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

Wilson disease-causing mutations in the carboxyl terminus of ATP7B regulates its localization and Golgi exit selectively in the unpolarized cells.

Metallomics : integrated biometal science - 5 Sept 2023

Chakraborty Kaustav, Das Santanu, Pal Anusree, Maji Saptarshi, Rai Bhawana, Gupta Arnab, Bhattacharjee Ashima

Abstract excerpt

Mutational inactivation of the P-type Cu-ATPase ATP7B interferes with its cellular functions to varying extent leading to varied cellular phenotypes. Wilson's disease (WD) primarily affects organs composed of polarized/differentiated epithelial cells. Therefore, phenotypic variability might differ depending on the polarization/differentiation of the cells. The present study investigates the intracellular...

Read the complete abstract on PubMed

Topics

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

Share to Cell Differentiation
Share to Golgi Apparatus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to Hepatolenticular Degeneration

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 37660282
DOI: 10.1093/mtomcs/mfad051
PMCID: PMC10506129

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Wilson disease-causing mutations in the carboxyl terminus of ATP7B regulates its localization and Golgi exit selectively in the unpolarized cells.PMID 37660282Read ↗

Polarized trafficking and copper transport activity of ATP7B: A mutational approach to establish genotype-phenotype correlation in Wilson disease.Semantic proximity Read ↗

Critical roles for the COOH terminus of the Cu-ATPase ATP7B in protein stability, trans-Golgi network retention, copper sensing, and retrograde trafficking.Semantic proximity Read ↗

Distinct phenotype of a Wilson disease mutation reveals a novel trafficking determinant in the copper transporter ATP7B.Semantic proximity Read ↗

Defective cellular localization of mutant ATP7B in Wilson's disease patients and hepatoma cell lines.Semantic proximity Read ↗

Regulation of apico-basolateral trafficking polarity of homologous Copper-ATPases ATP7A and ATP7BSemantic proximity Read ↗

Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis.Semantic proximity Read ↗

Identification of p38 MAPK and JNK as new targets for correction of Wilson disease-causing ATP7B mutants.Semantic proximity Read ↗

A glimpse into the regulation of the Wilson disease protein, ATP7B, sheds light on the complexity of mammalian apical trafficking pathways.Semantic proximity Read ↗

Wilson disease protein ATP7B is localized in the late endosomes in a polarized human hepatocyte cell line.Semantic proximity Read ↗

Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis.Semantic proximity Read ↗

A systems biology approach reveals new endoplasmic reticulum-associated targets for the correction of the ATP7B mutant causing Wilson disease.Semantic proximity Read ↗

The Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 protein.Semantic proximity Read ↗

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