ArticleJournal of basic microbiology2010
Characterization of an unusual cold shock protein from Staphylococcus aureus.
Article in Journal of basic microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Multi-omics revealed antibacterial mechanisms of licochalcone A against MRSA and its antimicrobic potential on pork meat.Food chemistry: X · 2024Article
- From freezing to functioning: cellular strategies of cold-adapted bacteria for surviving in extreme environments.Archives of microbiology · 2024Review
- Overlapping and Distinct Functions of the Paralogous PagR Regulators of Bacillus anthracis.Journal of bacteriology · 2022Article
- Selected Metabolites Profiling ofFrontiers in microbiology · 2020Article
- Adaptive Metabolism in Staphylococci: Survival and Persistence in Environmental and Clinical Settings.Journal of pathogens · 2018Review
- Identification and characterization of an operon, msaABCR, that controls virulence and biofilm development in Staphylococcus aureus.BMC microbiology · 2014Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Of the three cold shock proteins expressed by Staphylococcus aureus, CspC is induced poorly by cold but strongly by various antibiotics and toxic chemicals. Using a purified CspC, here we demonstrate that it exists as a monomer in solution, possesses primarily β-sheets, and bears substantial structural similarity with other bacterial Csps. Aggregation of CspC was initiated rapidly at temperatures above 40 °C, whereas, the Gibbs free energy of stabilization of CspC at 0 M GdmCl was estimated to be +1.6 kcal mol(-1), indicating a less stable protein. Surprisingly, CspC showed stable binding with ssDNA carrying a stretch of more than three thymine bases and binding with such ssDNA had not only stabilized CspC against proteolytic degradation but also quenched the fluorescence intensity from its exposed Trp residue. Analysis of quenching data indicates that each CspC molecule binds with ∼5 contiguous thymine bases of the above ssDNA and binding is cooperative in nature.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.