Hadassah Medical Center: Gabizon Ruth

1.

Qubty D, Frid K, Har-Even M, Rubovitch V, Gabizon R, Pick CG. Nano-PSO Administration Attenuates Cognitive and Neuronal Deficits Resulting from Traumatic Brain Injury. Molecules [Internet]. 2022;27(9). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85129081113&doi=10.3390%252fmolecules27092725&partnerID=40&md5=78896b40eefd26abbaedb2d68fe545a0

2.

Binyamin O, Frid K, Keller G, Saada A, Gabizon R. Comparing anti–aging hallmark activities of Metformin and Nano-PSO in a mouse model of genetic Creutzfeldt-Jakob Disease. Neurobiology of Aging [Internet]. 2022;110:77–87. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85120616965&doi=10.1016%252fj.neurobiolaging.2021.11.001&partnerID=40&md5=4b0165bb1f2eb3335e940dff278a56cc

3.

Binyamin O, Nitzan K, Frid K, Ungar Y, Rosenmann H, Gabizon R. Author Correction: Brain targeting of 9c,11t-Conjugated Linoleic Acid, a natural calpain inhibitor, preserves memory and reduces Aβ and P25 accumulation in 5XFAD mice (Scientific Reports, (2019), 9, 1, (18437), 10.1038/s41598-019-54971-9). Scientific Reports [Internet]. 2020;10(1). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85078192471&doi=10.1038%252fs41598-020-58232-y&partnerID=40&md5=89f028f9cacd7baf782e522a40532d19

4.

Frid K, Binyamin O, Usman A, Gabizon R. Delay of gCJD aggravation in sick TgMHu2ME199K mice by combining NPC transplantation and Nano-PSO administration. Neurobiology of Aging [Internet]. 2020;95:231–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85089822817&doi=10.1016%252fj.neurobiolaging.2020.07.030&partnerID=40&md5=0dec672b1f1b315f9f66cca7ebbd89ec

5.

Friedman-Levi Y, Binyamin O, Frid K, Ovadia H, Gabizon R. Erratum: Genetic prion disease: No role for the immune system in disease pathogenesis? (Human Molecular Genetics (2014) 23:15 (4134-4141) DOI: 10.1093/hmg/ddu134). Human Molecular Genetics [Internet]. 2020;29(6):1055. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85083545100&doi=10.1093%252fhmg%252fddz302&partnerID=40&md5=09eb573e71c23e6b3cc82bba9bca324d

6.

Binyamin O, Nitzan K, Frid K, Ungar Y, Rosenmann H, Gabizon R. Brain targeting of 9c,11t-Conjugated Linoleic Acid, a natural calpain inhibitor, preserves memory and reduces Aβ and P25 accumulation in 5XFAD mice. Scientific Reports [Internet]. 2019;9(1). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85076054200&doi=10.1038%252fs41598-019-54971-9&partnerID=40&md5=d0a3aa4173a226b030a26859a3454a27

7.

Keller G, Binyamin O, Frid K, Saada A, Gabizon R. Mitochondrial dysfunction in preclinical genetic prion disease: A target for preventive treatment? Neurobiology of Disease [Internet]. 2019;124:57–66. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85056595323&doi=10.1016%252fj.nbd.2018.11.003&partnerID=40&md5=718b7ac0f02b156e22a3ad17c621ec73

8.

Frid K, Binyamin O, Fainstein N, Keller G, Ben-Hur T, Gabizon R. Autologous neural progenitor cell transplantation into newborn mice modeling for E200K genetic prion disease delays disease progression. Neurobiology of Aging [Internet]. 2018;65:192–200. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85042469349&doi=10.1016%252fj.neurobiolaging.2018.01.004&partnerID=40&md5=47b5f1ff3b1866ddadb9694ea78cc36d

9.

Lasmézas C, Gabizon R. Identifying therapeutic targets and treatments in model systems. Handbook of Clinical Neurology [Internet]. 2018;153:409–18. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85048614263&doi=10.1016%252fB978-0-444-63945-5.00022-2&partnerID=40&md5=bc382bad63fb3cba363d229c4b53e3b3

10.

Binyamin O, Keller G, Frid K, Larush L, Magdassi S, Gabizon R. Continues administration of Nano-PSO significantly increased survival of genetic CJD mice. Neurobiology of Disease [Internet]. 2017;108:140–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85028443697&doi=10.1016%252fj.nbd.2017.08.012&partnerID=40&md5=2e7f17bd9d2d60e4572562bca80aaea0

11.

Canello T, Frid K, Gabizon R, Lisa S, Friedler A, Moskovitz J, et al. Erratum: Correction: Oxidation of Helix-3 Methionines Precedes the Formation of PK Resistant PrPSc (PLoS pathogens (2010) 6 7 (e1000977)). PLoS pathogens [Internet]. 2017;13(5):e1006293. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063709246&doi=10.1371%252fjournal.ppat.1006293&partnerID=40&md5=acfdccd9ad2bd86ae8a26622d7be75b5

12.

Friedman-Levi Y, Meiner Z, Canello T, Frid K, Kovacs GG, Budka H, et al. Erratum: Correction: Fatal Prion Disease in a Mouse Model of Genetic E200K Creutzfeldt-Jakob Disease (PLoS pathogens (2011) 7 11 (e1002350)). PLoS pathogens [Internet]. 2017;13(5):e1006294. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063708809&doi=10.1371%252fjournal.ppat.1006294&partnerID=40&md5=b2937085d2d5d8f59760d9844a55eba7

13.

Fainstein N, Dori D, Frid K, Fritz AT, Shapiro I, Gabizon R, et al. Chronic progressive neurodegeneration in a transgenic mouse model of prion disease. Frontiers in Neuroscience [Internet]. 2016;10(NOV). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85009813132&doi=10.3389%252ffnins.2016.00510&partnerID=40&md5=cb5cb3afea990bbbbfd93308ce9066af

14.

Binyamin O, Larush L, Frid K, Keller G, Friedman-Levi Y, Ovadia H, et al. Treatment of a multiple sclerosis animal model by a novel nanodrop formulation of a natural antioxidant. International Journal of Nanomedicine [Internet]. 2015;10:7165–74. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84948671573&doi=10.2147%252fIJN.S92704&partnerID=40&md5=67c157e7c64a9eaf76eefa0991f0e750

15.

Friedman-Levi Y, Mizrahi M, Frid K, Binyamin O, Gabizon R. Erratum: PrPST, a soluble, protease resistant and truncated PrP form features in the pathogenesis of a genetic prion disease (PLoS ONE (2013) 8:7 (e69583) DOI: 10.1371/journal.pone.0069583). PLoS ONE [Internet]. 2015;10(7). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84942011852&doi=10.1371%252fjournal.pone.0133911&partnerID=40&md5=e2f27042c2aab193a06eac8c1e6ff6a6

16.

Frid K, Einstein O, Friedman-Levi Y, Binyamin O, Ben-Hur T, Gabizon R. Aggregation of MBP in chronic demyelination. Annals of Clinical and Translational Neurology [Internet]. 2015;2(7):711–21. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84945177024&doi=10.1002%252facn3.207&partnerID=40&md5=fe64509976fd96ddc9482633c099361f

17.

Mizrahi M, Friedman-Levi Y, Larush L, Frid K, Binyamin O, Dori D, et al. Pomegranate seed oil nanoemulsions for the prevention and treatment of neurodegenerative diseases: The case of genetic CJD. Nanomedicine: Nanotechnology, Biology, and Medicine [Internet]. 2014;10(6):1353–63. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84905254678&doi=10.1016%252fj.nano.2014.03.015&partnerID=40&md5=a10603d42297661fc16ffcad1805fe33

18.

Friedman-Levi Y, Binyamin O, Frid K, Ovadia H, Gabizon R. Genetic prion disease: No role for the immune system in disease pathogenesis? Human Molecular Genetics [Internet]. 2014;23(15):4134–41. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84903991234&doi=10.1093%252fhmg%252fddu134&partnerID=40&md5=a36ac3451151f9e5fab25f06231ecd84

19.

Friedman-Levi Y, Mizrahi M, Frid K, Binyamin O, Gabizon R. PrPST, a Soluble, Protease Resistant and Truncated PrP Form Features in the Pathogenesis of a Genetic Prion Disease. PLoS ONE [Internet]. 2013;8(7). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84880773815&doi=10.1371%252fjournal.pone.0069583&partnerID=40&md5=186236d40d9b4130d72fe2dec804c959

20.

Cohen E, Avrahami D, Frid K, Canello T, Levy Lahad E, Zeligson S, et al. Snord 3A: A Molecular Marker and Modulator of Prion Disease Progression. PLoS ONE [Internet]. 2013;8(1). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84872665858&doi=10.1371%252fjournal.pone.0054433&partnerID=40&md5=3af9fe45b59d4b5faadc280dd46c7cf0

21.

Tzour A, Sosial E, Meir T, Canello T, Naveh-Many T, Gabizon R, et al. Multiple Pathways for High Voltage-Activated Ca2+ Influx in Anterior Pituitary Lactotrophs and Somatotrophs. Journal of Neuroendocrinology [Internet]. 2013;25(1):76–86. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84871517949&doi=10.1111%252fj.1365-2826.2012.02372.x&partnerID=40&md5=78fa5aa93d6cbeb9ac9069cd36516e23

22.

Friedman-Levi Y, Hoftberger R, Budka H, Mayer-Sonnenfeld T, Abramsky O, Ovadia H, et al. Targeting of prion-infected lymphoid cells to the central nervous system accelerates prion infection. Journal of Neuroinflammation [Internet]. 2012;9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84858593205&doi=10.1186%252f1742-2094-9-58&partnerID=40&md5=201f9ca94a5373bdf1ae6475ac721ebb

23.

Canello T, Friedman-Levi Y, Mizrahi M, Binyamin O, Cohen E, Frid K, et al. Copper is toxic to PrP-ablated mice and exacerbates disease in a mouse model of E200K genetic prion disease. Neurobiology of Disease [Internet]. 2012;45(3):1010–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84856573192&doi=10.1016%252fj.nbd.2011.12.020&partnerID=40&md5=be1486bed8c7a2bf4839fafb21b10c9d

24.

Avrahami D, Gabizon R. Age-related alterations affect the susceptibility of mice to prion infection. Neurobiology of Aging [Internet]. 2011;32(11):2006–15. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-80052617393&doi=10.1016%252fj.neurobiolaging.2009.12.015&partnerID=40&md5=60aaf696cf75897b7489827c490c7772

25.

Meiner Z, Kahana E, Baitcher F, Korczyn AD, Chapman J, Cohen OS, et al. Tau and 14-3-3 of genetic and sporadic Creutzfeldt-Jakob disease patients in Israel. Journal of Neurology [Internet]. 2011;258(2):255–62. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-79953798376&doi=10.1007%252fs00415-010-5738-6&partnerID=40&md5=33833fe09e74117b83b5bf0126bad13b

26.

Friedman-Levi Y, Meiner Z, Canello T, Frid K, Kovacs GG, Budka H, et al. Fatal prion disease in a mouse model of genetic E200K Creutzfeldt-Jakob disease. PLoS Pathogens [Internet]. 2011;7(11). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-81755183039&doi=10.1371%252fjournal.ppat.1002350&partnerID=40&md5=dd803946a53a68e1963b4c41e2a8960a

27.

Lisa S, Meli M, Cabello G, Gabizon R, Colombo G, Gasset M. The structural intolerance of the PrP α-fold for polar substitution of the helix-3 methionines. Cellular and Molecular Life Sciences [Internet]. 2010;67(16):2825–38. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-77955680774&doi=10.1007%252fs00018-010-0363-1&partnerID=40&md5=d87fcf334e67d6452008db326446515e

28.

Canello T, Frid K, Gabizon R, Lisa S, Friedler A, Moskovitz J, et al. Oxidation of Helix-3 methionines precedes the formation of PK resistant PrPSc. PLoS Pathogens [Internet]. 2010;6(7):1–10. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-77958126446&doi=10.1371%252fjournal.ppat.1000977&partnerID=40&md5=cfbd0c1e0a8d10eb1e376d8f49bbf2e3

29.

Oien DB, Canello T, Gabizon R, Gasset M, Lundquist BL, Burns JM, et al. Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies. Archives of Biochemistry and Biophysics [Internet]. 2009;485(1):35–40. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-64549133370&doi=10.1016%252fj.abb.2009.01.020&partnerID=40&md5=cb3fb653a6ba1b6125a95a44665c8b54

30.

Colombo G, Meli M, Morra G, Gabizon R, Gasset M. Methionine sulfoxides on prion protein helix-3 switch on the α-fold destabilization required for conversion. PLoS ONE [Internet]. 2009;4(1). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-59349116776&doi=10.1371%252fjournal.pone.0004296&partnerID=40&md5=419b6119916adcac03216608d835cb08

31.

Avrahami D, Dayan-Amouyal Y, Tal S, Mincberg M, Davis C, Abramsky O, et al. Virus-induced alterations of membrane lipids affect the incorporation of PrPSc into cells. Journal of Neuroscience Research [Internet]. 2008;86(12):2753–62. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-57049109793&doi=10.1002%252fjnr.21720&partnerID=40&md5=6af80ed52765205089aeb1fc287f6cbf

32.

Mayer-Sonnenfeld T, Avrahami D, Friedman-Levi Y, Gabizon R. Chemically induced accumulation of GAGs delays PrPSc clearance but prolongs prion disease incubation time. Cellular and Molecular Neurobiology [Internet]. 2008;28(7):1005–15. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-55349133045&doi=10.1007%252fs10571-008-9274-1&partnerID=40&md5=ad7e150947b704814b85a0d0f8519631

33.

Canello T, Engelstein R, Moshel O, Xanthopoulos K, Juanes ME, Langeveld J, et al. Methionine sulfoxides on PrPSc: A prion-specific covalent signature 1. Biochemistry [Internet]. 2008;47(34):8866–73. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-50149103534&doi=10.1021%252fbi800801f&partnerID=40&md5=2545316792c555be155cd36d1d3cb965

34.

Haviv Y, Avrahami D, Ovadia H, Ben-Hur T, Gabizon R, Sharon R. Induced neuroprotection independently from PrPSc accumulation in a mouse model for prion disease treated with simvastatin. Archives of Neurology [Internet]. 2008;65(6):762–75. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-45149109366&doi=10.1001%252farchneur.65.6.762&partnerID=40&md5=ec3339902b727ba169648ca86c593425

35.

Petrakis S, Irinopoulou T, Panagiotidis CH, Engelstein R, Lindstrom J, Orr-Urtreger A, et al. Cellular prion protein co-localizes with nAChR β4 subunit in brain and gastrointestinal tract (European Journal of Neuroscience (2007) 27, (612-620)). European Journal of Neuroscience [Internet]. 2008;27(8):2212. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-42049098831&doi=10.1111%252fj.1460-9568.2008.06243.x&partnerID=40&md5=5ece88e3ac05359c1567a4c29f6f6e15

36.

Petrakis S, Irinopoulou T, Panagiotidis CH, Engelstein R, Lindstrom J, Orr-Urtreger A, et al. Cellular prion protein co-localizes with nAChR β4 subunit in brain and gastrointestinal tract. European Journal of Neuroscience [Internet]. 2008;27(3):612–20. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-39049117884&doi=10.1111%252fj.1460-9568.2008.06037.x&partnerID=40&md5=9c422ccea4981acf36e76c48abdf0956

37.

Friedman-Levi Y, Ovadia H, Hoftberger R, Einstein O, Abramsky O, Budka H, et al. Fatal neurological disease in scrapie-infected mice induced for experimental autoimmune encephalomyelitis. Journal of Virology [Internet]. 2007;81(18):9942–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-35348849521&doi=10.1128%252fJVI.00780-07&partnerID=40&md5=e534bfbdfc99b1386a0291e241490d7d

38.

Engelstein R, Ovadia H, Gabizon R. Copaxone interferes with the PrPSc-GAG interaction. European Journal of Neurology [Internet]. 2007;14(8):877–84. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-34547125777&doi=10.1111%252fj.1468-1331.2007.01803.x&partnerID=40&md5=6eafe1c364fa009d28b9ed48bb9cc3e7

39.

Kariv-Inbal Z, Ben-Hur T, Grigoriadis NC, Engelstein R, Gabizon R. Urine from scrapie-infected hamsters comprises low levels of prion infectivity. Neurodegenerative Diseases [Internet]. 2006;3(3):123–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33748440083&doi=10.1159%252f000094770&partnerID=40&md5=a5c884d1d2ff0040c8595f5c633e79f1

40.

Halimi M, Dayan-Amouyal Y, Kariv-Inbal Z, Friedman-Levi Y, Mayer-Sonnenfeld T, Gabizon R. Prion urine comprises a glycosaminoglycan-light chain IgG complex that can be stained by Congo red. Journal of Virological Methods [Internet]. 2006;133(2):205–10. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33645282505&doi=10.1016%252fj.jviromet.2005.11.011&partnerID=40&md5=0c57aec896474d05e0a755b5ff8bd2f5

41.

Mayer-Sonnenfeld T, Zeigler M, Halimi M, Dayan Y, Herzog C, Lasmezas CI, et al. The metabolism of glycosaminoglycans is impaired in prion diseases. Neurobiology of Disease [Internet]. 2005;20(3):738–43. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-27744465417&doi=10.1016%252fj.nbd.2005.05.009&partnerID=40&md5=68c14f5e3c44ca55367846a29781badb

42.

Hijazi N, Kariv-Inbal Z, Gasset M, Gabizon R. PrPSc incorporation to cells requires endogenous glycosaminoglycan expression. Journal of Biological Chemistry [Internet]. 2005;280(17):17057–61. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-19444376065&doi=10.1074%252fjbc.M411314200&partnerID=40&md5=ebf4929283dc5c3139ceae57b1db92ce

43.

Kariv-Inbal Z, Halimi M, Dayan Y, Engelstein R, Gabizon R. Characterization of light chain immunoglobulin in urine from animals and humans infected with prion diseases. Journal of Neuroimmunology [Internet]. 2005;162(1–2):12–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-17044413714&doi=10.1016%252fj.jneuroim.2004.12.013&partnerID=40&md5=bfee7db1ebf24ec7a89572ad9e5f86f9

44.

Engelstein R, Grigoriadis N, Greig NH, Ovadia H, Gabizon R. Inhibition of P53-related apoptosis had no effect on PrPSc accumulation and prion disease incubation time. Neurobiology of Disease [Internet]. 2005;18(2):282–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-15944386993&doi=10.1016%252fj.nbd.2004.10.008&partnerID=40&md5=ea9cbd71dab957563273b24b9176b599

45.

Hijazi N, Shaked Y, Rosenmann H, Ben-Hur T, Gabizon R. Copper binding to PrPC may inhibit prion disease propagation. Brain Research [Internet]. 2003;993(1–2):192–200. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345714734&doi=10.1016%252fj.brainres.2003.09.014&partnerID=40&md5=2622ff7d5ea1a92ee5f575a173af2a62

46.

Schonberger O, Horonchik L, Gabizon R, Papy-Garcia D, Barritault D, Taraboulos A. Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis. Biochemical and Biophysical Research Communications [Internet]. 2003;312(2):473–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344845037&doi=10.1016%252fj.bbrc.2003.10.150&partnerID=40&md5=c549e09744e98e6b7da50a70268b7fc6

47.

Shaked GM, Engelstein R, Avraham I, Kahana E, Gabizon R. Dimethyl sulfoxide delays PrPsc accumulation and disease symptoms in prion-infected hamsters. Brain Research [Internet]. 2003;983(1–2):137–43. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042160180&doi=10.1016%2fS0006-8993%2803%2903045-2&partnerID=40&md5=82ebccca691425938943b5c52de519f8

48.

Shaked Y, Hijazi N, Gabizon R. Doppel and PrPC do not share the same membrane microenvironment. FEBS Letters [Internet]. 2002;530(1–3):85–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037163874&doi=10.1016%2fS0014-5793%2802%2903430-0&partnerID=40&md5=62fa222be75b92ab1205be39332a80f7

49.

Tzaban S, Friedlander G, Schonberger O, Horonchik L, Yedidia Y, Shaked G, et al. Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes. Biochemistry [Internet]. 2002;41(42):12868–75. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037159185&doi=10.1021%252fbi025958g&partnerID=40&md5=e4d3eeff47f742a9a62ee528aa5aee84

50.

Shaked GM, Engelstein R, Avraham I, Rosenmann H, Gabizon R. Valproic acid treatment results in increased accumulation of prion proteins. Annals of Neurology [Internet]. 2002;52(4):416–20. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036791879&doi=10.1002%252fana.10298&partnerID=40&md5=10176a73c845ee3d1e4592105ea843cb

51.

Shaked Y, Engelstein R, Gabizon R. The binding of prion proteins to serum components is affected by detergent extraction conditions. Journal of Neurochemistry [Internet]. 2002;82(1):1–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036310430&doi=10.1046%252fj.1471-4159.2002.00995.x&partnerID=40&md5=c43eb2af0d00ec482823966301d5f3e6

52.

Shaked GM, Shaked Y, Kariv-Inbal Z, Halimi M, Avraham I, Gabizon R. A Protease-resistant Prion Protein Isoform Is Present in Urine of Animals and Humans Affected with Prion Diseases. Journal of Biological Chemistry [Internet]. 2001;276(34):31479–82. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035943651&doi=10.1074%252fjbc.C100278200&partnerID=40&md5=f9c3b75a01c3811da2049ec0fc3bf853

53.

Shaked Y, Rosenmann H, Hijazi N, Halimi M, Gabizon R. Copper binding to the PrP isoforms: A putative marker of their conformation and function. Journal of Virology [Internet]. 2001;75(17):7872–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034869272&doi=10.1128%252fJVI.75.17.7872-7874.2001&partnerID=40&md5=2d4d876af66b8f21a636a4a3a4babb78

54.

Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R. Reconstitution of Prion Infectivity from Solubilized Protease-resistant PrP and Nonprotein Components of Prion Rods. Journal of Biological Chemistry [Internet]. 2001;276(17):14324–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035957944&doi=10.1074%252fjbc.M007815200&partnerID=40&md5=6aeb9e98c56a42072b42c364a9800640

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Rosenmann H, Talmor G, Halimi M, Yanai A, Gabizon R, Meiner Z. Prion protein with an E200K mutation displays properties similar to those of the cellular isoform PrPC. Journal of Neurochemistry [Internet]. 2001;76(6):1654–62. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035100183&doi=10.1046%252fj.1471-4159.2001.00195.x&partnerID=40&md5=d2c88fa688c2d078ce6caa387fc13189

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Keshet GI, Bar-Peled O, Yaffe D, Nudel U, Gabizon R. The cellular prion protein colocalizes with the dystroglycan complex in the brain. Journal of Neurochemistry [Internet]. 2000;75(5):1889–97. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033793094&doi=10.1046%252fj.1471-4159.2000.0751889.x&partnerID=40&md5=53907c64b45ca7586e8a1c4e0d6e47c4

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Simon ES, Kahana E, Chapman J, Treves TA, Gabizon R, Rosenmann H, et al. Creutzfeldt-Jakob disease profile in patients homozygous for the PRNP E200k mutation. Annals of Neurology [Internet]. 2000;47(2):257–60. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033966706&doi=10.1002%2f1531-8249%28200002%2947%3a2%3c257%3a%3aAID-ANA20%3e3.0.CO%3b2-U&partnerID=40&md5=47374bc9766c664588d65aa2d3e9ba4f

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Shaked Y, Rosenmann H, Talmor G, Gabizon R. A C-terminal-truncated PrP isoform is present in mature sperm. Journal of Biological Chemistry [Internet]. 1999;274(45):32153–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033527644&doi=10.1074%252fjbc.274.45.32153&partnerID=40&md5=aed03afd31adea1a778c9e9ddbf6cf80

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Yanai A, Meiner Z, Gahali I, Gabizon R, Taraboulos A. Subcellular trafficking abnormalities of a prion protein with a disrupted disulfide loop. FEBS Letters [Internet]. 1999;460(1):11–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032885260&doi=10.1016%2fS0014-5793%2899%2901316-2&partnerID=40&md5=2a49c53e445d129317a8571a666daec4

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Rosenmann H, Kahana E, Korczyn AD, Kahana I, Chapman J, Gabizon R. Preliminary evidence for anticipation in genetic E200K Creutzfeldt-Jakob disease. Neurology [Internet]. 1999;53(6):1328–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032852301&doi=10.1212%252fwnl.53.6.1328&partnerID=40&md5=db5083889d50aaaa97fc947f8d7689b1

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Shaked GM, Fridlander G, Meiner Z, Taraboulos A, Gabizon R. Protease-resistant and detergent-insoluble prion protein is not necessarily associated with prion infectivity. Journal of Biological Chemistry [Internet]. 1999;274(25):17981–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033580818&doi=10.1074%252fjbc.274.25.17981&partnerID=40&md5=83d7652881546b8ffe72dca6d2f5e383

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Keshet GI, Ovadia H, Taraboulos A, Gabizon R. Scrapie-infected mice and PrP knockout mice share abnormal localization and activity of neuronal nitric oxide synthase. Journal of Neurochemistry [Internet]. 1999;72(3):1224–31. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033012137&doi=10.1046%252fj.1471-4159.1999.0721224.x&partnerID=40&md5=3f1dcc21930530d59211a3760fe7d7f4

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Meiner Z, Gabizon R. A new variant of Creutzfeldt-Jakob disease and its relation to bovine spongiform encephalopathy (BSE) in Great Britain. Harefuah [Internet]. 1998;134(6):465–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032520293&partnerID=40&md5=95ff7ce01ee349f03fdf8c77b1775910

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Caspi S, Halimi M, Yanai A, Sasson SB, Taraboulos A, Gabizon R. The anti-prion activity of Congo red. Putative mechanism. Journal of Biological Chemistry [Internet]. 1998;273(6):3484–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032488921&doi=10.1074%252fjbc.273.6.3484&partnerID=40&md5=d9fbd53d26e1d73076f72119ba283f4f

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Rosenmann H, Vardi J, Finkelstein Y, Chapman J, Gabizon R. Identification in Israel of 2 Jewish Creutzfeldt-Jakob disease patients with a 178 mutation at their PrP gene. Acta Neurologica Scandinavica [Internet]. 1998;97(3):184–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031802443&doi=10.1111%252fj.1600-0404.1998.tb00634.x&partnerID=40&md5=4491de2bc8cf21ed112b0ac63ebc7823

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Gabizon R, Taraboulos A. Of mice and (mad) cows - Transgenic mice help to understand prions. Trends in Genetics [Internet]. 1997;13(7):264–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030941209&doi=10.1016%2fS0168-9525%2897%2901116-5&partnerID=40&md5=2a6bcf96e46d92accbf34a57064e136a

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Friedman G, Gabizon R, Ben-Yehuda A. Apolipoprotein Eε4 allele, a risk factor for late onset nonfamilial Alzheimer’s disease among Israeli Jews. Archives of Gerontology and Geriatrics [Internet]. 1997;24(2):175–81. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031025524&doi=10.1016%2fS0167-4943%2896%2900750-9&partnerID=40&md5=10d60b46bc7bc057a384cc215406ea10

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Meiner Z, Gabizon R, Prusiner SB. Familial Creutzfeldt-Jakob Disease Codon 200 Prion Disease in Libyan Jews. Medicine [Internet]. 1997;76(4):227–37. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031183207&doi=10.1097%252f00005792-199707000-00001&partnerID=40&md5=e1f9fb9e2082c05d879803fb1785e288

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Rosenmann H, Halimi M, Kahana I, Biran I, Gabizon R. Differential allelic expression of PrP mRNA in carriers of the E200K mutation. Neurology [Internet]. 1997;49(3):851–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030774622&doi=10.1212%252fWNL.49.3.851&partnerID=40&md5=b385e0567482487b58df8effbaf6d783

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Rosenmann H, Meiner Z, Kahana E, Halimi M, Lenetsky E, Abramsky O, et al. Detection of 14-3-3 protein in the CSF of genetic Creutzfeldt Jakob disease. Neurology [Internet]. 1997;49(2):593–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030766643&doi=10.1212%252fWNL.49.2.593&partnerID=40&md5=6d5ee78ab675605cd42c0ac4fa9bfcc9

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Telling GC, Parchi P, DeArmond SJ, Cortelli P, Montagna P, Gabizon R, et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science [Internet]. 1996;274(5295):2079–82. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-12644272790&doi=10.1126%252fscience.274.5295.2079&partnerID=40&md5=49f6395dd474fa6a7da89efbc6ad2e76

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Ovadia H, Rosenmann H, Shezen E, Halimi M, Ofran I, Gabizon R. Effect of scrapie infection on the activity of neuronal nitric-oxide synthase in brain and neuroblastoma cells. Journal of Biological Chemistry [Internet]. 1996;271(28):16856–61. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030008814&doi=10.1074%252fjbc.271.28.16856&partnerID=40&md5=a6fb075347b2a67cc3d7a1a5cffd27e7

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Gabizon R, Telling G, Meiner Z, Halimi M, Kahana I, Prusiner SB. Insoluble wild-type and protease-resistant mutant prion protein in brains of patients with inherited prion disease. Nature Medicine [Internet]. 1996;2(1):59–64. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030069023&doi=10.1038%252fnm0196-59&partnerID=40&md5=b9182f3cbdcd989341e8148f990cc74b

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Kaneko K, Peretz D, Pan KM, Blochberger TC, Wille H, Gabizon R, et al. Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1995;92(24):11160–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028867086&doi=10.1073%252fpnas.92.24.11160&partnerID=40&md5=9c021299433c958355055c290384cd21

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Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell [Internet]. 1995;83(1):79–90. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028882424&doi=10.1016%2f0092-8674%2895%2990236-8&partnerID=40&md5=9a9e6585c9b429c6593d32be35d7c29c

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Spudich S, Mastrianni JA, Wrensch M, Gabizon R, Meiner Z, Kahana I, et al. Complete penetrance of Cruetzfeldt-Jakob disease in Libyan Jews carrying the E200K mutation in the prion protein gene. Molecular Medicine [Internet]. 1995;1(6):607–13. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028981199&doi=10.1007%252fbf03401601&partnerID=40&md5=dc972bec5f336973f9d8be68257d6ba6

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Gabizon R, Halimi M, Meiner Z. Genetics and biochemistry of Creutzfeldt-Jakob disease in Libyan Jews. Biomedicine and Pharmacotherapy [Internet]. 1994;48(8–9):385–90. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028100125&doi=10.1016%2f0753-3322%2894%2990056-6&partnerID=40&md5=2b824365c8cd24b6c57b526b81c60ab7

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Prusiner SB, Groth D, Serban A, Stahl N, Gabizon R. Attempts to restore scrapie prion infectivity after exposure to protein denaturants. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1993;90(7):2793–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027509675&doi=10.1073%252fpnas.90.7.2793&partnerID=40&md5=42d12d70dce5e5d592c0676691645e02

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Goldhammer Y, Gabizon R, Meiner Z, Sadeh M. An israeli family with gerstmann-straussler-scheinker disease manifesting the codon 102 mutation in the prion protein gene. Neurology [Internet]. 1993;43(12):2718–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027730422&doi=10.1212%252fwnl.43.12.2718&partnerID=40&md5=a04a9ff278282c1e92b6fcd8b8682258

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Gabizon R, Meiner Z, Halimi M, Ben‐Sasson SA. Heparin‐like molecules bind differentially to prion‐proteins and change their intracellular metabolic fate. Journal of Cellular Physiology [Internet]. 1993;157(2):319–25. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027458091&doi=10.1002%252fjcp.1041570215&partnerID=40&md5=efb5de716d2b8b3b2899919aec7fcf0b

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Gabizon R, Rosenmann H, Meiner Z, Kahana I, Kahana E, Shugart Y, et al. Mutation and polymorphism of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease (CJD). American Journal of Human Genetics [Internet]. 1993;53(4):828–35. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027373649&partnerID=40&md5=70a6bf292df7a34c9a492f271d56e8bb

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Meiner Z, Halimi M, Polakiewicz RD, Prusiner SB, Gabizon R. Presence of prion protein in peripheral tissues of libyan jews with Creutzfeldt-Jakob disease. Neurology [Internet]. 1992;42(7):1355–60. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026696176&doi=10.1212%252fwnl.42.7.1355&partnerID=40&md5=6158701b980a542224180172c2d43a6b

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Hsiao K, Meiner Z, Kahana E, Cass C, Kahana I, Avrahami D, et al. Mutation of the prion protein in libyan jews with creutzfeldt–jakob disease. New England Journal of Medicine [Internet]. 1991;324(16):1091–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025869213&doi=10.1056%252fNEJM199104183241604&partnerID=40&md5=7a5f1e9fd249287e99a0895e90a4cd7e

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Meiner Z, Gabizon R, Kahana E. Creutzfeldt-Jacob disease: etiology and epidemiology. Harefuah [Internet]. 1991;120(1):19–22. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025928709&partnerID=40&md5=b8c0614af7388686d409a6dcdcdc9438

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Gabizon R, Prusiner SB. Prion liposomes. Biochemical Journal [Internet]. 1990;266(1):1–14. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025100762&doi=10.1042%252fbj2660001&partnerID=40&md5=5c4333250a57dc60014310b8958c91e7

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Gabizon R, McKinley MP, Groth D, Westaway D, DeArmond SJ, Carlson GA, et al. Immunoaffinity purification and neutralization of scrapie prions. Progress in clinical and biological research [Internet]. 1989;317:583–600. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024823529&partnerID=40&md5=49e5057f434df2bfbcb173409ba7acd4

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Gabizon R, McKinley MP, Groth DF, Kenaga L, Prusiner SB. Properties of scrapie prion protein liposomes. Journal of Biological Chemistry [Internet]. 1988;263(10):4950–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023948526&partnerID=40&md5=42658e3cc3c502a93b7aa8cfacb902ca

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Bellinger-Kawahara CG, Kempner E, Groth D, Gabizon R, Prusiner SB. Scrapie prion liposomes and rods exhibit target sizes of 55,000 Da. Virology [Internet]. 1988;164(2):537–41. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023888782&doi=10.1016%2f0042-6822%2888%2990569-7&partnerID=40&md5=7886c7f115c956586009043bab361aff

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Gabizon R, McKinley MP, Prusiner SB. Properties of scrapie prion proteins in liposomes and amyloid rods. Ciba Foundation symposium [Internet]. 1988;135:182–96. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023679496&partnerID=40&md5=03f3d72f4bc757fdbcae6c10bd76dd82

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Gabizon R, McKinley MP, Groth D, Prusiner SB. Immunoaffinity purification and neutralization of scrapie prion infectivity. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1988;85(18):6617–21. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0003279877&doi=10.1073%252fpnas.85.18.6617&partnerID=40&md5=8c90bf7f9e300a79a03d20947338ec3e

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Prusiner SB, Gabizon R, McKinley MP. On the biology of prions. Acta Neuropathologica [Internet]. 1987;72(4):299–314. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023139256&doi=10.1007%252fBF00687261&partnerID=40&md5=0bd576d8e0bc2cc20c0aac2d9776ecf2

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Gabizon R, McKinley MP, Prusiner SB. Purified prion proteins and scrapie infectivity copartition into liposomes. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1987;84(12):4017–21. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0343364948&doi=10.1073%252fpnas.84.12.4017&partnerID=40&md5=32a843f0f3e013b8cb8d7697b7c80c7b

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SCHULDINER S, GABIZON R, STERN Y, SUCHI R. The Amine Transporter from Bovine Chromaffin Granules: Photolabeling and Partial Purification. Annals of the New York Academy of Sciences [Internet]. 1987;493(1):189–93. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023065776&doi=10.1111%252fj.1749-6632.1987.tb27200.x&partnerID=40&md5=ba7876f45d035882a449de348a7f0aac

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SCHULDINER S, GABIZON R, MARON R, SUCHI R, STERN Y. The Amine Transporter from Bovine Chromaffin Granules. Annals of the New York Academy of Sciences [Internet]. 1985;456(1):268–76. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022273191&doi=10.1111%252fj.1749-6632.1985.tb14875.x&partnerID=40&md5=46f0acfdefda8807ef2b658f87902f86

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Gabizon R, Schuldiner S. The amine transporter from bovine chromaffin granules. Partial purification. Journal of Biological Chemistry [Internet]. 1985;260(5):3001–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021988236&partnerID=40&md5=267d9e159d8706ee11d6a852a38b80e6

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Gabizon R, Yetinson T, Schuldiner S. Photoinactivation and identification of the biogenic amine transporter in chromaffin granules from bovine adrenal medulla. Journal of Biological Chemistry [Internet]. 1982;257(24):15145–50. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020448945&partnerID=40&md5=278185581fb835cbddca3c4de737c32b