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Molecular and structural characterization of RNA binding proteins acting as potential disease targets in cancer and neurology

Abstract

With the aim of expanding the druggable proteome and lead to the discovery of new medicines, we work on the characterization of understudied human proteins, which show preliminary connection to disease. Within this aim, research has been expanded on the importance of protein related to RNA biology as antibody and drug targets, including the proteins 'per se' and their upstream modulators as kinases and methyltranferases. Thus, RNA binding proteins as well as kinase proteins constitute important biological targets for the advancement of biopharma. Those proteins can be targeted by small-molecule chemical probes, which are molecules defined as having high affinity and selectivity for a target and which can enter the cell to engage the target in vivo. Probes work as a complement to biological reagents for target validation and can be refined to become new drugs. In addition, biological targets can also lead to immunotherapy. In this project we aim to contribute for the characterization of the RNA binding protein BICC (Bicaudal C Homology 1) and UHMK (U2AF homology motif Serine/Threonine-Protein kinase) as potential drug targets related to cancer and neurological. We will characterize its interactors, target mRNAs and search for new chemical ligands. (AU)

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VEICULO: TITULO (DATA)
VEICULO: TITULO (DATA)

Scientific publications (6)
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
DE SOUZA, LUCAS RODRIGO; POLY DA SILVA, ITALO ESPOSTI; CELIS-SILVA, GABRIELE; RADDATZ, BRUNA WINKERT; IMAMURA, LOUISE MATIE; KIM, EDSON YU SIN; VALDERRAMA, GABRIEL VIEIRA; RIEDI, HALANNA DE PAULA; ROGAL JR, SERGIO RENATO; MACHADO DE ALMEIDA, BERNARDO MONTESANTI; et al. Improved protocol for Bst polymerase and reverse transcriptase production and application to a point-of-care diagnostics system. Experimental Biology and Medicine, v. 248, n. 19, p. 13-pg., . (20/16094-8, 20/02006-0, 14/50897-0, 19/11320-2)
CUNHA, MICAEL R.; DO AMARAL, BRUNO S.; TAKARADA, JESSICA E.; VALDERRAMA, GABRIEL V.; BATISTA, ANDREA N. L.; BATISTA JR, JOAO M.; CASS, QUEZIA B.; COUNAGO, RAFAEL M.; MASSIRER, KATLIN B.. (S)-ML-SA1 Activates Autophagy via TRPML1-TFEB Pathway. CHEMBIOCHEM, v. 25, n. 22, p. 7-pg., . (20/02006-0, 21/04853-4, 14/50897-0, 19/22319-5)
WU, QIN; NIE, DAVID Y.; BA-ALAWI, WAIL; JI, YISHUAI; ZHANG, ZIWEN; CRUICKSHANK, JENNIFER; HAIGHT, JILLIAN; CIAMPONI, FELIPE E.; CHEN, JOCELYN; DUAN, SHILI; et al. PRMT inhibition induces a viral mimicry response in triple-negative breast cancer. Nature Chemical Biology, v. N/A, p. 22-pg., . (15/25134-5, 20/02006-0, 16/25521-1, 14/50897-0)
MARCELINO, TIAGO DE PAULA; FALA, ANGELA MARIA; SILVA, MATHEUS MONTEIRO DA; SOUZA-MELO, NORMANDA; MALVEZZI, AMARANTA MUNIZ; KLIPPEL, ANGELICA HOLLUNDER; ZOLTNER, MARTIN; PADILLA-MEJIA, NORMA; KOSTO, SAMANTHA; FIELD, MARK C.; et al. Identification of inhibitors for the transmembrane Trypanosoma cruzi eIF2α kinase relevant for parasite proliferation. Journal of Biological Chemistry, v. 299, n. 7, p. 18-pg., . (17/02496-4, 20/07870-4, 19/15909-0, 14/50897-0, 20/02006-0, 17/02416-0)
ARFELLI, VANESSA C.; CHANG, YUN-CHIEN; BAGNOLI, JOHANNES W.; KERBS, PAUL; CIAMPONI, FELIPE E.; PAZ, LAISSA M. DA S.; PANKIVSKYI, SERHII; SALONE, JEAN DE MATHA; MAUCUER, ALEXANDRE; MASSIRER, KATLIN B.; et al. UHMK1 is a novel splicing regulatory kinase. Journal of Biological Chemistry, v. 299, n. 4, p. 22-pg., . (22/08648-9, 14/01458-3, 20/02006-0)
ZHANG, KEJING; WEI, JUAN; ZHANG, SHEYU; FEI, LIYAN; GUO, LU; LIU, XUEYING; JI, YISHUAI; CHEN, WENJUN; CIAMPONI, FELIPE E.; CHEN, WEICHANG; et al. A chemical screen identifies PRMT5 as a therapeutic vulnerability for paclitaxel-resistant triple-negative breast cancer. CELL CHEMICAL BIOLOGY, v. 31, n. 11, p. 23-pg., . (20/02006-0)