Evidence map›Paper›PMID 15173190›Full record

ArticleThe Journal of cell biology2004

Dynamics of putative raft-associated proteins at the cell surface.

Anne K Kenworthy, Benjamin J Nichols, Catha L Remmert, Glenn M Hendrix, Mukesh Kumar, Joshua Zimmerberg, Jennifer Lippincott-Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 223 papers.

0numbers the graph read from it
0cells of the map it votes in
223citing papers in PubMed
15.5field-weighted citation impact, top 1% 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

223 citing papers in PubMed, 450 citations in OpenAlex.

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  14. Sensitive and selective polymer condensation at membrane surface driven by positive co-operativity.Proceedings of the National Academy of Sciences of the United States of America · 2023
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163 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Anne K KenworthyCell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bldg. 18T, Rm. 101, 18 Library Dr., Bethesda, MD 20895, USA.
Benjamin J Nichols
Catha L Remmert
Glenn M Hendrix
Mukesh Kumar
Joshua Zimmerberg
Jennifer Lippincott-Schwartz
National Institutes of Health · USVanderbilt University · USMedical Research Council · GB

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI OWEN P MCGUINNESS · 2012 to 2026
$29.3M
TRANSGENIC MOUSE/ ES CELL SHARES RESOURCESP60DK020593 · NIDDK · VANDERBILT UNIVERSITY · PI MCGUINNESS, OWEN P · 1986 to 2011
$28.1M
Secretory Membrane Trafficking/Sorting/CompartmentalizatZ01HD001609 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI LIPPINCOTT-SCHWARTZ, JENNIFER · 1992 to 2008
$3.1M
MEMBRANE TRANSPORT AND FUSIONZ01HD001409 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ZIMMERBERG, JOSHUA · 1991 to 2008
$2.8M
NCI NIH HHS CA68485NCI NIH HHS P30 CA068485NIDDK NIH HHS DK20593NIDDK NIH HHS DK58404NIDDK NIH HHS P30 DK020593NIDDK NIH HHS P30 DK058404NIDDK NIH HHS P60 DK020593Wellcome Trust
6 · The paper itself

Abstract

Lipid rafts are conceptualized as membrane microdomains enriched in cholesterol and glycosphingolipid that serve as platforms for protein segregation and signaling. The properties of these domains in vivo are unclear. Here, we use fluorescence recovery after photobleaching to test if raft association affects a protein's ability to laterally diffuse large distances across the cell surface. The diffusion coefficients (D) of several types of putative raft and nonraft proteins were systematically measured under steady-state conditions and in response to raft perturbations. Raft proteins diffused freely over large distances (> 4 microm), exhibiting Ds that varied 10-fold. This finding indicates that raft proteins do not undergo long-range diffusion as part of discrete, stable raft domains. Perturbations reported to affect lipid rafts in model membrane systems or by biochemical fractionation (cholesterol depletion, decreased temperature, and cholesterol loading) had similar effects on the diffusional mobility of raft and nonraft proteins. Thus, raft association is not the dominant factor in determining long-range protein mobility at the cell surface.

Indexed as

beta-CyclodextrinsModels, BiologicalAnimalsCell LineChlorocebus aethiopsCholesterolCOS CellsCricetinaeCyclodextrinsDiffusionFluorescence Recovery After PhotobleachingMembrane LipidsMembrane MicrodomainsMembrane ProteinsNonlinear DynamicsRatsbeta-CyclodextrinsCholesterolCyclodextrinsMembrane LipidsMembrane Proteinsmethyl-beta-cyclodextrin

Identifiers

PMID15173190
PMCPMC2172371
OpenAlexW2023993671

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.