ArticleBiomolecular NMR assignments2026
Article in Biomolecular NMR assignments, 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
3 authors.
Funding
Abstract
Knotted Methyltransferases (MTase) from the SpoU-TrmD (SPOUT) family offer a unique opportunity to study a protein knot topology and enzymatic function. The knotted methyltransferase from Staphylococcus aureus, MTTSA (PDB: 1vh0, 4fak), is an ɑ/β-knotted 23s rRNA MTase containing only the minimal scaffold among the SPOUT family members. This dimeric enzyme is a minimalist model to study the deep + 31 knot. Here, we report the non-proline backbone assignments with 98.8% completion using TROSY-based NMR experiments on uniformly labeled 2H/13C/15N-labeled protein. Complementary HBHA(CO)NH experiments on 13C/15N-labeled protein were completed for Hα/Hβ sidechain assignments. Both backbone and sidechain assignments were deposited in the Biological Magnetic Resonance Bank (BMRB ID: 53391). Of 164 assigned residues, TALOS-N predictions provided 88.4% unambiguous assignments based on the HN, Hα, Cα, Cβ and N chemical shifts. In addition, the predicted secondary structure based on torsion angles and the ΔδCα-ΔδCβ profile are in agreement with the crystal structures.
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.