Full Professor at the Institute of Chemistry, UNICAMP. Previously, he was a researcher at LNLS (19992007). He holds a Livre-Docência degree (2005) and a PhD (1996) in Biochemistry from the University of São Paulo, a postdoctoral fellowship in Molecular Biophysics from Stanford University (1998), and a Bachelor's degree in Biological Sciences (Biochemistry) from the Federal University of Minas Gerais (1991). Has expertise in Biochemistry, with an emphasis on proteins, focusing primarily on the following topics: protein folding, molecular chaperones and stress, structural biochemistry, and molecular biology and biophysics. Several alumni from his research group now hold positions in universities, research institutes, and industry. Key administrative roles: Currently serves as the Graduate Program Coordinator in Chemistry; served as Associate Director of the Institute of Chemistry (20142018); Head of the Department of Organic Chemistry (20112014); and Biotechnology Manager at LNLS (20012003). He is an active participant on committees for international, national, and state funding agencies. Presently, he is an associate editor of a scientific journal and a member of the editorial boards of three others. Laboratories and collaborative/multi-user projects: He was responsible for the Laboratory of Spectroscopy-Calorimetry-Hydrodynamics (19992007), involved in three multi-user LNLS projects, and participated in the CEPID-CBME/FAPESP, IMBEBB/CNPq, and INCTBEB networks (serving on the management committee for the latter). He coordinated the institutional molecular biology and circular dichroism laboratories at the Institute of Chemistry and contributed to UNICAMP's multi-user laboratory in the areas of Bioinformatics, Genomics, Proteomics, and Cellular Biology (as a member of the advisory committee). Notable awards: Zeferino Vaz Academic Recognition Award, 2024.CA-BF 2023.. FIRCA 2005. PEW Latin American Fellow 1997. (Source: Lattes Curriculum)
| News published in Agência FAPESP Newsletter about the researcher |
| More itemsLess items |
| TITULO |
| Articles published in other media outlets ( ): |
| More itemsLess items |
| VEICULO: TITULO (DATA) |
| VEICULO: TITULO (DATA) |
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 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)
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…
(Only some records are available in English at this moment)
| 3 / 3 | Ongoing grants |
| 9 / 5 | Completed research grants |
| 10 / 10 | Ongoing scholarships in Brazil |
| 90 / 46 | Completed scholarships in Brazil |
| 7 / 6 | Completed scholarships abroad |
| 119 / 70 | All research grants and scholarships |
| Associated processes | |
CV Lattes
ORCID