Protein aggregation is a feature of both normal cellular assemblies and pathological protein depositions. Although the limited order of aggregates has often impeded their structural characterization, 3D domain swapping has been implicated in the formation of several protein aggregates. Here, we review known structures displaying 3D domain swapping in the context of amyloid and related fibrils, prion proteins, and macroscopic aggregates, and we discuss the possible involvement of domain swapping in protein deposition diseases
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are an im...
This mini-review focuses on the processes and consequences of protein folding and misfolding. The la...
Many proteins function as multimeric assemblies into which the folded individual promoters organize ...
Protein aggregation is a feature of both normal cellular assemblies and pathological protein deposit...
Protein aggregation occurs in vivo as a result of improper folding or misfolding. Diverse diseases a...
For several different proteins an apparent correlation has been observed between the propensity for ...
Three-dimensional (3D) domain swapping creates a bond between two or more protein molecules as they ...
Functional repertoire, molecular pathways and diseases associated with 3D domain swapping in the hum...
AbstractThe assembly and misassembly of normally soluble proteins into fibrilar structures is though...
Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined th...
Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined th...
Protein aggregation underlies a wide range of human disorders. The polypeptides involved in these pa...
The amyloidoses constitute a large group of diseases caused by an alteration in the conformation and...
The majority of protein molecules must fold into defined three-dimensional structures to acquire fun...
This mini-review focuses on the processes and consequences of protein folding and misfolding. The la...
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are an im...
This mini-review focuses on the processes and consequences of protein folding and misfolding. The la...
Many proteins function as multimeric assemblies into which the folded individual promoters organize ...
Protein aggregation is a feature of both normal cellular assemblies and pathological protein deposit...
Protein aggregation occurs in vivo as a result of improper folding or misfolding. Diverse diseases a...
For several different proteins an apparent correlation has been observed between the propensity for ...
Three-dimensional (3D) domain swapping creates a bond between two or more protein molecules as they ...
Functional repertoire, molecular pathways and diseases associated with 3D domain swapping in the hum...
AbstractThe assembly and misassembly of normally soluble proteins into fibrilar structures is though...
Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined th...
Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined th...
Protein aggregation underlies a wide range of human disorders. The polypeptides involved in these pa...
The amyloidoses constitute a large group of diseases caused by an alteration in the conformation and...
The majority of protein molecules must fold into defined three-dimensional structures to acquire fun...
This mini-review focuses on the processes and consequences of protein folding and misfolding. The la...
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are an im...
This mini-review focuses on the processes and consequences of protein folding and misfolding. The la...
Many proteins function as multimeric assemblies into which the folded individual promoters organize ...