The tetrameric protein transthyretin dissociates to a non-native monomer in solution: a novel model for amyloidogenesis
In amyloidosis, normally innocuous soluble proteins polymerize to form insoluble fibrils.
Amyloid fibril formation and deposition have been associated with a wide range of diseases …
Amyloid fibril formation and deposition have been associated with a wide range of diseases …
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 …
The pathway by which the tetrameric protein transthyretin dissociates
TR Foss, RL Wiseman, JW Kelly - Biochemistry, 2005 - ACS Publications
The homotetrameric protein transthyretin (TTR) must undergo rate-limiting dissociation to its
constituent monomers in order to enable partial denaturation that allows the process of …
constituent monomers in order to enable partial denaturation that allows the process of …
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
W Colon, JW Kelly - Biochemistry, 1992 - ACS Publications
Revised Manuscript Received May 21, 1992 abstract: Amyloid diseases are caused by the
self-assembly of a given proteininto an insoluble cross-jS-sheet quaternary structural form …
self-assembly of a given proteininto an insoluble cross-jS-sheet quaternary structural form …
The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution
Amyloid fibril formation and deposition are the basis for a wide range of diseases, including
spongiform encephalopathies, Alzheimer's and familial amyloidotic polyneuropathies …
spongiform encephalopathies, Alzheimer's and familial amyloidotic polyneuropathies …
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin
A Hörnberg, T Eneqvist, A Olofsson, E Lundgren… - Journal of molecular …, 2000 - Elsevier
Self-assembly of the human plasma protein transthyretin (TTR) into unbranched insoluble
amyloid fibrils occurs as a result of point mutations that destabilize the molecule, leading to …
amyloid fibrils occurs as a result of point mutations that destabilize the molecule, leading to …
Pathogenesis of transthyretin amyloidosis
MD Benson - Amyloid, 2012 - Taylor & Francis
Current dogma for transthyretin (TTR) pathogenesis is that mutations in TTR alter its
structure such that the tetramer becomes unstable and prone to release of monomer which …
structure such that the tetramer becomes unstable and prone to release of monomer which …
Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants
G Goldsteins, H Persson… - Proceedings of the …, 1999 - National Acad Sciences
The structural requirements for generation of amyloid from the plasma protein transthyretin
(TTR) are not known, although it is assumed that TTR is partly misfolded in amyloid. In a …
(TTR) are not known, although it is assumed that TTR is partly misfolded in amyloid. In a …
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 …
Acidic pH-induced conformational changes in amyloidogenic mutant transthyretin
Several proteins, including transthyretin (TTR), can generate in tissues extracellular
insoluble aggregates, in the form of fibrils, that are associated with pathological states …
insoluble aggregates, in the form of fibrils, that are associated with pathological states …