A number of proteins undergo specific aggregation into amyloid fibrils in vivo, leading to the pathological disorder known as amyloidosis. These diseases are characterised by the deposition of normally soluble proteins into insoluble fibrils with a cross-β structure. A general feature o
Abstractβ2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in di...
The assembly of soluble proteins into ordered fibrillar aggregates with cross-beta structure is an e...
Amyloidosis is a pathological condition in which protein is deposited extracellularly in the form of...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins which then ...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins which then ...
Fibrillar protein aggregation is a hallmark of a variety of human diseases. Examples include the dep...
Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition an...
The molecular bases of amyloid aggregation propensity are still poorly understood, especially for pr...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
The amyloidoses constitute a large group of diseases caused by an alteration in the conformation and...
Spurred by the appreciation that protein aggregation, leadingto amyloid fibril formation, is linked ...
A general discovery in protein science in the past few decades has been the finding that a number of...
The inability of a protein to adopt its native and soluble conformation (protein misfolding) is the ...
Abstractβ2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in di...
The assembly of soluble proteins into ordered fibrillar aggregates with cross-beta structure is an e...
Amyloidosis is a pathological condition in which protein is deposited extracellularly in the form of...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins which then ...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins which then ...
Fibrillar protein aggregation is a hallmark of a variety of human diseases. Examples include the dep...
Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition an...
The molecular bases of amyloid aggregation propensity are still poorly understood, especially for pr...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
The amyloidoses constitute a large group of diseases caused by an alteration in the conformation and...
Spurred by the appreciation that protein aggregation, leadingto amyloid fibril formation, is linked ...
A general discovery in protein science in the past few decades has been the finding that a number of...
The inability of a protein to adopt its native and soluble conformation (protein misfolding) is the ...
Abstractβ2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in di...
The assembly of soluble proteins into ordered fibrillar aggregates with cross-beta structure is an e...
Amyloidosis is a pathological condition in which protein is deposited extracellularly in the form of...