A number of proteins are capable of converting from their soluble, monomeric form into highly-ordered, insoluble aggregates known as amyloid fibrils. In vivo, these fibrils, which accumulate in organs and tissues, are associated with a wide range of amyloid diseases for which there are currently no therapeutic solutions. The molecular details of the pathway from native monomer through oligomeric intermediates to the final amyloid fibril remain a challenging enigma. Over the past few years, mass spectrometry has been applied to investigate the various stages of amyloid fibril formation, and this report summarizes the key steps achieved to date
AbstractAmyloid-β, the protein implicated in Alzheimer’s disease, along with a number of other prote...
Growth and deposition of amyloid fibrils, polymers of proteins with a cross beta-sheet structure, ar...
The inability of a protein to adopt its native and soluble conformation (protein misfolding) is the ...
A number of proteins are capable of converting from their soluble, monomeric form into highly-ordere...
Amyloidogenic peptide oligomers are responsible for a variety of neurodegenerative disorders such as...
From small molecules to macromolecules, mass spectrometry has evolved significantly over the past de...
Numerous debilitating human disorders result from protein misfolding and amyloid formation. Despite...
Oligomers which form during amyloid fibril assembly are considered to be key contributors towards am...
In vivo beta-2 microglobulin (βm) forms amyloid fibrils that are associated with the disease dialysi...
AbstractSeveral widespread and severe degenerative diseases are characterized by the deposition of a...
In this thesis I have used electrospray mass spectrometry (ESI-MS) to investigate various aspects of...
The defining feature of the extensive family of amyloid diseases is the formation of networks of ent...
Fibrillar protein aggregation is a hallmark of a variety of human diseases. Examples include the dep...
Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in nu...
All amyloid comprises fibrillar polymers of tightly associated protein monomers. Central to the fibr...
AbstractAmyloid-β, the protein implicated in Alzheimer’s disease, along with a number of other prote...
Growth and deposition of amyloid fibrils, polymers of proteins with a cross beta-sheet structure, ar...
The inability of a protein to adopt its native and soluble conformation (protein misfolding) is the ...
A number of proteins are capable of converting from their soluble, monomeric form into highly-ordere...
Amyloidogenic peptide oligomers are responsible for a variety of neurodegenerative disorders such as...
From small molecules to macromolecules, mass spectrometry has evolved significantly over the past de...
Numerous debilitating human disorders result from protein misfolding and amyloid formation. Despite...
Oligomers which form during amyloid fibril assembly are considered to be key contributors towards am...
In vivo beta-2 microglobulin (βm) forms amyloid fibrils that are associated with the disease dialysi...
AbstractSeveral widespread and severe degenerative diseases are characterized by the deposition of a...
In this thesis I have used electrospray mass spectrometry (ESI-MS) to investigate various aspects of...
The defining feature of the extensive family of amyloid diseases is the formation of networks of ent...
Fibrillar protein aggregation is a hallmark of a variety of human diseases. Examples include the dep...
Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in nu...
All amyloid comprises fibrillar polymers of tightly associated protein monomers. Central to the fibr...
AbstractAmyloid-β, the protein implicated in Alzheimer’s disease, along with a number of other prote...
Growth and deposition of amyloid fibrils, polymers of proteins with a cross beta-sheet structure, ar...
The inability of a protein to adopt its native and soluble conformation (protein misfolding) is the ...