Full Professor at the Institute of Chemistry at UNICAMP (University of Campinas), was a researcher at LNLS (Brazilian Synchrotron Light Laboratory) from 1999 to 2007, holds a "Privat-Dozent" degree (2005) and a Ph.D. (1996) in Biochemistry from the University of São Paulo. He completed his postdoctoral research in Molecular Biophysics at Stanford University in 1998. He received his undergraduate degree in Biological Sciences (Bachelor's in Biochemistry) from the Federal University of Minas Gerais in 1991.Expertise lies in the field of Biochemistry, with a focus on Proteins: protein folding, chaperones, molecular stress, structural biochemistry, molecular biology, and biophysics. Many former members of his research group hold positions in universities, research institutes, or the industry. He has held various administrative positions, including the current role of Coordinator of Graduate Studies in Chemistry, Associate Director of the Institute of Chemistry (2014-2018), Head of the Department of Organic Chemistry (2011-2014), and Biotechnology Manager (2001-2003) at LNLS. Actively participates in Committees in international, national, and state funding agencies. Currently serves as an Associate Editor of one journal and as a member of the editorial boards of three other journals. He has been involved in multi-center and/or multi-user projects and laboratories, such as the Spectroscopy-Calorimetry-Hydrodynamics Laboratory (1999-2007) engaged in three multi-user projects at LNLS. Also involved in networks such as CEPID-CBME/FAPESP, IMBEBB/CNPq, and INCTBEB (as a member of the management committee). He has coordinated the institutional molecular biology and circular dichroism laboratories at IQ (Institute of Chemistry). Additionally, he is part of the committee advisory board for the UNICAMP Multi-User Laboratory in the areas of Bioinformatics-Genomics-Proteomics-Cell Biology. (Source: Lattes Curriculum)
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The reports of diseases related to protein misfolding have increased considerably since the discovery that protein aggregates can be formed in cells and can trigger cytotoxic action. Therefore, molecular chaperones and/or heat shock proteins (HSPs) have become natural candidates in the study of strategies for treatment of these diseases. The chaperones of the Hsp70 family are involved in …
Amyloid-type protein aggregation is a common feature of many neuro/neuromuscular degenerative disorders such as Huntington's disease (HD). Although these diseases show distinct clinical features, at the molecular level, protein aggregation modulates disease progression by a gain-of-toxicity mechanism(s). Recent epidemiological studies by the World Health Organization revealed that >55 mil…
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…
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…
The coordinator of this proposal, Carlos Ramos, has a research project financed by FAPESP, which has as its objective the use of the technique of isothermal titration calorimetry (ITC) to study the interaction between proteins and small molecules. The proteins studied in the research group are those involved in protein homeostasis, especially molecular chaperones and sirtuins. With the gr…
Our yet little understanding of the protein folding process holds back the understanding of several cellular processes because the conversion of a backbone into a native protein is a key element in the translation of organism's genetic information. As the organism ages, the folding seems to deviates becoming a signal to several diseases (mainly neurodegenerative). Protein misfolding cause…
(Only some records are available in English at this moment)
The R2TP complex (Rvb1-Rvb2-Tah1/RPAP3-Pih1/Pih1D1) is involved in the assembly and stabilization of macromolecular complexes associated with several pathways essential for cell growth and proliferation. More specifically, one of the components proteins of this complex, RPAP3, was shown to be essential for the development and survival of Drosophila melanogaster fruit fly larvae. Interesti…
(Only some records are available in English at this moment)
The reports of diseases related to protein misfolding have increased considerably since the discovery that protein aggregates can be formed in cells and can trigger cytotoxic action. Therefore, molecular chaperones and/or heat shock proteins (HSPs) have become natural candidates in the study of strategies for treatment of these diseases. The chaperones of the Hsp70 family are involved in …
(Only some records are available in English at this moment)
Molecular chaperones play an important role in protein quality control and are pivotal in protein folding processes. In recent years, it has been discovered that chaperones participate in many membraneless organelles (MLOs). These MLOs are also known as biomolecular condensates and compartmentalize proteins and nucleic acids without lipid membranes, unlike typical vesicle-like organelles.…
Neurodegeneration in Parkinson's disease is correlated with the occurrence of Lewy bodies, intracellular inclusions containing aggregates of the intrinsically disordered protein (IDP) a-synuclein (a-syn). In the cell, however, a-syn aggregation can be prevented by a class of proteins known as molecular chaperones, also called heat shock proteins. While numerous chaperones interact with a-…
The chaperones of the Hsp70 family have central role in the cellular network of molecular chaperones. These chaperones are engaged in many biological processes, including the folding of recently synthesized proteins to the native state, prevention of aggregation, solubilization and refolding of misfolded or aggregated proteins and transport of proteins across membranes. Hsp70 generally de…
The Hsp90 (heat shock protein 90 kDa) plays a key role in the maturation of at least 10% of all proteins produced by the cell, which makes it important for many cellular processes such signaling, proteostasis, epigenetics, telomere maintenance, innate immunity, etc. Obviously, changes in this 'highly connected node' leads to disturbances in cell function resulting in drastic consequences …
(Only some records are available in English at this moment)
| 3 / 3 | Ongoing research grants |
| 9 / 5 | Completed research grants |
| 6 / 6 | Ongoing scholarships in Brazil |
| 87 / 43 | Completed scholarships in Brazil |
| 1 / 1 | Ongoing scholarships abroad |
| 6 / 5 | Completed scholarships abroad |
| 112 / 63 | All research grants and scholarships |
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CV Lattes
ORCID