Evidence map›Paper›PMID 32096279›Full record

ReviewThe FEBS journal2020

FLIP(L): the pseudo-caspase.

Peter Smyth, Tamas Sessler, Christopher J Scott, Daniel B Longley

Open access · hybridAbstract readReview
In one paragraph

Review in The FEBS journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Helicobacter Pylori-induced BRD2 mInternational journal of biological sciences · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Acute lung injury: a view from the perspective of necroptosis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
    Review
  13. Review
  14. Targeting caspase-8/c-FLIPFrontiers in cell and developmental biology · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The deubiquitinase Usp27x as a novel regulator of cFLIPApoptosis : an international journal on programmed cell death · 2022
    Article
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

4 authors at 1 institution in 1 country.

Peter SmythThe Patrick G Johnston Centre for Cancer Research, Queen's University, Belfast, UK.
Tamas SesslerThe Patrick G Johnston Centre for Cancer Research, Queen's University, Belfast, UK.
Christopher J ScottThe Patrick G Johnston Centre for Cancer Research, Queen's University, Belfast, UK.
Daniel B LongleyThe Patrick G Johnston Centre for Cancer Research, Queen's University, Belfast, UK.ORCID 0000-0003-2495-2033
Queen's University Belfast · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R009112/1Cancer Research UK C11884/A24387
6 · The paper itself

Abstract

Possessing structural homology with their active enzyme counterparts but lacking catalytic activity, pseudoenzymes have been identified for all major enzyme groups. Caspases are a family of cysteine-dependent aspartate-directed proteases that play essential roles in regulating cell death and inflammation. Here, we discuss the only human pseudo-caspase, FLIP(L), a paralog of the apoptosis-initiating caspases, caspase-8 and caspase-10. FLIP(L) has been shown to play a key role in regulating the processing and activity of caspase-8, thereby modulating apoptotic signaling mediated by death receptors (such as TRAIL-R1/R2), TNF receptor-1 (TNFR1), and Toll-like receptors. In this review, these canonical roles of FLIP(L) are discussed. Additionally, a range of nonclassical pseudoenzyme roles are described, in which FLIP(L) functions independently of caspase-8. These nonclassical pseudoenzyme functions enable FLIP(L) to play key roles in the regulation of a wide range of biological processes beyond its canonical roles as a modulator of cell death.

Indexed as

CaspasesApoptosisCASP8 and FADD-Like Apoptosis Regulating ProteinHumansCASP8 and FADD-Like Apoptosis Regulating ProteinCaspasesapoptosisautophagycaspaseDISCFLIP(L)necroptosispseudo-caspasepseudoenzymes

Identifiers

PMID32096279
PMCPMC7586951
OpenAlexW3007286507

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.