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

Characterisation of the biochemical and cellular roles of native and pathogenic amelogenesis imperfecta mutants of FAM83H.

Cellular signalling - 1 Aug 2020

Tachie-Menson Theresa, Gázquez-Gutiérrez Ana, Fulcher Luke J, Macartney Thomas J, Wood Nicola T, Varghese Joby, Gourlay Robert, Soares Renata F, Sapkota Gopal P

Abstract excerpt

The majority of mutations identified in patients with amelogenesis imperfecta have been mapped to FAM83H. As FAM83H expression is not limited to the enamel, how FAM83H contributes to amelogenesis is still largely unknown. We previously reported that members of the FAM83 family of proteins interact with and regulate the subcellular distribution of the promiscuous serine-threonine protein kinase CK1 family, through...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Amelogenesis Imperfecta

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amino Acid Motifs

Share to Apoptosis Regulatory Proteins

Share to Cell Nucleus

Share to HEK293 Cells

Share to Oncogene Proteins

Share to Protein Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 32289446
DOI: 10.1016/j.cellsig.2020.109632
PMCID: PMC7284315

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterisation of the biochemical and cellular roles of native and pathogenic amelogenesis imperfecta mutants of FAM83H.PMID 32289446Read ↗

FAM83H and Autosomal Dominant Hypocalcified Amelogenesis ImperfectaSemantic proximity Read ↗

<i>FAM83H</i> Mutations Cause ADHCAI and Alter Intracellular Protein LocalizationSemantic proximity Read ↗

Fam83h is Associated with Intracellular Vesicles and ADHCAISemantic proximity Read ↗

Fam83h null mice support a neomorphic mechanism for human ADHCAISemantic proximity Read ↗

Novel FAM83H mutations in patients with amelogenesis imperfecta.Semantic proximity Read ↗

A Novel FAM83H Truncation Mutation Disrupts Enamel Mineralization in Autosomal Dominant Hypocalcified Amelogenesis Imperfecta.Semantic proximity Read ↗

Mutational spectrum of FAM83H: the C-terminal portion is required for tooth enamel calcification.Semantic proximity Read ↗

FAM83H and casein kinase I regulate the organization of the keratin cytoskeleton and formation of desmosomes.Semantic proximity Read ↗

The gain-of-function FAM83H mutation caused hypocalcification amelogenesis imperfecta in a Chinese family.Semantic proximity Read ↗

Molecular characterization of amelogenesis imperfecta in Chinese patients.Semantic proximity Read ↗

FAM83F regulates canonical Wnt signalling through an interaction with CK1αSemantic proximity Read ↗

FAM83H mutations in families with autosomal-dominant hypocalcified amelogenesis imperfecta.Semantic proximity Read ↗

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