Evidence map›Paper›PMID 25690298›Full record

ArticleMolecules (Basel, Switzerland)2015

Nkrp1 family, from lectins to protein interacting molecules.

Daniel Rozbeský, Ljubina Ivanova, Lucie Hernychová, Valéria Grobárová, Petr Novák, Jan Černý

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.1field-weighted citation impact, top 48% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. 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

6 authors at 2 institutions in 1 country.

Daniel RozbeskýInstitute of Microbiology, v.v.i., Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 414220, Czech Republic. rozbesky@gmail.com.
Ljubina IvanovaInstitute of Microbiology, v.v.i., Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 414220, Czech Republic. ivanova@biomed.cas.cz.
Lucie HernychováInstitute of Microbiology, v.v.i., Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 414220, Czech Republic. valeria.grobarova@natur.cuni.cz.
Valéria GrobárováDepartment of Cell Biology, Faculty of Science, Charles University, Viničná 7, Prague 212843, Czech Republic. valeria.grobarova@natur.cuni.cz.
Petr NovákInstitute of Microbiology, v.v.i., Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 414220, Czech Republic. pnovak@biomed.cas.cz.
Jan ČernýDepartment of Cell Biology, Faculty of Science, Charles University, Viničná 7, Prague 212843, Czech Republic. valeria.grobarova@natur.cuni.cz.
Charles University · CZCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-type lectin-like receptors include the Nkrp1 protein family that regulates the activity of natural killer (NK) cells. Rat Nkrp1a was reported to bind monosaccharide moieties in a Ca2+-dependent manner in preference order of GalNac > GlcNAc >> Fuc >> Gal > Man. These findings established for rat Nkrp1a have been extrapolated to all additional Nkrp1 receptors and have been supported by numerous studies over the past two decades. However, since 1996 there has been controversy and another article showed lack of interactions with saccharides in 1999. Nevertheless, several high affinity saccharide ligands were synthesized in order to utilize their potential in antitumor therapy. Subsequently, protein ligands were introduced as specific binders for Nkrp1 proteins and three dimensional models of receptor/protein ligand interaction were derived from crystallographic data. Finally, for at least some members of the NK cell C-type lectin-like proteins, the "sweet story" was impaired by two reports in recent years. It has been shown that the rat Nkrp1a and CD69 do not bind saccharide ligands such as GlcNAc, GalNAc, chitotetraose and saccharide derivatives (GlcNAc-PAMAM) do not directly and specifically influence cytotoxic activity of NK cells as it was previously described.

Indexed as

Antigens, CDAntigens, Differentiation, T-LymphocyteKiller Cells, NaturalLectins, C-TypeNK Cell Lectin-Like Receptor Subfamily BOligosaccharidesAnimalsCD69 AntigensHumansMaleProtein Structure, TertiaryRatsAntigens, CDAntigens, Differentiation, T-LymphocyteCD69 AntigensKLRB1 protein, humanLectins, C-TypeNK Cell Lectin-Like Receptor Subfamily BOligosaccharides

Identifiers

PMID25690298
PMCPMC6272133
OpenAlexW1966515269

What OpenQuestion holds

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Registered trials

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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.