Article

Structure-based probe reveals the presence of large transthyretin aggregates in plasma of ATTR amyloidosis patients

2024-03-10

Abstract excerpt

ATTR amyloidosis is a relentlessly progressive disease caused by the misfolding and systemic accumulation of amyloidogenic transthyretin into amyloid fibrils. These fibrils cause diverse clinical phenotypes, mainly cardiomyopathy and/or polyneuropathy. Little is known about the aggregation of transthyretin during disease development and whether this has implications for diagnosis and treatment. Using the cryogenic...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 563ef774-d2c5-56ff-81a3-b8be265f0038
DOI: 10.1101/2024.03.09.584228

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Structure-based probe reveals the presence of large transthyretin aggregates in plasma of ATTR amyloidosis patientsDOI 10.1101/2024.03.09.584228Read

Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients.Semantic proximity Read

Transthyretin amyloid fibrils adopt distinct folds in the brainSemantic proximity Read

Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patientSemantic proximity Read

Structural polymorphism of amyloid fibrils in cardiac transthyretin amyloidosis revealed by cryo-electron microscopySemantic proximity Read

Detection of ATTR aggregates in plasma of polyneuropathic ATTR-V30M amyloidosis patientsSemantic proximity Read

A Shared Amyloid Architecture in Cardiac Fibrils from Three Neuropathy-Associated ATTR VariantsSemantic proximity Read

Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosisSemantic proximity Read

ATTRv-V30M Type A amyloid fibrils from heart and nerves exhibit structural homogeneitySemantic proximity Read

A Brief Journey through Protein Misfolding in Transthyretin Amyloidosis (ATTR Amyloidosis).Semantic proximity Read

Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.Semantic proximity Read

Amyloid fibril polymorphism in the heart and liver of an ATTR amyloidosis patient with polyneuropathy attributed to the ATTRv-V122Δ variantSemantic proximity Read

3D Visualization and Proteomic Analysis of Human Cardiac Transthyretin Amyloidosis Tissue Reveals Microangiopathy and Capillary OcclusionSemantic proximity Read