ArticleMethods in molecular biology (Clifton, N.J.)2026
Engineering and Adapting Disulfide-Containing Proteins to Enable Intracellular Functionality.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide bonds are key structural components ensuring proper protein folding. Those bonds, however, do not form in the reducing intracellular environment, often resulting in misfolded, unstable proteins with subpar function. To enable intracellular functionality of such proteins, disulfide-free variants with restored stability and function should be engineered. Here, we present a method to substitute the cysteine residues with optimal amino acid combinations using site saturation mutagenesis and screening for improved disulfide-free variants using yeast surface display. We provide a detailed protocol to directly screen for thermal stability of proteins using conformationally specific ligands, and an alternative to harness the correlation between protein stability and expression levels in yeast. We also discuss different strategies for randomizing cysteine residues and approaches for handling proteins with multiple disulfide bonds.
Indexed as
Identifiers
42400845What 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.