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Elisabet Mandon PhD

TitleAssociate Professor
InstitutionUMass Chan Medical School
DepartmentMicrobiology and Physiological Systems
AddressUMass Chan Medical School
364 Plantation Street LRB-970
Worcester MA 01605
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    Other Positions
    InstitutionT.H. Chan School of Medicine
    DepartmentGene Therapy Center

    InstitutionT.H. Chan School of Medicine
    DepartmentMicrobiology and Physiological Systems

    InstitutionT.H. Chan School of Medicine
    DepartmentNeuroNexus Institute

    InstitutionMorningside Graduate School of Biomedical Sciences
    DepartmentBiochemistry and Molecular Biotechnology

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    National University of La Plata, Buenos Aires, BA, ArgentinaPHDBiochemistry

    Collapse Overview 
    Collapse Summary
    Focus: Mitochondria and the endoplasmic reticulum
    Collapse overview
    Lab web-page: www.umassmed.edu/mandonlab
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    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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    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. Yi JK, Fujita H, Mandon EC, Gilmore R. Rapid inactivation of the yeast Sec complex selectively blocks transport of post-translationally translocated proteins. J Biol Chem. 2021 10; 297(4):101171. PMID: 34492269.
      Citations:    Fields:    Translation:AnimalsCells
    2. Shrimal S, Cherepanova NA, Mandon EC, Venev SV, Gilmore R. Asparagine-linked glycosylation is not directly coupled to protein translocation across the endoplasmic reticulum in Saccharomyces cerevisiae. Mol Biol Cell. 2019 10 01; 30(21):2626-2638. PMID: 31433728.
      Citations: 9     Fields:    Translation:HumansAnimalsCells
    3. 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 08 31; 293(35):13662-13672. PMID: 29986881.
      Citations: 4     Fields:    Translation:AnimalsCells
    4. Braunger K, Pfeffer S, Shrimal S, Gilmore R, Berninghausen O, Mandon EC, Becker T, F?rster 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.
      Citations: 91     Fields:    Translation:HumansCells
    5. 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 05 12; 292(19):8007-8018. PMID: 28286332.
      Citations: 24     Fields:    Translation:AnimalsCells
    6. 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.
      Citations: 32     Fields:    Translation:Cells
    7. 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.
      Citations: 35     Fields:    Translation:AnimalsCells
    8. 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.
      Citations: 2     Fields:    Translation:AnimalsCells
    9. 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.
      Citations: 21     Fields:    Translation:AnimalsCells
    10. 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 04; 326(5958):1369-73. PMID: 19933108.
      Citations: 145     Fields:    Translation:AnimalsCells
    11. 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.
      Citations: 24     Fields:    Translation:Cells
    12. 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.
      Citations: 35     Fields:    Translation:AnimalsCells
    13. Mandon EC, Gilmore R. The tail end of membrane insertion. Cell. 2007 Mar 23; 128(6):1031-2. PMID: 17382875.
      Citations: 3     Fields:    Translation:AnimalsCells
    14. 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 03; 168(1):67-77. PMID: 15631991.
      Citations: 45     Fields:    Translation:HumansAnimalsCells
    15. Mandon EC, Gilmore R. GTPase twins in the SRP family. Nat Struct Mol Biol. 2004 Feb; 11(2):115-6. PMID: 14749771.
      Citations:    Fields:    Translation:Cells
    16. 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.
      Citations: 19     Fields:    Translation:AnimalsCells
    17. 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.
      Citations: 101     Fields:    Translation:HumansAnimalsCells
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