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Elisabet Mandon PhD

TitleAssociate Professor
InstitutionUniversity of Massachusetts Medical School
DepartmentBiochemistry and Molecular Pharmacology
AddressUniversity of Massachusetts Medical School
364 Plantation Street, LRB-970
Worcester MA 01605
Phone508-856-6051
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    Other Positions
    InstitutionUMMS - School of Medicine
    DepartmentBiochemistry and Molecular Pharmacology

    InstitutionUMMS - School of Medicine
    DepartmentNeuroNexus Institute

    InstitutionUMMS - Graduate School of Biomedical Sciences
    DepartmentBiochemistry and Molecular Pharmacology


    Collapse Biography 
    Collapse education and training
    National University of La Plata, Buenos Aires, BA, ArgentinaPHDBiochemistry

    Collapse Overview 
    Collapse overview
    Lab web-page: www.umassmed.edu/mandonlab

    Collapse Post Docs

    A postdoctoral research position is available  to investigate Amyotrophic LateralSclerosis (ALS) mitochondrial dysfunction. ALS causes motor neurondegeneration, then paralysis and death. An early target in ALS is themitochondrion, whose dysfunction enhances ALS progression. The most commonALS-causing mutations are found in the copper-zinc superoxide dismutase (SOD1)gene. Most wild type (WT) SOD1 protein (SOD1WT) resides in the cytosol and only1% is targeted to the inner mitochondrial space (IMS). In contrast, mutant SOD1protein (SOD1mut) accumulates in the mitochondrial outer membrane and in thematrix, and subsequently impairs mitochondrial function by a mechanism that ispoorly understood. Abnormal SOD1mut accumulation leads to mitochondrialdysfunction found in the early stage of presymptomatic ALS mice, before theonset of motor neuron degeneration. Thus, it is critical to determine the firstevent induced by SOD1mut and devise a strategy to stop or delay it beforemitochondrial damage becomes irreversible. The objective of future studies willbe to determine which step/steps are affected by the SOD1 mutation byidentifying the sequence of events involved in SOD1mut and SOD1WT mitochondrialtargeting, import and IMS-sorting. This project will provide important basicinformation on the mechanisms underlying mitochondrial dysfunction in ALS andwill identify possible targets for future therapies.

                 Applicants must have (or expect toobtain shortly) a Ph.D. in Biochemistry, Cell Biology, Molecular Biology or arelated field and be strongly motivated to conduct research in an excitingresearch environment. 

     




    Collapse Bibliographic 
    Collapse selected publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    1. Mandon EC, Butova C, Lachapelle A, Gilmore R. Conserved motifs on the cytoplasmic face of the protein translocation channel are critical for the transition between resting and active conformations. J Biol Chem. 2018 Jul 09. PMID: 29986881.
      View in: PubMed
    2. Braunger K, Pfeffer S, Shrimal S, Gilmore R, Berninghausen O, Mandon EC, Becker T, Förster F, Beckmann R. Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum. Science. 2018 04 13; 360(6385):215-219. PMID: 29519914.
      View in: PubMed
    3. Tripathi A, Mandon EC, Gilmore R, Rapoport TA. Two alternative binding mechanisms connect the protein translocation Sec71/Sec72 complex with heat shock proteins. J Biol Chem. 2017 Mar 12. PMID: 28286332.
      View in: PubMed
    4. Mandon EC, Trueman SF, Gilmore R. Protein translocation across the rough endoplasmic reticulum. Cold Spring Harb Perspect Biol. 2013 Feb 01; 5(2). PMID: 23251026.
      View in: PubMed
    5. Trueman SF, Mandon EC, Gilmore R. A gating motif in the translocation channel sets the hydrophobicity threshold for signal sequence function. J Cell Biol. 2012 Dec 10; 199(6):907-18. PMID: 23229898.
      View in: PubMed
    6. Gilmore R, Mandon EC. Understanding integration of a-helical membrane proteins: the next steps. Trends Biochem Sci. 2012 Aug; 37(8):303-8. PMID: 22748693.
      View in: PubMed
    7. Trueman SF, Mandon EC, Gilmore R. Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity. Mol Biol Cell. 2011 Sep; 22(17):2983-93. PMID: 21737680.
      View in: PubMed
    8. Becker T, Bhushan S, Jarasch A, Armache JP, Funes S, Jossinet F, Gumbart J, Mielke T, Berninghausen O, Schulten K, Westhof E, Gilmore R, Mandon EC, Beckmann R. Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome. Science. 2009 Dec 4; 326(5958):1369-73. PMID: 19933108.
      View in: PubMed
    9. Mandon EC, Trueman SF, Gilmore R. Translocation of proteins through the Sec61 and SecYEG channels. Curr Opin Cell Biol. 2009 Aug; 21(4):501-7. PMID: 19450960.
      View in: PubMed
    10. Jiang Y, Cheng Z, Mandon EC, Gilmore R. An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation. J Cell Biol. 2008 Mar 24; 180(6):1149-61. PMID: 18347066.
      View in: PubMed
    11. Mandon EC, Gilmore R. The tail end of membrane insertion. Cell. 2007 Mar 23; 128(6):1031-2. PMID: 17382875.
      View in: PubMed
    12. Cheng Z, Jiang Y, Mandon EC, Gilmore R. Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation. J Cell Biol. 2005 Jan 3; 168(1):67-77. PMID: 15631991.
      View in: PubMed
    13. Mandon EC, Gilmore R. GTPase twins in the SRP family. Nat Struct Mol Biol. 2004 Feb; 11(2):115-6. PMID: 14749771.
      View in: PubMed
    14. Mandon EC, Jiang Y, Gilmore R. Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum. J Cell Biol. 2003 Aug 18; 162(4):575-85. PMID: 12913112.
      View in: PubMed
    15. Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R. Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul; 12(1):101-11. PMID: 12887896.
      View in: PubMed
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