Evidence map›Paper›PMID 38264980›Full record

ArticleNano letters2024

Narrowing Signal Distribution by Adamantane Derivatization for Amino Acid Identification Using an α-Hemolysin Nanopore.

Xiaojun Wei, Dumei Ma, Junlin Ou, Ge Song, Jiawei Guo, Joseph W F Robertson, Yi Wang, Qian Wang, Chang Liu

Open access · greenAbstract read
In one paragraph

Article in Nano letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 16 citations in OpenAlex.

  1. RSC advances · 2026
    Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Xiaojun WeiDepartment of Biomedical Engineering, University of South Carolina, Columbia, South Carolina 29208, United States.ORCID 0000-0002-6229-6228
Dumei MaDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, United States.
Junlin OuDepartment of Mechanical Engineering, University of South Carolina, Columbia, South Carolina 29208, United States.ORCID 0000-0003-2735-5840
Ge SongDepartment of Mechanical Engineering, University of South Carolina, Columbia, South Carolina 29208, United States.ORCID 0000-0001-5679-0329
Jiawei GuoDepartment of Mechanical Engineering, University of South Carolina, Columbia, South Carolina 29208, United States.
Joseph W F RobertsonBiophysics and Biomedical Measurement Group, Microsystems and Nanotechnology Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, United States.ORCID 0000-0002-2087-3939
Yi WangDepartment of Mechanical Engineering, University of South Carolina, Columbia, South Carolina 29208, United States.ORCID 0000-0002-5750-3181
Qian WangDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, United States.ORCID 0000-0002-2149-384X
Chang LiuDepartment of Biomedical Engineering, University of South Carolina, Columbia, South Carolina 29208, United States.ORCID 0000-0001-8097-9631
University of South Carolina · USNational Institute of Standards and Technology · US

Funding

Nanopore-Based HIV Self-Test for Ultrasensitive p24 Quantification in FingerPrick BloodR61AI174295 · NIAID · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI LIU, CHANG · 2023 to 2025
$1.2M
A Solid-State Nanopore Biosensor for Rapid Detection of Mycobacterium tuberculosis Antigens in Pediatric Blood SamplesK22AI136686 · NIAID · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI LIU, CHANG · 2019 to 2020
$265k
NIAID NIH HHS K22 AI136686NIAID NIH HHS R61 AI174295
6 · The paper itself

Abstract

The rapid progress in nanopore sensing has sparked interest in protein sequencing. Despite recent notable advancements in amino acid recognition using nanopores, chemical modifications usually employed in this process still need further refinements. One of the challenges is to enhance the chemical specificity to avoid downstream misidentification of amino acids. By employing adamantane to label proteinogenic amino acids, we developed an approach to fingerprint individual amino acids using the wild-type α-hemolysin nanopore. The unique structure of adamantane-labeled amino acids (ALAAs) improved the spatial resolution, resulting in distinctive current signals. Various nanopore parameters were explored using a machine-learning algorithm and achieved a validation accuracy of 81.3% for distinguishing nine selected amino acids. Our results not only advance the effort in single-molecule protein characterization using nanopores but also offer a potential platform for studying intrinsic and variant structures of individual molecules.

Indexed as

Hemolysin ProteinsNanoporesAlgorithmsAmino AcidsAmino Acid SequenceAmino AcidsHemolysin ProteinsAdamantane derivatizationAmino acidSignal distributionα-Hemolysin nanopore

Identifiers

PMID38264980
PMCPMC10947511
OpenAlexW4391157056

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.