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Jill A Zitzewitz PhD

TitleAssociate Professor
InstitutionUniversity of Massachusetts Medical School
DepartmentBiochemistry and Molecular Pharmacology
AddressUniversity of Massachusetts Medical School
364 Plantation Street, LRB
Worcester MA 01605
Phone508-856-2251
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    Other Positions
    InstitutionUMMS - School of Medicine
    DepartmentBiochemistry and Molecular Pharmacology

    InstitutionUMMS - School of Medicine
    DepartmentNeurology

    InstitutionUMMS - School of Medicine
    DepartmentNeuroNexus Institute

    InstitutionUMMS - Graduate School of Biomedical Sciences
    DepartmentBiochemistry and Molecular Pharmacology

    InstitutionUMMS - Graduate School of Biomedical Sciences
    DepartmentNeuroscience


    Collapse Biography 
    Collapse education and training
    Carthage College, Kenosha, WI, United StatesBAChemistry
    Washington State University, Pullman, WA, United StatesPHDBioorganic Chemistry

    Collapse Overview 
    Collapse overview


    Protein Misfolding and Disease



    The overall goal of our research program is to probe the folding of ALS-linked proteins in order to provide a molecular level understanding of how misfolding contributes to disease.  A thermodynamic analysis of the molecular interactions stabilizing the native, functional conformation is a key first step to the development of small molecule screening assays for identifying therapeutic compounds that prevent misfolding.  Current research efforts focus on utilizing biophysical methods to probe the folding, misfolding and aberrant aggregation processes in ALS variants of SOD1 and TDP-43.  It is our expectation that these studies will not only lead to new insights into how to prevent misfolding in a set of human diseases, they will also provide guidelines for the biotechnological development of therapeutic small molecules and antibodies to treat disease.



    Academic Background



    Jill Zitzewitz received her B.A. in Chemistry from Carthage College in 1986 and her PhD in Bioorganic Chemistry from Washington University in St. Louis in 1991.  She completed postdoctoral training in protein folding at The Pennsylvania State University, where she was awarded an NIH fellowship.  Jill joined the faculty of Biochemistry and Molecular Pharmacology at UMass Medical School in 2001.




    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. Niu B, Mackness BC, Rempel DL, Zhang H, Cui W, Matthews CR, Zitzewitz JA, Gross ML. Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements. J Am Soc Mass Spectrom. 2017 Feb; 28(2):389-392. PMID: 27924496.
      View in: PubMed
    2. Boopathy S, Silvas TV, Tischbein M, Jansen S, Shandilya SM, Zitzewitz JA, Landers JE, Goode BL, Schiffer CA, Bosco DA. Structural basis for mutation-induced destabilization of profilin 1 in ALS. Proc Natl Acad Sci U S A. 2015 Jun 30; 112(26):7984-9. PMID: 26056300.
      View in: PubMed
    3. Mackness BC, Tran MT, McClain SP, Matthews CR, Zitzewitz JA. Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state. J Biol Chem. 2014 Mar 21; 289(12):8264-76. PMID: 24497641.
      View in: PubMed
    4. Wu CH, Fallini C, Ticozzi N, Keagle PJ, Sapp PC, Piotrowska K, Lowe P, Koppers M, McKenna-Yasek D, Baron DM, Kost JE, Gonzalez-Perez P, Fox AD, Adams J, Taroni F, Tiloca C, Leclerc AL, Chafe SC, Mangroo D, Moore MJ, Zitzewitz JA, Xu ZS, van den Berg LH, Glass JD, Siciliano G, Cirulli ET, Goldstein DB, Salachas F, Meininger V, Rossoll W, Ratti A, Gellera C, Bosco DA, Bassell GJ, Silani V, Drory VE, Brown RH, Landers JE. Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis. Nature. 2012 Aug 23; 488(7412):499-503. PMID: 22801503.
      View in: PubMed
    5. Svensson AK, Bilsel O, Kayatekin C, Adefusika JA, Zitzewitz JA, Matthews CR. Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species. PLoS One. 2010 Apr 09; 5(4):e10064. PMID: 20404910.
      View in: PubMed
    6. Kayatekin C, Zitzewitz JA, Matthews CR. Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species. J Mol Biol. 2010 Apr 30; 398(2):320-31. PMID: 20184893.
      View in: PubMed
    7. Noel AF, Bilsel O, Kundu A, Wu Y, Zitzewitz JA, Matthews CR. The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors. J Mol Biol. 2009 Apr 10; 387(4):1002-16. PMID: 19150359.
      View in: PubMed
    8. Kayatekin C, Zitzewitz JA, Matthews CR. Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase. J Mol Biol. 2008 Dec 12; 384(2):540-55. PMID: 18840448.
      View in: PubMed
    9. Gu Z, Zitzewitz JA, Matthews CR. Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus. J Mol Biol. 2007 Apr 27; 368(2):582-94. PMID: 17359995.
      View in: PubMed
    10. Svensson AK, Bilsel O, Kondrashkina E, Zitzewitz JA, Matthews CR. Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase. J Mol Biol. 2006 Dec 15; 364(5):1084-102. PMID: 17046019.
      View in: PubMed
    11. Svensson AK, Zitzewitz JA, Matthews CR, Smith VF. The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli. Protein Eng Des Sel. 2006 Apr; 19(4):175-85. PMID: 16452118.
      View in: PubMed
    12. Ibarra-Molero B, Zitzewitz JA, Matthews CR. Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1. J Mol Biol. 2004 Mar 5; 336(5):989-96. PMID: 15037063.
      View in: PubMed
    13. Knappenberger JA, Smith JE, Thorpe SH, Zitzewitz JA, Matthews CR. A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding. J Mol Biol. 2002 Aug 2; 321(1):1-6. PMID: 12139928.
      View in: PubMed
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