Transthyretin: from structural stability to osteoarticular and cardiovascular diseases

E Wieczorek, A Ożyhar - Cells, 2021 - mdpi.com
Transthyretin (TTR) is a tetrameric protein transporting hormones in the plasma and brain,
which has many other activities that have not been fully acknowledged. TTR is a positive …

Transthyretin and familial amyloidotic polyneuropathy: recent progress in understanding the molecular mechanism of neurodegeneration

X Hou, MI Aguilar, DH Small - The FEBS journal, 2007 - Wiley Online Library
Familial amyloidotic polyneuropathy (FAP) is an inherited autosomal dominant disease that
is commonly caused by accumulation of deposits of transthyretin (TTR) amyloid around …

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

AM Fernandez-Escamilla, F Rousseau… - Nature …, 2004 - nature.com
We have developed a statistical mechanics algorithm, TANGO, to predict protein
aggregation. TANGO is based on the physico-chemical principles of β-sheet formation …

Transthyretin aggregation under partially denaturing conditions is a downhill polymerization

AR Hurshman, JT White, ET Powers, JW Kelly - Biochemistry, 2004 - ACS Publications
The deposition of fibrils and amorphous aggregates of transthyretin (TTR) in patient tissues
is a hallmark of TTR amyloid disease, but the molecular details of amyloidogenesis are …

Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants

A Quintas, DC Vaz, I Cardoso, MJM Saraiva… - Journal of Biological …, 2001 - ASBMB
Amyloid fibril formation and deposition is a common feature of a wide range of fatal diseases
including spongiform encephalopathies, Alzheimer's disease, and familial amyloidotic …

Uncovering the mechanism of aggregation of human transthyretin

L Saelices, LM Johnson, WY Liang, MR Sawaya… - Journal of Biological …, 2015 - ASBMB
The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon
dissociation and monomer unfolding. The aggregation of transthyretin has been reported as …

Predicting protein stability changes from sequences using support vector machines

E Capriotti, P Fariselli, R Calabrese, R Casadio - Bioinformatics, 2005 - academic.oup.com
Motivation: The prediction of protein stability change upon mutations is key to understanding
protein folding and misfolding. At present, methods are available to predict stability changes …

The Ims paradox: a perspective on structural ion mobility‐mass spectrometry

JW McCabe, MJ Hebert, M Shirzadeh… - Mass spectrometry …, 2021 - Wiley Online Library
Studies of large proteins, protein complexes, and membrane protein complexes pose new
challenges, most notably the need for increased ion mobility (IM) and mass spectrometry …

Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry

J Kardos, K Yamamoto, K Hasegawa, H Naiki… - Journal of Biological …, 2004 - ASBMB
Amyloid fibril deposition is associated with over 20 degenerative diseases, including
Alzheimer's, Parkinson's, and prion diseases. Although research over the last few years has …

Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between …

AR Hurshman Babbes, ET Powers, JW Kelly - Biochemistry, 2008 - ACS Publications
Urea denaturation studies were carried out as a function of transthyretin (TTR) concentration
to quantify the thermodynamically linked quaternary and tertiary structural stability and to …