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

Destabilization of transthyretin by pathogenic mutations in the DE loop.

Proteins - 15 Feb 2007

Takeuchi Makoto, Mizuguchi Mineyuki, Kouno Takahide, Shinohara Yoshinori, Aizawa Tomoyasu, Demura Makoto, Mori Yoshihiro, Shinoda Hiroyuki, Kawano Keiichi

Abstract excerpt

Transthyretin single-amino-acid variants are responsible for familial amyloidotic polyneuropathy, in which transthyretin variants accumulate extracellularly in the form of fibrillar aggregates. We studied the structural stabilities of four transthyretin variants (L58H, L58R, T59K, and E61K), in which a positively charged amino acid is introduced in a loop region between the D- and E-strands. In addition to being...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Calorimetry, Differential Scanning

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Circular Dichroism

Share to Deuterium

Share to Drug Stability

Share to Hydrogen

Share to Magnetic Resonance Spectroscopy

Share to Prealbumin

Source

Identifiers

PMID: 17143887
DOI: 10.1002/prot.21252

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Destabilization of transthyretin by pathogenic mutations in the DE loop.PMID 17143887Read ↗

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

The hydrophobic residue Leu73 is crucial for the high stability and low aggregation properties of murine transthyretin.Semantic proximity Read ↗

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

Different disease-causing mutations in transthyretin trigger the same conformational conversion.Semantic proximity Read ↗

Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.Semantic proximity Read ↗

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

Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry.Semantic proximity Read ↗

Intrinsic versus mutation dependent instability/flexibility: a comparative analysis of the structure and dynamics of wild-type transthyretin and its pathogenic variants.Semantic proximity Read ↗

A molecular basis for tetramer destabilization and aggregation of transthyretin Ala97Ser.Semantic proximity Read ↗

Mutation and low pH effect on the stability as well as unfolding kinetics of transthyretin dimer.Semantic proximity Read ↗

Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin.Semantic proximity Read ↗

Transthyretin: a review from a structural perspective.Semantic proximity Read ↗

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