David Harris | Profiles RNS

David A. Harris, MD, PhD

Chair of Biochemistry

Boston University Chobanian & Avedisian School of Medicine

Biochemistry & Cell Biology

MD, Columbia University
PhD, Columbia University
BS, Yale University

Websites

Biochemistry Faculty

ORCID : 0000-0002-6985-5790

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.

Edgar Minas Housepian, MD Professor
Boston University Chobanian & Avedisian School of Medicine
Biochemistry & Cell Biology

Member
Boston University
Evans Center for Interdisciplinary Biomedical Research

Member
Boston University
Genome Science Institute

Graduate Faculty (Primary Mentor of Grad Students)
Boston University Chobanian & Avedisian School of Medicine, Graduate Medical Sciences

BU Research
NIH RePORTER Research

Mechanisms of Prion Protein Toxicity
07/01/2021 - 06/30/2026 (PI)
NIH/National Institute of Neurological Disorders & Stroke
5R01NS065244-13

Discovering How Cu(II)/Zn(II) Uptake by the Prion Protein Controls Structure, Function and Neurotoxicity
07/01/2019 - 04/30/2024 (Subcontract PI)
The University of California, Santa Cruz NIH NIGMS
5R35GM131781-04

Micro-Mapping to Identify Receptors for Toxic Protein Oligomers in Neurodegenerative Diseases
02/10/2022 - 02/09/2024 (PI)
Merck, Sharp & Dohme LLC

Identification of Receptors for TDP-43 That Mediate Cellular Uptake and Neurotoxicity
02/15/2021 - 08/14/2023 (Key Person / Mentor)
PI: Robert C. Mercer, PhD
Department of Defense/Army Medical Research Acquisition Activity

Signaling Pathways Underlying Prion Neurotoxicity
05/01/2019 - 04/30/2022 (Key Person / Mentor)
PI: Nhat Le, PhD
Warren Alpert Foundation

Genomic and Proteomic Analysis of Prion Synaptotoxicity
09/15/2018 - 08/31/2021 (PI)
NIH/National Institute of Neurological Disorders & Stroke
5R21NS107755-02

Mechanisms of Prion Protein Toxicity
03/01/2016 - 06/30/2021 (PI)
NIH/National Institute of Neurological Disorders & Stroke
5R01NS065244-10

Modeling prion diseases using human iPSC-derived neurons
03/15/2019 - 02/28/2021 (Multi-PI)
PI: David A. Harris, MD, PhD
NIH/National Institute of Neurological Disorders & Stroke
1R21NS111499-01

Molecular Aspects of Copper and Zinc Binding to the Prion Protein
07/01/2015 - 06/30/2019 (Subcontract PI)
The University of California, Santa Cruz NIH NIGMS
5R01GM065790-16

Identification of Anti-Prion Drug Targets
04/01/2017 - 03/31/2019 (PI)
NIH/National Institute of Neurological Disorders & Stroke
5R21NS101659-02

Showing 10 of 18 results. Show All Results

Title

Yr	Title	Project-Sub Proj	Pubs
2023	Mechanisms of Prion Protein Toxicity	5R01NS065244-13
2022	Mechanisms of Prion Protein Toxicity	5R01NS065244-12
2021	Mechanisms of Prion Protein Toxicity	2R01NS065244-11A1	29
2020	Mechanisms of Prion Protein Toxicity	5R01NS065244-10	29
2019	Modeling prion diseases using human iPSC-derived neurons	1R21NS111499-01
2019	Genomic and Proteomic Analysis of Prion Synaptotoxicity	5R21NS107755-02	2
2019	Mechanisms of Prion Protein Toxicity	5R01NS065244-09	29
2018	Genomic and Proteomic Analysis of Prion Synaptotoxicity	1R21NS107755-01A1	2
2018	Identification of Anti-Prion Drug Targets	5R21NS101659-02	2
2018	Mechanisms of Prion Protein Toxicity	5R01NS065244-08	29

Showing 10 of 85 results. Show All Results

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.

iCite Analysis Copy PMIDs To Clipboard

Mercer RCC, Le NTT, Houser MCQ, Beeler AB, Harris DA. Sigma receptor ligands are potent anti-prion compounds that act independently of sigma receptor binding. bioRxiv. 2023 Nov 29.View Related Profiles.

Harris, David
Mercer, Robert

PMID: 38077011; PMCID: PMC10705434; DOI: 10.1101/2023.11.28.569035;

Schilling KM, Jorwal P, Ubilla-Rodriguez NC, Assafa TE, Gatdula JRP, Vultaggio JS, Harris DA, Millhauser GL. N-glycosylation is a potent regulator of prion protein neurotoxicity. J Biol Chem. 2023 Sep; 299(9):105101.View Related Profiles.

Harris, David
Jorwal, Pooja

PMID: 37507020; PMCID: PMC10469999; DOI: 10.1016/j.jbc.2023.105101;

Mercer RCC, Harris DA. Mechanisms of prion-induced toxicity. Cell Tissue Res. 2023 Apr; 392(1):81-96.View Related Profiles.

Harris, David
Mercer, Robert

PMID: 36070155

Shafiq M, Da Vela S, Amin L, Younas N, Harris DA, Zerr I, Altmeppen HC, Svergun D, Glatzel M. The prion protein and its ligands: Insights into structure-function relationships. Biochim Biophys Acta Mol Cell Res. 2022 06; 1869(6):119240.View Related Profiles.

Harris, David
Amin, Ladan

PMID: 35192891

Linsenmeier L, Mohammadi B, Shafiq M, Frontzek K, Bär J, Shrivastava AN, Damme M, Song F, Schwarz A, Da Vela S, Massignan T, Jung S, Correia A, Schmitz M, Puig B, Hornemann S, Zerr I, Tatzelt J, Biasini E, Saftig P, Schweizer M, Svergun D, Amin L, Mazzola F, Varani L, Thapa S, Gilch S, Schätzl H, Harris DA, Triller A, Mikhaylova M, Aguzzi A, Altmeppen HC, Glatzel M. Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies. Sci Adv. 2021 Nov 26; 7(48):eabj1826.View Related Profiles.

Harris, David
Amin, Ladan
Massignan, Tania

PMID: 34818048; PMCID: PMC8612689; DOI: 10.1126/sciadv.abj1826;

Amin L, Harris DA. Aß receptors specifically recognize molecular features displayed by fibril ends and neurotoxic oligomers. Nat Commun. 2021 06 08; 12(1):3451.View Related Profiles.

Harris, David
Amin, Ladan

PMID: 34103486; PMCID: PMC8187732; DOI: 10.1038/s41467-021-23507-z;

Kim SY, Zhang F, Harris DA, Linhardt RJ. Structural Features of Heparin and Its Interactions With Cellular Prion Protein Measured by Surface Plasmon Resonance. Front Mol Biosci. 2020; 7:594497. PMID: 33324681; PMCID: PMC7726446; DOI: 10.3389/fmolb.2020.594497;

Schilling KM, Tao L, Wu B, Kiblen JTM, Ubilla-Rodriguez NC, Pushie MJ, Britt RD, Roseman GP, Harris DA, Millhauser GL. Both N-Terminal and C-Terminal Histidine Residues of the Prion Protein Are Essential for Copper Coordination and Neuroprotective Self-Regulation. J Mol Biol. 2020 07 24; 432(16):4408-4425. PMID: 32473880; PMCID: PMC7387163; DOI: 10.1016/j.jmb.2020.05.020;

Roseman GP, Wu B, Wadolkowski MA, Harris DA, Millhauser GL. Intrinsic toxicity of the cellular prion protein is regulated by its conserved central region. FASEB J. 2020 06; 34(6):8734-8748. PMID: 32385908; PMCID: PMC7442283; DOI: 10.1096/fj.201902749RR;

Corbett GT, Wang Z, Hong W, Colom-Cadena M, Rose J, Liao M, Asfaw A, Hall TC, Ding L, DeSousa A, Frosch MP, Collinge J, Harris DA, Perkinton MS, Spires-Jones TL, Young-Pearse TL, Billinton A, Walsh DM. PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins. Acta Neuropathol. 2020 03; 139(3):503-526. PMID: 31853635; PMCID: PMC7035229; DOI: 10.1007/s00401-019-02114-9;

Showing 10 of 145 results. Show More

McDonald AJ, Leon DR, Markham KA, Wu B, Heckendorf CF, Schilling K, Showalter HD, Andrews PC, McComb ME, Pushie MJ, Costello CE, Millhauser GL, Harris DA. Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR. Structure. 2019 06 04; 27(6):907-922.e5.View Related Profiles.

Wu, Bei
Costello, Catherine
Harris, David
McComb, Mark

PMID: 30956132; PMCID: PMC6736647; DOI: 10.1016/j.str.2019.03.008;

Mercer RC, Harris DA. Identification of anti-prion drugs and targets using toxicity-based assays. Curr Opin Pharmacol. 2019 02; 44:20-27.View Related Profiles.

Harris, David
Mercer, Robert

PMID: 30684854; PMCID: PMC6561806; DOI: 10.1016/j.coph.2018.12.005;

Le NTT, Wu B, Harris DA. Prion neurotoxicity. Brain Pathol. 2019 03; 29(2):263-277.View Related Profiles.

Wu, Bei
Harris, David
Le, Nhat

PMID: 30588688; PMCID: PMC6894960; DOI: 10.1111/bpa.12694;

Mengel D, Hong W, Corbett GT, Liu W, DeSousa A, Solforosi L, Fang C, Frosch MP, Collinge J, Harris DA, Walsh DM. PrP-grafted antibodies bind certain amyloid ß-protein aggregates, but do not prevent toxicity. Brain Res. 2019 05 01; 1710:125-135. PMID: 30593771; PMCID: PMC6431553; DOI: 10.1016/j.brainres.2018.12.038;

Fang C, Wu B, Le NTT, Imberdis T, Mercer RCC, Harris DA. Prions activate a p38 MAPK synaptotoxic signaling pathway. PLoS Pathog. 2018 09; 14(9):e1007283.View Related Profiles.

Wu, Bei
Harris, David
Le, Nhat
Mercer, Robert

PMID: 30235355; PMCID: PMC6147624; DOI: 10.1371/journal.ppat.1007283;

McDonald AJ, Wu B, Harris DA. An inter-domain regulatory mechanism controls toxic activities of PrPC. Prion. 2017 11 02; 11(6):388-397.View Related Profiles.

Wu, Bei
Harris, David

PMID: 28960140; PMCID: PMC5786360; DOI: 10.1080/19336896.2017.1384894;

Bove-Fenderson E, Urano R, Straub JE, Harris DA. Cellular prion protein targets amyloid-ß fibril ends via its C-terminal domain to prevent elongation. J Biol Chem. 2017 Oct 13; 292(41):16858-16871.View Related Profiles.

Harris, David
Bove-Fenderson, Erin
Straub, John

PMID: 28842494; PMCID: PMC5641888; DOI: 10.1074/jbc.M117.789990;

Wu B, McDonald AJ, Markham K, Rich CB, McHugh KP, Tatzelt J, Colby DW, Millhauser GL, Harris DA. The N-terminus of the prion protein is a toxic effector regulated by the C-terminus. Elife. 2017 05 20; 6.View Related Profiles.

Wu, Bei
Harris, David

PMID: 28527237; PMCID: PMC5469617; DOI: 10.7554/eLife.23473;

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.View Related Profiles.

Beeler, Aaron
Fang, Cheng
Harris, David

PMID: 27803163; PMCID: PMC5207084; DOI: 10.1074/jbc.M116.745612;

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.View Related Profiles.

Fang, Cheng
Harris, David

PMID: 27227882; PMCID: PMC4881977; DOI: 10.1371/journal.ppat.1005623;

Saá P, Harris DA, Cervenakova L. Mechanisms of prion-induced neurodegeneration. Expert Rev Mol Med. 2016 Apr 08; 18:e5.View Related Profiles.

Harris, David
Saa, Paula

PMID: 27055367; DOI: 10.1017/erm.2016.8;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 26860872; PMCID: PMC4748561; DOI: 10.1186/s13024-016-0076-5;

Imberdis T, Harris DA. Synthetic Prions Provide Clues for Understanding Prion Diseases. Am J Pathol. 2016 Apr; 186(4):761-4. PMID: 26854642; PMCID: PMC5808135; DOI: 10.1016/j.ajpath.2015.12.005;

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.View Related Profiles.

Harris, David
Bove-Fenderson, Erin

PMID: 25217642; PMCID: PMC4208020; DOI: 10.1074/jbc.M114.587345;

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.View Related Profiles.

Abraham, Carmela
Chen, Ci-Di
Harris, David
Zeldich, Ella
Bove-Fenderson, Erin
Colvin, Teresa

PMID: 25037225; PMCID: PMC4148892; DOI: 10.1074/jbc.M114.567321;

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; PMCID: PMC4198046; DOI: 10.15252/embj.201489071;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Bian, Hejiao
Luebke, Jennifer
Toselli, Paul
Massignan, Tania
Unterberger, Ursula

PMID: 23392670; PMCID: PMC3711660; DOI: 10.1523/JNEUROSCI.3406-12.2013;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 23362282; PMCID: PMC3597823; DOI: 10.1074/jbc.M112.423954;

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.

Biasini E, Harris DA. Targeting the cellular prion protein to treat neurodegeneration. Future Med Chem. 2012 Sep; 4(13):1655-8.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 22924502; DOI: 10.4155/fmc.12.114;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Saa, Paula
Massignan, Tania
Unterberger, Ursula

PMID: 22745483; PMCID: PMC3433751; DOI: 10.1523/JNEUROSCI.1103-12.2012;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Massignan, Tania

PMID: 22428057; PMCID: PMC3299791; DOI: 10.1371/journal.pone.0033472;

Solomon IH, Biasini E, Harris DA. Ion channels induced by the prion protein: mediators of neurotoxicity. Prion. 2012 Jan-Mar; 6(1):40-5.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 22453177; PMCID: PMC3338964; DOI: 10.4161/pri.6.1.18627;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Unterberger, Ursula

PMID: 22137337; PMCID: PMC3273588; DOI: 10.1016/j.tins.2011.10.002;

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; PMCID: PMC3243553; DOI: 10.1074/jbc.M111.286195;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Unterberger, Ursula

PMID: 21980526; PMCID: PMC3183058; DOI: 10.1371/journal.pone.0025675;

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; PMCID: PMC3227396; DOI: 10.1523/JNEUROSCI.1243-11.2011;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Khatri, Natasha
Massignan, Tania

PMID: 21385869; PMCID: PMC3077669; DOI: 10.1074/jbc.M110.214973;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Massignan, Tania

PMID: 21115124; PMCID: PMC3384733; DOI: 10.1016/j.ymeth.2010.11.005;

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; PMCID: PMC2924115; DOI: 10.1074/jbc.M110.134619;

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; PMCID: PMC2877832; DOI: 10.2353/ajpath.2010.091007;

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; PMCID: PMC2864797; DOI: 10.1016/j.jneumeth.2010.03.019;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Massignan, Tania

PMID: 19996123; PMCID: PMC2860234; DOI: 10.1074/mcp.M900271-MCP200;

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.View Related Profiles.

Harris, David
Biasini, Emiliano
Massignan, Tania

PMID: 19940127; PMCID: PMC2844219; DOI: 10.1074/jbc.M109.064949;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 19915706; PMCID: PMC2773113; DOI: 10.1371/journal.pone.0007816;

Solomon IH, Schepker JA, Harris DA. Prion neurotoxicity: insights from prion protein mutants. Curr Issues Mol Biol. 2010; 12(2):51-61. PMID: 19767650; PMCID: PMC4821541

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; PMCID: PMC2731139; DOI: 10.2353/ajpath.2009.090125;

Chiesa R, Harris DA. Fishing for prion protein function. PLoS Biol. 2009 Mar 31; 7(3):e75. PMID: 19338390; PMCID: PMC2661967; DOI: 10.1371/journal.pbio.1000075;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 19052217; PMCID: PMC2646838; DOI: 10.1523/JNEUROSCI.3109-08.2008;

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; DOI: 10.1111/j.1471-4159.2008.05719.x;

Christensen HM, Harris DA. Prion protein lacks robust cytoprotective activity in cultured cells. Mol Neurodegener. 2008; 3:11. PMID: 18718018; PMCID: PMC2546390; DOI: 10.1186/1750-1326-3-11;

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; PMCID: PMC2614895; DOI: 10.1016/j.virol.2008.07.006;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 18298665; DOI: 10.1111/j.1471-4159.2008.05306.x;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 18514536; PMCID: PMC2536573; DOI: 10.1016/j.nbd.2008.03.006;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 18034781

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; PMCID: PMC1934519; DOI: 10.2353/ajpath.2007.070262;

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; PMCID: PMC1952097; DOI: 10.1128/MCB.02127-06;

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; PMCID: PMC1888682; DOI: 10.1038/sj.emboj.7601726;

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 17456603; PMCID: PMC1863438; DOI: 10.1073/pnas.0610827104;

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; PMCID: PMC1986710; DOI: 10.1016/j.bbadis.2007.02.011;

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; PMCID: PMC6672905; DOI: 10.1523/JNEUROSCI.4244-06.2007;

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; PMCID: PMC1783448; DOI: 10.1038/sj.emboj.7601507;

Harris DA, True HL. New insights into prion structure and toxicity. Neuron. 2006 May 4; 50(3):353-7. PMID: 16675391

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; PMCID: PMC6724869; DOI: 10.1523/JNEUROSCI.1192-05.2005;

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; PMCID: PMC6724892; DOI: 10.1523/JNEUROSCI.0105-05.2005;

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

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

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

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.View Related Profiles.

Harris, David
Massignan, Tania

PMID: 15607951

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; PMCID: PMC544044

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

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

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.
Harris, DA (Ed.). Volume 284 of Curr. Topics in Microbiol. and Immunol. Mad Cow Disease. Springer-Verlag. Berlin. 2004.

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

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

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; PMCID: PMC164780

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

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.View Related Profiles.

Harris, David
Biasini, Emiliano

PMID: 12663673

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

Harris DA. Trafficking, turnover and membrane topology of PrP. Br Med Bull. 2003; 66:71-85. PMID: 14522850

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

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.
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.

Chiesa R, Harris DA. Prion diseases: what is the neurotoxic molecule? Neurobiol Dis. 2001 Oct; 8(5):743-63. PMID: 11592845

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

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; PMCID: PMC32273

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

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

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.
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.

Harris DA. Biosynthesis and cellular processing of the prion protein. Adv Protein Chem. 2001; 57:203-28. PMID: 11447691

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; DOI: 10.1385/1-59259-134-5:149;

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

Harris DA. Prion diseases. Nutrition. 2000 Jul-Aug; 16(7-8):554-6. PMID: 10906553

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

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; PMCID: PMC25870

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

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

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; PMCID: PMC111542

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

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

Harris DA. Cellular biology of prion diseases. Clin Microbiol Rev. 1999 Jul; 12(3):429-44. PMID: 10398674; PMCID: PMC100247

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

Harris DA. Cell biological studies of the prion protein. Curr Issues Mol Biol. 1999; 1(1-2):65-75. PMID: 11475702

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.
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.
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.

Pauly PC, Harris DA. Copper stimulates endocytosis of the prion protein. J Biol Chem. 1998 Dec 11; 273(50):33107-10. PMID: 9837873

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

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.
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.
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.
Harris DA. Clathrin-coated vesicles and detergent-resistant rafts in prion biology. Bull. Inst. Pasteur. 1998; 96:207-212.

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

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

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

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

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.

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; PMCID: PMC39295

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

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

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.

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

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

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

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; PMCID: PMC2120430

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; PMCID: PMC2290925

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

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; PMCID: PMC46496

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

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.
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.

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; PMCID: PMC52362

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

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.

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

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

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.

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; PMCID: PMC279906

Harris DA, Sherbany AA, Schwartz JH. Purification and characterization of muscle proteins from Aplysia californica. Biological Bulletin. 1984; 166:482-493.

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

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

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; PMCID: PMC349138

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; PMCID: PMC350521

This graph shows the total number of publications by year, by first, middle/unknown, or last author.

Bar chart showing 145 publications over 39 distinct years, with a maximum of 9 publications in 2001

Bar chart showing 145 publications over 39 distinct years, with a maximum of 9 publications in 2001

Year	Publications
1980	1
1981	1
1982	1
1983	1
1984	1
1988	1
1989	2
1990	1
1991	3
1993	5
1994	1
1995	4
1996	4
1997	5
1998	6
1999	7
2000	8
2001	9
2002	3
2003	7
2004	5
2005	6
2006	1
2007	8
2008	6
2009	6
2010	4
2011	5
2012	4
2013	3
2014	3
2016	5
2017	3
2018	2
2019	4
2020	3
2021	2
2022	2
2023	2

Media Mentions

Recent (within 3 months)

Foiling Deadly Prions

Science Magazine 3/21/2024

Five Faculty Receive Edward Avedisian Professorships

BU Today 3/21/2024

Older

Prion Disease Harms Neurons via Stress Pathway

Genetic Engineering & Biotechnology News 9/24/2018

1991-1994 Klingenstein Fellowship Award in the Neurosciences

1986-1991 National Institutes of Health: Clinical Investigator Development Award

1983 Columbia College of Physicians & Surgeons: Titus Munson Coan Prize

1983-1985 National Institutes of Health: Individual National Research Service Award

1983 Columbia College of Physicians & Surgeons: Frederick P. Gay Memorial Award

1981 Columbia College of Physicians & Surgeons: Alfred Steiner Research Award

In addition to these self-described keywords below, a list of MeSH based concepts is available here.

Prion Diseases
Alzheimer's Disease

Contact for Mentoring:

72 E. Concord St Silvio Conte (K)
Boston MA 02118
Google Map

617.358.4280

Download vCard

Harris's Networks

Click the "See All" links for more information and interactive visualizations

Concepts

See all (446) concept(s)

Media Mentions

Co-Authors

See all (14) people

Similar People

See all (60) people

Same Department

Search Department

Yr	Title	Project-Sub Proj	Pubs
2023	Mechanisms of Prion Protein Toxicity	5R01NS065244-13
2022	Mechanisms of Prion Protein Toxicity	5R01NS065244-12
2021	Mechanisms of Prion Protein Toxicity	2R01NS065244-11A1	29
2020	Mechanisms of Prion Protein Toxicity	5R01NS065244-10	29
2019	Modeling prion diseases using human iPSC-derived neurons	1R21NS111499-01
2019	Genomic and Proteomic Analysis of Prion Synaptotoxicity	5R21NS107755-02	2
2019	Mechanisms of Prion Protein Toxicity	5R01NS065244-09	29
2018	Genomic and Proteomic Analysis of Prion Synaptotoxicity	1R21NS107755-01A1	2
2018	Identification of Anti-Prion Drug Targets	5R21NS101659-02	2
2018	Mechanisms of Prion Protein Toxicity	5R01NS065244-08	29
2017	Identification of Anti-Prion Drug Targets	1R21NS101659-01	2
2017	Mechanisms of Prion Protein Toxicity	5R01NS065244-07	29
2016	Mechanisms of Prion Protein Toxicity	2R01NS065244-06A1	29
2015	Murine Transgenic Models of Prion Diseases	5R01NS040975-16	40
2014	ION CHANNEL MODULATION BY THE PRION PROTEIN: A NOVEL TOXIC MECHANISM	5R01NS065244-05	29
2014	Murine Transgenic Models of Prion Diseases	5R01NS040975-15	40
2013	ION CHANNEL MODULATION BY THE PRION PROTEIN: A NOVEL TOXIC MECHANISM	5R01NS065244-04	29
2013	Murine Transgenic Models of Prion Diseases	5R01NS040975-14	40
2012	ION CHANNEL MODULATION BY THE PRION PROTEIN: A NOVEL TOXIC MECHANISM	5R01NS065244-03	29
2012	Murine Transgenic Models of Prion Diseases	5R01NS040975-13	40
2011	ION CHANNEL MODULATION BY THE PRION PROTEIN: A NOVEL TOXIC MECHANISM	5R01NS065244-02	29
2011	ION CHANNEL MODULATION BY THE PRION PROTEIN: A NOVEL TOXIC MECHANISM	3R01NS065244-01A2S1	29
2011	Murine Transgenic Models of Prion Diseases	2R01NS040975-12A1	40
2010	ION CHANNEL MODULATION BY THE PRION PROTEIN: A NOVEL TOXIC MECHANISM	1R01NS065244-01A2	29
2010	UPTAKE, TRANSPORT, AND SPREAD OF PRIONS	5R01NS056376-03	5
2010	Cellular Functions of the Prion Protein	5R01NS052526-06	19
2010	Murine Transgenic Models of Prion Diseases	5R01NS040975-11	40
2009	UPTAKE, TRANSPORT, AND SPREAD OF PRIONS	7R01NS056376-02	5
2009	MURINE TRANSGENIC MODELS OF PRION DISEASES	5P41RR000954-32-8051	995
2009	Cellular Functions of the Prion Protein	7R01NS052526-05	19
2009	Cellular Functions of the Prion Protein	5R01NS052526-04	19
2009	Murine Transgenic Models of Prion Diseases	7R01NS040975-10	40
2009	Murine Transgenic Models of Prion Diseases	5R01NS040975-09	40
2008	MURINE TRANSGENIC MODELS OF PRION DISEASES	5P41RR000954-31-7601	995
2008	Cellular Functions of the Prion Protein	5R01NS052526-03	19
2008	Murine Transgenic Models of Prion Diseases	5R01NS040975-08	40
2008	Training Program in Cellular and Molecular Biology	5T32GM007067-34	296
2007	MURINE TRANSGENIC MODELS OF PRION DISEASES	5P41RR000954-30-5538	995
2007	Cellular Functions of the Prion Protein	5R01NS052526-02	19
2007	Murine Transgenic Models of Prion Diseases	5R01NS040975-07	40
2007	Training Program in Cellular and Molecular Biology	5T32GM007067-33	296
2006	Cellular Functions of the Prion Protein	1R01NS052526-01A1	19
2006	MURINE TRANSGENIC MODELS OF PRION DISEASES	5P41RR000954-29-6584	995
2006	Murine Transgenic Models of Prion Diseases	2R01NS040975-06A1	40
2006	Training Program in Cellular and Molecular Biology	2T32GM007067-32	296
2005	MURINE TRANSGENIC MODELS OF PRION DISEASES	5R01NS040975-05	40
2005	TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGY	5T32GM007067-31	296
2004	MURINE TRANSGENIC MODELS OF PRION DISEASES	5R01NS040975-04	40
2004	MURINE TRANSGENIC MODELS OF PRION DISEASES	3R01NS040975-04S1	40
2004	THE ROLE OF COPPER IN PRION PROTEIN BIOLOGY	5R01NS040061-05	3
2004	TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGY	5T32GM007067-30	296
2003	MURINE TRANSGENIC MODELS OF PRION DISEASES	5R01NS040975-03	40
2003	THE ROLE OF COPPER IN PRION PROTEIN BIOLOGY	5R01NS040061-04	3
2003	TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGY	5T32GM007067-29	296
2002	MURINE TRANSGENIC MODELS OF PRION DISEASES	5R01NS040975-02	40
2002	THE ROLE OF COPPER IN PRION PROTEIN BIOLOGY	5R01NS040061-03	3
2002	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	5R01NS035496-07	12
2001	MURINE TRANSGENIC MODELS OF PRION DISEASES	1R01NS040975-01	40
2001	THE ROLE OF COPPER IN PRION PROTEIN BIOLOGY	5R01NS040061-02	3
2001	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	5R01NS035496-06	12
2000	THE ROLE OF COPPER IN PRION PROTEIN BIOLOGY	1R01NS040061-01	3
2000	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	5R01NS035496-05	12
2000	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	3R01NS035496-05S2	12
2000	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	3R01NS035496-05S1	12
1999	PROPERTIES OF CELLULAR PRION PROTEINS	3P50AG005681-16S2-22	1288
1999	PROPERTIES OF CELLULAR PRION PROTEINS	3P50AG005681-16S1-22	1288
1999	PROPERTIES OF CELLULAR PRION PROTEINS	5P50AG005681-16-22	1288
1999	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	2R01NS035496-04	12
1999	PROPERTIES OF CELLULAR PRION PROTEINS	5R01AG012925-05	3
1998	CELLULAR PRION PROTEIN AND COPPER UPTAKE	1R03AG016462-01	1
1998	PROPERTIES OF CELLULAR PRION PROTEINS	3P50AG005681-15S1-22	1288
1998	PROPERTIES OF CELLULAR PRION PROTEINS	5P50AG005681-15-22	1288
1998	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	5R01NS035496-03	12
1998	PROPERTIES OF CELLULAR PRION PROTEINS	5R01AG012925-04	3
1998	PROPERTIES OF CELLULAR PRION PROTEINS	3R01AG012925-04S1	3
1996	MOLECULAR MECHANISMS UNDERLYING FAMILIAL PRION DISEASES	1R01NS035496-01	12
1996	PROPERTIES OF CELLULAR PRION PROTEINS	5R01AG012925-02	3
1996	MOLECULAR AND CELLULAR STUDIES OF A PRION-LIKE PROTEIN	5R29NS030137-05	7
1996	PROPERTIES OF CELLULAR PRION PROTEINS	5P50AG005681-13-22	1288
1995	PROPERTIES OF CELLULAR PRION PROTEINS	1R01AG012925-01	3
1995	MOLECULAR AND CELLULAR STUDIES OF A PRION-LIKE PROTEIN	5R29NS030137-04	7
1994	MOLECULAR AND CELLULAR STUDIES OF A PRION-LIKE PROTEIN	5R29NS030137-03	7
1993	MOLECULAR AND CELLULAR STUDIES OF A PRION-LIKE PROTEIN	5R29NS030137-02	7
1992	MOLECULAR AND CELLULAR STUDIES OF A PRION-LIKE PROTEIN	1R29NS030137-01	7
1989	MOLECULAR MECHANISMS OF SYNAPTOGENESIS	5K08NS001200-03