloshin, Harald Kühnel & Michael Maurer. (2020) IGF1 inclusion bodies: A QbD based process approach for efficient USP as well as early DSP unit operations. Journal of Biotechnology 312, pages 23-34.
Crossref
V. D. Jäger, R. Kloss, A. Grünberger, S. Seide, D. Hahn, T. Karmainski, M. Piqueray, J. Embruch, S. Longerich, U. Mackfeld, K.-E. Jaeger, W. Wiechert, M. Pohl & U. Krauss. (2019) Tailoring the properties of (catalytically)-active inclusion bodies. Microbial Cell Factories 18:1.
Crossref
Mireia Pesarrodona, Toni Jauset, Zamira V. Díaz‐Riascos, Alejandro Sánchez‐Chardi, Marie‐Eve Beaulieu, Joaquin Seras‐Franzoso, Laura Sánchez‐García, Ricardo Baltà‐Foix, Sandra Mancilla, Yolanda Fernández, Ursula Rinas, Simó SchwartzJrJr, Laura Soucek, Antonio Villaverde, Ibane Abasolo & Esther Vázquez. (2019) Targeting Antitumoral Proteins to Breast Cancer by Local Administration of Functional Inclusion Bodies. Advanced Science 6:18, pages 1900849.
Crossref
Kalyani Sanagavarapu, Elisabeth Nüske, Irem Nasir, Georg Meisl, Jasper N. Immink, Pietro Sormanni, Michele Vendruscolo, Tuomas P. J. Knowles, Anders Malmendal, Celia Cabaleiro-Lago & Sara Linse. (2019) A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli. Scientific Reports 9:1.
Crossref
Robin Curtis, James Austerberry & Luke Holloway. 2019. Comprehensive Biotechnology. Comprehensive Biotechnology 860 878 .
Romana Koszagova, Tomas Krajcovic, Klaudia Palencarova-Talafova, Vladimir Patoprsty, Alica Vikartovska, Kristyna Pospiskova, Ivo Safarik & Jozef Nahalka. (2018) Magnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformations. Microbial Cell Factories 17:1.
Crossref
Wouter S. P. Jong, David Vikström, Diane Houben, H. Bart van den Berg van Saparoea, Jan-Willem de Gier & Joen Luirink. (2017) Application of an E. coli signal sequence as a versatile inclusion body tag. Microbial Cell Factories 16:1.
Crossref
Ursula Rinas, Elena Garcia-Fruitós, José Luis Corchero, Esther Vázquez, Joaquin Seras-Franzoso & Antonio Villaverde. (2017) Bacterial Inclusion Bodies: Discovering Their Better Half. Trends in Biochemical Sciences 42:9, pages 726-737.
Crossref
Ulrich Krauss, Vera D. Jäger, Martin Diener, Martina Pohl & Karl-Erich Jaeger. (2017) Catalytically-active inclusion bodies—Carrier-free protein immobilizates for application in biotechnology and biomedicine. Journal of Biotechnology 258, pages 136-147.
Crossref
Douglas B. Kell & Etheresia Pretorius. (2017) Proteins behaving badly. Substoichiometric molecular control and amplification of the initiation and nature of amyloid fibril formation: lessons from and for blood clotting. Progress in Biophysics and Molecular Biology 123, pages 16-41.
Crossref
Paul J. Focke, Christopher Hein, Beate Hoffmann, Kimberly Matulef, Frank Bernhard, Volker Dötsch & Francis I. Valiyaveetil. (2016) Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression . Biochemistry 55:30, pages 4212-4219.
Crossref
Jesús de Pedro-Cuesta, Pablo Martínez-Martín, Alberto Rábano, María Ruiz-Tovar, Enrique Alcalde-Cabero & Miguel Calero. (2016) Etiologic Framework for the Study of Neurodegenerative Disorders as Well as Vascular and Metabolic Comorbidities on the Grounds of Shared Epidemiologic and Biologic Features. Frontiers in Aging Neuroscience 8.
Crossref
Britta Eggenreich, Melissa Willim, David Johannes Wurm, Christoph Herwig & Oliver Spadiut. (2016) Production strategies for active heme-containing peroxidases from E. coli inclusion bodies – a review. Biotechnology Reports 10, pages 75-83.
Crossref
Arun Kumar Dangi, Praveen Rishi & Rupinder Tewari. (2016) Enhancing the Yield of Active Recombinant Chitobiase by Physico-Chemical and In Vitro Refolding Studies. The Protein Journal 35:1, pages 72-79.
Crossref
Katia Pane, Lorenzo Durante, Elio Pizzo, Mario Varcamonti, Anna Zanfardino, Valeria Sgambati, Antimo Di Maro, Andrea Carpentieri, Viviana Izzo, Alberto Di Donato, Valeria Cafaro & Eugenio Notomista. (2016) Rational Design of a Carrier Protein for the Production of Recombinant Toxic Peptides in Escherichia coli. PLOS ONE 11:1, pages e0146552.
Crossref
Anupam Singh, Vaibhav Upadhyay, Arun Kumar Upadhyay, Surinder Mohan Singh & Amulya Kumar Panda. (2015) Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process. Microbial Cell Factories 14:1.
Crossref
Yuxiang Bai, Rachel Maria van der Kaaij, Albert Jan Jacob Woortman, Zhengyu Jin & Lubbert Dijkhuizen. (2015) Characterization of the 4,6-α-glucanotransferase GTFB enzyme of Lactobacillus reuteri 121 isolated from inclusion bodies. BMC Biotechnology 15:1.
Crossref
Amira Refai, Meriam Haoues, Houcemeddine Othman, Mohamed Ridha Barbouche, Philippe Moua, Arnaud Bondon, Liza Mouret, Najet Srairi-Abid & Makram Essafi. (2015) Two distinct conformational states of Mycobacterium tuberculosis virulent factor early secreted antigenic target 6 kDa are behind the discrepancy around its biological functions . FEBS Journal 282:21, pages 4114-4129.
Crossref
Simon Poepsel, Andreas Sprengel, Barbara Sacca, Farnusch Kaschani, Markus Kaiser, Christos Gatsogiannis, Stefan Raunser, Tim Clausen & Michael Ehrmann. (2015) Determinants of amyloid fibril degradation by the PDZ protease HTRA1. Nature Chemical Biology 11:11, pages 862-869.
Crossref
Yihua Loo, Melis Goktas, Ayse B. Tekinay, Mustafa O. Guler, Charlotte A. E. Hauser & Anna Mitraki. (2015) Self-Assembled Proteins and Peptides as Scaffolds for Tissue Regeneration. Advanced Healthcare Materials 4:16, pages 2557-2586.
Crossref
Ángela J. Espejo-Mojica, Carlos J. Alméciga-Díaz, Alexander Rodríguez, Ángela Mosquera, Dennis Díaz, Laura Beltrán, Sergio Díaz, Natalia Pimentel, Jefferson Moreno, Jhonnathan Sánchez, Oscar F. Sánchez, Henry Córdoba, Raúl A. Poutou-Piñales & Luis A. Barrera. (2015) Human recombinant lysosomal enzymes produced in microorganisms. Molecular Genetics and Metabolism 116:1-2, pages 13-23.
Crossref
Careen Khachatoorian, Rigoberto A. Ramirez, Fernando Hernandez, Raphael Serna & Ernest Y. Kwok. (2015) Overexpressed Arabidopsis Annexin4 accumulates in inclusion body-like structures. Acta Histochemica 117:3, pages 279-287.
Crossref
Neus Ferrer-Miralles, Paolo Saccardo, José Luis Corchero, Zhikun Xu & Elena García-Fruitós. 2015. Insoluble Proteins. Insoluble Proteins 1 24 .
Govindan Raghunathan, Ganapathiraman Munussami, Hyojin Moon, Hyun-jong Paik, Seong Soo A An, Yong-Sung Kim, Sebyung Kang & Sun-Gu Lee. (2014) A variant of green fluorescent protein exclusively deposited to active intracellular inclusion bodies. Microbial Cell Factories 13:1.
Crossref
Anna Villar-Piqué & Salvador Ventura. 2014. Protein Aggregation in Bacteria. Protein Aggregation in Bacteria 93 116 .
Claudia Capitini, Simona Conti, Michele Perni, Francesca Guidi, Roberta Cascella, Angela De Poli, Amanda Penco, Annalisa Relini, Cristina Cecchi & Fabrizio Chiti. (2014) TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells. PLoS ONE 9:1, pages e86720.
Crossref
Manmeet Kaur, Jackie Healy, Madhusudan Vasudevamurthy, Moritz Lassé, Ljiljana Puskar, Mark J. Tobin, Celine Valery, Juliet A. Gerrard & Luigi Sasso. (2014) Stability and cytotoxicity of crystallin amyloid nanofibrils. Nanoscale 6:21, pages 13169-13178.
Crossref
Olivia Cano-Garrido, Escarlata Rodríguez-Carmona, César Díez-Gil, Esther Vázquez, Elisa Elizondo, Rafael Cubarsi, Joaquin Seras-Franzoso, José Luis Corchero, Ursula Rinas, Imma Ratera, Nora Ventosa, Jaume Veciana, Antonio Villaverde & Elena García-Fruitós. (2013) Supramolecular organization of protein-releasing functional amyloids solved in bacterial inclusion bodies. Acta Biomaterialia 9:4, pages 6134-6142.
Crossref
Aleš Berlec & Borut Štrukelj. (2013) Current state and recent advances in biopharmaceutical production in Escherichia coli , yeasts and mammalian cells . Journal of Industrial Microbiology and Biotechnology 40:3-4, pages 257-274.
Crossref
Seung Phill Choi, Yong-Cheol Park, JungHwa Lee, Sang Jun Sim & Ho-Nam Chang. (2011) Effects of l-arginine on refolding of lysine-tagged human insulin-like growth factor 1 expressed in Escherichia coli. Bioprocess and Biosystems Engineering 35:1-2, pages 255-263.
Crossref
Erica P. Vogel, Jaime Curtis-Fisk, Kaitlin M. Young & David P. Weliky. (2011) Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy of Human Immunodeficiency Virus gp41 Protein That Includes the Fusion Peptide: NMR Detection of Recombinant Fgp41 in Inclusion Bodies in Whole Bacterial Cells and Structural Characterization of Purified and Membrane-Associated Fgp41. Biochemistry 50:46, pages 10013-10026.
Crossref
Daniel Camsund, Ellenor Devine, Marie Holmqvist, Peter Yohanoun, Peter Lindblad & Karin Stensjö. (2011) A HupS-GFP fusion protein demonstrates a heterocyst-specific localization of the uptake hydrogenase in Nostoc punctiforme. FEMS Microbiology Letters 316:2, pages 152-159.
Crossref
Britta Jürgen, Antje Breitenstein, Vlada Urlacher, Knut Büttner, Hongying Lin, Michael Hecker, Thomas Schweder & Peter Neubauer. (2010) Quality control of inclusion bodies in Escherichia coli. Microbial Cell Factories 9:1.
Crossref
César Díez-Gil, Sven Krabbenborg, Elena García-Fruitós, Esther Vazquez, Escarlata Rodríguez-Carmona, Imma Ratera, Nora Ventosa, Joaquin Seras-Franzoso, Olivia Cano-Garrido, Neus Ferrer-Miralles, Antonio Villaverde & Jaume Veciana. (2010) The nanoscale properties of bacterial inclusion bodies and their effect on mammalian cell proliferation. Biomaterials 31:22, pages 5805-5812.
Crossref
Raimon Sabate, Natalia S. de Groot & Salvador Ventura. (2010) Protein folding and aggregation in bacteria. Cellular and Molecular Life Sciences 67:16, pages 2695-2715.
Crossref
Lei Wang, David Schubert, Michael R. Sawaya, David Eisenberg & Roland Riek. (2010) Multidimensional Structure–Activity Relationship of a Protein in Its Aggregated States. Angewandte Chemie International Edition 49:23, pages 3904-3908.
Crossref
Lei Wang, David Schubert, Michael R. Sawaya, David Eisenberg & Roland Riek. (2010) Multidimensional Structure–Activity Relationship of a Protein in Its Aggregated States. Angewandte Chemie 122:23, pages 3996-4000.
Crossref

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.