Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Rescue of deleterious mutations by the compensatory Y30F mutation in ketosteroid isomerase.

Molecules and cells - 1 Jul 2013

Cha Hyung Jin, Jang Do Soo, Kim Yeon-Gil, Hong Bee Hak, Woo Jae-Sung, Kim Kyong-Tai, Choi Kwan Yong

Abstract excerpt

Proteins have evolved to compensate for detrimental mutations. However, compensatory mechanisms for protein defects are not well understood. Using ketosteroid isomerase (KSI), we investigated how second-site mutations could recover defective mutant function and stability. Previous results reveale...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biocatalysis
Share to Enzyme Stability
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isomerism

Share to Mutant Proteins

Share to Pseudomonas putida

Share to Steroid Isomerases

Source

Open in PubMed Open full text

Identifiers

PMID: 23740430
DOI: 10.1007/s10059-013-0013-1
PMCID: PMC3887930

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23740430-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rescue of deleterious mutations by the compensatory Y30F mutation in ketosteroid isomerase.PMID 23740430Read ↗

Compensatory mutations in the L30e kink-turn RNA-protein complex.Semantic proximity Read ↗

Isolation of Temperature-sensitive p53 Mutations from a Comprehensive Missense Mutation LibrarySemantic proximity Read ↗

Maintenance of alpha-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B.Semantic proximity Read ↗

Evaluating the catalytic contribution from the oxyanion hole in ketosteroid isomerase.Semantic proximity Read ↗

A Critical Test of the Electrostatic Contribution to Catalysis with Noncanonical Amino Acids in Ketosteroid Isomerase.Semantic proximity Read ↗

Characterization of six mutations in five Spanish patients with mitochondrial acetoacetyl-CoA thiolase deficiency: effects of amino acid substitutions on tertiary structure.Semantic proximity Read ↗

Mutant protein chemical rescue: From mechanisms to therapeutics.Semantic proximity Read ↗

Evaluation of the Catalytic Contribution from a Positioned General Base in Ketosteroid Isomerase.Semantic proximity Read ↗

Role of conserved Met112 residue in the catalytic activity and stability of ketosteroid isomerase.Semantic proximity Read ↗

Chemical rescue of mutant proteins in living Saccharomyces cerevisiae cells by naturally occurring small molecules.Semantic proximity Read ↗

Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B.Semantic proximity Read ↗

Kemp Eliminase Activity of Ketosteroid Isomerase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.