G
Gabriela Camporeale
Researcher at Fundación Instituto Leloir
Publications - 8
Citations - 102
Gabriela Camporeale is an academic researcher from Fundación Instituto Leloir. The author has contributed to research in topics: Cysteine & Viral replication. The author has an hindex of 5, co-authored 8 publications receiving 54 citations.
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Journal ArticleDOI
Deconstructing virus condensation.
Nora Lopez,Gabriela Camporeale,Mariano Salgueiro,Silvia S. Borkosky,Araceli Visentin,Ramon Peralta-Martinez,María Eugenia Loureiro,Gonzalo de Prat-Gay +7 more
TL;DR: In this paper, the basic principles of liquid-liquid phase separation are discussed in connection with several examples of VFs and a view which integrates viral replication mechanisms with the biochemistry underlying liquid-like organelles is proposed.
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Cysteine-Rich Positions Outside the Structural Zinc Motif of Human Papillomavirus E7 Provide Conformational Modulation and Suggest Functional Redox Roles
Lucía B. Chemes,Gabriela Camporeale,Ignacio E. Sánchez,Gonzalo de Prat-Gay,Leonardo G. Alonso +4 more
TL;DR: A functional redox activity is proposed that adds to the previously discovered chaperone activity of E7 and supports the picture of a moonlighting pathological role of this paradigmatic viral oncoprotein.
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The non-structural NS1 protein unique to respiratory syncytial virus: a two-state folding monomer in quasi-equilibrium with a stable spherical oligomer.
TL;DR: A unique protein without homologs, structure or mechanistic information may switch between monomers and oligomers in conditions compatible with the cellular environment and be potentially modulated by crowding or compartmentalization.
Journal ArticleDOI
Hidden Structural Codes in Protein Intrinsic Disorder
Silvia S. Borkosky,Gabriela Camporeale,Lucía B. Chemes,Marikena Risso,Maria G. Noval,Ignacio E. Sánchez,Leonardo G. Alonso +6 more
TL;DR: Evolution pinpoints conformational hot spots that could have not been identified by direct experimental methods for analyzing or perturbing the equilibrium of an intrinsically disordered protein ensemble, and uncovers the existence of local structural elements that oppose canonical folding.
Journal ArticleDOI
Degenerate cysteine patterns mediate two redox sensing mechanisms in the papillomavirus E7 oncoprotein
Gabriela Camporeale,Juan R. Lorenzo,María Gabriela Thomas,Edgardo Salvatierra,Silvia S. Borkosky,Marikena Risso,Ignacio E. Sánchez,Leonardo G. Alonso +7 more
TL;DR: This work dissected the molecular mechanisms by which E7 oncoprotein can sense and manage the potentially harmful oxidative environment of the papillomavirus-infected cell and identified a couple of low pKa nucleophilic cysteines that can form a disulfide bridge upon the exposure to ROS and regulate the cytoplasm to nucleus transport.