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 …
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 …
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 …
aggregation. TANGO is based on the physico-chemical principles of β-sheet formation …
Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
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 …
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
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 …
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 …
dissociation and monomer unfolding. The aggregation of transthyretin has been reported as …
Predicting protein stability changes from sequences using support vector machines
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 …
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 …
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
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 …
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 …
to quantify the thermodynamically linked quaternary and tertiary structural stability and to …