Evidence map›Paper›PMID 1351678›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

Spontaneous incorporation of the glycosyl-phosphatidylinositol-linked protein Thy-1 into cell membranes.

F Zhang, W G Schmidt, Y Hou, A F Williams, K Jacobson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. 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
3.5field-weighted citation impact, top 6% 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, 86 citations in OpenAlex.

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  8. Microvesicles/exosomes as potential novel biomarkers of metabolic diseases.Diabetes, metabolic syndrome and obesity : targets and therapy · 2012
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  20. Construction, purification, and functional incorporation on tumor cells of glycolipid-anchored human B7-1 (CD80).Proceedings of the National Academy of Sciences of the United States of America · 1995
    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.

F ZhangDepartment of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599-7090.
W G Schmidt
Y Hou
A F Williams
K Jacobson
University of North Carolina at Chapel Hill · US

Funding

NIGMS NIH HHS GM41402
6 · The paper itself

Abstract

Thy-1 is a membrane protein that is attached to the plasma membrane by a glycosyl-phosphatidylinositol anchor. Purified rat brain Thy-1 could be reincorporated into the plasma membrane of murine Thy-1- cells directly from aqueous suspension and without the use of detergents. A peripheral staining pattern similar to that observed for endogenous Thy-1 was achieved. Treatment with phosphatidylinositol-specific phospholipase C removed nearly all antibody staining due to either endogenous or inserted Thy-1. Fluorescence recovery after photobleaching (FRAP) was used to compare the lateral mobility of endogenous and inserted Thy-1. Both forms exhibited large lateral diffusion coefficients, but with a substantial immobile fraction (approximately 50%) indicating that the immobile fraction was not due either to chemical differences between inserted and native Thy-1 or to some surface Thy-1 molecules having a protein anchor. However, the inserted Thy-1 failed to activate mouse T lymphocytes upon crosslinking as assayed by [3H]thymidine uptake. Since Thy-1 could be directly labeled with rhodamine, the effect of the size of the labeling ligand on the mobility obtained by the FRAP technique could be explored. Rhodamine-conjugated MRC-OX7 monoclonal antibody or its fragments [R-F(ab)2 or R-Fab] were compared with rhodamine as labels for Thy-1. The measured diffusion coefficients were 1.6 x 10(-9), 2.0 x 10(-9), and 3.2 x 10(-9) cm2/sec for Thy-1 labeled with R-F(ab)2, R-Fab, and rhodamine, respectively; mobile fractions were all in the 40-50% range. Thus, the size of the ligand affects the lateral mobility of this labeled membrane protein to a measurable extent.

Indexed as

AnimalsAntibodies, MonoclonalAntigens, SurfaceBrainCell LineCell MembraneGlycolipidsGlycosylphosphatidylinositolsLymphocyte ActivationLymphomaMembrane GlycoproteinsMiceMice, Inbred AKRPhosphatidylinositol Diacylglycerol-LyasePhosphatidylinositolsPhosphoinositide Phospholipase CAntibodies, MonoclonalAntigens, SurfaceGlycolipidsGlycosylphosphatidylinositolsMembrane GlycoproteinsPhosphatidylinositol Diacylglycerol-LyasePhosphatidylinositolsPhosphoinositide Phospholipase CPhosphoric Diester HydrolasesThy-1 Antigens

Identifiers

PMID1351678
PMCPMC49265
OpenAlexW2023235169

What OpenQuestion holds

Textmetadata
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.