Evidence map›Paper›PMID 35955839›Full record

ArticleInternational journal of molecular sciences2022

Conjugation of the 9-kDa Isoform of Granulysin with Liposomes Potentiates Its Cytotoxicity.

Ruth Soler-Agesta, Patricia Guerrero-Ochoa, Joaquín Marco-Brualla, Raquel Ibáñez-Pérez, Isabel Marzo, Luis Martínez-Lostao, Alberto Anel

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Review
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 2 institutions in 1 country.

Ruth Soler-AgestaApoptosis, Immunity & Cancer Group, Department of Biochemistry and Molecular and Cell Biology, Faculty of Sciences, Aragón Health Research Institute (IIS Aragón), University of Zaragoza, 50009 Zaragoza, Spain.ORCID 0000-0003-3153-389X
Patricia Guerrero-OchoaApoptosis, Immunity & Cancer Group, Department of Biochemistry and Molecular and Cell Biology, Faculty of Sciences, Aragón Health Research Institute (IIS Aragón), University of Zaragoza, 50009 Zaragoza, Spain.ORCID 0000-0002-1657-4792
Joaquín Marco-BruallaApoptosis, Immunity & Cancer Group, Department of Biochemistry and Molecular and Cell Biology, Faculty of Sciences, Aragón Health Research Institute (IIS Aragón), University of Zaragoza, 50009 Zaragoza, Spain.ORCID 0000-0002-1710-4821
Raquel Ibáñez-PérezApoptosis, Immunity & Cancer Group, Department of Biochemistry and Molecular and Cell Biology, Faculty of Sciences, Aragón Health Research Institute (IIS Aragón), University of Zaragoza, 50009 Zaragoza, Spain.
Isabel MarzoApoptosis, Immunity & Cancer Group, Department of Biochemistry and Molecular and Cell Biology, Faculty of Sciences, Aragón Health Research Institute (IIS Aragón), University of Zaragoza, 50009 Zaragoza, Spain.ORCID 0000-0002-2315-9079
Luis Martínez-LostaoNanoscience Institute of Aragon (INA), 50018 Zaragoza, Spain.
Alberto AnelApoptosis, Immunity & Cancer Group, Department of Biochemistry and Molecular and Cell Biology, Faculty of Sciences, Aragón Health Research Institute (IIS Aragón), University of Zaragoza, 50009 Zaragoza, Spain.ORCID 0000-0002-5175-8394
Universidad de Zaragoza · ESInstituto de Nanociencia y Materiales de Aragón · ES

Funding

Gobierno de Aragón B31_20RMinisterio de Ciencia e Innovación PID2019-105128RB-I00
6 · The paper itself

Abstract

Nine kDa granulysin (GRNLY) is a human cytolytic protein secreted by cytotoxic T lymphocytes (CTL) and NK cells of the immune system whose demonstrated physiological function is the elimination of bacteria and parasites. In previous studies by our group, the anti-tumor capacity of recombinant granulysin was demonstrated, both in vitro and in vivo. In the present work, we developed lipid nanoparticles whose surfaces can bind recombinant granulysin through the formation of a complex of coordination between the histidine tail of the protein and Ni

Indexed as

Antigens, Differentiation, T-LymphocyteLiposomesApoptosisHumansJurkat CellsNanoparticlesProtein IsoformsAntigens, Differentiation, T-LymphocyteLipid NanoparticlesLiposomesProtein Isoformsacute lymphoid leukemiaapoptosisgranulysinimmunotherapylipid nanoparticles

Identifiers

PMID35955839
PMCPMC9369117
OpenAlexW4290594483

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.