ArticleNucleic acids research2025
TmDet 4.0: determining membrane orientation of transmembrane proteins from 3D structure.
Article in Nucleic acids research, 2025. 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
Abstract
During the structural determination of transmembrane proteins, one crucial piece of information is lost: the orientation of the protein within the lipid bilayer. The TmDet algorithm was developed in the early 2000s to determine the relative position of membrane proteins with respect to the lipid bilayer using the atomic coordinates of the protein. In the past 20 years, new types of transmembrane protein structures have emerged, such as the bacterial multidrug efflux pump, which is embedded in both the outer and inner membranes, or the piezo-type mechanosensitive ion channel, which is in a highly curved membrane. The breakthrough of artificial intelligence in protein structure prediction in recent years has also brought a new challenge to the field of transmembrane proteins; How can we determine the accuracy of a model structure if the actual three-dimensional structure of the protein is unknown? How can we determine the membrane orientation of a modeled transmembrane protein structure if the model contains errors? The new TmDet web server, available at https://tmdet.unitmp.org, provides answers to all these challenges, allowing researchers to determine how a transmembrane protein is in the membrane, to obtain information about the type of structural elements, and to determine whether the modeled structure can be embedded into the membrane.
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.