ArticleBiochemistry2013
Internal disulfide bond acts as a switch for intein activity.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 31 citations in OpenAlex.
- Conditional protein splicing of the Mycobacterium tuberculosis RecA intein in its native host.Scientific reports · 2024Article
- Conditional protein splicing of thebioRxiv : the preprint server for biology · 2024Article
- Conditional Alternative Protein Splicing Promoted by Inteins fromBiochemistry · 2022Article
- The Evolution of Intein-Based Affinity Methods as Reflected in 30 years of Patent History.Frontiers in molecular biosciences · 2022Review
- Protein Splicing Activity of theBiochemistry · 2020Article
- Methods to Study the Structure and Catalytic Activity of cis-Splicing Inteins.Methods in molecular biology (Clifton, N.J.) · 2020Article
- A mesophilic cysteine-less split intein for proteinProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Spliceosomal Prp8 intein at the crossroads of protein and RNA splicing.PLoS biology · 2019Article
- Mycobacterial DnaB helicase intein as oxidative stress sensor.Nature communications · 2018Article
- Review
- Article
- Thiol-based redox switches.Biochimica et biophysica acta · 2014Review
- Enigmatic distribution, evolution, and function of inteins.The Journal of biological chemistry · 2014Review
- Protein splicing: how inteins escape from precursor proteins.The Journal of biological chemistry · 2014Review
- 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
8 authors at 2 institutions in 1 country.
Funding
Abstract
Inteins are intervening polypeptides that catalyze their own removal from flanking exteins, concomitant to the ligation of the exteins. The intein that interrupts the DP2 (large) subunit of DNA polymerase II from Methanoculleus marisnigri (Mma) can promote protein splicing. However, protein splicing can be prevented or reduced by overexpression under nonreducing conditions because of the formation of a disulfide bond between two internal intein Cys residues. This redox sensitivity leads to differential activity in different strains of E. coli as well as in different cell compartments. The redox-dependent control of in vivo protein splicing in an intein derived from an anaerobe that can occupy multiple environments hints at a possible physiological role for protein splicing.
Indexed as
Identifiers
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.