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Article

Global suppression of protein folding defects and inclusion body formation.

Science (New York, N.Y.) - 5 Jul 1991

Mitraki A, Fane B, Haase-Pettingell C, Sturtevant J, King J

Abstract excerpt

Amino acid substitutions at a site in the center of the bacteriophage protein P22 tailspike polypeptide chain suppress temperature-sensitive folding mutations at many sites throughout the chain. Characterization of the intracellular folding and chain assembly process reveals that the suppressors act in the folding pathway, inhibiting the aggregation of an early folding intermediate into the kinetically trapped...

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Identifiers

PMID: 1648264
DOI: 10.1126/science.1648264

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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Global suppression of protein folding defects and inclusion body formation.PMID 1648264Read ↗

Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein.Semantic proximity Read ↗

Intragenic suppressors of folding defects in the P22 tailspike protein.Semantic proximity Read ↗

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

A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Semantic proximity Read ↗

Mechanistic insights into global suppressors of protein folding defects.Semantic proximity Read ↗

Suppressor mutations derived from the most severe protein folding mutation known.Semantic proximity Read ↗

A tail of protein folding.Semantic proximity Read ↗

Isolation of suppressors of temperature-sensitive folding mutations.Semantic proximity Read ↗

Invivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes.Semantic proximity Read ↗

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

Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.Semantic proximity Read ↗

Genetic properties of temperature-sensitive folding mutants of the coat protein of phage P22.Semantic proximity Read ↗

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