graduation at Farmácia from Universidade Federal de Minas Gerais (1999) and doctorate at Biochemistry from Universidade Estadual de Campinas (2004). Has experience in Biochemistry, focusing on Biochemistry, acting on the following subjects: hsp70, proteins in solution, hsp90, analytical ultracentrifugation and chaperones. (Source: Lattes Curriculum)
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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…
The Hsp90 chaperone (heat shock protein 90 kDa) is found in all organisms and in all cellular compartments, and the two types found in the eukaryotic cytosol interact with at least 10% of all proteins produced by the cell. The Hsp90 plays a key role in the maturation of these proteins, which makes it important for many cellular processes such signaling, proteostasis, epigenetics, telomere…
(Only some records are available in English at this moment)
The 70 kDa Heat shock proteins (Hsp70) are molecular chaperones that act in the control of cell protein quality. They are monomeric, ubiquitous, highly conserved proteins and are composed of a Nucleotide Binding Domain (NBD) and a Peptide-substrate Binding Domain (PBD). To direct their functional cycle, Hsp70 rely on the help of adenosine nucleotides and auxiliary proteins: co-chaperones.…
The main objective of this research is the cellular study of human mortalin together with co-chaperones and chaperones that possibly assists it in the process of importation and folding of cytoplasmic proteins. Experiments from our group (in submission) indicate that mortalin and Hsp70-1A undergo temperature-induced oligomerization and that thermal oligomers (or supramolecular complexes) …
The HSP90 molecular chaperone is a central player in the maintenance of proteostasis, being essential to cell viability in normal and stress conditions. Abnormal HSP90 activity contributes to the development of several diseases, such as cancer, neurodegeneration, among others. This chaperone also plays a critical role in the proteostasis maintenance in protozoa and the unbalancing of its …
The 70 kDa Heat shock protein (Hsp70 or HSPA) is part of a family of molecular chaperones that, in addition to being highly conserved, is expressed in several cell compartments. HSPAs are associated with several pathologies, such as neurodegenerative diseases and cancer. In humans, mitochondrial HSPA (HSPA9, GRP75, or mortalin) acts on the import of proteins synthesized in the cytosol int…
(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)
| 1 / 1 | Ongoing research grants |
| 5 / 4 | Completed research grants |
| 2 / 2 | Ongoing scholarships in Brazil |
| 28 / 17 | Completed scholarships in Brazil |
| 4 / 4 | Completed scholarships abroad |
| 40 / 28 | All research grants and scholarships |
| Associated processes | |
CV Lattes
ORCID