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

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

Science translational medicine - 13 Sept 2017

Schonhoft Joseph D, Monteiro Cecilia, Plate Lars, Eisele Yvonne S, Kelly John M, Boland Daniel, Parker Christopher G, Cravatt Benjamin F, Teruya Sergio, Helmke Stephen, Maurer Mathew, Berk John, Sekijima Yoshiki, Novais Marta, Coelho Teresa, Powers Evan T, Kelly Jeffery W

Abstract excerpt

Increasing evidence supports the hypothesis that soluble misfolded protein assemblies contribute to the degeneration of postmitotic tissue in amyloid diseases. However, there is a dearth of reliable nonantibody-based probes for selectively detecting oligomeric aggregate structures circulating in plasma or deposited in tissues, making it difficult to scrutinize this hypothesis in patients. Hence, understanding the...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidosis, Familial
Share to Cross-Linking Reagents

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Probes

Share to Molecular Weight

Share to Prealbumin

Share to Proteolysis

Share to Solubility

Source

Open in PubMed Open full text

Identifiers

PMID: 28904227
DOI: 10.1126/scitranslmed.aam7621
PMCID: PMC5628019

Genes

TTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients.PMID 28904227Read ↗

Structure-based probe reveals the presence of large transthyretin aggregates in plasma of ATTR amyloidosis patientsSemantic proximity Read ↗

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

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

Serum Proteomic Variability Associated with Clinical Phenotype in Familial Transthyretin Amyloidosis (ATTRm).Semantic proximity Read ↗

Pathogenic Characterization of a Novel G47R Transthyretin Mutation in Early-Onset Amyloid Cardiomyopathy.Semantic proximity Read ↗

Transthyretin (ATTR) amyloidosis: clinical spectrum, molecular pathogenesis and disease-modifying treatments.Semantic proximity Read ↗

Disease-Specific Biomarkers in Transthyretin Cardiac Amyloidosis.Semantic proximity Read ↗

Updates on hereditary transthyretin amyloidosis polyneuropathy.Semantic proximity Read ↗

Transthyretin monomers: a new plasma biomarker for pre-symptomatic transthyretin-related amyloidosis.Semantic proximity Read ↗

Disease-Modifying Treatments for Transthyretin Amyloidosis.Semantic proximity Read ↗

Familial amyloidotic polyneuropathy: protein aggregation in the peripheral nervous system.Semantic proximity Read ↗

Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology.Semantic proximity Read ↗

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