Protein aggregation as bacterial inclusion bodies is reversible (Q34513908)

2 August 2017

title

Protein aggregation as bacterial inclusion bodies is reversible (English)

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ORCID Public Data File 2021

2 August 2017

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author name string

Carrió MM

series ordinal

1

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2 August 2017

Villaverde A

series ordinal

2

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2 August 2017

language of work or name

English

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publication date

1 January 2001

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2 August 2017

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2 August 2017

volume

489

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2 August 2017

issue

1

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2 August 2017

page(s)

29-33

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The purification of eukaryotic polypeptides synthesized in Escherichia coli

2 August 2017

cites work

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Refolding of recombinant proteins

21 January 2018

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Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies

21 January 2018

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Protein folding in vivo and renaturation of recombinant proteins from inclusion bodies

21 January 2018

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21 January 2018

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Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteria

21 January 2018

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Fine architecture of bacterial inclusion bodies

21 January 2018

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Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition

21 January 2018

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Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies

21 January 2018

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Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains

21 January 2018

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Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant

21 January 2018

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Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

21 January 2018

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

21 January 2018

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Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR.

21 January 2018

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Structure and morphology of protein inclusion bodies in Escherichia coli

21 January 2018

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Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer

21 January 2018

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Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins

21 January 2018

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21 January 2018

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Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils

21 January 2018

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Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease

21 January 2018

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21 January 2018

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Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

21 January 2018

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Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

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The position of the heterologous domain can influence the solubility and proteolysis of β-galactosidase fusion proteins in E. coli

21 January 2018

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21 January 2018

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Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms

21 January 2018

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Formation of Fibrous Aggregates from a Non-native Intermediate: The Isolated P22 Tailspike β-Helix Domain

21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

Global suppression of protein folding defects and inclusion body formation

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21 January 2018

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The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

21 January 2018

1 reference

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Recovery of soluble, active recombinant protein from inclusion bodies

21 January 2018

1 reference

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Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates.

7 January 2021

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Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli

7 January 2021

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0014-5793(01)02073-7

1 reference

2 August 2017

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