Alleviation of a defect in protein folding by increasing the rate of subunit assembly (Q43576570)

24 November 2017

title

Alleviation of a defect in protein folding by increasing the rate of subunit assembly (English)

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24 November 2017

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Aramli LA

1

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24 November 2017

Teschke CM

series ordinal

2

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24 November 2017

language of work or name

English

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publication date

13 April 2001

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Journal of Biological Chemistry

24 November 2017

published in

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24 November 2017

volume

276

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24 November 2017

issue

27

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24 November 2017

page(s)

25372-25377

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Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.

24 November 2017

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There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike

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The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid

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The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways

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Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30 degrees C.

21 January 2018

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

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Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation

21 January 2018

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Catalytic head assembling protein in virus morphogenesis.

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GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.

21 January 2018

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Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro

21 January 2018

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Identification and characterization of the domain structure of bacteriophage P22 coat protein.

21 January 2018

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21 January 2018

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Folding of the phage P22 coat protein in vitro.

21 January 2018

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A natural polymorphism in beta-lactamase is a global suppressor

21 January 2018

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Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force

21 January 2018

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P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain

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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Regulation of coat protein polymerization by the scaffolding protein of bacteriophage P22.

21 January 2018

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Genetic analysis of the folding pathway for the tail spike protein of phage P22

21 January 2018

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Genetic studies of protein stability and mechanisms of folding

21 January 2018

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Misfolding of chloramphenicol acetyltransferase due to carboxy-terminal truncation can be corrected by second-site mutations.

21 January 2018

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Role of Entropic Interactions in Viral Capsids: Single Amino Acid Substitutions in P22 Bacteriophage Coat Protein Resulting in Loss of Capsid Stability

21 January 2018

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Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype

21 January 2018

1 reference

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Folding defects caused by single amino acid substitutions in a subunit are not alleviated by assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M101759200

Stability of wild-type and temperature-sensitive protein subunits of the phage P22 capsid

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M101759200

Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype

21 January 2018

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Improvement and simplification of low-background silver staining of proteins by using sodium dithionite

21 January 2018

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In vitro unfolding/refolding of wild type phage P22 scaffolding protein reveals capsid-binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M101759200

Global suppression of protein folding defects and inclusion body formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M101759200

21 January 2018

Identifiers

DOI

10.1074/JBC.M101759200

1 reference

24 November 2017

1 reference