CV Lattes
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Universidade de São Paulo (USP). Instituto de Química de São Carlos (IQSC) (Institutional affiliation from the last research proposal) Birthplace: Brazil
Holds a degree in Pharmacy from the School of Pharmacy at the Federal University of Minas Gerais UFMG (19961999) and a Ph.D. in Functional and Molecular Biology with an emphasis on Biochemistry from the Institute of Biology at the University of Campinas IB/UNICAMP (20002004). The experimental part of the Ph.D. research project was conducted at the Center for Structural Molecular Biology of the National Synchrotron Light Laboratory in Campinas CBME/LNLS, currently the National Laboratory of Biosciences at the Brazilian Center for Research in Energy and Materials LNBio/CNPEM/Campinas.Completed postdoctoral training at the Institute of Biosciences, Humanities and Exact Sciences IBILCE/UNESP (20052006) and at CBME/LNLS (20062007). Since 2007, has been a Tenured Professor (RDIDP) at the Institute of Chemistry of São Carlos, University of São Paulo IQSC/USP, where obtained the title of Livre-Docente (Habilitation) in 2015, with a focus on Biochemistry. Currently serves as Associate Professor (MS5.2) at IQSC/USP, teaching undergraduate and graduate courses in Biochemistry and Protein Biophysics.Supervises master's and doctoral students in the graduate program in Chemistry at IQSC/USP and is currently Chair of the Undergraduate Committee at IQSC (term 20222024, reappointed for the 20242026 term), while also actively participating in several academic committees and boards. Main research interests include Heterologous Protein Expression, Molecular Biology, Structural Biology, Protein Biophysics, Molecular Chaperones (Hsp70, Hsp90), and techniques such as Circular Dichroism, Fluorescence, Calorimetry, and Analytical Ultracentrifugation.Serves as a reviewer for FAPESP, CNPq, CNPEM, and scientific journals, and has coordinated several research projects funded by FAPESP and CNPq. Currently, Principal Investigator of a Thematic Project supported by FAPESP and a CNPq Research Productivity Fellow since 2009. Also qualified to provide consultancy services to pharmaceutical and biotechnology companies. (Source: Lattes Curriculum)
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This project investigates the regulatory role of phosphorylation in modulating protein-protein interactions and chaperone activity of the Hsp90/SGT and Hsp90/Aha1 complex in Leishmania braziliensis. Hsp90 acts as a molecular chaperone assisting in folding, maturation and stabilization of several client proteins, in addition to integrating and coordinating crucial cell signaling pathways. …
One of the most interesting challenges in science is the understanding of the structure/function relationship of proteins because these macromolecules are involved in virtually all cellular physiological functions. Accordingly, this knowledge can have several applications, including the production of proteins with specific functions and defined biotechnological applications. As the loss o…
Among all molecular chaperones, Hsp70 family stands out due to its important role in cellular homeostasis, since they act as a pivot receiving and delivering client proteins from/to other chaperone molecules. Hsp70 act assisting the folding of nascent proteins, preventing protein aggregation, directing of proteins to organelles or for degradation and recovering proteins from aggregates, a…
Hsp70 is a major molecular chaperones and function as pivot receiving and distributing substrates from/to other molecular chaperones, both in the cytoplasm and in organelles. The mitochondrial Hsp70 (mtHsp70) is involved in the import of mitochondrial proteins produced in the cytoplasm and their subsequent folding, is essential for mitochondrial biogenesis. In mammals, the mtHsp70 is call…
Protein-protein and protein-ligand interactions are crucial events for the regulation of proteins and protein activity, for instance, it is responsible for enzyme activation or inhibition, by conformational changes in proteins for cell signaling, transport and storage of substances, etc. Few experimental techniques allow studying these types of interactions in solution, and provide a wide…
(Only some records are available in English at this moment)
hHep1 (human Hsp70-escort protein 1) is a small molecular chaperone often found in the mitochondria, aiding in the import of nuclear-encoded proteins. Under heat stress conditions, it is also found in the nucleus and cytoplasm, playing a crucial role in maintaining cellular proteostasis. hHep1 directly interacts with Hsp70s, increasing their solubility, preventing its aggregation and stim…
Molecular chaperones are proteins responsible for protein quality control, including the identification of misfolded proteins and directing them for degradation. Human heat shock proteins of 70 kDa (Hsp70 or HSPA in humans) comprise a family of chaperones that also participate in the proteasome system via ubiquitin through a complex mechanism involving cytoplasmic Hsp90 and co-chaperones,…
This project investigates the regulatory role of phosphorylation in modulating protein-protein interactions and chaperone activity of the Hsp90/SGT and Hsp90/Aha1 complexes in Leishmania braziliensis. Hsp90 functions as a molecular chaperone, assisting in the folding, maturation, and stabilization of various client proteins, as well as integrating and coordinating crucial cellular signali…
(Only some records are available in English at this moment)
HSP70s represent a crucial class of Molecular Chaperones playing vital roles in cellular protein homeostasis. Within this family, HSPA5 stands out, also known as BiP (Binding immunoglobulin Protein), the most abundantly expressed form of Hsp70 and the only one found in the lumen of the endoplasmic reticulum (ER) in eukaryotes. In addition to the ER, HSPA5 can be found in mitochondria, cyt…
(Only some records are available in English at this moment)
Heat shock proteins (HSPs) are important components of cell protein quality control, acting on protein folding, intracellular traffic, protein degradation, etc. Central in protein quality control is the HSP70 family that consists of highly conserved, ubiquitous and ATP-dependent molecular chaperones. In humans, there are several HSP70 isoforms, most of these are found in the cytosol while…
70 kDa heat shock proteins (Hsp70s) are critical molecular chaperones for proteostasis capable of assisting protein folding, transportation through membranes, targeting to degradation, as well as preventing protein aggregation. Hsp70s are thus critical players of the protein quality control (PQC) system which includes protein synthesis, molecular chaperones and degradation systems. Upon s…
Heat shock proteins (Hsps) are important components of the cellular chaperone pool, playing an important role in the protein folding, intracellular traffic, degradation and assisting proteins to obtain their native structure, etc. Having around 40-60% of identity among its prokaryotic and eukaryotic members, the Hsp70 superfamily corresponds to a family of proteins highly conserved. In hu…
(Only some records are available in English at this moment)
| 2 / 2 | Ongoing grants |
| 5 / 4 | Completed research grants |
| 4 / 4 | Ongoing scholarships in Brazil |
| 30 / 19 | Completed scholarships in Brazil |
| 4 / 4 | Completed scholarships abroad |
| 45 / 33 | All research grants and scholarships |
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