Evidence map›Paper›PMID 20080967›Full record

ArticleThe Journal of biological chemistry2010

Differential mechanisms of shedding of the glycosylphosphatidylinositol (GPI)-anchored NKG2D ligands.

Lola Fernández-Messina, Omodele Ashiru, Philippe Boutet, Sonia Agüera-González, Jeremy N Skepper, Hugh T Reyburn, Mar Valés-Gómez

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

91 citing papers in PubMed, 159 citations in OpenAlex.

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31 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 1 institution in 1 country.

Lola Fernández-MessinaDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.
Omodele Ashiru
Philippe Boutet
Sonia Agüera-González
Jeremy N Skepper
Hugh T Reyburn
Mar Valés-Gómez
University of Cambridge · GB

Funding

Medical Research Council G0601165Medical Research Council G9800943
6 · The paper itself

Abstract

Tumor cells release NKG2D ligands to evade NKG2D-mediated immune surveillance. The purpose of our investigation was to explore the cellular mechanisms of release used by various members of the ULBP family. Using biochemical and cellular approaches in both transfectant systems and tumor cell lines, this paper shows that ULBP1, ULBP2, and ULBP3 are released from cells with different kinetics and by distinct mechanisms. Whereas ULBP2 is mainly shed by metalloproteases, ULBP3 is abundantly released as part of membrane vesicles known as exosomes. Interestingly, exosomal ULBP3 protein is much more potent for down-modulation of the NKG2D receptor than soluble ULBP2 protein. This is the first report showing functionally relevant differences in the biochemistry of the three members of the ULBP family and confirms that in depth study of the biochemical features of individual NKG2D ligands will be necessary to understand and manipulate the biology of these proteins for therapy.

Indexed as

LigandsAnimalsBiochemistryCell LineCHO CellsCricetinaeCricetulusExosomesFlow CytometryGlycosylphosphatidylinositolsGPI-Linked ProteinsHumansImmune SystemIntercellular Signaling Peptides and ProteinsKineticsModels, BiologicalGlycosylphosphatidylinositolsGPI-Linked ProteinsIntercellular Signaling Peptides and ProteinsKLRK1 protein, humanLigandsNK Cell Lectin-Like Receptor Subfamily KULBP3 protein, human

Identifiers

PMID20080967
PMCPMC2838276
OpenAlexW2046701977

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.