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

Role of Drosophila EDEMs in the degradation of the alpha-1-antitrypsin Z variant.

International journal of molecular medicine - 1 Apr 2015

Jang Bo-Yun, Ryoo Hyung Don, Son Jaekyoung, Choi Kyung-Chul, Shin Dong-Myoung, Kang Sang-Wook, Kang Min-Ji

Abstract excerpt

The synthesis of proteins in the endoplasmic reticulum (ER) that exceeds the protein folding capacity of this organelle is a frequent cause of cellular dysfunction and disease. An example of such a disease is alpha-1-antitrypsin (A1AT) deficiency, caused by destabilizing mutations in this glycoprotein. It is considered that the mutant proteins are recognized in the ER by lectins and are subsequently degraded...

Read the complete abstract on PubMed

Topics

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

Share to alpha 1-Antitrypsin
Share to Drosophila

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drosophila Proteins

Share to Endoplasmic Reticulum Stress

Share to Gene Knockdown Techniques

Share to Protein Folding

Share to Proteolysis

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 25716426
DOI: 10.3892/ijmm.2015.2109
PMCID: PMC4356437

Genes

EDEM2
EDEM1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of Drosophila EDEMs in the degradation of the alpha-1-antitrypsin Z variant.PMID 25716426Read ↗

ER-to-lysosome-associated degradation acts as failsafe mechanism upon ERAD dysfunctionSemantic proximity Read ↗

Natural <i>SEL1L</i> variants modify ERAD, proteasome function, and survival in a <i>Drosophila</i> model of NGLY1 deficiencySemantic proximity Read ↗

Expression of the Z Variant of α1-Antitrypsin Suppresses Hepatic Cholesterol Biosynthesis in Transgenic ZebrafishSemantic proximity Read ↗

Transcriptome and functional analysis in a Drosophila model of NGLY1 deficiency provides insight into therapeutic approachesSemantic proximity Read ↗

NGLY1 Deficiency, a Congenital Disorder of Deglycosylation: From Disease Gene Function to Pathophysiology.Semantic proximity Read ↗

Drosophila as a model for unfolded protein response researchSemantic proximity Read ↗

Loss of peptide:N-glycanase causes proteasome dysfunction mediated by a sugar-recognizing ubiquitin ligase.Semantic proximity Read ↗

Genetic disruption of mammalian endoplasmic reticulum-associated protein degradation: Human phenotypes and animal and cellular disease models.Semantic proximity Read ↗

The <i>Drosophila</i> metallopeptidase <i>superdeath</i> decouples apoptosis from the activation of the ER stress responseSemantic proximity Read ↗

Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes.Semantic proximity Read ↗

NorUDCA promotes degradation of α1-antitrypsin mutant Z protein by inducing autophagy through AMPK/ULK1 pathwaySemantic proximity Read ↗

Chaperone-mediated autophagy degrades SERPINA1 E342K /α1-antitrypsin Z variant and alleviates cell stressSemantic proximity Read ↗

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