CV Lattes
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Universidade Estadual de Campinas (UNICAMP). Instituto de Química (IQ) (Institutional affiliation from the last research proposal) Birthplace: Brazil
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)
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Reports of diseases associated with protein misfolding have increased significantly since the discovery that protein aggregates form within cells and can trigger cytotoxicity, as observed in the relationship between ¿-synuclein and Parkinson's disease. Consequently, molecular chaperones and heat shock proteins (HSPs) have emerged as natural candidates for the development of therapeutic st…
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…
A função biológica das proteínas está diretamente ligada à sua estrutura tridimensional obtida através do processo de enovelamento protéico. Em razão disso, a prevenção do comportamento anormal de proteínas é fundamental para a vida celular e processos homeostáticos estão presentes nas células para estabilizar as conformações da proteína e para reenovelar ou degradar proteínas evitando qu…
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…
(Only some records are available in English at this moment)
Um dos desafios mais interessantes em ciência é compreender a relação estrutura/função de proteínas pois estas estão envolvidas em praticamente todas as funções fisiológicas celulares. Ou seja, este conhecimento pode ter diversas aplicações, inclusive na produção de proteínas com funções específicas e aplicações biotecnológicas definidas. Como a perda da estrutura leva também à perda de f…
This postdoctoral project seeks to examine the role of zinc and copper in the regulation of the human cochaperone DNAJA1 and its influence on the interaction with the chaperone Hsp70, with an innovative focus on modifications at the single-cell level. DNAJA1 is a zinc-binding protein essential for the proper functioning of the Hsp70 system, particularly under conditions of metal stress. T…
Alpha-synuclein (a-syn) is a protein of 140 amino acid residues that plays multiple roles in the synaptic activity of vertebrates. Adverse conditions or mutations can lead to the polymerization of this protein into amyloid fibrils, which are associated with certain neurodegenerative diseases known as synucleinopathies. For example, a-syn is one of the main components of amyloid plaques in…
(Only some records are available in English at this moment)
Nosso grupo de pesquisa estuda chaperonas com potencial para auxiliar no enovelamento de proteínas, além de protegê-las contra agregação. Contudo, nossos resultados mais recentes indicam que é necessário caracterizar os mecanismos de atividade dessas chaperonas. Para tanto, é necessário produzir proteínas em larga escala, purificá-las e proceder com experimentos envolvendo o estudo da int…
The regulation of cellular proteostasis, maintained by the protein quality control (PQC) system, is an intricate process involving the action of molecular chaperones, also known as HSPs (heat shock proteins), and the ubiquitin-proteasome system. These factors coordinate the synthesis, folding, maintenance of conformation, and degradation of polypeptide proteins. Imbalance in these factors…
Nosso grupo de pesquisa estuda chaperonas com potencial para auxiliar no enovelamento de proteínas, além de protegê-las contra agregação. Contudo, nossos resultados mais recentes indicam que é necessário caracterizar os mecanismos de atividade dessas chaperonas. Para tanto, é necessário produzir proteínas em larga escala, purificá-las e proceder com experimentos envolvendo o estudo da int…
(Only some records are available in English at this moment)
Carboxylate clamp tetracopeptide repeat (CC-TPR) proteins, e.g., HSP70-HSP90 organizing protein (HOP), protein phosphatase 5 (PP5) and carboxy-terminus of HSP70 interacting protein (CHIP), are cochaperones that interact with cytosolic HSP70 and HSP90 through a conserved EEVD motif at their C-terminus. Recent research from Professor Jason Gestwicki's laboratory has identified optimized EEV…
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)