Results overview: Found 3 records in 0.03 seconds.
Articles, 3 records found
Articles 3 records found  
1.
8 p, 1.2 MB SGnn : A Web Server for the Prediction of Prion-Like Domains Recruitment to Stress Granules Upon Heat Stress / Iglesias, Valentin (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Santos-Suárez, Juan (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pintado-Grima, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Proteins bearing prion-like domains (PrLDs) are essential players in stress granules (SG) assembly. Analysis of data on heat stress-induced recruitment of yeast PrLDs to SG suggests that this propensity might be connected with three defined protein biophysical features: aggregation propensity, net charge, and the presence of free cysteines. [...]
2021 - 10.3389/fmolb.2021.718301
Frontiers in Molecular Biosciences, Vol. 8 (August 2021) , art. 718301  
2.
12 p, 1.4 MB DispHred : a server to predict pH-dependent order-disorder transitions in intrinsically disordered proteins / Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Pintado-Grima, Carlos (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Santos-Suárez, Juan (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
The natively unfolded nature of intrinsically disordered proteins (IDPs) relies on several physicochemical principles, of which the balance between a low sequence hydrophobicity and a high net charge appears to be critical. [...]
2020 - 10.3390/ijms21165814
International journal of molecular sciences, Vol. 21, Issue 16 (August 2020) , art. 5814  
3.
14 p, 2.0 MB PH-dependent aggregation in intrinsically disordered proteins is determined by charge and lipophilicity / Santos, Jaime (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Mangiagalli, Marco (Department of Biotechnology and Biosciences, University of Milano-Bicocca) ; Santos-Suárez, Juan (Galicia Supercomputing Center (CESGA)) ; Brocca, Stefania (Department of Biotechnology and Biosciences, University of Milano-Bicocca) ; Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Protein aggregation is associated with an increasing number of human disorders and premature aging. Moreover, it is a central concern in the manufacturing of recombinant proteins for biotechnological and therapeutic applications. [...]
2020 - 10.3390/cells9010145
Cells, Vol. 9 (2020)  

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