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Search: WFRF:(Lema Rafael)

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1.
  • Orellana, Laura, et al. (author)
  • Oncogenic mutations at the EGFR ectodomain structurally converge to remove a steric hindrance on a kinase-coupled cryptic epitope
  • 2019
  • In: Proceedings of the National Academy of Sciences of the United States of America. - : NATL ACAD SCIENCES. - 0027-8424 .- 1091-6490. ; 116:20, s. 10009-10018
  • Journal article (peer-reviewed)abstract
    • Epidermal growth factor receptor (EGFR) signaling is initiated by a large ligand-favored conformational change of the extracellular domain (ECD) from a closed, self-inhibited tethered monomer, to an open untethered state, which exposes a loop required for strong dimerization and activation. In glioblastomas (GBMs), structurally heterogeneous missense and deletion mutations concentrate at the ECD for unclear reasons. We explore the conformational impact of GBM missense mutations, combining elastic network models (ENMs) with multiple molecular dynamics (MD) trajectories. Our simulations reveal that the main missense class, located at the I-II interface away from the self-inhibitory tether, can unexpectedly favor spontaneous untethering to a compact intermediate state, here validated by small-angle X-ray scattering (SAXS). Significantly, such intermediate is characterized by the rotation of a large ECD fragment (N-TR1), deleted in the most common GBM mutation, EGFRvIII, and that makes accessible a cryptic epitope characteristic of cancer cells. This observation suggested potential structural equivalence of missense and deletion ECD changes in GBMs. Corroborating this hypothesis, our FACS, in vitro, and in vivo data demonstrate that entirely different ECD variants all converge to remove N-TR1 steric hindrance from the 806-epitope, which we show is allosterically coupled to an intermediate kinase and hallmarks increased oncogenicity. Finally, the detected extraintracellular coupling allows for synergistic cotargeting of the intermediate with mAb806 and inhibitors, which is proved herein.
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2.
  • Rojas-Lema, Sandra, et al. (author)
  • “Faba bean protein films reinforced with cellulose nanocrystals as edible food packaging material”
  • 2021
  • In: Food Hydrocolloids. - : Elsevier B.V.. - 0268-005X .- 1873-7137. ; 121
  • Journal article (peer-reviewed)abstract
    • In the present work, transparent films were obtained by the solution casting method from faba bean protein isolate (FBP), reinforced with different cellulose nanocrystals (CNCs) content (1, 3, 5 and 7 wt%), obtained by acid hydrolysis of pine cone, and using glycerol as plasticizer. The influence of different CNCs loadings on the mechanical, thermal, barrier, optical, and morphological properties was discussed. Microstructurally, the FTIR and FESEM results corroborated the formation of intramolecular interactions between the CNCs and proteins that lead to more compact and homogeneous films. These interactions had a positive influence on the mechanical strength properties, which is reflected in higher tensile strength and Young's modulus in reinforced films with respect to the control film, resulting in stiffer films as the CNCs content increases. Thermal stability of the FBP films was also improved with the presence of CNCs, by increasing the characteristic onset degradation temperature. In addition, the linkages formed between the CNCs, and proteins reduced the water affinity of the reinforced films, leading to a reduction in their moisture content and water solubility, and an increase in their water contact angle, obtaining more hydrophobic films as the CNCs content in the matrix increased. The addition of CNCs in the FBP film also considerably improved its barrier properties, reducing its water vapour transmission rate (WVTR) and oxygen transmission rate (OTR). The present work shows the possibility of obtaining biobased and biodegradable films of CNC-reinforced FBP with improved mechanical, thermal and barrier properties, and low water susceptibility, which can be of great interest in the food packaging sector as edible food packaging material.
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