Evidence map›Paper›PMID 28191954›Full record

ArticleThe journal of physical chemistry letters2017

Glycosylation and Lipids Working in Concert Direct CD2 Ectodomain Orientation and Presentation.

Anirban Polley, Adam Orłowski, Reinis Danne, Andrey A Gurtovenko, Jorge Bernardino de la Serna, Christian Eggeling, Simon J Davis, Tomasz Róg, Ilpo Vattulainen

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Review
  7. Article
  8. CD2 Immunobiology.Frontiers in immunology · 2020
    Review
  9. Article
  10. Article
  11. Review
  12. Article
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  15. Review
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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

9 authors at 6 institutions in 5 countries.

Anirban PolleyDepartment of Physics, Tampere University of Technology , Korkeakoulunkatu 10, P.O. Box 692, FI-33101 Tampere, Finland.
Adam OrłowskiDepartment of Physics, Tampere University of Technology , Korkeakoulunkatu 10, P.O. Box 692, FI-33101 Tampere, Finland.ORCID http://orcid.org/0000-0003-1599-1022
Reinis DanneDepartment of Physics, Tampere University of Technology , Korkeakoulunkatu 10, P.O. Box 692, FI-33101 Tampere, Finland.
Andrey A GurtovenkoInstitute of Macromolecular Compounds, Russian Academy of Sciences , Bolshoi Prospect V.O. 31, St. Petersburg, 199004 Russia.
Jorge Bernardino de la SernaScience and Technology Facilities Council , Rutherford Appleton Laboratory, Central Laser Facility, Research Complex at Harwell, Harwell-Oxford Campus, OX11 0FA Didcot, United Kingdom.ORCID http://orcid.org/0000-0002-1396-3338
Christian EggelingMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford , Headley Way, OX3 9DS Oxford, United Kingdom.
Simon J DavisMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford , Headley Way, OX3 9DS Oxford, United Kingdom.
Tomasz RógDepartment of Physics, Tampere University of Technology , Korkeakoulunkatu 10, P.O. Box 692, FI-33101 Tampere, Finland.ORCID http://orcid.org/0000-0001-6765-7013
Ilpo VattulainenDepartment of Physics, Tampere University of Technology , Korkeakoulunkatu 10, P.O. Box 692, FI-33101 Tampere, Finland.ORCID http://orcid.org/0000-0001-7408-3214
Tampere University · FIUniversity of Helsinki · FIUniversity of Oxford · GBRutherford Appleton Laboratory · GBSt Petersburg University · RUUniversity of Limerick · IE

Funding

Medical Research Council G0902418Medical Research Council MC_EX_MR/K015591/1Medical Research Council MC_UU_00008/4Medical Research Council MC_UU_00008/9Medical Research Council MC_UU_12010/4Medical Research Council MC_UU_12010/9Medical Research Council MR/K01577X/1Wellcome Trust 207547/Z/17/Z
6 · The paper itself

Abstract

Proteins embedded in the plasma membrane mediate interactions with the cell environment and play decisive roles in many signaling events. For cell-cell recognition molecules, it is highly likely that their structures and behavior have been optimized in ways that overcome the limitations of membrane tethering. In particular, the ligand binding regions of these proteins likely need to be maximally exposed. Here we show by means of atomistic simulations of membrane-bound CD2, a small cell adhesion receptor expressed by human T-cells and natural killer cells, that the presentation of its ectodomain is highly dependent on membrane lipids and receptor glycosylation acting in apparent unison. Detailed analysis shows that the underlying mechanism is based on electrostatic interactions complemented by steric interactions between glycans in the protein and the membrane surface. The findings are significant for understanding the factors that render membrane receptors accessible for binding and signaling.

Identifiers

PMID28191954
PMCPMC5445502
OpenAlexW2588089291

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.