Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology (Q37875224)

24 August 2017

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title

Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology (English)

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24 August 2017

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2

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24 August 2017

Diletta Ami

3

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Pietro Gatti-Lafranconi

object named as

Pietro Gatti-Lafranconi

series ordinal

1

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Marina Lotti

object named as

Marina Lotti

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5

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author name string

Silvia Maria Doglia

series ordinal

4

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24 August 2017

language of work or name

English

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publication date

31 May 2011

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24 August 2017

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24 August 2017

volume

278

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24 August 2017

issue

14

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24 August 2017

page(s)

2408-2418

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An inventory of the bacterial macromolecular components and their spatial organization.

24 August 2017

cites work

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Crowding and hydrodynamic interactions likely dominate in vivo macromolecular motion

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Molecular crowding enhances native state stability and refolding rates of globular proteins

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Protein folding in the cell: challenges and progress

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

The Yin and Yang of protein folding

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Recombinant protein folding and misfolding in Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Converging concepts of protein folding in vitro and in vivo

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Protein aggregates: an aging factor involved in cell death

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Cellular strategies for controlling protein aggregation

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Errors of heterologous protein expression

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Stability effects of mutations and protein evolvability

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

An evolutionarily conserved mechanism for controlling the efficiency of protein translation

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Proteome-level interplay between folding and aggregation propensities of proteins.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Translationally optimal codons associate with aggregation-prone sites in proteins

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

21 January 2018

(p)ppGpp: still magical?

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Stringent control in E. coli

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Stress responses and replication of plasmids in bacterial cells

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Regulation of the heat-shock response

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Convergence of Molecular, Modeling, and Systems Approaches for an Understanding of the Escherichia coli Heat Shock Response

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Chaperones: A story of thrift unfolds

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Global transcriptome response of recombinant Escherichia coli to heat-shock and dual heat-shock recombinant protein induction

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Monitoring of transcriptome and proteome profiles to investigate the cellular response of E. coli towards recombinant protein expression under defined chemostat conditions

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

A comparative study of global stress gene regulation in response to overexpression of recombinant proteins in Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

The transcriptional response of Escherichia coli to recombinant protein insolubility.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Stress responses to heterologous membrane protein expression in Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Components of the E. coli envelope are affected by and can react to protein over-production in the cytoplasm

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Effects of recombinant protein misfolding and aggregation on bacterial membranes.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Refolding solubilized inclusion body proteins

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

E. coli transports aggregated proteins to the poles by a specific and energy-dependent process

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Localization of functional polypeptides in bacterial inclusion bodies

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Structure and morphology of protein inclusion bodies in Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Characterization of inclusion bodies in recombinant Escherichia coli producing high levels of porcine somatotropin.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Fine architecture of bacterial inclusion bodies

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Tunable geometry of bacterial inclusion bodies as substrate materials for tissue engineering

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Atomic force microscopy as a multifunctional molecular toolbox in nanobiotechnology.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Bacterial inclusion bodies contain amyloid-like structure

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

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

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Tetracycline and its analogues protect Caenorhabditis elegans from β amyloid-induced toxicity by targeting oligomers

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

In vivo aggregation of bovine beta-lactoglobulin is affected by Cys at position 121.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Secondary structure characterization of beta-lactamase inclusion bodies.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Raman spectroscopy of protein pharmaceuticals

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Multidimensional structure-activity relationship of a protein in its aggregated states

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Protein aggregation profile of the bacterial cytosol

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D.

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Fusion to a pull-down domain: a novel approach of producing Trigonopsis variabilisD-amino acid oxidase as insoluble enzyme aggregates

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3).

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to alpha-D-glucose-1-phosphate

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

A crosslinked inclusion body process for sialic acid synthesis

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Activity of maize transglutaminase overexpressed in escherichia coli inclusion bodies: An alternative to protein refolding

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Production of nonclassical inclusion bodies from which correctly folded protein can be extracted

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Engineering inclusion bodies for non denaturing extraction of functional proteins

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Carrier-free immobilized enzymes for biocatalysis

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

In vivo enzyme immobilization by inclusion body display

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Characterization of the aggregates formed during recombinant protein expression in bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Impact of different cultivation and induction regimes on the structure of cytosolic inclusion bodies of TEM1-beta-lactamase

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Principles of Fluorescence Spectroscopy

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

Inclusion bodies: Specificity in their aggregation process and amyloid-like structure

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

21 January 2018

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08163.X

10.1111/J.1742-4658.2011.08163.X

21 January 2018

Identifiers

DOI

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24 August 2017

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