Ignacio Enrique Sanchez

Affiliations: 
Protein Physiology Lab Universidad de Buenos Aires, Buenos Aires, Ciudad Autónoma de Buenos Aires, Argentina 
Area:
proteins, sequence-function relationships, virus-host interactions, linear motifs, molecular information theory
Website:
http://www.proteinphysiologylab.tk
Google:
"Ignacio Sanchez"
Bio:

Postdoc with Luis Serrano.
Founder of A2B2C (Argentine Association for Bioinformatics and Computational Biology, www.a2b2c.org.ar)

Parents

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Thomas Kiefhaber grad student 1999-2003 University of Basel (Chemistry Tree)
Luis Serrano post-doc 2004-2006 EMBL
BETA: Related publications

Publications

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Sánchez IE, Galpern EA, Ferreiro DU. (2024) Solvent constraints for biopolymer folding and evolution in extraterrestrial environments. Proceedings of the National Academy of Sciences of the United States of America. 121: e2318905121
Sánchez IE, Galpern EA, Garibaldi MM, et al. (2022) Molecular Information Theory Meets Protein Folding. The Journal of Physical Chemistry. B. 126: 8655-8668
Lorenzo R, Leonetti CO, Alonso LG, et al. (2020) NGOME-Lite: Proteome-wide prediction of spontaneous protein deamidation highlights differences between taxa. Methods (San Diego, Calif.)
Alvarez-Paggi D, Lorenzo JR, Camporale G, et al. (2019) Topology dictates evolution of regulatory cysteines in a family of viral oncoproteins. Molecular Biology and Evolution
Glavina J, Román EA, Espada R, et al. (2018) Interplay between sequence, structure and linear motifs in the adenovirus E1A hub protein. Virology. 525: 117-131
Borkosky SS, Camporeale G, Chemes LB, et al. (2017) Hidden Structural Codes in Protein Intrinsic Disorder. Biochemistry
Espada R, Sánchez IE, Ferreiro DU. (2016) Detailing Protein Landscapes under Pressure. Biophysical Journal. 111: 2339-2341
Camporeale G, Lorenzo JR, Thomas MG, et al. (2016) Degenerate cysteine patterns mediate two redox sensing mechanisms in the papillomavirus E7 oncoprotein. Redox Biology. 11: 38-50
Lorenzo JR, Alonso LG, Sánchez IE. (2015) Prediction of Spontaneous Protein Deamidation from Sequence-Derived Secondary Structure and Intrinsic Disorder. Plos One. 10: e0145186
Pretel E, Sánchez IE, Fassolari M, et al. (2015) Conformational Heterogeneity Determined by Folding and Oligomer Assembly Routes of the Interferon Response Inhibitor NS1 Protein, Unique to Human Respiratory Syncytial Virus. Biochemistry. 54: 5136-46
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