Evidence map›Paper›PMID 40181024›Full record

ArticleScientific data2025

Fast Single-Particle Tracking of Membrane Proteins Combined with Super-Resolution Imaging of Actin Nanodomains.

Hanieh Mazloom-Farsibaf, William K Kanagy, Diane S Lidke, Keith A Lidke

Abstract readDataset
In one paragraph

Article in Scientific data, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

4 authors.

Hanieh Mazloom-FarsibafDepartment of Physics and Astronomy, University of New Mexico, Albuquerque, New Mexico, USA. hanieh.mazloomfarsibaf@utsouthwestern.edu.ORCID http://orcid.org/0000-0002-2571-0418
William K KanagyDepartment of Pathology, University of New Mexico, Albuquerque, New Mexico, USA.
Diane S LidkeDepartment of Pathology, University of New Mexico, Albuquerque, New Mexico, USA.
Keith A LidkeDepartment of Physics and Astronomy, University of New Mexico, Albuquerque, New Mexico, USA. klidke@unm.edu.

Funding

UNM TRAININGP50GM085273 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI LIDKE, KEITH A · 2009 to 2018
$26.1M
TRAINING GRANT IN MICROBIOLOGY/CANCER RESEARCHT32CA009138 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI Scott M. Dehm · 1985 to 2026
$11.3M
Imaging the Early Events in Membrane Receptor SignalingR35GM126934 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Diane Lidke · 2018 to 2026
$3.1M
Adaptive Tracking and Quantum Imaging for Protein-Protein InteractionsR01GM140284 · NIGMS · UNIVERSITY OF NEW MEXICO · PI BECERRA CHAVEZ, FRANCISCO ELOHIM, LIDKE, KEITH A · 2022 to 2025
$1.8M
Structural and Functional Interactions within the Neuronal ER/PM JunctionR01GM109888 · NIGMS · COLORADO STATE UNIVERSITY · PI BEAM, KURT G, KRAFT, MARY L · 2014 to 2017
$1.5M
NCI NIH HHS T32 CA009138NIGMS NIH HHS P50 GM085273NIGMS NIH HHS R01 GM109888NIGMS NIH HHS R01 GM140284NIGMS NIH HHS R35 GM126934U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM109888U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM126934
6 · The paper itself

Abstract

Membrane protein dynamics regulates cell functions by initiating downstream signaling cascades. The cell membrane is compartmentalized into nanodomains by actin structures, restricting lateral protein diffusion. Single-particle tracking offers high spatiotemporal resolution for studying protein dynamics in living cells. However, directly observing actin filaments that form barriers of nanodomains for fast protein diffusion is challenging due to their size being below the diffraction limit. Single-molecule localization microscopy resolves these structures but requires imaging in fixed cells. We integrated fast single-particle tracking with single-molecule localization microscopy to generate a dataset of membrane protein dynamics and actin filaments within the same cells at the nanoscales. Optimizing the fixation protocol enabled transition from live-cell tracking to fixed-cell super-resolution imaging. Data for the high-affinity IgE receptor, a transmembrane protein, and the GPI-anchored protein, an outer leaflet protein, was collected at 490 Hz. After fixation, actin filaments were imaged using dSTORM. The treatment of actin structures with phalloidin and PMA generated a dataset of distinct actin architectures for studying their potential influence on membrane protein dynamics.

Indexed as

Actin CytoskeletonActinsMembrane ProteinsSingle Molecule ImagingAnimalsHumansActinsMembrane Proteins

Identifiers

PMID40181024
PMCPMC11968936

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.