Evidence map›Paper›PMID 28297680›Full record

ArticleCell reports2017

Measurement of Rapid Protein Diffusion in the Cytoplasm by Photo-Converted Intensity Profile Expansion.

Rotem Gura Sadovsky, Shlomi Brielle, Daniel Kaganovich, Jeremy L England

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.4field-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

24 citing papers in PubMed, 49 citations in OpenAlex.

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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 at 3 institutions in 2 countries.

Rotem Gura SadovskyPhysics of Living Systems Group, Massachusetts Institute of Technology, Cambridge, MA 02138, USA; Computational and Systems Biology Graduate Program, Massachusetts Institute of Technology, Cambridge, MA 02138, USA.
Shlomi BrielleDepartment of Cell and Developmental Biology, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel; Alexander Grass Center for Bioengineering, Hebrew University of Jerusalem, Jerusalem 91904, Israel.
Daniel KaganovichDepartment of Cell and Developmental Biology, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel. Electronic address: dan@cc.huji.ac.il.
Jeremy L EnglandPhysics of Living Systems Group, Massachusetts Institute of Technology, Cambridge, MA 02138, USA. Electronic address: jengland@mit.edu.
Hebrew University of Jerusalem · ILLiving Systems (United States) · USMassachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fluorescence microscopy methods presently used to characterize protein motion in cells infer protein motion from indirect observables, rather than measuring protein motion directly. Operationalizing these methods requires expertise that can constitute a barrier to their broad utilization. Here, we have developed PIPE (photo-converted intensity profile expansion) to directly measure the motion of tagged proteins and quantify it using an effective diffusion coefficient. PIPE works by pulsing photo-convertible fluorescent proteins, generating a peaked fluorescence signal at the pulsed region, and analyzing the spatial expansion of the signal. We demonstrate PIPE's success in measuring accurate diffusion coefficients in silico and in vitro and compare effective diffusion coefficients of native cellular proteins and free fluorophores in vivo. We apply PIPE to measure diffusion anomality in the cell and use it to distinguish free fluorophores from native cellular proteins. PIPE's direct measurement and ease of use make it appealing for cell biologists.

Indexed as

LightAnimalsChlorocebus aethiopsComputer SimulationCOS CellsCytoplasmDiffusionGreen Fluorescent ProteinsPhotochemistryProteinsReproducibility of ResultsSolutionsGreen Fluorescent ProteinsProteinsSolutionsanomalous diffusionfluorescence-based techniquesmolecular crowdingmolecular diffusionphoto-conversionprotein aggregationprotein mobilityprotein oligomerizationprotein quality controlSod1

Identifiers

PMID28297680
PMCPMC5368347
OpenAlexW2528370140

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.