Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Interplay between Endoplasmic Reticulum (ER) Stress and Autophagy Induces Mutant p53H273 Degradation.

Biomolecules - 3 Mar 2020

Garufi Alessia, Federici Giulia, Gilardini Montani Maria Saveria, Crispini Alessandra, Cirone Mara, D'Orazi Gabriella

Abstract excerpt

The unfolded protein response (UPR) is an adaptive response to intrinsic and external stressors, and it is mainly activated by the accumulation of misfolded proteins at the endoplasmic reticulum (ER) lumen producing ER stress. The UPR signaling network is interconnected with autophagy, the proteolytic machinery specifically devoted to clearing misfolded proteins in order to survive bioenergetic stress and/or...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Autophagy
Share to Endoplasmic Reticulum-Associated Degradation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum Stress

Share to HCT116 Cells

Share to HT29 Cells

Share to Mutation

Share to Neoplasms

Share to Tumor Suppressor Protein p53

Source

Open in PubMed Open full text

Identifiers

PMID: 32138264
DOI: 10.3390/biom10030392
PMCID: PMC7175121

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interplay between Endoplasmic Reticulum (ER) Stress and Autophagy Induces Mutant p53H273 Degradation.PMID 32138264Read ↗

Degradation of mutant p53H175 protein by Zn(II) through autophagy.Semantic proximity Read ↗

A role for bioinorganic chemistry in the reactivation of mutant p53 in cancer.Semantic proximity Read ↗

Regulation of p53 stability as a therapeutic strategy for cancer.Semantic proximity Read ↗

Glutathionylation-dependent proteasomal degradation of wide-spectrum mutant p53 proteins by engineered zeolitic imidazolate framework-8.Semantic proximity Read ↗

Mutant p53 and Cellular Stress Pathways: A Criminal Alliance That Promotes Cancer ProgressionSemantic proximity Read ↗

Chemical Genomics Identifies the Unfolded Protein Response as a Target for Selective Cancer Cell Killing during Glucose DeprivationSemantic proximity Read ↗

Effect of Alpha-1 Antitrypsin Deficiency on Zinc Homeostasis Genes Regulation and Interaction with Endoplasmic Reticulum Stress Response Associated GenesSemantic proximity Read ↗

Zinc Supplementation Enhances the Pro-Death Function of UPR in Lymphoma Cells Exposed to RadiationSemantic proximity Read ↗

Mutant p53 rescue and modulation of p53 redox state.Semantic proximity Read ↗

Zinc shapes the folding landscape of p53 and establishes a new pathway for reactivating structurally diverse p53 mutantsSemantic proximity Read ↗

DNAJA1 controls the fate of misfolded mutant p53 through the mevalonate pathway.Semantic proximity Read ↗

Review. The endoplasmic reticulum: a target for new anticancer drugs.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.