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Article

Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA.

The Journal of biological chemistry - 15 Aug 1992

Ondek B, Hardy R W, Baker E K, Stamnes M A, Shieh B H, Zuker C S

Abstract excerpt

Cyclophilins, the intracellular receptors for the widely used immunosuppressant cyclosporin A have been found to be peptidyl-prolyl cis/trans isomerases and have been implicated in intracellular protein folding and trafficking. The Drosophila ninaA gene encodes a photoreceptor-specific cyclophilin homolog involved in rhodopsin biogenesis. ninaA mutants have a 90% reduction in the levels of Rh1 rhodopsin. To gain...

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PMID: 1644830

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Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA.PMID 1644830Read ↗

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The cyclophilin homolog ninaA is required in the secretory pathway.Semantic proximity Read ↗

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Differential loss of prolyl isomerase or chaperone activity of Ran-binding protein 2 (Ranbp2) unveils distinct physiological roles of its cyclophilin domain in proteostasis.Semantic proximity Read ↗

Innexins: members of an evolutionarily conserved family of gap-junction proteins.Semantic proximity Read ↗

Peptidyl-prolyl cis-trans isomerases, cyclophilin, FK506-binding protein, and ninaA: four of a kind.Semantic proximity Read ↗

Genetic deficiency and polymorphisms of cyclophilin A reveal its essential role for Human Coronavirus 229E replication.Semantic proximity Read ↗

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