Evidence map›Paper›PMID 40545238›Full record

ArticleJournal of lipid research2025

Nanodisc single-molecule pulldown to study lipid-protein interactions.

Adriana Reyes-Ordoñez, Shweta Shree, Nilmani Singh, Stephen G Sligar, Jie Chen

Abstract read
In one paragraph

Article in Journal of lipid research, 2025. 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
–field-weighted citation impact
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.

  1. Design of Fluorescent Membrane Scaffold Proteins for Nanodiscs.bioRxiv : the preprint server for biology · 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

5 authors.

Adriana Reyes-OrdoñezDepartment of Cell and Developmental Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Shweta ShreeDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Nilmani SinghCarl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Stephen G SligarDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA; Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA; Cancer Center at Illinois, University of Illinois at Urbana-Champaign, Urbana, IL, USA. Electronic address: s-sligar@illinois.edu.
Jie ChenDepartment of Cell and Developmental Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA; Cancer Center at Illinois, University of Illinois at Urbana-Champaign, Urbana, IL, USA; Department of Biomedical and Translational Sciences, Carle Illinois College of Medicine, University of Illinois at Urbana-Champaign, Urbana, IL, USA. Electronic address: jiechen@illinois.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Beyond serving structural roles in the cell membrane, many phospholipids, including phosphatidylinositol phosphates (PIPs), are key signaling molecules that regulate a myriad of cellular processes. Specific interactions with PIPs are crucial for the functions of many signaling proteins, highlighting the need for a convenient and robust method to study lipid-protein interactions. Previously, we established a fluorescence microscopy-based lipid single-molecule pulldown (lipid-SiMPull) assay for detecting interactions between fluorescently tagged proteins of interest in whole-cell lysates and small unilamellar vesicles containing phospholipids of interest. Despite unique advantages of the lipid-SiMPull assay, small unilamellar vesicle is not an optimal membrane model due to its instability, heterogeneity in size, and a membrane curvature inconsistent with the relative flatness of the cell membrane. Here, we report the use of lipid Nanodiscs in lipid-SiMPull. Using PIP-protein pairs of known interactions, we show that Nanodiscs containing various PIPs can pull down protein targets specifically, with an estimated detection threshold of K

Indexed as

NanostructuresSingle Molecule ImagingHumansPhosphatidylinositol PhosphatesProtein BindingPhosphatidylinositol PhosphatesAKTlipidNanodiscphosphatidylinositol phosphateSiMPullsingle-molecule

Identifiers

PMID40545238
PMCPMC12284033

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.