Evidence map›Paper›PMID 29180998›Full record

ArticleFrontiers in immunology2017

Cystatin F Affects Natural Killer Cell Cytotoxicity.

Milica Perišić Nanut, Jerica Sabotič, Urban Švajger, Anahid Jewett, Janko Kos

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 16% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cystatin F Depletion inInternational journal of molecular sciences · 2024
    Article
  11. Article
  12. Article
  13. CD56Frontiers in immunology · 2024
    Article
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  15. Article
  16. Article
  17. Review
  18. Article
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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

5 authors at 4 institutions in 2 countries.

Milica Perišić NanutDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Jerica SabotičDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Urban ŠvajgerBlood Transfusion Center, Ljubljana, Slovenia.
Anahid JewettThe Jane and Jerry Weintraub Center for Reconstructive Biotechnology, Division of Oral Biology and Medicine, UCLA School of Dentistry, University of California-Los Angeles, Los Angeles, CA, United States.
Janko KosDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Jožef Stefan Institute · SIBlood Transfusion Centre of Slovenia · SIUniversity of California, Los Angeles · USUniversity of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cystatin F is a cysteine peptidase inhibitor which, unlike other cystatin family members, is targeted to endosomal/lysosomal compartments. It is synthesized as an inactive disulfide-linked dimer which is then converted to an active monomer by proteolytic cleavage of 15 N-terminal residues. Cystatin F has been suggested to regulate the cytotoxicity of natural killer (NK) cells by inhibiting the major granzyme convertases, cathepsins C and H. To test this hypothesis, we prepared variants of cystatin F and analyzed their uptake, subcellular trafficking, and peptidase inhibition, as well as their impact on the cytotoxicity of NK-92 cells and primary NK cells. The N-glycosylation pattern is responsible for the secretion, uptake, and subcellular sorting of cystatin F in HeLa and Hek293 cells, whereas the legumain binding site had no effect on these processes. Active, N-terminally truncated, monomeric cystatin F can also be internalized by recipient cells and targeted to endo/lysosomes, affecting also cells lacking the activating peptidase. Cystatin F mutants capable of cell internalization and trafficking through the endo/lysosomal pathway significantly decreased cathepsin C and H activities, both

Indexed as

cathepsin Ccystatin Fcytotoxic cellsgranule-mediated cytotoxicitygranzyme B

Identifiers

PMID29180998
PMCPMC5693851
OpenAlexW2767746507

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.