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

Paradoxical roles of ATF6α and ATF6β in modulating disease severity caused by mutations in collagen X.

Matrix biology : journal of the International Society for Matrix Biology - 1 Sept 2018

Forouhan M, Mori K, Boot-Handford R P

Abstract excerpt

Whilst the role of ATF6α in modulating the unfolded protein response (UPR) has been well documented, the function of its paralogue ATF6β is less well understood. Using knockdown in cell culture and gene ablation in mice we have directly compared the roles of ATF6α & β in responding to the increased ER stress induced by mutant forms of type X collagen that cause the ER stress-associated metaphyseal...

Read the complete abstract on PubMed

Topics

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

Share to Activating Transcription Factor 6
Share to Chondrocytes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Collagen Type X

Share to Endoplasmic Reticulum Stress

Share to Growth Plate

Share to Osteochondrodysplasias

Share to Primary Cell Culture

Share to Unfolded Protein Response

Source

Open in PubMed Open full text

Identifiers

PMID: 29522813
DOI: 10.1016/j.matbio.2018.03.004
PMCID: PMC6090092

Genes

ATF6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Paradoxical roles of ATF6α and ATF6β in modulating disease severity caused by mutations in collagen X.PMID 29522813Read ↗

XBP1-Independent UPR Pathways Suppress C/EBP-β Mediated Chondrocyte Differentiation in ER-Stress Related Skeletal DiseaseSemantic proximity Read ↗

Inhibiting the integrated stress response pathway prevents aberrant chondrocyte differentiation thereby alleviating chondrodysplasia.Semantic proximity Read ↗

Transcriptional Profiling of Chondrodysplasia Growth Plate Cartilage Reveals Adaptive ER-Stress Networks That Allow Survival but Disrupt HypertrophySemantic proximity Read ↗

Transmission of ER stress response by ATF6 promotes endochondral bone growthSemantic proximity Read ↗

The unfolded protein response and its relevance to connective tissue diseasesSemantic proximity Read ↗

Human iPSC-derived hypertrophic chondrocytes reveal a mutation-specific unfolded protein response in chondrodysplasiasSemantic proximity Read ↗

In vivo cellular adaptation to ER stress: survival strategies with double-edged consequences.Semantic proximity Read ↗

Collagen misfolding mutations: the contribution of the unfolded protein response to the molecular pathology.Semantic proximity Read ↗

The unfolded protein response regulator ATF6 promotes mesodermal differentiation.Semantic proximity Read ↗

XBP1s-Mediated ER Proteostasis Network Enhancement Can Selectively Improve the Folding and Secretion of an Osteogenesis Imperfecta-Causing Collagen-I VariantSemantic proximity Read ↗

Mechanisms and models of endoplasmic reticulum stress in chondrodysplasia.Semantic proximity Read ↗

Osteoblast Malfunction Caused by Cell Stress Response to Procollagen Misfolding in α2(I)-G610C Mouse Model of Osteogenesis Imperfecta.Semantic proximity Read ↗

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