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

Reticulon1-C modulates protein disulphide isomerase function.

Cell death & disease - 4 Apr 2013

Bernardoni P, Fazi B, Costanzi A, Nardacci R, Montagna C, Filomeni G, Ciriolo M R, Piacentini M, Di Sano F

Abstract excerpt

Endoplasmic reticulum (ER) is the primary site for the synthesis and folding of secreted and membrane-bound proteins. Accumulation of unfolded and misfolded proteins in ER underlies a wide range of human neurodegenerative disorders. Hence, molecules regulating the ER stress response represent potential candidates as drug targets for tackling these diseases. Protein disulphide isomerase (PDI) is a chaperone...

Read the complete abstract on PubMed

Topics

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

Share to Endoplasmic Reticulum
Share to Endoplasmic Reticulum Stress

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microtubules

Share to Nerve Tissue Proteins

Share to Protein Disulfide-Isomerases

Share to Protein Folding

Share to Protein Isoforms

Share to Transport Vesicles

Source

Open in PubMed Open full text

Identifiers

PMID: 23559015
DOI: 10.1038/cddis.2013.113
PMCID: PMC3641336

Genes

RTN1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reticulon1-C modulates protein disulphide isomerase function.PMID 23559015Read ↗

Emerging roles of protein disulfide isomerase in cancerSemantic proximity Read ↗

Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity.Semantic proximity Read ↗

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Protein disulphide isomerase (PDI) is protective against several types of DNA damage, including that induced by amyotrophic lateral sclerosis-associated mutant TDP-43 in neuronal cells/ in vitro modelsSemantic proximity Read ↗

Thioredoxin-interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress.Semantic proximity Read ↗

The thioredoxin‐like fold: Hidden domains in protein disulfide isomerases and other chaperone proteinsSemantic proximity Read ↗

Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.Semantic proximity Read ↗

Protein disulphide isomerase inhibition as a potential cancer therapeutic strategySemantic proximity Read ↗

The Drosophila reticulon, Rtnl-1, has multiple differentially expressed isoforms that are associated with a sub-compartment of the endoplasmic reticulum.Semantic proximity Read ↗

Manipulation of oxidative protein folding and PDI redox state in mammalian cells.Semantic proximity Read ↗

SERCA activity is reduced in <i>DJ-1</i> mutant flies and human cells due to oxidative modificationSemantic proximity Read ↗

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