Personal Information

Education

1959-1964	B.Sc. Polytechnic Institute, Iassy, Romania, Chemical Engineering M.Sc. Polytechnic Institute, Iassy, Romania, Chemical Engineering
1972-1976	PhD. Weizmann Institute of Science, Rehovot, Israel, Biophysics & Biochemistry

Academic and Professional Experience

1979-1985	Investigator, Department of Molecular Microbiology and Biotechnology, Tel Aviv University
1985-1989	Senior investigator, Department of Molecular Microbiology and Biotechnology, Tel Aviv University
1987-1988	Visiting Lecturer, Center for Biophysics and Biochemistry, Harvard Medical School, Boston, Ma., USA & Brigham and Women's Hospital, Boston, Ma. USA
1989 - 1996	Senior lecturer, Department of Molecular Microbiology and Biotechnology, Tel Aviv University
1996 - 2002	Associate Professor, Department of Molecular Microbiology and Biotechnology, Tel Aviv University
2002-present	Full Professor, Department of Molecular Microbiology and Biotechnology, Tel Aviv University
2002	Tel-Aviv University, Incumbent of the Chair for Biotechnology of Neurodegenerative Diseases
2007	Selected by Scientific American for their list of The 50 Leading Scientists in the World for 2007.

Research Interests

My scientific interest is focused on investigation of biorecognition in general and on the nature of the interactions of antibodies and their corresponding antigens in particular. In my research work I am involved in the elucidation of the mode of action of monoclonal antibodies (mAbs) on the structure and function of their corresponding antigens in in vitro and in vivo environments. Antibodies were found to act as reporting probes for the detection of conformational changes induced in various protein antigens by environmental factors, as well as playing active roles in inducing changes and rearrangements in the antigen molecule. The following topics are being investigated:

1. detection of conformation changes in the protein antigen by their mAbs.
2. stabilization of the antigen structure by mAbs.
3. Chaperone characteristics of mAbs leading to the refolding of the respective antigen.
4. Prevention of aggregation and solubilization of previously formed protein aggregates.

My group prepared monoclonal antibodies towards several proteins, such as carboxypeptidase A, Che Y, hexosaminidase A, horseradish peroxidase, p53 protein, calmodulin and against aluminium ions, and recently against Alzheimer¹s ß-amyloid peptide and prion peptides 106-126, in order to study conformational changes occurring in these proteins when exposed to various working conditions. The monoclonal antibodies were used as probes to assay conformation changes of interacting epitopes in these target proteins, induced by temperature, pH, proteolytic cleavage or metal interactions. The availability of the mAbs enabled me and my collaborators to develop new immobilization techniques yielding fully active immobilized Ab-carrier conjugates, which led to novel techniques for enzyme immobilization and stabilization. The immobilized mAbs permitted the development of novel immunoaffinity techniques and original immunoassay techniques. A microalbuminuria assay based on the above techniques was especially appreciated and received an Award for Excellence in a Meeting of Clinical Biochemistry held in Japan in 1991.

Protein aggregation plays an important role in various human diseases, such as Down¹s syndrome, Alzheimer¹s disease, diabetes and/or cataracts, and in many other so-called amyloidosis disorders. In order to reduce or eliminate the extent of pathological protein depositions my group focused on the development of potent and selective inhibitors of aggregate formation. We commenced our studies by using carboxypeptidase A (CPA) as a model system and a large panel of mAbs prepared against it. We found that appropriate mAbs interact at strategic sites where protein unfolding is initiated, thereby stabilizing the protein and suppressing further aggregation. These studies were extended on the suppression of Alzheimer ß-amyloid peptide by immunocomplexation with highly specific monoclonal antibodies raised against the peptide. The amyloid ß-peptide is a main component of the senile plaques ­ amyloid ­ found in the brain tissues of Alzheimer¹s diseased patients. Amyloid stability, even under harsh conditions, was one of the unsurmountable problems in the initial characterization of its constituents.

We recently found that selected mAbs against ß-amyloid peptide can solubilize preformed ß-amyloid aggregated filaments by reversal of the ß-sheet insoluble conformation into a corresponding soluble random coil. Such Œchaperone-like¹ properties of mAbs were found to be related to so-called anti-aggregating epitopes on each antigen. We found that mAbs directed to these regions are able to interfer with the dynamics and rearrangement of whole molecules.

1. Brain delivery of anti-ß-amyloid antibodies obtained by EFRH-phage immunization
Filamentous phages, which are excellent vehicles for the expression and presentation of foreign peptides, were found to induce a strong immunological response to all the phage proteins after in vivo administration. The efficacy of this procedure is directly dependent on the immunogenicity of the peptide displayed. Due to the high antigenicity of the EFRH peptide, which belongs to the immunodominant region of ßAP, high affinity (IgG) antibodies were obtained after a very short immunization time (one week) compared to protein carrier immunization (one year). Immunogenicity of the phage enables administration via intranasal route without any use of adjuvant. Intranasal administration appears to be a more effective route of mice immunization in terms of timing and reproducibility of response.

2. Intranasal delivery of engineered antibodies
In preliminary experiments we found that vectors carrying single-chain Fv (ScFv) antibodies may be delivered directly to the CNS by intranasal administration via olfactory receptor neurons. Their axons traverse the cribriform plate and project to the first synapse of the olfactory pathway in the olfactory bulb of the brain. They form a highway by which viruses or other transported substances may gain access to the CNS. To our knowledge, this is the first attempt to deliver antibodies to the CNS.

ß-Amyloid is only one example of at least 15 different polypeptides known to cause in vivo different forms of pathological amyloidosis via their deposition in particular organs and tissues as insoluble protein fibrils. The prevention of aggregation and solubilizations of other peptides that form amyloid in tissues, such as amylin, serum amyloid A, prion protein, are being investigated at present. Since properly selected mAbs can be prepared against virtually any antigen, their immunocomplexation may provide a general and convenient method for the stabilization of the soluble physiological conformation of the above proteins without affecting their biological properties.

Our recent findings on the chaperone-like activity of mAbs in stabilization, refolding and solubilization of the already aggregated antigens, as well as the introduction of antibody engineering techniques, open up new possibilities for the potential use of mAbs in immunotherapy of Alzheimer¹s disease. The development of therapeutic antibodies for use as a future vaccine in Alzheimer¹s disease and/or other amyloidogenic diseases, such as prion disease, are the subject of the Master of Science and Ph.D. theses of students in my lab.

We have started to apply our novel procedures for the production of anti-aggregating antibodies by active and passive immunization, as well as by direct delivery to the brain avoiding the blood brain barrier in the Alzheimer¹s disease model of transgenic mice.

We recently commenced another project based on a search for biological markers in body fluids from Alzheimer¹s disease and control patients to enable evaluation of the pathophysiological hypothesis of this disease, taking into consideration the fact that a defect in the transduction system might play a central role in the pathogenesis of Alzheimer¹s disease. An early detection test for Alzheimer¹s disease is not yet available and there is an urgent need to develop technologies for its production, as wel as the accurate detection of AD. Our laboratories will study the metabolism of ßAPP in the human circulation. Such studies are aimed at elucidating environmental or nutritional factors which may alter the levels of ßAPP production and determine whether abnormalities of ßAPP metabolism evident in the brain in AD are reflected in the blood.

Full Publications

1. Solomon, B., Taraboulos, A. and Katchalski-Katzir, E. Conformational Diseases. Amyloid: Int. J. Exp. Clin. Invest. 6 (1999) 225-228.

B. REFEREED ARTICLES

22. G. Fleminger, E. Hadas, T. Wolf and B. Solomon, Oriented immobilization of periodate oxidized monoclonal antibodies on amino and hydrazide derivatives of Eupergit C. Applied Biochem. Biotech. 23, (1990) 123 139.

23. Fleminger G., Solomon B., Wolf T. and Hadas E. The effect of polyethylene glycol on the nonspecific adsorption of protein to Eupergit C and agarose. J. of Chromatography, 510, (1990) 271 279.

24. Fleminger G., Solomon B., Wolf T. and Hadas E. Single step oxidative binding of antibodies to hydrazide modified Eupergit C. Applied Biochem. Biotech. 26, (1990) 231 238.

25. Fleminger G., Wolf T., Hadas E. and Solomon B. Application of Eupergit C to high performance immunoaffinity of antigens and antibodies. J. of Chromatography, 510, (1990) 311 319.

26. F. Schwartz, E. Hadas, M. Harnik and B. Solomon, Evaluation of an Enzyme Linked Immunosorbent Assay for Determination of Plasma Aldosterone. J. of Immunoassay. 11(2), (1990) 215 234.

27. Solomon, B., Larsen, K.S. and Riordan, J.F. Catalytic and conformational changes induced by limited
subtilisin cleavage of bovine Carboxypeptidase A. Biochemistry 29, (1990) 7303 7309.

28. Solomon B., Kopel R., Schwartz F., and Fleminger G. Enzymatic oxidation of monoclonal antibodies by soluble and immobilized bifunctional enzyme complexes. J. of Chromatography, 510, (1990) 321 329.

29. Solomon, B., Hadas, E., Koppel, R, Schwartz, F. and Fleminger, G. Highly active enzyme preparations immobilized via matrix conjugated anti Fc antibodies. J. of Chromatography. 539 (2) (1991) 335 341.

30. Solomon, B. and Balas, N. Thermostabilization of Carboxypeptidase A by interaction with its monoclonal antibodies. Biotechnol. and App. Biochem. 14, (1991) 202 211.

31. Solomon, B., Ravit, O., Libman, E. and Fleminger, G. Affinity purification of antibodies using immobilized FB domain of Protein A. J. of Chromatography. 597, (1991) 257 262.

32. Fleminger, G., Neufeld, T., Star-Weinstock, M. and Solomon, B. Conformation-dependent affinity chromatography-application to Ca2+ binding proteins. J. of Chromatography. 597, (1992) 263-270.

33. Solomon, B., Fleminger, G., Schwartz, F., Doolman, R. and Sela, B.A. Microalbuminuria immunoassay based on antibodies covalently conjugated to Eupergit C coated beads. Diabetes Care, 15, (1992) 1451-1454.

34. Solomon, B., Schmitt, S., Schwartz, F., Levi, A. and Fleminger, G. Eupergit C-coated membranes as solid support for a sensitive immunoassay of human albumin. J. of Immunol. Meth. 157, (1993) 209-215.

35. Koppel, R., Litvak, M. and Solomon, B. Affinity purification of a mannose-binding protein, a sensitive tool in the diagnostics of IgM, via site-directed phosphorylated mannan bound to alumina. J. Chrom. B. Biomed. Appl. 662, (1994) 191-196. (Invited paper).

36. Solomon, B. and Schwartz, F. Chaperone-like effect of monoclonal antibodies on refolding of heat-denatured carboxypeptidase A. J. of Molec. Recognition. 8, (1995) 72-76.

37. Wolf, T., Fleminger, G. and Solomon, B. Functional conformations of Calmodulin: I. preparation and characterization of a conformational specific anti-bovine calmodulin monoclonal antibody. J. Molec. Recognition. 8, (1995) 67-71.

38. Ron, E., Freeman, A. and Solomon, B. Stabilization and surface modification of monoclonal antibodies by 'bi-layer encagement`. J. Immunol. Meth. 180 (1995) 237-245.

39. Solomon, B., Koppel, R., Hanan, E. and Katzav, T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer's β-amyloid peptide. Proc.Nat.Acad.Sci. USA 93 (1) (1996) 452-455.

40. Hanan, E. and Solomon, B. Protective effect of monoclonal antibodies against Alzheimer's β-amyloid aggregation. Amyloid. Int. J. of Exp. Clin. Invest. 3 (1996) 130-133.

41. Katzav, T., Hanan, E. and Solomon, B. Effect of monoclonal antibodies in preventing Carboxypeptidase A aggregation. Appl. Biochem. Biotechnol. 23 (1996) 227-230.

42. Solomon, B., Koppel, R., Frankel, D. and Hanan-Aharon, E. Disaggregation of Alzheimer -amyloid by site-directed mAb. Proc. Natl. Acad. Sci. USA 94 (1997) 4109-4112.

44. Levy, R., Shohat, L. and Solomon, B. Specificity of an anti-aluminium monoclonal antibody toward free and protein-bound aluminium. J. Inorg. Biochem. 69 (1998) 159-163.

45. Frenkel, D., Balass, M. and Solomon, B. N-terminal EFRH sequence of Alzheimer’s -amyloid peptide represents the epitope of its anti-aggregating antibodies. J. Neuroimmunology 88 (1998) 85-90.

46. Ivnitsky, D., Wolf, T., Solomon, B., Fleminger, G. and Rishpon, J. An amperometric biosensor for real-time analysis of molecular recognition. Bioelectrochem. Bioenerg. 45 (1998) 27-32.

47. Levy, R., Wolf, T., Fleminger, G. and Solomon, B. Immuno-detection of aluminium and aluminium induced conformational changes in calmodulin implications in Alzheimer’s disease. Molec. Cell. Biochemistry. 189 (1998) 41-46.

48. Wolf, T., Solomon, B., Ivnitski, D., Rishpon, J. and Fleminger, G. Interactions of calmodulin with metal ions and with its target proteins revealed by conformation-sensitive monoclonal antibodies. J. Molec. Recogn. 11 (1998) 1-6.

49. Frenkel, D. Balass, M., Katchalski-Katzir, E. and Solomon, B. High affinity binding of monoclonal antibodies to the sequential epitope EFRH of -amyloid peptide is essential for modulation of fibrillar aggregation. J. Neuroimmunology 95 (1999) 136-142.

51. Frenkel, D., Solomon, B. and Benhar, I. Modulation of Alzheimer’s -amyloid neurotoxicity by site-directed single-chain antibody. J. Neuroimmunol. 106 (2000) 23-31.

52. Solomon, B. and Frenkel, D. Vaccination towards prevention and treatment of Alzheimer’s disease. Drugs of Today 36 (2000) 655-663.

53. Frenkel, D., Katz, O. and Solomon, B. Immunization against Alzheimer’s β-amyloid plaques via EFRH administration. Proc. Natl. Acad. Sci. USA 97 (2000) 11455-11459.

54. Steingart, R.A., Solomon, B., Brenneman, D.E., Fridkin, M. and Gozes, I. VIP and peptides related to activity-dependent neurotrophic factor protect PC12 cells against oxidative stress. J. Molec. Neurosci. 15 (2000) 137-145.

56. Frenkel, D., Kariv, N. and Solomon, B. Generation of auto-antibodies towards Alzheimer’s disease vaccination. VACCINE 19 (2001) 2615-2619.

57. Frenkel, D. and Solomon, B. Towards Alzheimer’s β-amyloid vaccination. Biologicals 29, (2001) 243-247.

58. Xinhui Li and Solomon, B. Zinc-mediated thermal stabilization of carboxypeptidase A. Bioengin. Molec. 18 (2001) 179-183.

59. Xinhui Li and Solomon, B. Zinc-mediated thermal stabilization of carboxypeptidase A. Bioengin. Molec. 18 (2001) 179-183.

60. Solomon, B. Imunotherapeutic strategies towards prevention and treatment of Alzheimer’s disease. DNA and Cell Biology 20 (2001) 697-703.

61. Solomon, B., Koppel, R. and Jossiphov, J. Immunostaining of calmodulin and aluminium in Alzheimer’s diseaseaffected brains. Brain Research Bull. 55, (2001) 253-256.

62. Solomon, B. and R. Koppel. IgM detection via selective recognition by mannose-binding protein. J. Biochem.Biophys. Meth. 49 (2001) 641-647.

63. Govorko, D., Cohen, G. and Solomon, B. Single chain antibody against the common epitope of mutant p53: isolation and intracytosolic expression in mammalian cells. J. Immunol. Meth. 258 (2001) 169-181.

64. Hanan, E., Priola, S.A. and Solomon, B. Anti-aggregating antibody raised against human PrP 106-126 recognizes pathological and normal isoforms of the whole prion protein. Cellular and Molec. Neurobiology. (2001). 21(6):693-703.

65. Levy, Y., Hanan, E., Solomon, B., Becker, O.M. Helix-coil transition of PrP106-126: Molecular dynamic study. Proteins (2001) 1;45(4):382-96.

66. Frenkel, D., and Solomon, B. Filamentous phage as vector-mediated antibody delivery to the brain. Proc. Natl. Acad. Sc. USA. (2002) 99(8):5675-9.

70. Pan, W., Solomon, B., Maness, L.M., Kastin, A.J. Antibodies to beta-amyloid decrease the blood-to-brain transfer of beta-amyloid peptide. Exp. Biol Med (Maywood) (2002) 227(8): 609-15.

71. Solomon, B. and Frenkel, D. Generation and brain delivery of anti-aggregating antibodies against β-amyloid plaques using phage display technology. J. Neural Transmission. (2002) 62: 321-325.

73. Frenkel, D., Dewachter, I., van Leuven, F. and Solomon, B. Reduction of β-amyloid plaques in brain of transgenic mouse model of Alzheimer’s disease by EFRH-phage immunization. Vaccine (2003) 21:1060-1065.

75. Arbel M, Lavie V, Solomon B. Generation of antibodies against prion protein in wild-type mice via helix 1 peptide immunization. J Neuroimmunol. 2003 144(1-2):38-45.

76. Solomon B. Immunological approach for the treatment of Alzheimer's disease. J Mol Neurosci. 2003;20(3):283-6.

77. Frenkel D, Dori M, Solomon B. Generation of anti-beta-amyloid antibodies via phage display technology. Vaccine (2004) 22(19):2505-8.

78. Lavie V, Becker M, Cohen-Kupiec R, Yacoby I, Koppel R, Wedenig M, Hutter-Paier B, Solomon B. EFRH-Phage immunization of Alzheimer's disease animal model improves behavioral performance in Morris Water Maze trials. J Molec Neurosc (2004) 24:105-113.

79. Solomon B. Alzheimer's disease and immunotherapy. Curr Alz Res (2004) 1:149-163.

80. Solomon B. Generation of anti-beta amyloid antibodies via phage display technology towards Alzheimer's disease vaccination. Vaccine (2005) 18:2327-30.

81. Arbel M, Yacobi I, Solomon B. Inhibition of amyloid precursor protein processing by beta-secretase through site-directed antibodies. Proc Natl Acad Sci USA (2005) 10:102(21):7718-23.

82. Solomon, B. Peptide vaccine for Alzheimer's disease. Handbook of Biologically Active Peptides (2005) 535-540.

83. Solomon, B. In vivo targeting of amyloid plaques via intranasal administration of phage anti-β-amyloid antibodies. Proceedings of ADPD Conference 2005.

84. Rebe S. and Solomon B. Deglycosylation of anti-β amyloid antibodies inhibit microglia activation in bv-2 cellular model. American Journal of Alzheimer's and Related Diseases. (2005) 20(5):303-13.

85. Solomon B. Alzheimer's disease immunotherapy: from in vitro amyloid immunomodulation to in vivo vaccination. J. Alzheimer's Dis. (2006)1387-2877, 9: (3, Supplement), 433-438.

86. Orgad, S., Goldfinger N., Cohen, G., Rotter, V., Solomon, B. Single chain antibody against the common epitope of mutant p53 restores wild-type activity to mutant p53 protein. FEBS Lett. Oct 24;579(25):5609-15 (2005).

87. Istrin G, Bosis E, Solomon B. Intravenous immunoglobulin enhances the clearance of fibrillar amyloid-beta peptide. J. Neurosci. Res. (2006) 84(2):434-43.

88. Rakover I., Arbel M. and Solomon B. APP β-site-specific antibody improves cognitive function and reduces microhemmorhage and neuroinflammation in Tg 2576 mice without affecting brain Aβ levels. Neurodegen Dis (2007) 4(5):392-402.

89. Becker M., Lavie V. and Solomon B. Stimulation of endogenous neurogenesis by anti-EFRH immunization in transgenic mice model of Alzheimer’s disease. Proc Natl Acad Sci USA (2007) 104(5):1691-6.

90. Solomon B. Active Immunization against Alzheimer's beta-amyloid peptide using phage display technology. Vaccine (2007) 25(16):3053-6.

91. B. Solomon. Immunological approaches for amyloid beta clearance toward Alzheimer's disease treatment. Rejuvenation Research. (2007). In Press.

C. CHAPTERS IN BOOKS

4. Solomon, B., Larsen, K.S. and Riordan, J.F. A neo isoform of Carboxypeptidase A produced by a single proteolytic cleavage. Ann. N.Y. Acad. of Sc. 613, (1990) 594 600.

5. B. Solomon and G. Fleminger. Application of Highly Active Matrix Conjugated Monoclonal Antibodies for the Isolation and Analysis of Enzymes, Monoclonal Antibodies. Applications in Clinical Oncology. (Chapman and Hall, eds.) England, Chap. 20, (1991) 193 201.

6. Solomon, B., Schwartz, F. and Levi, A. Dot enzyme linked immunoassay of urine albumin. Progress in Clin. Biochem.( K. Miyai, T. Tanno and E. Ishikawa, eds.) (1992) 247 249.

7. Solomon, B. and Goldstein, L. Modulation of the catalytic pathway of carboxypeptidase A by conjugation with polyvinylalcohols.
Advances in Molecular and Cell Biology (E. E. Bittar, B. Danielsson and L. Bulow, eds.) (1996) 15A, 33-45.

8. Solomon, B. and Goldstein, L. Modulation of the catalytic pathway of carboxypeptidase A by conjugation with polyvinylalcohols. Advances in
Molecular and Cell Biology (E. E. Bittar, B. Danielsson and L. Bulow, eds.) (1996) 15A, 33-45.

9. Solomon, B., Hanan, E., Koppel, R., Frankel, D., Ophir, I. and Schenck, D.
The amino terminus of the -amyloid peptide contains an essential epitope for maintaining its solubility. In Progress in Alzheimer’s and Parkinson’s Diseases. 49 (1998) 201-213 (Eds. A. Fisher, I. Hanin, M. Yoshida).

10. Solomon, B., Gozanski-Katzav,T., Koppel, R. and Hanan-Aharon, E. Activity of monclonal antibodies in prevention of in vitro aggregation of their antigens. Stability and Stabilization of Biocatalysts. ( A. Ballesteros, F.J. Plou, J.L. Iborra and P.J. Halling, eds.) 183 (1998) 183-188.

11. Solomon, B. and Frenkel, D. Generation of autoantibodies towards Alzheimer’s disease vaccination. In Alzheimer’s Disease: Advances in Etiology, Pathogenesis and Therapeutics. (ed. K. Iqbal). (2001) 769-775.

12. Solomon, B. Aluminium, Calmodulin and Alzheimer’s Disease. Aluminium in Alzheimer’s Disease.Elsevier (Ed. C. Exley). (2001) 393-409.

13. Solomon, B. and Frenkel, D. Fast induction of anti-β-amyloid peptide immune response. Research and Practice in Alzheimer’s Disease and Other Dementias 5 (2001) 27-31.

14. Solomon, B. Therapeutic antibodies, a new approach for treatment of Alzheimer’s disease. Conformational Diseases (Eds. B. Solomon, A. Taraboulos, E. Katzir). (2001) 276-281.

15. Solomon, B. Towards Diagnosis and Treatment of Alzheimer’s Disease. Research and Perspectives in Alzheimer’s Disease. Fondation IPSEN (Eds. K. Beyreuther, Y. Christen, C.L. Masters) (2003) 11-19.

16. Solomon, B. Peptide vaccine for Alzheimer's disease. Handbook of Biologically Active Peptides (2005) 535-540.

17. Solomon, B. In vivo targeting of amyloid plaques via intranasal administration of phage anti-β-amyloid antibodies. Proceedings of ADPD Conference (2005).

18. Solomon, B. Alzheimer's disease immunotherapy: from in vitro amyloid immunomodulation to in vivo vaccination. Alzheimer Anniversary Issue (2005).

19. Alzheimer’s Disease: New Advances: Collection of Selected Articles of Papers Presented at the 10th International Conference on Alzheimer’s Disease and Related Disorders. Editors Khalid Iqbal, Bengt Winblad, Jesus Avila, Madrid, Spain, July 15-20, 2006.

D. REVIEWS

1. Solomon, B. Towards Alzheimer’s disease vaccination. Mini-Reviews in Medicinal Chemistry. (2002) 2(1): 85-92.

2. Solomon, B. Anti-aggregating antibodies, a new approach towards treatment of conformational diseases. Current Medicinal Chemistry. (2002) 9(19): 1667-75.

3. Solomon, B. Immunological concept in the treatment of Alzheimer’s disease. Drug Development Research. Review (2002) 56(2): 163-167.

4. Solomon, B. Immunological approaches as therapy for Alzheimer’s disease. Exp. Opp. Biol. Therapy (2002) 2 (8) 907-17.

5. Solomon, B. Anti-aggregating antibodies, a new approach towards treatment of conformational diseases. Current Medicinal Chemistry. (2002) 9(19): 1737-49.

6. Solomon, B. Protective molecules in Alzheimer’s disease: Therapeutic antibodies. (2002) Drug News Perspectives. 15(7): 410-416.

7. Solomon B. Alzheimer's disease and immunotherapy. Curr Alz Res (2004) 1:149-163.

8. Solomon, B. Intravenous immunoglobulin and Alzheimer's disease immunotherapy. Curr Opin Mol Ther. (2007);9(1):79-85.

9. Solomon, B. Clinical immunologic approaches for the treatment of Alzheimer's disease. Expert Opinion on Investigational Drugs (2007) 16(6):819-828.

10. Solomon, B. A neuroimmunologist's perspective on Alzheimer's disease therapy. Expert Rev Neurother. (2007) 7(5):439-41.

11. Solomon B. Antibody mediated immunotherapy of Alzheimer’s disease. Current Opinion in Investigational Drugs (2007) 9(1):79-85.

12. Solomon B. Beta-amyloid-based immunotherapy as a treatment of Alzheimer's disease. Drugs of Today (2007) 43(5):333-342.

13. Arbel M, Solomon B. A Novel Immunotherapy for Alzheimer's Disease: Antibodies against the beta-secretase cleavage site of APP. Curr Alzheimer Res. (2007) 4(4):437-45.

14. Arbel M. and B. Solomon. Attacking amyloid-beta from the inside. Trends in Immunology. (2007) 28(12): 511-3.

E. PATENTS

1. Z. Hollander, B. Solomon and E. Katchalski Katzir
"Reagent for the Assay of Enzymes (and Isoenzymes) in Clinical Systems using Monoclonal Antibodies"
Israel Patent No. 75828 (1985)
U.S. Patent No. 52692/1988
Japanese Patent No. 165708/1986
German Patent No. 3623845.5/87

2 . B. Solomon, G. Fleminger and E. Hadas
"Immobilization of Monoclonal Antibodies on Eupergit C and its Derivatives"
German Patent No. P 373872 1.9/87
U.S. Patent No.4 948836/90
Filed also in Denmark, France, United Kingdom, Israel,
The Netherlands, Sweden, and Switzerland

3. B. Solomon
"Prevention of protein aggregation"
U.S. Patent PCT/US94/16092. 1997.

4. E. Paley and B. Solomon
“Diagnostic test of Alzheimer’s disease”
Patent application 1999.

5. D. Govorko, G. Cohen and B. Solomon
“Construction of a single-chain antibody (scFv) against the conserved epitope of mutant p53 protein in human tumors and its application for cancer therapy”.
Patent application 1999.

6. D. Frenkel and B. Solomon
“Therapeutic antibodies against Alzheimer’s disease via EFRH immunization.”
Patent application, 1999.

7. E. Hanan and B. Solomon
“Immunomodulation of prion toxicity.”
Patent application 2000.