Keywords
Last Name

David A. Harris, MD, PhD

TitleProfessor
InstitutionBoston University School of Medicine
DepartmentBiochemistry
Address72 E. Concord St Silvio Conte (K)
Boston MA 02118
Phone(617) 638-5090
ORCID ORCID Icon0000-0002-6985-5790
Other Positions
TitleChair of Biochemistry
InstitutionBoston University School of Medicine
DepartmentBiochemistry

TitleGraduate Faculty (Primary Mentor of Grad Students)
InstitutionBoston University School of Medicine, Division of Graduate Medical Sciences

 Awards and Honors

Start-EndDescription
1983Columbia College of Physicians & Surgeons: Frederick P. Gay Memorial Award
1983Columbia College of Physicians & Surgeons: Titus Munson Coan Prize
1981Columbia College of Physicians & Surgeons: Alfred Steiner Research Award
1983-1985National Institutes of Health: Individual National Research Service Award
1986-1991National Institutes of Health: Clinical Investigator Development Award
1991-1994Klingenstein Fellowship Award in the Neurosciences
 Research Expertise & Professional Interests
Expertise in prion diseases and Alzheimer’s disease.

My laboratory investigates the molecular and cellular mechanisms underlying two classes of human neurodegenerative disorders: prion diseases and Alzheimer’s disease. Alzheimer’s disease afflicts 5 million people in the U.S., a number that will increase dramatically as the population ages. Prion diseases are much rarer, but are of great public health concern because of the global emergence of bovine spongiform encephalopathy (“mad cow disease”), and its likely transmission to human beings. Moreover, prions exemplify a novel mechanism of biological information transfer based on self-propagating changes in protein conformation, rather than on inheritance of nucleic acid sequence. Prion and Alzheimer’s diseases are part of a larger group of neurodegenerative disorders, including Parkinson’s, Huntington’s and several other diseases, which are due to protein misfolding and aggregation. A prion-like process may be responsible for the spread of brain pathology in several of these disorders, and there is evidence that the prion protein itself may serve as a cell-surface receptor mediating the neurotoxic effects of multiple kinds of misfolded protein. Thus, our work on prion and Alzheimer’s diseases will likely provide important insights into a number of other chronic, neurodegenerative disorders.

Our work has several broad objectives. First, we wish to understand how the cellular form of the prion protein (PrPC) is converted into the infectious form (PrPSc). To address this question, we have investigated the cellular localization and trafficking of both PrPC and PrPSc, the nature of their association with cell membranes, as well as the molecular features of the conversion process itself. Second, we want to understand how prions and other misfolded protein aggregates cause neurodegeneration, neuronal death and synaptic dysfunction. In this regard, we seek to identify what molecular forms of PrP and the Alzheimer’s Aß peptide represent the proximate neurotoxic species, and what receptors and cellular pathways they activate that lead to pathology. Third, we aim to use our knowledge of the cell biology of prion and Alzheimer’s diseases to develop drug molecules for treatment of these disorders.

We utilize a range of experimental systems and models, including transgenic mice, cultured mammalian cells, yeast (S. cerevisiae), and in vitro systems. We employ a wide variety of techniques, including protein chemistry, light and electron microscopy, mouse transgenetics, high-throughput screening, neuropathological analysis, biophysical techniques (surface plasmon resonance, NMR, X-ray crystallography), electrophysiology (patch-clamping), medicinal chemistry, and drug discovery approaches.

 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. Imberdis T, Heeres JT, Yueh H, Fang C, Zhen J, Rich CB, Glicksman M, Beeler AB, Harris DA. Identification of Anti-prion Compounds using a Novel Cellular Assay. J Biol Chem. 2016 Dec 09; 291(50):26164-26176. PMID: 27803163.
    View in: PubMed
  2. Fang C, Imberdis T, Garza MC, Wille H, Harris DA. A Neuronal Culture System to Detect Prion Synaptotoxicity. PLoS Pathog. 2016 May; 12(5):e1005623. PMID: 27227882.
    View in: PubMed
  3. Saá P, Harris DA, Cervenakova L. Mechanisms of prion-induced neurodegeneration. Expert Rev Mol Med. 2016 Apr 08; 18:e5. PMID: 27055367.
    View in: PubMed
  4. Sempou E, Biasini E, Pinzón-Olejua A, Harris DA, Málaga-Trillo E. Activation of zebrafish Src family kinases by the prion protein is an amyloid-ß-sensitive signal that prevents the endocytosis and degradation of E-cadherin/ß-catenin complexes in vivo. Mol Neurodegener. 2016 Feb 09; 11:18. PMID: 26860872.
    View in: PubMed
  5. Imberdis T, Harris DA. Synthetic Prions Provide Clues for Understanding Prion Diseases. Am J Pathol. 2016 Apr; 186(4):761-4. PMID: 26854642.
    View in: PubMed
  6. Chu NK, Shabbir W, Bove-Fenderson E, Araman C, Lemmens-Gruber R, Harris DA, Becker CF. A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes. J Biol Chem. 2014 Oct 24; 289(43):30144-60. PMID: 25217642.
    View in: PubMed
  7. Zeldich E, Chen CD, Colvin TA, Bove-Fenderson EA, Liang J, Tucker Zhou TB, Harris DA, Abraham CR. The neuroprotective effect of Klotho is mediated via regulation of members of the redox system. J Biol Chem. 2014 Aug 29; 289(35):24700-15. PMID: 25037225.
    View in: PubMed
  8. Imberdis T, Harris DA. Prion permissive pathways: extracellular matrix genes control susceptibility to prion infection. EMBO J. 2014 Jul 17; 33(14):1506-8. PMID: 24952893.
    View in: PubMed
  9. Biasini E, Unterberger U, Solomon IH, Massignan T, Senatore A, Bian H, Voigtlaender T, Bowman FP, Bonetto V, Chiesa R, Luebke J, Toselli P, Harris DA. A mutant prion protein sensitizes neurons to glutamate-induced excitotoxicity. J Neurosci. 2013 Feb 6; 33(6):2408-18. PMID: 23392670.
    View in: PubMed
  10. Fluharty BR, Biasini E, Stravalaci M, Sclip A, Diomede L, Balducci C, La Vitola P, Messa M, Colombo L, Forloni G, Borsello T, Gobbi M, Harris DA. An N-terminal fragment of the prion protein binds to amyloid-ß oligomers and inhibits their neurotoxicity in vivo. J Biol Chem. 2013 Mar 15; 288(11):7857-66. PMID: 23362282.
    View in: PubMed
  11. Biasini E, Harris DA. Prions and Diseases (Volume 1). Zou, W.-Q. and Gambetti, P. (Eds.). Infectious and pathogenic forms of PrP. Springer Verlag. New York. 2013; 135-146.
  12. Biasini E, Harris DA. Targeting the cellular prion protein to treat neurodegeneration. Future Med Chem. 2012 Sep; 4(13):1655-8. PMID: 22924502.
    View in: PubMed
  13. Turnbaugh JA, Unterberger U, Saá P, Massignan T, Fluharty BR, Bowman FP, Miller MB, Supattapone S, Biasini E, Harris DA. The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc). J Neurosci. 2012 Jun 27; 32(26):8817-30. PMID: 22745483.
    View in: PubMed
  14. Biasini E, Turnbaugh JA, Massignan T, Veglianese P, Forloni G, Bonetto V, Chiesa R, Harris DA. The toxicity of a mutant prion protein is cell-autonomous, and can be suppressed by wild-type prion protein on adjacent cells. PLoS One. 2012; 7(3):e33472. PMID: 22428057.
    View in: PubMed
  15. Solomon IH, Biasini E, Harris DA. Ion channels induced by the prion protein: mediators of neurotoxicity. Prion. 2012 Jan-Mar; 6(1):40-5. PMID: 22453177.
    View in: PubMed
  16. Biasini E, Turnbaugh JA, Unterberger U, Harris DA. Prion protein at the crossroads of physiology and disease. Trends Neurosci. 2012 Feb; 35(2):92-103. PMID: 22137337.
    View in: PubMed
  17. Westergard L, Turnbaugh JA, Harris DA. A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation. J Biol Chem. 2011 Dec 23; 286(51):44234-42. PMID: 22025612.
    View in: PubMed
  18. Turnbaugh JA, Westergard L, Unterberger U, Biasini E, Harris DA. The N-terminal, polybasic region is critical for prion protein neuroprotective activity. PLoS One. 2011; 6(9):e25675. PMID: 21980526.
    View in: PubMed
  19. Westergard L, Turnbaugh JA, Harris DA. A nine amino acid domain is essential for mutant prion protein toxicity. J Neurosci. 2011 Sep 28; 31(39):14005-17. PMID: 21957261.
    View in: PubMed
  20. Solomon IH, Khatri N, Biasini E, Massignan T, Huettner JE, Harris DA. An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity. J Biol Chem. 2011 Apr 22; 286(16):14724-36. PMID: 21385869.
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  21. Massignan T, Biasini E, Harris DA. A Drug-Based Cellular Assay (DBCA) for studying cytotoxic and cytoprotective activities of the prion protein: A practical guide. Methods. 2011 Mar; 53(3):214-9. PMID: 21115124.
    View in: PubMed
  22. Solomon IH, Huettner JE, Harris DA. Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cells. J Biol Chem. 2010 Aug 20; 285(34):26719-26. PMID: 20573963.
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  23. Christensen HM, Dikranian K, Li A, Baysac KC, Walls KC, Olney JW, Roth KA, Harris DA. A highly toxic cellular prion protein induces a novel, nonapoptotic form of neuronal death. Am J Pathol. 2010 Jun; 176(6):2695-706. PMID: 20472884.
    View in: PubMed
  24. Li M, Husic N, Lin Y, Christensen H, Malik I, McIver S, LaPash Daniels CM, Harris DA, Kotzbauer PT, Goldberg MP, Snider BJ. Optimal promoter usage for lentiviral vector-mediated transduction of cultured central nervous system cells. J Neurosci Methods. 2010 May 30; 189(1):56-64. PMID: 20347873.
    View in: PubMed
  25. Massignan T, Biasini E, Lauranzano E, Veglianese P, Pignataro M, Fioriti L, Harris DA, Salmona M, Chiesa R, Bonetto V. Mutant prion protein expression is associated with an alteration of the Rab GDP dissociation inhibitor alpha (GDI)/Rab11 pathway. Mol Cell Proteomics. 2010 Apr; 9(4):611-22. PMID: 19996123.
    View in: PubMed
  26. Massignan T, Stewart RS, Biasini E, Solomon IH, Bonetto V, Chiesa R, Harris DA. A novel, drug-based, cellular assay for the activity of neurotoxic mutants of the prion protein. J Biol Chem. 2010 Mar 5; 285(10):7752-65. PMID: 19940127.
    View in: PubMed
  27. Biasini E, Tapella L, Mantovani S, Stravalaci M, Gobbi M, Harris DA, Chiesa R. Immunopurification of pathological prion protein aggregates. PLoS One. 2009; 4(11):e7816. PMID: 19915706.
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  28. Solomon IH, Schepker JA, Harris DA. Prion neurotoxicity: insights from prion protein mutants. Curr Issues Mol Biol. 2010; 12(2):51-61. PMID: 19767650.
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  29. Jeffrey M, Goodsir C, McGovern G, Barmada SJ, Medrano AZ, Harris DA. Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes. Am J Pathol. 2009 Sep; 175(3):1208-17. PMID: 19700753.
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  30. Chiesa R, Harris DA. Fishing for prion protein function. PLoS Biol. 2009 Mar 31; 7(3):e75. PMID: 19338390.
    View in: PubMed
  31. Chiesa R, Piccardo P, Biasini E, Ghetti B, Harris DA. Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities. J Neurosci. 2008 Dec 3; 28(49):13258-67. PMID: 19052217.
    View in: PubMed
  32. Christensen HM, Harris DA. A deleted prion protein that is neurotoxic in vivo is localized normally in cultured cells. J Neurochem. 2009 Jan; 108(1):44-56. PMID: 19046329.
    View in: PubMed
  33. Christensen HM, Harris DA. Prion protein lacks robust cytoprotective activity in cultured cells. Mol Neurodegener. 2008; 3:11. PMID: 18718018.
    View in: PubMed
  34. Greil CS, Vorberg IM, Ward AE, Meade-White KD, Harris DA, Priola SA. Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent. Virology. 2008 Sep 30; 379(2):284-93. PMID: 18692214.
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  35. Biasini E, Seegulam ME, Patti BN, Solforosi L, Medrano AZ, Christensen HM, Senatore A, Chiesa R, Williamson RA, Harris DA. Non-infectious aggregates of the prion protein react with several PrPSc-directed antibodies. J Neurochem. 2008 Jun 1; 105(6):2190-204. PMID: 18298665.
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  36. Medrano AZ, Barmada SJ, Biasini E, Harris DA. GFP-tagged mutant prion protein forms intra-axonal aggregates in transgenic mice. Neurobiol Dis. 2008 Jul; 31(1):20-32. PMID: 18514536.
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  37. Biasini E, Medrano AZ, Thellung S, Chiesa R, Harris DA. Multiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion. J Neurochem. 2008 Mar; 104(5):1293-308. PMID: 18034781.
    View in: PubMed
  38. Dong J, Li A, Yamaguchi N, Sakaguchi S, Harris DA. Doppel induces degeneration of cerebellar Purkinje cells independently of Bax. Am J Pathol. 2007 Aug; 171(2):599-607. PMID: 17569776.
    View in: PubMed
  39. Tank EM, Harris DA, Desai AA, True HL. Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Mol Cell Biol. 2007 Aug; 27(15):5445-55. PMID: 17548473.
    View in: PubMed
  40. Li A, Piccardo P, Barmada SJ, Ghetti B, Harris DA. Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice. EMBO J. 2007 Jun 6; 26(11):2777-85. PMID: 17510630.
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  41. Yin S, Pham N, Yu S, Li C, Wong P, Chang B, Kang SC, Biasini E, Tien P, Harris DA, Sy MS. Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans. Proc Natl Acad Sci U S A. 2007 May 1; 104(18):7546-51. PMID: 17456603.
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  42. Westergard L, Christensen HM, Harris DA. The cellular prion protein (PrP(C)): its physiological function and role in disease. Biochim Biophys Acta. 2007 Jun; 1772(6):629-44. PMID: 17451912.
    View in: PubMed
  43. Li A, Christensen HM, Stewart LR, Roth KA, Chiesa R, Harris DA. Neonatal lethality in transgenic mice expressing prion protein with a deletion of residues 105-125. EMBO J. 2007 Jan 24; 26(2):548-58. PMID: 17245437.
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  44. Li A, Barmada SJ, Roth KA, Harris DA. N-terminally deleted forms of the prion protein activate both Bax-dependent and Bax-independent neurotoxic pathways. J Neurosci. 2007 Jan 24; 27(4):852-9. PMID: 17251426.
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  45. Harris DA, True HL. New insights into prion structure and toxicity. Neuron. 2006 May 4; 50(3):353-7. PMID: 16675391.
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  46. Barmada SJ, Harris DA. Visualization of prion infection in transgenic mice expressing green fluorescent protein-tagged prion protein. J Neurosci. 2005 Jun 15; 25(24):5824-32. PMID: 15958749.
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  47. Stewart RS, Piccardo P, Ghetti B, Harris DA. Neurodegenerative illness in transgenic mice expressing a transmembrane form of the prion protein. J Neurosci. 2005 Mar 30; 25(13):3469-77. PMID: 15800202.
    View in: PubMed
  48. Li A, Harris DA. Mammalian prion protein suppresses Bax-induced cell death in yeast. J Biol Chem. 2005 Apr 29; 280(17):17430-4. PMID: 15753097.
    View in: PubMed
  49. Stewart RS, Harris DA. A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons. J Biol Chem. 2005 Apr 22; 280(16):15855-64. PMID: 15671025.
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  50. Fioriti L, Dossena S, Stewart LR, Stewart RS, Harris DA, Forloni G, Chiesa R. Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations. J Biol Chem. 2005 Mar 25; 280(12):11320-8. PMID: 15632159.
    View in: PubMed
  51. Fioriti L, Quaglio E, Massignan T, Colombo L, Stewart RS, Salmona M, Harris DA, Forloni G, Chiesa R. The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species. Mol Cell Neurosci. 2005 Jan; 28(1):165-76. PMID: 15607951.
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  52. Chiesa R, Piccardo P, Dossena S, Nowoslawski L, Roth KA, Ghetti B, Harris DA. Bax deletion prevents neuronal loss but not neurological symptoms in a transgenic model of inherited prion disease. Proc Natl Acad Sci U S A. 2005 Jan 4; 102(1):238-43. PMID: 15618403.
    View in: PubMed
  53. Barmada S, Piccardo P, Yamaguchi K, Ghetti B, Harris DA. GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice. Neurobiol Dis. 2004 Aug; 16(3):527-37. PMID: 15262264.
    View in: PubMed
  54. Li A, Dong J, Harris DA. Cell surface expression of the prion protein in yeast does not alter copper utilization phenotypes. J Biol Chem. 2004 Jul 9; 279(28):29469-77. PMID: 15090539.
    View in: PubMed
  55. Harris, DA (Ed.). Volume 284 of Curr. Topics in Microbiol. and Immunol. Mad Cow Disease. Springer-Verlag. Berlin. 2004.
  56. Harris DA, Peters PJ, Taraboulos A, Lingappa V, DeArmond SJ, Prusiner SB. Prion Biology and Diseases. Second Edition. Prusiner SB (Ed). Cell biology of prions. Cold Spring Harbor Laboratory Press. Cold Spring Harbor. 2004; 483-544.
  57. Brown LR, Harris DA. Copper and zinc cause delivery of the prion protein from the plasma membrane to a subset of early endosomes and the Golgi. J Neurochem. 2003 Oct; 87(2):353-63. PMID: 14511113.
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  58. Stewart RS, Harris DA. Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J Biol Chem. 2003 Nov 14; 278(46):45960-8. PMID: 12933795.
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  59. Chiesa R, Piccardo P, Quaglio E, Drisaldi B, Si-Hoe SL, Takao M, Ghetti B, Harris DA. Molecular distinction between pathogenic and infectious properties of the prion protein. J Virol. 2003 Jul; 77(13):7611-22. PMID: 12805461.
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  60. Deleault NR, Dolph PJ, Feany MB, Cook ME, Nishina K, Harris DA, Supattapone S. Post-transcriptional suppression of pathogenic prion protein expression in Drosophila neurons. J Neurochem. 2003 Jun; 85(6):1614-23. PMID: 12787080.
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  61. Drisaldi B, Stewart RS, Adles C, Stewart LR, Quaglio E, Biasini E, Fioriti L, Chiesa R, Harris DA. Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J Biol Chem. 2003 Jun 13; 278(24):21732-43. PMID: 12663673.
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  62. Harris DA, Chiesa R, Drisaldi B, Quaglio E, Migheli A, Piccardo P, Ghetti B. A murine model of a familial prion disease. Clin Lab Med. 2003 Mar; 23(1):175-86. PMID: 12733431.
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  63. Harris DA. Trafficking, turnover and membrane topology of PrP. Br Med Bull. 2003; 66:71-85. PMID: 14522850.
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  64. Mangé A, Milhavet O, Umlauf D, Harris D, Lehmann S. PrP-dependent cell adhesion in N2a neuroblastoma cells. FEBS Lett. 2002 Mar 13; 514(2-3):159-62. PMID: 11943143.
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  65. Brown LR, Harris DA. Handbook of Copper Pharmacology and Toxicology. Massaro EJ (Ed). The prion protein and copper: what is the connection?. Human Press. Totowa. 2002; 103-113.
  66. Harris DA, Brown LR, Quaglio E, Drisaldi B, Chiesa R. Prion Diseases and Copper Metabolism. Brown, DR (Ed). The effects of copper on the cellular trafficking and biochemical properties of the prion protein. Horwood Publishing, Ltd. Chichester. 2002; 25-35.
  67. Chiesa R, Harris DA. Prion diseases: what is the neurotoxic molecule? Neurobiol Dis. 2001 Oct; 8(5):743-63. PMID: 11592845.
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  68. Ivanova L, Barmada S, Kummer T, Harris DA. Mutant prion proteins are partially retained in the endoplasmic reticulum. J Biol Chem. 2001 Nov 9; 276(45):42409-21. PMID: 11527974.
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  69. Chiesa R, Pestronk A, Schmidt RE, Tourtellotte WG, Ghetti B, Piccardo P, Harris DA. Primary myopathy and accumulation of PrPSc-like molecules in peripheral tissues of transgenic mice expressing a prion protein insertional mutation. Neurobiol Dis. 2001 Apr; 8(2):279-88. PMID: 11300723.
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  70. Stewart RS, Drisaldi B, Harris DA. A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum. Mol Biol Cell. 2001 Apr; 12(4):881-9. PMID: 11294893.
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  71. Quaglio E, Chiesa R, Harris DA. Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform. J Biol Chem. 2001 Apr 6; 276(14):11432-8. PMID: 11278539.
    View in: PubMed
  72. Harris DA, Chiesa R, Migheli A, Piccardo P, Ghetti B. Cellular and transgenic models of familial prion diseases. Methods Mol Med. 2001; 59:149-61. PMID: 21374503.
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  73. Harris DA. Biosynthesis and cellular processing of the prion protein. Adv Protein Chem. 2001; 57:203-28. PMID: 11447691.
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  74. Lehmann S, Laude H, Harris DA, Carp C, Vilette D, Katamine S, Madec JY, Nishida N. Alzheimer’s Disease: Advances in Etiology, Pathogenesis and Therapeutics. Iqbal K, Sisodia SS, Winblad B (Eds). Ex vivo transmission of mouse-adapted scrapie strains to N2a and GT1-7 cell lines. John Wiley and Sons. Chichester. 2001; 679-686.
  75. Harris DA. Advances in Protein Chemistry: Prion Proteins. Caughey, B. (Ed.). Biosynthesis and cellular processing of the prion protein. Academic Press. San Diego. 2001; 57:203-228.
  76. Stewart RS, Harris DA. Most pathogenic mutations do not alter the membrane topology of the prion protein. J Biol Chem. 2001 Jan 19; 276(3):2212-20. PMID: 11053411.
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  77. Harris DA. Prion diseases. Nutrition. 2000 Jul-Aug; 16(7-8):554-6. PMID: 10906553.
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  78. Chiesa R, Harris DA. Nerve growth factor-induced differentiation does not alter the biochemical properties of a mutant prion protein expressed in PC12 cells. J Neurochem. 2000 Jul; 75(1):72-80. PMID: 10854249.
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  79. Chiesa R, Drisaldi B, Quaglio E, Migheli A, Piccardo P, Ghetti B, Harris DA. Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation. Proc Natl Acad Sci U S A. 2000 May 9; 97(10):5574-9. PMID: 10805813.
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  80. Waggoner DJ, Drisaldi B, Bartnikas TB, Casareno RL, Prohaska JR, Gitlin JD, Harris DA. Brain copper content and cuproenzyme activity do not vary with prion protein expression level. J Biol Chem. 2000 Mar 17; 275(11):7455-8. PMID: 10713045.
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  81. Soto C, Kascsak RJ, Saborío GP, Aucouturier P, Wisniewski T, Prelli F, Kascsak R, Mendez E, Harris DA, Ironside J, Tagliavini F, Carp RI, Frangione B. Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides. Lancet. 2000 Jan 15; 355(9199):192-7. PMID: 10675119.
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  82. Nishida N, Harris DA, Vilette D, Laude H, Frobert Y, Grassi J, Casanova D, Milhavet O, Lehmann S. Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J Virol. 2000 Jan; 74(1):320-5. PMID: 10590120.
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  83. Harris DA, Chiesa R, Drisaldi B, Quaglio E, Migheli A, Piccardo P, Ghetti B. A transgenic model of a familial prion disease. Arch Virol Suppl. 2000; (16):103-12. PMID: 11214912.
    View in: PubMed
  84. Narwa R, Harris DA. Prion proteins carrying pathogenic mutations are resistant to phospholipase cleavage of their glycolipid anchors. Biochemistry. 1999 Jul 6; 38(27):8770-7. PMID: 10393552.
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  85. Harris DA. Cellular biology of prion diseases. Clin Microbiol Rev. 1999 Jul; 12(3):429-44. PMID: 10398674.
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  86. Saborío GP, Soto C, Kascsak RJ, Levy E, Kascsak R, Harris DA, Frangione B. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem Biophys Res Commun. 1999 May 10; 258(2):470-5. PMID: 10329411.
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  87. Harris DA. Cell biological studies of the prion protein. Curr Issues Mol Biol. 1999; 1(1-2):65-75. PMID: 11475702.
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  88. Harris DA. Molecular and Cellular Biology. Harris, D.A., (Ed.). Cell biological studies of the prion protein. Horizon Scientific Press. Wymondham (UK). 1999; 53-65.
  89. Chiesa R, Piccardo P, Ghetti B, Harris DA. Alzheimer’s Disease and Related Disorders: Etiology, Pathogenesis, and Therapeutics. Iqbal, K., Swaab, D.F., Winblad, B., and Wisniewski, H.M. (Eds.). A transgenic mouse model of a familial prion disease with an insertional mutation. John Wiley and Sons. Chichester. 1999; 569-580.
  90. Harris DA. GPI-Anchored Membrane Proteins and Carbohydrates. Hoessli, D.C., and Ilangumaran, S. (Eds.). GPI-anchored proteins in the nervous system. R.G. Landes. Austin, Texas. 1999; 93-108.
  91. Pauly PC, Harris DA. Copper stimulates endocytosis of the prion protein. J Biol Chem. 1998 Dec 11; 273(50):33107-10. PMID: 9837873.
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  92. Chiesa R, Piccardo P, Ghetti B, Harris DA. Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron. 1998 Dec; 21(6):1339-51. PMID: 9883727.
    View in: PubMed
  93. Harris DA, Lehmann S, Daude N. Prions and Brain Diseases in Animals and Humans; Morrison, D.R.O. (Ed.). Familial prion diseases modeled in cell culture. Plenum. New York. 1998; 295:87-98.
  94. Harris DA. Advances in Neurodegenerative Disorders Volume 2: Alzheimer’s and Aging. Marwah J, Teitelbaum H (Eds). Generation of prions in cultured cells. Prominent Press. Scottsdale, Arizona. 1998; 183-202.
  95. Harris DA. Clathrin-coated vesicles and detergent-resistant rafts in prion biology. Bull. Inst. Pasteur. 1998; 96:207-212.
  96. Harris DA. Amyloid: Int. J. Exp. Clin. Invest. Book review of: Prion Diseases of Mammals and Yeast: Molecular Mechanisms and Genetic Features by R.B. Wickner. Chapman and Hall. New York. 1998; 5:145.
  97. Lehmann S, Daude N, Harris DA. A wild-type prion protein does not acquire properties of the scrapie isoform when coexpressed with a mutant prion protein in cultured cells. Brain Res Mol Brain Res. 1997 Dec 1; 52(1):139-45. PMID: 9450686.
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  98. Lehmann S, Harris DA. Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J Biol Chem. 1997 Aug 22; 272(34):21479-87. PMID: 9261166.
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  99. Lehmann S, Chiesa R, Harris DA. Evidence for a six-transmembrane domain structure of presenilin 1. J Biol Chem. 1997 May 2; 272(18):12047-51. PMID: 9115271.
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  100. Daude N, Lehmann S, Harris DA. Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J Biol Chem. 1997 Apr 25; 272(17):11604-12. PMID: 9111077.
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  101. Harris DA, Lehmann S. Alzheimer’s Disease: Biology, Diagnosis and Therapeutics. Iqbal K, Winblad B, Nishimura T, Takeda M, Wisniewski HM (Eds). Mutant prion proteins acquire PrPSc-like properties in cultured cells: an experimental model of familial prion diseases. John Wiley and Sons. Chichester. 1997; 631-643.
  102. Lehmann S, Harris DA. Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc Natl Acad Sci U S A. 1996 May 28; 93(11):5610-4. PMID: 8643624.
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  103. Lehmann S, Harris DA. Mutant and infectious prion proteins display common biochemical properties in cultured cells. J Biol Chem. 1996 Jan 19; 271(3):1633-7. PMID: 8576163.
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  104. Harris DA, Gorodinsky A, Lehmann S, Moulder K, Shyng SL. Cell biology of the prion protein. Curr Top Microbiol Immunol. 1996; 207:77-93. PMID: 8575208.
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  105. Harris DA, Lehmann S. Transmissible Subacute Spongiform Encephalopathies: Prion Diseases; Court L, Dodet B (Eds). A cell culture model of familial prion diseases. Elsevier. Paris. 1996; 339-346.
  106. Shyng SL, Lehmann S, Moulder KL, Harris DA. Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells. J Biol Chem. 1995 Dec 15; 270(50):30221-9. PMID: 8530433.
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  107. Lehmann S, Harris DA. A mutant prion protein displays an aberrant membrane association when expressed in cultured cells. J Biol Chem. 1995 Oct 13; 270(41):24589-97. PMID: 7592679.
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  108. Shyng SL, Moulder KL, Lesko A, Harris DA. The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits. J Biol Chem. 1995 Jun 16; 270(24):14793-800. PMID: 7782345.
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  109. Gorodinsky A, Harris DA. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J Cell Biol. 1995 May; 129(3):619-27. PMID: 7537273.
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  110. Shyng SL, Heuser JE, Harris DA. A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits. J Cell Biol. 1994 Jun; 125(6):1239-50. PMID: 7911471.
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  111. Shyng SL, Huber MT, Harris DA. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J Biol Chem. 1993 Jul 25; 268(21):15922-8. PMID: 8101844.
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  112. Harris DA, Lele P, Snider WD. Localization of the mRNA for a chicken prion protein by in situ hybridization. Proc Natl Acad Sci U S A. 1993 May 1; 90(9):4309-13. PMID: 8483948.
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  113. Harris DA, Huber MT, van Dijken P, Shyng SL, Chait BT, Wang R. Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry. 1993 Feb 2; 32(4):1009-16. PMID: 8093841.
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  114. Harris DA, Lele P, Snider WD. Localization of the mRNA for a chicken prion-like protein by in situ hybridization. Proc. Natl. Acad. Sci. USA. 1993; 90:4309-4313.
  115. Shyng SL, Huber M, Harris DA. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 1993; 268:15922-15928.
  116. Harris DA, Falls DL, Johnson FA, Fischbach GD. A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity. Proc Natl Acad Sci U S A. 1991 Sep 1; 88(17):7664-8. PMID: 1715573.
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  117. Harris DA, Sherbany AA. Cloning of non-polyadenylated RNAs from rat brain. Brain Res Mol Brain Res. 1991 Apr; 10(1):83-90. PMID: 1647486.
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  118. Harris DA, Falls DL, Johnson FA, Fischbach GD. A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity. Proc. Natl. Acad. Sci USA. 1991; 88:7664-7668.
  119. Falls DL, Harris DA, Johnson FA, Morgan MM, Corfas G, Fischbach GD. Mr 42,000 ARIA: a protein that may regulate the accumulation of acetylcholine receptors at developing chick neuromuscular junctions. Cold Spring Harb Symp Quant Biol. 1990; 55:397-406. PMID: 2132829.
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  120. Harris DA, Falls DL, Fischbach GD. Differential activation of myotube nuclei following exposure to an acetylcholine receptor-inducing factor. Nature. 1989 Jan 12; 337(6203):173-6. PMID: 2911351.
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  121. Fischbach GD, Harris DA, Falls DL, Dubinsky JM, Morgan M, Engisch KL, Johnson FA. Neuromuscular Junction. Fernstrom Foundation Series; Sellin LC, Libelius R, Thesleff S (Eds.). The accumulation of acetylcholine receptors at developing chick nerve-muscle synapses. Elsevier. Amsterdam. 1989; 13:515-532.
  122. Harris DA, Falls DL, Dill-Devor RM, Fischbach GD. Acetylcholine receptor-inducing factor from chicken brain increases the level of mRNA encoding the receptor alpha subunit. Proc Natl Acad Sci U S A. 1988 Mar; 85(6):1983-7. PMID: 2831539.
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  123. Harris DA, Sherbany AA, Schwartz JH. Purification and characterization of muscle proteins from Aplysia californica. Biological Bulletin. 1984; 166:482-493.
  124. Wilkins JA, Schwartz JH, Harris DA. Brevin, a serum protein that acts on the barbed end of actin filaments. Cell Biol Int Rep. 1983 Dec; 7(12):1097-1104. PMID: 6667506.
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  125. Goldberg DJ, Harris DA, Schwartz JH. Studies on the mechanism of fast axoplasmic transport using microinjection into single giant neurons. Cold Spring Harb Symp Quant Biol. 1982; 46 Pt 1:135-40. PMID: 6179691.
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  126. Harris DA, Schwartz JH. Characterization of brevin, a serum protein that shortens actin filaments. Proc Natl Acad Sci U S A. 1981 Nov; 78(11):6798-802. PMID: 6947253.
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  127. Goldberg DJ, Harris DA, Lubit BW, Schwartz JH. Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: evidence for a possible role of actin filaments. Proc Natl Acad Sci U S A. 1980 Dec; 77(12):7448-52. PMID: 6164061.
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