Evidence map›Paper›PMID 28402886›Full record

ArticleBiophysical journal2017

Three-Dimensional Super-Resolution in Eukaryotic Cells Using the Double-Helix Point Spread Function.

Alexander R Carr, Aleks Ponjavic, Srinjan Basu, James McColl, Ana Mafalda Santos, Simon Davis, Ernest D Laue, David Klenerman, Steven F Lee

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Volumetric Single-Molecule Tracking Inside Subcellular Structures.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
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  15. Real-Time Feedback-Driven Single-Particle Tracking: A Survey and Perspective.Small (Weinheim an der Bergstrasse, Germany) · 2022
    Review
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  20. A cell topography-based mechanism for ligand discrimination by the T cell receptor.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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 3 institutions in 1 country.

Alexander R CarrDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Aleks PonjavicDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Srinjan BasuDepartment of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
James McCollDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Ana Mafalda SantosRadcliffe Department of Clinical Medicine and Medical Research Council Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, United Kingdom.
Simon DavisRadcliffe Department of Clinical Medicine and Medical Research Council Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, United Kingdom.
Ernest D LaueDepartment of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
David KlenermanDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Steven F LeeDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom. Electronic address: sl591@cam.ac.uk.
University of Cambridge · GBMRC Human Immunology Unit · GBUniversity of Oxford · GB

Funding

Medical Research Council MC_UU_12010/4Medical Research Council MR/M010082/1Medical Research Council MR/P019471/1Wellcome Trust 206291/Z/17/ZWellcome Trust 207547/Z/17/Z
6 · The paper itself

Abstract

Single-molecule localization microscopy, typically based on total internal reflection illumination, has taken our understanding of protein organization and dynamics in cells beyond the diffraction limit. However, biological systems exist in a complicated three-dimensional environment, which has required the development of new techniques, including the double-helix point spread function (DHPSF), to accurately visualize biological processes. The application of the DHPSF approach has so far been limited to the study of relatively small prokaryotic cells. By matching the refractive index of the objective lens immersion liquid to that of the sample media, we demonstrate DHPSF imaging of up to 15-μm-thick whole eukaryotic cell volumes in three to five imaging planes. We illustrate the capabilities of the DHPSF by exploring large-scale membrane reorganization in human T cells after receptor triggering, and by using single-particle tracking to image several mammalian proteins, including membrane, cytoplasmic, and nuclear proteins in T cells and embryonic stem cells.

Indexed as

AlgorithmsImaging, Three-DimensionalAnimalsCalibrationCell NucleusDiffusionEukaryotic CellsFluorescenceHumansJurkat CellsMiceMouse Embryonic Stem CellsT-Lymphocytes

Identifiers

PMID28402886
PMCPMC5390298
OpenAlexW2607476891

What OpenQuestion 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 OpenQuestion graph.