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Article

Co-aggregate formation of CADASIL-mutant NOTCH3: a single-particle analysis.

Human molecular genetics - 15 Aug 2011

Duering Marco, Karpinska Anna, Rosner Stefanie, Hopfner Franziska, Zechmeister Martin, Peters Nils, Kremmer Elisabeth, Haffner Christof, Giese Armin, Dichgans Martin, Opherk Christian

Abstract excerpt

CADASIL (cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy) is the most common monogenic cause of stroke and vascular dementia. Accumulation and deposition of the NOTCH3 (N3) extracellular domain in small blood vessels has been recognized as a central pathological feature of the disease. Recent experiments suggested enhanced formation of higher order multimers for mutant...

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Source

Identifiers

PMID: 21628316
DOI: 10.1093/hmg/ddr237

Genes

NOTCH3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Co-aggregate formation of CADASIL-mutant NOTCH3: a single-particle analysis.PMID 21628316Read ↗

CADASIL mutations enhance spontaneous multimerization of NOTCH3.Semantic proximity Read ↗

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

NOTCH3 CADASIL Variant Receptor Aggregation Requires NOTCH3 Wild-Type Receptors: Identification of Highly Selective Inhibitors That Block the Process.Semantic proximity Read ↗

Lunatic fringe promotes the aggregation of CADASIL NOTCH3 mutant proteins.Semantic proximity Read ↗

Biochemical characterization and cellular effects of CADASIL mutants of NOTCH3.Semantic proximity Read ↗

Structural changes in NOTCH3 induced by CADASIL mutations: Role of cysteine and non-cysteine alterations.Semantic proximity Read ↗

Protein aggregates containing wild-type and mutant NOTCH3 are major drivers of arterial pathology in CADASIL.Semantic proximity Read ↗

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

Functional analysis of a recurrent missense mutation in Notch3 in CADASILSemantic proximity Read ↗

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

The N-acetylglucosaminyltransferase Radical fringe contributes to defects in JAG1-dependent turnover and signaling of NOTCH3 CADASIL mutants.Semantic proximity Read ↗

NOTCH3 active immunotherapy reduces NOTCH3 deposition in brain capillaries in a CADASIL mouse modelSemantic proximity Read ↗

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