Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
By A. Fernández-Escamilla, Frederic Rousseau, Joost Schymkowitz, Luis Serrano. Nature Biotechnology, 2004
1,595 citations recorded by the source corpus.
Subfields: Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/675f51eb740b9aeac413a9186efac02125c510ee
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- Silvio C. E. Tosatto
- Francois Stricher
- Frederic Rousseau
- Joost Schymkowitz
- Ian Walsh
- Mark A. DePristo
- Roland Riek
- Daniel M. Weinreich
Citations in the corpus
- Predicting antimicrobial peptides with improved accuracy by incorporating the compositional, physico-chemical and structural features into Chou’s general PseAAC (2017, neutral): “The compositional and PHYC features were computed by using the “Peptide” package 27 of R-software 28 , whereas the STRL features were computed by using the TANGO software 29 available at http://tango.crg.es/.”
- Missense meanderings in sequence space: a biophysical view of protein evolution (2005, background): “In addition, a class of mutations has been identified that affect aggregation rate independently of changes in stabilit”
- The FoldX web server: an online force field (2005, background): “In this fashion, TANGO predicts correctly both the disease causing and protective mutations in a wide range of proteins including Alzheimers’ A b peptide, lysozyme and transthyretin (12).”
- Identifying the amylome, proteins capable of forming amyloid-like fibrils (2010, methodology): “Aggregation Propensity Predictions with TANGO.”
- PASTA 2.0: an improved server for protein aggregation prediction (2014, methodology): “91) in this high specificity zone with the TANGO (11) method second to it (AUC 3.”
- AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, neutral): “These results, together with previous experimental [10,1720] and theoretical [21-24] data, suggest that specific short polypeptide stretches effectively promote and/or modulate protein amyloid formation.”