ArticleThe Journal of biological chemistry2018
Disulfide isomerase activity of the dynamic, trimeric
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 19 citations in OpenAlex.
- 2023 update of template tables for reporting biomolecular structural modelling of small-angle scattering data.Acta crystallographica. Section D, Structural biology · 2023Article
- Production and characterisation of modularly deuterated UBE2D1-Ub conjugate by small angle neutron and X-ray scattering.European biophysics journal : EBJ · 2022Article
- The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity.Acta crystallographica. Section D, Structural biology · 2022Article
- Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.Journal of molecular biology · 2020Review
- The Scs disulfide reductase system cooperates with the metallochaperone CueP inThe Journal of biological chemistry · 2019Article
- Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.Acta crystallographica. Section D, Structural biology · 2019Article
- The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase.Acta crystallographica. Section D, Structural biology · 2019Article
- CpxR/CpxA ControlsJournal of bacteriology · 2018Article
- Stress control for a well-structured life.The Journal of biological chemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Correct disulfide bond formation is essential for proper folding of many proteins, including bacterial virulence factors. The suppressor of copper sensitivity (Scs) proteins have roles in dithiol/disulfide interchange and the bacterial response to copper stress. Encoded in a four-gene cassette (ScsABCD) present in many Gram-negative bacteria, the Scs proteins are enigmatic and poorly characterized. Here, we show that the periplasmic α-domain of the membrane protein ScsB in the Gram-negative bacterium
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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.