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María G. Noval

Researcher at Fundación Instituto Leloir

Publications -  10
Citations -  301

María G. Noval is an academic researcher from Fundación Instituto Leloir. The author has contributed to research in topics: Protein structure & Immunology. The author has an hindex of 7, co-authored 7 publications receiving 214 citations. Previous affiliations of María G. Noval include Facultad de Ciencias Exactas y Naturales.

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Journal ArticleDOI

A New Inorganic Photolabile Protecting Group for Highly Efficient Visible Light GABA Uncaging

TL;DR: This research presents a probabilistic assessment of the phytochemical properties of quimica inorganica and its role in the response to infectious disease.
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

Gut microbiome dysbiosis in antibiotic-treated COVID-19 patients is associated with microbial translocation and bacteremia

TL;DR: In this paper , the authors provide evidence that Gut microbiome dysbiosis is associated with translocation of bacteria into the blood during COVID-19, causing life-threatening secondary infections.
Journal ArticleDOI

Conformational dissection of a viral intrinsically disordered domain involved in cellular transformation.

TL;DR: It is confirmed that pH-induced changes in α-helix content are governed by the intrinsically disordered E7N domain, which may modulate the exposure of linear binding motifs responsible for its multi-target binding properties, leading to interference with key cell signaling pathways and eventually to cellular transformation by the virus.
Journal ArticleDOI

Folding of a cyclin box: linking multitarget binding to marginal stability, oligomerization and aggregation of the retinoblastoma tumor suppressor AB pocket domain

TL;DR: It is proposed that marginal stability and associated oligomerization may be conserved for function as a “hub” protein, allowing the formation of multiprotein complexes, which could constitute a robust mechanism to retain its cell cycle regulatory role throughout evolution.