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

Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner.

Biochemistry - 17 Oct 2017

Sun Xun, Dyson H Jane, Wright Peter E

Abstract excerpt

Abnormal deposition of aggregated wild-type (WT) human transthyretin (TTR) and its pathogenic variants is responsible for cardiomyopathy and neuropathy related to TTR amyloidosis. The tryptophan (Trp) fluorescence measurements typically used to study structural changes of TTR do not yield site-specific information on the two Trp residues per TTR protomer. To obtain such information, tryptophan labeled with...

Read the complete abstract on PubMed

Topics

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

Share to Fluorescent Dyes
Share to Nuclear Magnetic Resonance, Biomolecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Prealbumin

Share to Protein Aggregation, Pathological

Share to Protein Denaturation

Share to Protein Unfolding

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 28920433
DOI: 10.1021/acs.biochem.7b00815
PMCID: PMC5645263

Genes

TTR

Variants

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner.PMID 28920433Read ↗

Thermodynamic Stability and Aggregation Kinetics of EF Helix and EF Loop Variants of Transthyretin.Semantic proximity Read ↗

Probing the dissociation pathway of a kinetically labile transthyretin mutantSemantic proximity Read ↗

Probing the Dissociation Pathway of a Kinetically Labile Transthyretin Mutant.Semantic proximity Read ↗

Conformational Dynamics of an Amyloidogenic Intermediate of Transthyretin: Implications for Structural Remodeling and Amyloid Formation.Semantic proximity Read ↗

Crystal structures of amyloidogenic segments of human transthyretin.Semantic proximity Read ↗

Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Semantic proximity Read ↗

Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics.Semantic proximity Read ↗

A new isoleucine substitution of Val-20 in transthyretin tetramers selectively impairs dimer-dimer contacts and causes systemic amyloidosis.Semantic proximity Read ↗

Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation.Semantic proximity Read ↗

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation.Semantic proximity Read ↗

Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease.Semantic proximity Read ↗

Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation.Semantic proximity Read ↗

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