ArticleCell stress & chaperones2012
The identification and characterization of IbpA, a novel α-crystallin-type heat shock protein from mycoplasma.
Article in Cell stress & chaperones, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Molecular Equilibrist: The Small Heat Shock Protein IbpA from Mycoplasma.Biomolecules · 2026Article
- The Functionality of IbpA fromInternational journal of molecular sciences · 2023Article
- Reorganization of Cell Compartmentalization Induced by Stress.Biomolecules · 2022Review
- Stress-Induced Membraneless Organelles in Eukaryotes and Prokaryotes: Bird's-Eye View.International journal of molecular sciences · 2022Review
- N- and C-terminal regions of the small heat shock protein IbpA fromRSC advances · 2020Article
- Unraveling the Molecular Mechanism of Selective Antimicrobial Activity of 2(5International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Crystallin-type small heat shock proteins (sHsps) are expressed in many bacteria, animals, plants, and archaea. Among mycoplasmas (Mollicutes), predicted sHsp homologues so far were found only in the Acholeplasmataceae family. In this report, we describe the cloning and functional characterization of a novel sHsp orthologue, IbpA protein, present in Acholeplasma laidlawii. Importantly, similar to the endogenously expressed sHsp proteins, the recombinant IbpA protein was able to spontaneously generate oligomers in vitro and to rescue chemically denatured bovine insulin from irreversible denaturation and aggregation. Collectively, these data suggest that IbpA is a bona fide member of the sHsps family. The immune-electron microscopy data using specific antibodies against IbpA have revealed different intracellular localization of this protein in A. laidlawii cells upon heat shock, which suggests that IbpA not only may participate in the stabilization of individual polypeptides, but may also play a protective role in the maintenance of various cellular structures upon temperature stress.
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Registered trials
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