Amanda Quijano

ORCID: 0000-0001-8639-8467
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About
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Research Areas
  • Glycosylation and Glycoproteins Research
  • Protein Tyrosine Phosphatases
  • Peptidase Inhibition and Analysis
  • HER2/EGFR in Cancer Research
  • Lung Cancer Treatments and Mutations
  • Cancer Research and Treatments
  • Chronic Lymphocytic Leukemia Research
  • Cancer-related Molecular Pathways
  • Lung Cancer Research Studies
  • Cancer, Hypoxia, and Metabolism
  • Mechanisms of cancer metastasis
  • Nanoplatforms for cancer theranostics
  • Glioma Diagnosis and Treatment
  • Advanced Drug Delivery Systems
  • Nanoparticle-Based Drug Delivery
  • Microtubule and mitosis dynamics
  • Neuroblastoma Research and Treatments

Yale University
2018

Asparagine (N)-linked glycosylation is a posttranslational modification essential for the function of complex transmembrane proteins. However, targeting cancer therapy has not been feasible due to generalized effects on all glycoproteins. Here, we perform sensitivity screening 94 lung cell lines using NGI-1, small-molecule inhibitor oligosaccharyltransferase (OST) that partially disrupts N-linked glycosylation, and demonstrate selective loss tumor viability. This screen revealed NGI-1 in...

10.1158/0008-5472.can-18-0505 article EN Cancer Research 2018-07-19

Abstract Purpose: Parallel signaling reduces the effects of receptor tyrosine kinase (RTK)–targeted therapies in glioma. We hypothesized that inhibition protein N-linked glycosylation, an endoplasmic reticulum co- and posttranslational modification crucial for RTK maturation activation, could provide a new therapeutic approach glioma radiosensitization. Experimental Design: investigated small-molecule inhibitor oligosaccharyltransferase (NGI-1) on EGFR family receptors, MET, PDGFR, FGFR1....

10.1158/1078-0432.ccr-18-0792 article EN public-domain Clinical Cancer Research 2018-07-02

<div>Abstract<p>Asparagine (N)-linked glycosylation is a posttranslational modification essential for the function of complex transmembrane proteins. However, targeting cancer therapy has not been feasible due to generalized effects on all glycoproteins. Here, we perform sensitivity screening 94 lung cell lines using NGI-1, small-molecule inhibitor oligosaccharyltransferase (OST) that partially disrupts N-linked glycosylation, and demonstrate selective loss tumor viability. This...

10.1158/0008-5472.c.6512343.v1 preprint EN 2023-03-31

<div>Abstract<p>Asparagine (N)-linked glycosylation is a posttranslational modification essential for the function of complex transmembrane proteins. However, targeting cancer therapy has not been feasible due to generalized effects on all glycoproteins. Here, we perform sensitivity screening 94 lung cell lines using NGI-1, small-molecule inhibitor oligosaccharyltransferase (OST) that partially disrupts N-linked glycosylation, and demonstrate selective loss tumor viability. This...

10.1158/0008-5472.c.6512343 preprint EN 2023-03-31

<div>AbstractPurpose:<p>Parallel signaling reduces the effects of receptor tyrosine kinase (RTK)–targeted therapies in glioma. We hypothesized that inhibition protein N-linked glycosylation, an endoplasmic reticulum co- and posttranslational modification crucial for RTK maturation activation, could provide a new therapeutic approach glioma radiosensitization.</p><p><b>Experimental Design:</b> investigated small-molecule inhibitor oligosaccharyltransferase...

10.1158/1078-0432.c.6528881 preprint EN 2023-03-31

<div>AbstractPurpose:<p>Parallel signaling reduces the effects of receptor tyrosine kinase (RTK)–targeted therapies in glioma. We hypothesized that inhibition protein N-linked glycosylation, an endoplasmic reticulum co- and posttranslational modification crucial for RTK maturation activation, could provide a new therapeutic approach glioma radiosensitization.</p><p><b>Experimental Design:</b> investigated small-molecule inhibitor oligosaccharyltransferase...

10.1158/1078-0432.c.6528881.v1 preprint EN 2023-03-31
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