Many different proteins aggregate into amyloid fibrils characterized by cross-beta structure. beta-strands contributed by distinct protein molecules are generally found in a parallel in-register alignment. Here, we describe the web server for a novel algorithm, prediction of amyloid structure aggregation (PASTA), to predict the most aggregation-prone portions and the corresponding beta-strand inter-molecular pairing for a given input sequence. PASTA was previously shown to yield results in excellent agreement with available experimental observations, when tested on both natively unfolded and structured proteins. The web server and downloadable source code are freely accessible from the URL: http://protein.cribi.unipd.it/pasta/
Background and Aims: Aggregation has been shown to be an intrinsic property of many proteins includ...
In the cell, protein folding into stable globular conformations is in competition with aggregation i...
We present a method for predicting the regions of the sequences of peptides and proteins that are mo...
Many different proteins aggregate into amyloid fibrils characterized by cross-beta structure. beta-s...
The formation of amyloid aggregates upon protein misfolding is related to several devastating degen-...
The formation of amyloid aggregates upon protein misfolding is related to several devastating degene...
The formation of amyloid aggregates upon protein misfolding is related to several devastating degen-...
The reliable identification of beta- aggregating stretches in protein sequences is essential for the...
The conversion from soluble states into cross-beta fibrillar aggregates is a property shared by many...
Amyloids and prion proteins are clinically and biologically important beta-structures, whose superse...
We present a method for predicting the regions of the sequences of peptides and proteins that are mo...
Background: Protein aggregation correlates with the development of several debilitating human disord...
The purpose of this work was to construct a consensus prediction algorithm of 'aggregation-prone' pe...
Protein aggregation results in beta-sheet-like assemblies that adopt either a variety of amorphous m...
Background and Aims: Aggregation has been shown to be an intrinsic property of many proteins includ...
Background and Aims: Aggregation has been shown to be an intrinsic property of many proteins includ...
In the cell, protein folding into stable globular conformations is in competition with aggregation i...
We present a method for predicting the regions of the sequences of peptides and proteins that are mo...
Many different proteins aggregate into amyloid fibrils characterized by cross-beta structure. beta-s...
The formation of amyloid aggregates upon protein misfolding is related to several devastating degen-...
The formation of amyloid aggregates upon protein misfolding is related to several devastating degene...
The formation of amyloid aggregates upon protein misfolding is related to several devastating degen-...
The reliable identification of beta- aggregating stretches in protein sequences is essential for the...
The conversion from soluble states into cross-beta fibrillar aggregates is a property shared by many...
Amyloids and prion proteins are clinically and biologically important beta-structures, whose superse...
We present a method for predicting the regions of the sequences of peptides and proteins that are mo...
Background: Protein aggregation correlates with the development of several debilitating human disord...
The purpose of this work was to construct a consensus prediction algorithm of 'aggregation-prone' pe...
Protein aggregation results in beta-sheet-like assemblies that adopt either a variety of amorphous m...
Background and Aims: Aggregation has been shown to be an intrinsic property of many proteins includ...
Background and Aims: Aggregation has been shown to be an intrinsic property of many proteins includ...
In the cell, protein folding into stable globular conformations is in competition with aggregation i...
We present a method for predicting the regions of the sequences of peptides and proteins that are mo...