Andrea C. de Barros

ORCID: 0000-0002-8869-9797
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About
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Research Areas
  • Nuclear Structure and Function
  • RNA Research and Splicing
  • RNA and protein synthesis mechanisms
  • Genomics and Chromatin Dynamics
  • interferon and immune responses
  • Enzyme Structure and Function
  • DNA Repair Mechanisms
  • RNA modifications and cancer
  • Bacterial Genetics and Biotechnology
  • Trace Elements in Health
  • Research on Leishmaniasis Studies
  • Photosynthetic Processes and Mechanisms
  • Fungal and yeast genetics research
  • Ubiquitin and proteasome pathways
  • Trypanosoma species research and implications
  • Biochemical and Molecular Research
  • Mitochondrial Function and Pathology
  • Cellular transport and secretion
  • Cytokine Signaling Pathways and Interactions

Universidade Estadual Paulista (Unesp)
2011-2022

The Ohio State University
2022

Krasnoyarsk State Medical University
2022

Saarland University
2022

Morpho (United States)
2022

Ku70 and Ku80 form a heterodimeric complex involved in multiple nuclear processes. This plays key role DNA repair due to its ability bind double-strand breaks facilitate by the nonhomologous end-joining pathway. have been proposed contain bipartite monopartite localization sequences (NLSs), respectively, that allow them be translocated nucleus independently of each other via classical importin-α (Impα)/importin-β-mediated import To determine structural basis recognition proteins Impα, we...

10.1016/j.jmb.2011.07.038 article EN publisher-specific-oa Journal of Molecular Biology 2011-07-26

MLH1 and PMS2 proteins form the MutLα heterodimer, which plays a major role in DNA mismatch repair (MMR) humans. Mutations MMR-related are associated with cancer, especially colon cancer. The N-terminal region of comprises N-termini and, similarly, C-terminal is composed by C-termini MLH1, two connected linker region. nuclear localization sequences (NLSs) necessary for transport found this However, exact NLS have been controversial, different reported, particularly MLH1. individual...

10.1016/j.biochi.2017.11.013 article EN publisher-specific-oa Biochimie 2017-11-24

Flap endonuclease 1 (FEN1) is a member of the nuclease family and structurally conserved from bacteriophages to humans. This protein involved in multiple DNA-processing pathways, including Okazaki fragment maturation, stalled replication-fork rescue, telomere maintenance, long-patch base-excision repair apoptotic DNA fragmentation. FEN1 has three functional motifs that are responsible for its nuclease, PCNA-interaction nuclear localization activities, respectively. It been shown C-terminal...

10.1107/s0907444912010281 article EN Acta Crystallographica Section D Biological Crystallography 2012-06-15

Abstract Importin-α (Impα) is an adaptor protein that binds to cargo proteins (containing Nuclear Localization Sequences - NLSs), for their translocation the nucleus. The specificities of Impα/NLS interactions have been studied, since these features could be used as important tools find potential NLSs in nuclear or even development targets inhibit import design peptides drug delivery. Few structural studies compared different Impα variants from same organism organisms. Previously, we...

10.1038/s41598-020-58316-9 article EN cc-by Scientific Reports 2020-01-29

The classical nuclear import pathway is mediated by importin (Impα and Impβ), which recognizes the cargo protein its localization sequence (NLS). NLSs have been extensively studied resulting in different proposed consensus; however, recent studies showed that exceptions may occur. This mechanism be also dependent on specific characteristics of Impα. Aiming to better understand importance residues from consensus adjacent regions NLSs, we mutations a high-affinity NLS complexed Impα...

10.1042/bcj20210401 article EN cc-by Biochemical Journal 2021-07-01
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