Evidence map›Paper›PMID 33672324›Full record

ReviewInternational journal of molecular sciences2021

The Multifaceted Role of CMA in Glioma: Enemy or Ally?

Alessia Lo Dico, Cristina Martelli, Cecilia Diceglie, Luisa Ottobrini

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. CMA mediates resistance in breast cancer models.Cancer cell international · 2023
    Article
  4. Review
  5. 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.

Alessia Lo DicoDepartment of Pathophysiology and Transplantation, University of Milan, Via F.Cervi 93, Segrate, 20090 Milan, Italy.ORCID 0000-0002-8627-5050
Cristina MartelliDepartment of Pathophysiology and Transplantation, University of Milan, Via F.Cervi 93, Segrate, 20090 Milan, Italy.ORCID 0000-0003-0023-9110
Cecilia DiceglieDepartment of Pathophysiology and Transplantation, University of Milan, Via F.Cervi 93, Segrate, 20090 Milan, Italy.ORCID 0000-0003-1749-1080
Luisa OttobriniDepartment of Pathophysiology and Transplantation, University of Milan, Via F.Cervi 93, Segrate, 20090 Milan, Italy.ORCID 0000-0002-5002-6845
University of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chaperone-mediated autophagy (CMA) is a catabolic pathway fundamental for cell homeostasis, by which specific damaged or non-essential proteins are degraded. CMA activity has three main levels of regulation. The first regulatory level is based on the targetability of specific proteins possessing a KFERQ-like domain, which can be recognized by specific chaperones and delivered to the lysosomes. Target protein unfolding and translocation into the lysosomal lumen constitutes the second level of CMA regulation and is based on the modulation of Lamp2A multimerization. Finally, the activity of some accessory proteins represents the third regulatory level of CMA activity. CMA's role in oncology has not been fully clarified covering both pro-survival and pro-death roles in different contexts. Taking all this into account, it is possible to comprehend the actual complexity of both CMA regulation and the cellular consequences of its activity allowing it to be elected as a modulatory and not only catabolic machinery. In this review, the role covered by CMA in oncology is discussed with a focus on its relevance in glioma. Molecular correlates of CMA importance in glioma responsiveness to treatment are described to identify new early efficacy biomarkers and new therapeutic targets to overcome resistance.

Indexed as

Chaperone-Mediated AutophagyAntineoplastic Agents, AlkylatingGliomaHumansNuclear ProteinsPhosphoprotein PhosphatasesProteinsTemozolomideAntineoplastic Agents, AlkylatingNuclear ProteinsPHLPP1 protein, humanPhosphoprotein PhosphatasesProteinsTemozolomideautophagychaperone proteinsHypoxia Inducible Factor-1α (HIF-1α)oxidative stressPHLPP1Temozolomide (TMZ)therapeutic target

Identifiers

PMID33672324
PMCPMC7926390
OpenAlexW3129986680

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.