ArticleSmall (Weinheim an der Bergstrasse, Germany)2025
Conducting Atomic Force Microscopy of Protein Wires.
Article in Small (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Single-Molecule Conductance of Non-Redox Proteins: Mechanisms, Measurements, and Applications.Biomolecules · 2026Review
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
Scanning tunneling microscopy (STM) studies have shown that protein wires based on the consensus tetratricopetide repeat (CTPR) conduct with an electrical resistance proportional to length of the protein, consistent with long-range hopping transport along the long axis of the protein. However, the attempts to measure similar currents across proteins mounted in fixed-gap devices have not been successful. Here, the study reports conducting atomic force microscopy studies of CTPR8 and CTPR4, ≈8 and 4 nm in length, finding that substantial contact force (>50 nN) is required to observe conduction in CTPR8. Scrape-tests indicate that the probe penetrates the film by ≈1 nm at this force. Importantly, electrical contacts that resemble the STM data are rare-approximately 1% of all contacts. STM reports only successful contacts, so it does not predict statistically how the proteins will behave in a fixed junction.
Indexed as
Identifiers
What Socratic 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 Socratic graph.