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

De novo Mutation Enables NOTCH3ECD Aggregation and Mitochondrial Dysfunction via Interactions with BAX and BCL-2.

Journal of Alzheimer's disease : JAD - 1 Jan 2022

Liu Ruijie, Gao Chenhao, Shang Junkui, Sun Ruihua, Wang Wenjing, Li Wei, Gao Dandan, Huo Xuejing, Shi Yingying, Wang Yanliang, Wang Fengyu, Zhang Jiewen

Abstract excerpt

BACKGROUND: Cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL) caused by NOTCH3 mutations is the most common monogenic hereditary pattern of cerebral small vessel disease. The aggregation of the mutant NOTCH3 may play a cytotoxic role in CADASIL. However, the main mechanism of this process remains unclear. OBJECTIVE: We aimed to investigate the possible...

Read the complete abstract on PubMed

Topics

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

Share to bcl-2-Associated X Protein
Share to CADASIL

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondria

Share to Mutation

Share to Proto-Oncogene Proteins c-bcl-2

Share to Receptor, Notch3

Share to Receptors, Notch

Source

Identifiers

PMID: 35001891
DOI: 10.3233/JAD-215256

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

De novo Mutation Enables NOTCH3ECD Aggregation and Mitochondrial Dysfunction via Interactions with BAX and BCL-2.PMID 35001891Read ↗

Mutant NOTCH3ECD Triggers Defects in Mitochondrial Function and Mitophagy in CADASIL Cell Models.Semantic proximity Read ↗

Mutations in NOTCH3 cause the formation and retention of aggregates in the endoplasmic reticulum, leading to impaired cell proliferation.Semantic proximity Read ↗

Analysis of the pathogenicity and pathological characteristics of NOTCH3 gene-sparing cysteine mutations in vitro and in vivo modelsSemantic proximity Read ↗

Notch3 Signaling and Aggregation as Targets for the Treatment of CADASIL and Other NOTCH3-Associated Small-Vessel Diseases.Semantic proximity Read ↗

Progress to Clarify How NOTCH3 Mutations Lead to CADASIL, a Hereditary Cerebral Small Vessel Disease.Semantic proximity Read ↗

NOTCH3 is non-enzymatically fragmented in inherited cerebral small-vessel disease.Semantic proximity Read ↗

NOTCH3 Mutations in CADASIL Alter Lipid Metabolism: Insights from Patient Plasma and In Vitro Models.Semantic proximity Read ↗

Cysteine-sparing CADASIL mutations in NOTCH3 show proaggregatory properties in vitro.Semantic proximity Read ↗

NOTCH3 signal activation by its extracellular domain accumulation in an iPSC line newly established from a CADASIL patient.Semantic proximity Read ↗

Heterogeneity of NOTCH3 activation mechanisms uncovers therapeutic potential for targeted therapies for CADASILSemantic proximity Read ↗

A midposition NOTCH3 truncation in inherited cerebral small vessel disease may affect the protein interactome.Semantic proximity Read ↗

Pericytes are involved in the pathogenesis of cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy.Semantic proximity Read ↗

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