L
Leonardo G. Alonso
Researcher at University of Buenos Aires
Publications - 36
Citations - 877
Leonardo G. Alonso is an academic researcher from University of Buenos Aires. The author has contributed to research in topics: Intrinsically disordered proteins & Protein structure. The author has an hindex of 16, co-authored 32 publications receiving 774 citations. Previous affiliations of Leonardo G. Alonso include Fundación Instituto Leloir & Facultad de Ciencias Exactas y Naturales.
Papers
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Journal ArticleDOI
UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates.
TL;DR: It was confirmed that BiP (binding protein, a chaperone of the heat shock protein 70 family) preferentially recognized neoglycoproteins displaying extended conformations, thus providing a molecular rationale for the sequential BiP-CNX/CRT interaction with folding glycoprotein observed in vivo.
Book ChapterDOI
Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains.
TL;DR: This chapter presents the basic methodology for performing Far-UV CD measurements on a protein of interest and for identifying and characterizing intrinsically disordered regions, and several protocols for the analysis of residual secondary structure present in the protein under study.
Journal ArticleDOI
High-risk (HPV16) human papillomavirus E7 oncoprotein is highly stable and extended, with conformational transitions that could explain its multiple cellular binding partners.
Leonardo G. Alonso,Maria Garcia-Alai,Alejandro D. Nadra,Alicia N. Lapena,Fabio L. Almeida,Peter Gualfetti,Gonzalo de Prat-Gay +6 more
TL;DR: It is shown that persistent residual structure in the monomer of E7 is responsible for its reported anomalous electrophoretic behavior and conformational properties that could have evolved to enable protein-protein recognition of the large number of cellular binding partners reported.
Journal ArticleDOI
The HPV16 E7 viral oncoprotein self-assembles into defined spherical oligomers.
Leonardo G. Alonso,Maria Garcia-Alai,Clara Smal,Juan M. Centeno,Rubén Iacono,Eduardo Castaño,Peter Gualfetti,Gonzalo de Prat-Gay +7 more
TL;DR: High-risk HPV16 E7, a nonglobular dimer with some properties of intrinsically disordered proteins, is capable of undergoing pH-dependent conformational transitions that expose hydrophobic surfaces to the solvent and is able to readily assemble into homogeneous spherical particles.
Journal ArticleDOI
The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein.
TL;DR: The HPV16 E7 oncoprotein is an extended dimer, with a stable and cooperative fold, but that displays properties of "natively unfolded" proteins, which allow adaptation to a variety of protein targets and expose the PEST degradation sequence that regulates its turnover in the cell.