Evidence map›Paper›PMID 32961826›Full record

ArticleInternational journal of molecular sciences2020

Cell-Penetrable Peptide-Conjugated FADD Induces Apoptosis and Regulates Inflammatory Signaling in Cancer Cells.

Kishu Ranjan, Bhargav N Waghela, Foram U Vaidya, Chandramani Pathak

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Insights of Endocytosis Signaling in Health and Disease.International journal of molecular sciences · 2023
    Review
  7. FADD as a key molecular player in cancer progression.Molecular medicine (Cambridge, Mass.) · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. 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

4 authors at 1 institution in 1 country.

Kishu RanjanDepartment of Cell Biology, School of Biological Sciences & Biotechnology, Indian Institute of Advanced Research, Koba Institutional Area, Gandhinagar 382 007, Gujarat, India.ORCID 0000-0003-1256-181X
Bhargav N WaghelaDepartment of Cell Biology, School of Biological Sciences & Biotechnology, Indian Institute of Advanced Research, Koba Institutional Area, Gandhinagar 382 007, Gujarat, India.
Foram U VaidyaDepartment of Cell Biology, School of Biological Sciences & Biotechnology, Indian Institute of Advanced Research, Koba Institutional Area, Gandhinagar 382 007, Gujarat, India.
Chandramani PathakDepartment of Cell Biology, School of Biological Sciences & Biotechnology, Indian Institute of Advanced Research, Koba Institutional Area, Gandhinagar 382 007, Gujarat, India.ORCID 0000-0002-9389-8096
Indian Institute of Advanced Research · IN

Funding

Department of Biotechnology, Ministry of Science and Technology, India 6242/P60/RGCB/PMD/DBT/CMPK/2015Department of Science & Technology EMR/2016/002574
6 · The paper itself

Abstract

Dysregulated expression of Fas-associated death domain (FADD) is associated with the impediment of various cellular pathways, including apoptosis and inflammation. The adequate cytosolic expression of FADD is critical to the regulation of cancer cell proliferation. Importantly, cancer cells devise mechanisms to suppress FADD expression and, in turn, escape from apoptosis signaling. Formulating strategies, for direct delivery of FADD proteins into cancer cells in a controlled manner, may represent a promising therapeutic approach in cancer therapy. We chemically conjugated purified FADD protein with cell permeable TAT (transactivator of transcription) peptide, to deliver in cancer cells. TAT-conjugated FADD protein internalized through the caveolar pathway of endocytosis and retained in the cytosol to augment cell death. Inside cancer cells, TAT-FADD rapidly constituted DISC (death inducing signaling complex) assembly, which in turn, instigate apoptosis signaling. The apoptotic competency of TAT-FADD showed comparable outcomes with the conventional apoptosis inducers. Notably, TAT-FADD mitigates constitutive NF-κB activation and associated downstream anti-apoptotic genes

Indexed as

Cell-Penetrating PeptidesFas-Associated Death Domain ProteinNeoplasmsAnimalsApoptosisGene Expression RegulationHCT116 CellsHEK293 CellsHeLa CellsHep G2 CellsHumansMCF-7 CellsMiceNeoplasm ProteinsRAW 264.7 CellsCell-Penetrating PeptidesFADD protein, humanFas-Associated Death Domain ProteinNeoplasm ProteinsapoptosiscancerFADDinflammationNF-κBpeptides

Identifiers

PMID32961826
PMCPMC7555701
OpenAlexW3087422657

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.