Rafaela Muniz de Queiroz

ORCID: 0000-0001-5962-9071
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About
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Research Areas
  • Cancer-related Molecular Pathways
  • Glycosylation and Glycoproteins Research
  • Ubiquitin and proteasome pathways
  • Carbohydrate Chemistry and Synthesis
  • Natural product bioactivities and synthesis
  • Galectins and Cancer Biology
  • Proteoglycans and glycosaminoglycans research
  • Fibroblast Growth Factor Research
  • Carbon and Quantum Dots Applications
  • Epigenetics and DNA Methylation
  • Sirtuins and Resveratrol in Medicine
  • Protein Kinase Regulation and GTPase Signaling
  • Cancer, Hypoxia, and Metabolism
  • Cancer Research and Treatments
  • DNA Repair Mechanisms
  • Natural Compounds in Disease Treatment
  • Electrochemical sensors and biosensors
  • Essential Oils and Antimicrobial Activity
  • Autophagy in Disease and Therapy
  • Cancer therapeutics and mechanisms
  • Protein Tyrosine Phosphatases
  • Drug Transport and Resistance Mechanisms
  • Heavy Metal Exposure and Toxicity
  • Lanthanide and Transition Metal Complexes
  • Protein Interaction Studies and Fluorescence Analysis

Columbia University
2018-2024

National Center on Addiction and Substance Abuse at Columbia University
2023

Universidade Federal do Rio de Janeiro
2014-2021

Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro
2016

University of Kansas Medical Center
2016

The Hexosamine Biosynthetic Pathway (HBP) is a branch of glycolysis responsible for the production key substrate protein glycosylation, UDP-GlcNAc. Cancer cells present altered glucose metabolism and aberrant pointing to alterations on HBP. Recently it was demonstrated that HBP influences many aspects tumor biology, including development metastasis. In this work we characterize in melanoma analyze its importance cellular processes related metastatic phenotype. We demonstrate an increase...

10.3389/fonc.2019.00116 article EN cc-by Frontiers in Oncology 2019-03-04

Current therapies for glioblastoma multiforme (GBM) are not effective. This study investigated the activity of M. officinalis essential oil (EO) and its major component (citral) in GBM cell lines. Both EO citral decreased viability induced apoptosis cells as demonstrated by DNA fragmentation caspase-3 activation. Antioxidant prevented citral-induced death, indicating dependence on production reactive oxygen species. Citral downmodulated inhibited expression multidrug resistance associated...

10.3109/07357907.2014.905587 article EN Cancer Investigation 2014-04-18

Although the E3 ligase Mdm2 and its homologue binding partner MdmX are major regulators of p53 tumor suppressor protein, it is now evident that have multiple functions do not involve p53. As one example, known can regulate cell migration, although mechanistic insight into this function still lacking. Here we show in cells lacking expression knockdown or MdmX, as well pharmacological inhibition Mdm2/MdmX complex, only reduces migration invasion, but also impairs spreading focal adhesion...

10.1038/s41467-024-51488-2 article EN cc-by-nc-nd Nature Communications 2024-08-20

The protein product of the CDKN1A gene, p21, has been extensively characterized as a negative regulator cell cycle. Nevertheless, it is clear that p21 manifold complex and context-dependent roles can be either tumor suppressive or oncogenic. Most well studied transcriptional target p53 suppressor protein, there are other means by which levels regulated. In this study, we show pharmacological inhibition siRNA-mediated reduction O-GlcNAc transferase (OGT), enzyme responsible for glycosylation...

10.1016/j.jbc.2022.102289 article EN cc-by Journal of Biological Chemistry 2022-07-20

O‐GlcNAcylation is a dynamic post‐translational modification (PTM) that consists of an addition single N‐acetylglucosamine sugar to serine and threonine residues in nuclear, cytoplasmic mitochondrial proteins. The enzyme O‐linked β‐N‐acetylglucosamine transferase (OGT) adds the modification, while O‐GlcNAcase (OGA) removes modification. O‐GlcNAc regulates enzymatic activity, localization, stability protein‐protein interactions on wide range proteins such as transcription factors, structural...

10.1096/fasebj.30.1_supplement.652.2 article EN The FASEB Journal 2016-04-01

Abstract Certain mutations can confer neomorphic gain of function (GOF) activities to the p53 protein that affect cancer progression. Yet concept mutant GOF has been challenged. Here, using various strategies alter status versions in different cell lines, we demonstrate stimulates invasion three-dimensional environments. Mechanistically, enhances RhoA/ROCK-dependent contractility and cell-mediated extracellular matrix (ECM) re-organization via increasing mevalonate pathway-dependent RhoA...

10.1101/2024.10.13.618100 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-10-15

Abstract Mdm2 and its homologue MdmX form an E3-ligase complex that is best understood as the major regulator of p53. Yet have functions in cells are independent their ability to degrade Amongst regulated by cell migration, although molecular mechanism(s) involved not been well characterized. We show, a p53 null model, either siRNA knockdown or pharmacological inhibition Mdm2/X can reduce migration grown monolayer invasion from pre-formed spheroids into collagen-based matrices. This...

10.1158/1538-7445.am2023-lb160 article EN Cancer Research 2023-04-14

Summary Although the E3 ligase Mdm2 and its homologue binding partner MdmX are major regulators of p53 tumor suppressor protein, it is now evident that have multiple functions independent p53. For example, can regulate cell migration, although mechanistic insight into this function still lacking. Here we show in cells lacking expression knockdown or MdmX, as well pharmacological inhibition Mdm2/MdmX complex, not only reduces migration invasion, but also impairs spreading focal adhesion...

10.1101/2023.05.08.539890 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-05-09
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