Biological role of bacterial inclusion bodies: a model for amyloid aggregation (Q37875227)

24 August 2017

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title

Biological role of bacterial inclusion bodies: a model for amyloid aggregation (English)

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24 August 2017

Natalia S de Groot

3

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Elena García-Fruitós

Elena García-Fruitós

1

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Raimon Sabaté

Raimon Sabate

2

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Salvador Ventura

Salvador Ventura

5

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Antonio Villaverde

Antonio Villaverde

4

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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)

2419-2427

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Microbial factories for recombinant pharmaceuticals

24 August 2017

cites work

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https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Protein aggregation in recombinant bacteria: biological role of inclusion bodies.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Advanced genetic strategies for recombinant protein expression in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Protein aggregation as bacterial inclusion bodies is reversible

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Amyloid-like properties of bacterial inclusion bodies.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Divergent genetic control of protein solubility and conformational quality in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Yield, solubility and conformational quality of soluble proteins are not simultaneously favored in recombinant Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Inclusion bodies: a new concept

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Learning about protein solubility from bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Amyloids in bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Construction and deconstruction of bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Quality control of inclusion bodies in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Role of the chaperone DnaK in protein solubility and conformational quality in inclusion body-forming Escherichia coli cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Protein quality in bacterial inclusion bodies.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Molecular chaperones and protein quality control

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Localization of chaperones DnaK and GroEL in bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Unscrambling an egg: protein disaggregation by AAA proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

In situ protein folding and activation in bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Side effects of chaperone gene co-expression in recombinant protein production

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

DnaK/DnaJ-assisted recombinant protein production in Trichoplusia ni larvae.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.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.1742-4658.2011.08165.X

Protein aggregation and amyloid fibril formation prediction software from primary sequence: towards controlling the formation of bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Localization of functional polypeptides in bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.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.1742-4658.2011.08165.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

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

A crosslinked inclusion body process for sialic acid synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

In vivo enzyme immobilization by inclusion body display

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Rationalization of the effects of mutations on peptide and protein aggregation rates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Observation of sequence specificity in the seeding of protein amyloid fibrils.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Protein misfolding, functional amyloid, and human disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fibrils

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Conformational constraints for amyloid fibrillation: the importance of being unfolded

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Folding versus aggregation: polypeptide conformations on competing pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Unraveling the mysteries of protein folding and misfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Molecular mechanisms of amyloidosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Functional amyloid--from bacteria to humans.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Protein folding and aggregation in bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Biology of Amyloid: Structure, Function, and Regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Recent atomic models of amyloid fibril structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Bacterial inclusion bodies contain amyloid-like structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Unraveling the secrets of Alzheimer's beta-amyloid fibrils

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Molecular structure of amyloid fibrils: insights from solid-state NMR.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Conversion of a yeast prion protein to an infectious form in bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Nuclear bodies in neurodegenerative disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Aggresomes, inclusion bodies and protein aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Effect of temperature on protein quality in bacterial inclusion bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Kinetic and thermodynamic stability of bacterial intracellular aggregates

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

The protofilament substructure of amyloid fibrils11Edited by F. E. Cohen

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

Recombinant protein solubility—does more mean better?

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

21 January 2018

1 reference

https://api.crossref.org/works/10.1111/J.1742-4658.2011.08165.X

10.1111/J.1742-4658.2011.08165.X

21 January 2018

Identifiers

DOI

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24 August 2017

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