Evidence map›Paper›PMID 38648680›Full record

ReviewCurrent opinion in structural biology2024

Investigations of membrane protein interactions in cells using fluorescence microscopy.

Mahmoud Abouelkheir, Tanaya Roy, Mateusz A Krzyscik, Ece Özdemir, Kalina Hristova

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current opinion in structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Endogenous forms of ATP-ATPProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. 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 at 1 institution in 1 country.

Mahmoud AbouelkheirDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore MD 21218, USA; Chemistry-Biology Interface Program, Johns Hopkins University, Baltimore MD 21218, USA.
Tanaya RoyDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore MD 21218, USA.
Mateusz A KrzyscikDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore MD 21218, USA.
Ece ÖzdemirDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore MD 21218, USA.
Kalina HristovaDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore MD 21218, USA; Chemistry-Biology Interface Program, Johns Hopkins University, Baltimore MD 21218, USA. Electronic address: kh@jhu.edu.
Johns Hopkins University · US

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM149382 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI STEVEN E ROKITA · 2023 to 2026
$1.4M
NIGMS NIH HHS R01 GM068619NIGMS NIH HHS T32 GM080189NIGMS NIH HHS T32 GM149382
6 · The paper itself

Abstract

The interactions between proteins in membranes govern many cellular functions. Our ability to probe for such interactions has greatly evolved in recent years due to the introduction of new fluorescence techniques. As a result, we currently have a choice of methods that can be used to assess the spatial distribution of a membrane protein, its association state, and the thermodynamic stability of the oligomers in the native milieu. These biophysical measurements have revealed new insights into important biological processes in cellular membranes.

Indexed as

Membrane ProteinsMicroscopy, FluorescenceAnimalsCell MembraneHumansProtein BindingMembrane ProteinsFluorescenceInteractionsMembrane proteinsReceptors

Identifiers

PMID38648680
PMCPMC11141325
OpenAlexW4394984344

What Socratic 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 Socratic graph.