RICARDO
GRAÑA MONTES
Investigador/a Distinguido/a M.Zambrano
Universitat Autònoma de Barcelona
Barcelona, EspañaPublicacions en col·laboració amb investigadors/es de Universitat Autònoma de Barcelona (16)
2020
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Reply to Comment on "n-terminal Protein Tail Acts as Aggregation Protective Entropic Bristles: The SUMO Case"
Biomacromolecules, Vol. 21, Núm. 8, pp. 3483-3484
2018
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A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation
Redox Biology, Vol. 14, pp. 566-575
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Global Protein Stabilization Does Not Suffice to Prevent Amyloid Fibril Formation
ACS Chemical Biology, Vol. 13, Núm. 8, pp. 2094-2105
2017
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Prediction of protein aggregation and amyloid formation
From Protein Structure to Function with Bioinformatics: Second Edition (Springer Netherlands), pp. 205-263
2015
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Protein aggregation and its prediction
NATO Science for Peace and Security Series A: Chemistry and Biology, Vol. 38, pp. 115-126
2014
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Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions
Journal of Biological Chemistry, Vol. 289, Núm. 49, pp. 33783-33796
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Association between foldability and aggregation propensity in small disulfide-rich proteins
Antioxidants and Redox Signaling, Vol. 21, Núm. 3, pp. 368-383
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N-terminal protein tails act as aggregation protective entropic bristles: The SUMO case
Biomacromolecules, Vol. 15, Núm. 4, pp. 1194-1203
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The importance of a gatekeeper residue on the aggregation of transthyretin implications for transthyretin-related amyloidoses
Journal of Biological Chemistry, Vol. 289, Núm. 41, pp. 28324-28337
2013
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About targets and causes in protein folding
Journal of Biomolecular Structure and Dynamics
2012
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AGGRESCAN: Method, application, and perspectives for drug design
Methods in Molecular Biology, Vol. 819, pp. 199-220
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Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: The PI3-SH3 domain case
Antioxidants and Redox Signaling, Vol. 16, Núm. 1, pp. 1-15
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Native structure protects SUMO proteins from aggregation into amyloid fibrils
Biomacromolecules, Vol. 13, Núm. 6, pp. 1916-1926
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Protein aggregation profile of the human kinome
Frontiers in Physiology, Vol. 3 NOV
2011
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Prediction of the aggregation propensity of proteins from the primary sequence: Aggregation properties of proteomes
Biotechnology Journal, Vol. 6, Núm. 6, pp. 674-685
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The aggregation properties of Escherichia coli proteins associated with their cellular abundance
Biotechnology Journal, Vol. 6, Núm. 6, pp. 752-760