ArticleMethods in molecular biology (Clifton, N.J.)2026
Sortase A Catalyzed Transpeptidation for Protein Bioengineering.
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
Sortase A, originating from Staphylococcus Aureus, has become the gold standard for site-specific transpeptidation of protein substrates. Wild-type and engineered variants of sortase A catalyze the recognition and cleavage of a five-amino acid substrate motif (LPxTG), followed by transpeptidation with oligoglycine nucleophiles (peptides that contain one or more glycines at their N-terminus). This LPxTG sortagging motif can be introduced by genetic engineering of recombinantly expressed proteins of interest. Oligoglycine nucleophiles can be readily synthesized on solid-phase resin and allow the introduction of a wide range of functional groups. Here, we describe the transpeptidation of two nanobodies (VHHs, variable region of the heavy chain of heavy-chain only antibodies) with various GGG-nucleophiles.
Indexed as
Identifiers
42542487What 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.