The Faculty of Medicine - Biochemistry and Molecular Biology: Razin Ehud

1.

Hidmi S, Nechushtan H, Razin E, Tshori S. Role of Nudt2 in Anchorage-Independent Growth and Cell Migration of Human Melanoma. International Journal of Molecular Sciences [Internet]. 2023;24(13). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85164844631&doi=10.3390%252fijms241310513&partnerID=40&md5=d580aab2a8607b38f6a5503d1fe22ae9

2.

Pavlyuchenkova AN, Chelombitko MA, Fedorov AV, Kuznetsova MK, Zinovkin RA, Razin E. The Distinct Effects of the Mitochondria-Targeted STAT3 Inhibitors Mitocur-1 and Mitocur-3 on Mast Cell and Mitochondrial Functions. International Journal of Molecular Sciences [Internet]. 2023;24(2). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85146699817&doi=10.3390%252fijms24021471&partnerID=40&md5=589df025ae600694573090188fea4ccf

3.

Paruchuru LB, Govindaraj S, Razin E. The Critical Role Played by Mitochondrial MITF Serine 73 Phosphorylation in Immunologically Activated Mast Cells. Cells [Internet]. 2022;11(3). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85124097295&doi=10.3390%252fcells11030589&partnerID=40&md5=3bf54ee6490df222692cb42d37f8207b

4.

Govindaraj S, Paruchuru LB, Razin E. The pLysRS-Ap4A pathway in mast cells regulates the switch from host defense to a pathological state. International Journal of Molecular Sciences [Internet]. 2021;22(11). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85106418917&doi=10.3390%252fijms22115620&partnerID=40&md5=ce782d4dac7baf385bb9eab0011a8229

5.

Rishiq A, Islam O, Golomb E, Gilon D, Smith Y, Savchenko I, et al. The role played by transcription factor e3 in modulating cardiac hypertrophy. International Heart Journal [Internet]. 2021;62(6):1358–68. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85120410177&doi=10.1536%252fihj.21-088&partnerID=40&md5=598a15e02dafbe861e802cb1644d9f65

6.

Chelombitko MA, Chernyak BV, Fedorov AV, Zinovkin RA, Razin E, Paruchuru LB. The Role Played by Mitochondria in FcεRI-Dependent Mast Cell Activation. Frontiers in Immunology [Internet]. 2020;11. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85094854877&doi=10.3389%252ffimmu.2020.584210&partnerID=40&md5=56d8fb8b5ef4b46210c5d1cba3ca72b8

7.

Yu J, Liu Z, Liang Y, Luo F, Zhang J, Tian C, et al. Second messenger Ap4A polymerizes target protein HINT1 to transduce signals in FcεRI-activated mast cells. Nature Communications [Internet]. 2019;10(1). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85073163293&doi=10.1038%252fs41467-019-12710-8&partnerID=40&md5=d0e017bdfaaa84674220474f08fbf004

8.

La Shu S, Paruchuru LB, Tay NQ, Chua YL, Yun Foo AS, Yang CM, et al. Ap4A Regulates Directional Mobility and Antigen Presentation in Dendritic Cells. iScience [Internet]. 2019;16:524–34. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85067613994&doi=10.1016%252fj.isci.2019.05.045&partnerID=40&md5=e1d2c84874e7e31df34c9c2345a7d91f

9.

Boulos S, Park MC, Zeibak M, Foo SY, Jeon YK, Kim YT, et al. Erratum: Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma (Oncotarget (2017) 8 (65186-65198) DOI:10.18632/oncotarget.18053). Oncotarget [Internet]. 2018;9(90):36250. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85056994589&partnerID=40&md5=9fdb65cde126fbed3a0f512231d628ca

10.

Erlich TH, Sharkia I, Landolina N, Assayag M, Goldberger O, Berkman N, et al. Modulation of allergic responses by mitochondrial STAT3 inhibitors. Allergy: European Journal of Allergy and Clinical Immunology [Internet]. 2018;73(11):2160–71. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85055619343&doi=10.1111%252fall.13467&partnerID=40&md5=7a68e45ffcde52073e5fd6e1bdd04606

11.

Motzik A, Amir E, Erlich T, Wang J, Kim BG, Han JM, et al. Post-translational modification of HINT1 mediates activation of MITF transcriptional activity in human melanoma cells. Oncogene [Internet]. 2017;36(33):4732–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85017196908&doi=10.1038%252fonc.2017.81&partnerID=40&md5=9d22b569274ff8dd3f0a7866eb6e7493

12.

Sharkia I, Hadad Erlich T, Landolina N, Assayag M, Motzik A, Rachmin I, et al. Pyruvate dehydrogenase has a major role in mast cell function, and its activity is regulated by mitochondrial microphthalmia transcription factor. Journal of Allergy and Clinical Immunology [Internet]. 2017;140(1):204-214.e8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85008156043&doi=10.1016%252fj.jaci.2016.09.047&partnerID=40&md5=427d4e0d826bc0de7f1ac248921ccd80

13.

Boulos S, Park MC, Zeibak M, Foo SY, Jeon YK, Kim YT, et al. Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma. Oncotarget [Internet]. 2017;8(39):65186–98. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85030119087&doi=10.18632%252foncotarget.18053&partnerID=40&md5=cf0324ccb1d7bdf981f1f5102ea292ad

14.

Wang J, Fang P, Chase P, Tshori S, Razin E, Spicer TP, et al. Development of an HTS-Compatible Assay for Discovery of Melanoma-Related Microphthalmia Transcription Factor Disruptors Using AlphaScreen Technology. Journal of Biomolecular Screening [Internet]. 2017;22(1):58–66. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85007189907&doi=10.1177%252f1087057116675274&partnerID=40&md5=58bb9cf5aed2f64092975e75fcf30ab4

15.

Boulos S, Razin E, Nechushtan H, Rachmin I. Diadenosine Tetraphosphate (Ap4A) in Health and Disease. RNA Technologies [Internet]. 2016;207–19. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85071583853&doi=10.1007%252f978-3-319-34175-0_9&partnerID=40&md5=a6dec6342c66cec3310977fa95fce40d

16.

Rachmin I, Amsalem E, Golomb E, Beeri R, Gilon D, Fang P, et al. FHL2 switches MITF from activator to repressor of Erbin expression during cardiac hypertrophy. International Journal of Cardiology [Internet]. 2015;195:85–94. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84937538756&doi=10.1016%252fj.ijcard.2015.05.108&partnerID=40&md5=1c47ae6a3ffb1e4662510144aadf7515

17.

Cohen-Saidon C, Nechushtan H, Kahlon S, Livni N, Nissim A, Razin E. Errata: A novel strategy using single-chain antibody to show the importance of Bcl-2 in mast cell survival (Blood (2003) 102, 7 (2506-2512)). Blood [Internet]. 2015;125(15):2451. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84927667291&doi=10.1182%252fblood-2015-02-631499&partnerID=40&md5=d952b924d22678e7c00a41779e9cc5f0

18.

Rachmin I, Tshori S, Smith Y, Oppenheim A, Marchetto S, Kay G, et al. Erbin is a negative modulator of cardiac hypertrophy. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 2014;111(16):5902–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84899079029&doi=10.1073%252fpnas.1320350111&partnerID=40&md5=5c717bf188f73b38e8e9d4a45b4d50ef

19.

Tshori S, Razin E, Nechushtan H. Amino-acyl tRNA synthetases generate dinucleotide polyphosphates as second messengers: functional implications. Topics in current chemistry [Internet]. 2014;344:189–206. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84906080977&doi=10.1007%252f128_2013_426&partnerID=40&md5=acacb0529e465d9efc0f686ac2f2fc71

20.

Erlich TH, Yagil Z, Kay G, Peretz A, Migalovich-Sheikhet H, Tshori S, et al. Mitochondrial STAT3 plays a major role in IgE-antigen-mediated mast cell exocytosis. Journal of Allergy and Clinical Immunology [Internet]. 2014;134(2):460-469.e10. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84905568336&doi=10.1016%252fj.jaci.2013.12.1075&partnerID=40&md5=6ea0dd36375de5ba16867f053e91c496

21.

Motzik A, Nechushtan H, Foo SY, Razin E. Non-canonical roles of lysyl-tRNA synthetase in health and disease. Trends in Molecular Medicine [Internet]. 2013;19(12):726–31. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84888437348&doi=10.1016%252fj.molmed.2013.07.011&partnerID=40&md5=89d08b24a59bf44af84f988daa914caa

22.

Ofir-Birin Y, Fang P, Bennett SP, Zhang HM, Wang J, Rachmin I, et al. Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription. Molecular Cell [Internet]. 2013;49(1):30–42. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84872269734&doi=10.1016%252fj.molcel.2012.10.010&partnerID=40&md5=9e5ea9dbc814535b92bd5c71fca828c4

23.

Kim DG, Choi JW, Lee JY, Kim H, Oh YS, Lee JW, et al. Interaction of two translational components, lysyl-tRNA synthetase and p40/37LRP, in plasma membrane promotes laminin-dependent cell migration. FASEB Journal [Internet]. 2012;26(10):4142–59. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84868110113&doi=10.1096%252ffj.12-207639&partnerID=40&md5=e2a3570553fbe18dec85e2dad635cca9

24.

Yagil Z, Hadad Erlich T, Ofir-Birin Y, Tshori S, Kay G, Yekhtin Z, et al. Transcription factor E3, a major regulator of mast cell-mediated allergic response. Journal of Allergy and Clinical Immunology [Internet]. 2012;129(5):1357-1366.e5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84860426179&doi=10.1016%252fj.jaci.2011.11.051&partnerID=40&md5=5b75089b0951d34434f3bf930cf6fa57

25.

Carmi-Levy I, Motzik A, Ofir-Birin Y, Yagil Z, Yang CM, Kemeny DM, et al. Importin beta plays an essential role in the regulation of the LysRS-Ap4A pathway in immunologically activated mast cells. Molecular and Cellular Biology [Internet]. 2011;31(10):2111–21. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-79956094884&doi=10.1128%252fMCB.01159-10&partnerID=40&md5=eb524289261f3b303008ab63b393f06e

26.

Tshori S, Razin E. Editorial: Mast cell degranulation and calcium entry - The Fyn-calcium store connection. Journal of Leukocyte Biology [Internet]. 2010;88(5):837–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-78649561338&doi=10.1189%252fjlb.0610365&partnerID=40&md5=81ef364892a049d2ad38e3db281d5b52

27.

Yagil Z, Nechushtan H, Kay G, Yang CM, Kemeny DM, Razin E. The enigma of the role of Protein inhibitor of Activated STAT3 (PIAS3) in the immune response. Trends in Immunology [Internet]. 2010;31(5):199–204. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-77951620484&doi=10.1016%252fj.it.2010.01.005&partnerID=40&md5=5c1dc8897a78c67a87fec6d91c0def0f

28.

Shapira SC, Vinker S, Razin E, Ash N. Military tract of medicine–the need and the vision. Harefuah [Internet]. 2010;149(2):89–90, 124. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-77955896075&partnerID=40&md5=e91fc9e7f38066c43f55aac696d1f95a

29.

Nechushtan H, Kim S, Kay G, Razin E. Chapter 1 The Physiological Role of Lysyl tRNA Synthetase in the Immune System. Advances in Immunology [Internet]. 2009;103:1–27. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-69949183262&doi=10.1016%2fS0065-2776%2809%2903001-6&partnerID=40&md5=03a8af6aa6c50646e6118fbd632c4bc3

30.

Yannay-Cohen N, Carmi-Levy I, Kay G, Yang CM, Han JM, Kemeny DM, et al. LysRS Serves as a Key Signaling Molecule in the Immune Response by Regulating Gene Expression. Molecular Cell [Internet]. 2009;34(5):603–11. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-66449115592&doi=10.1016%252fj.molcel.2009.05.019&partnerID=40&md5=7b1581b4d29029695853392468d88b02

31.

Yagil Z, Kay G, Nechushtan H, Razin E. A specific epitope of protein inhibitor of activated STAT3 is responsible for the induction of apoptosis in rat transformed mast cells. Journal of Immunology [Internet]. 2009;182(4):2168–75. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-61449150452&doi=10.4049%252fjimmunol.0803030&partnerID=40&md5=8fdeba227698dfa25199d005c911676c

32.

Carmi-Levy I, Yannay-Cohen N, Kay G, Razin E, Nechushtan H. Diadenosine tetraphosphate hydrolase is part of the transcriptional regulation network in immunologically activated mast cells. Molecular and Cellular Biology [Internet]. 2008;28(18):5777–84. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-51349130543&doi=10.1128%252fMCB.00106-08&partnerID=40&md5=3f25abc2fe353dc415c4659df3365a05

33.

Textor B, Licht AH, Tuckermann JP, Jessberger R, Razin E, Angel P, et al. JunB is required for IgE-mediated degranulation and cytokine release of mast cells. Journal of Immunology [Internet]. 2007;179(10):6873–80. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-38449090551&doi=10.4049%252fjimmunol.179.10.6873&partnerID=40&md5=35d3879acf9b8b1c905ec36f22a4cd1a

34.

Tshori S, Sonnenblick A, Yannay-Cohen N, Kay G, Nechushtan H, Razin E. Microphthalmia transcription factor isoforms in mast cells and the heart. Molecular and Cellular Biology [Internet]. 2007;27(11):3911–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-34347361649&doi=10.1128%252fMCB.01455-06&partnerID=40&md5=5c17393e21a1af3b2e9f2e490c7f8bf4

35.

Carmi I, Razin E. The role played by key transcription factors in activated mast cells. Immunological Reviews [Internet]. 2007;217(1):280–91. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-34248219047&doi=10.1111%252fj.1600-065X.2007.00508.x&partnerID=40&md5=4bb7682dde5b50f9adfda148ff8d8b60

36.

Jung MH, Min JL, Sang GP, Sun HL, Razin E, Choi EC, et al. Hierarchical network between the components of the multi-tRNA synthetase complex: Implications for complex formation. Journal of Biological Chemistry [Internet]. 2006;281(50):38663–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33846016966&doi=10.1074%252fjbc.M605211200&partnerID=40&md5=e0ffe79e7fe7713981c156ff02ec806c

37.

Tshori S, Gilon D, Beeri R, Nechushtan H, Kaluzhny D, Pikarsky E, et al. Transcription factor MITF regulates cardiac growth and hypertrophy. Journal of Clinical Investigation [Internet]. 2006;116(10):2673–81. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33749451494&doi=10.1172%252fJCI27643&partnerID=40&md5=427f73f939988800317a446f1218d8c4

38.

Yannay-Cohen N, Razin E. Translation and transcription: The dual functionality of LysRS in mast cells. Molecules and Cells [Internet]. 2006;22(2):127–32. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33847608837&partnerID=40&md5=951d0b0d5ebc852a00a3694323adfca8

39.

Levy C, Lee YN, Nechushtan H, Schueler-Furman O, Sonnenblick A, Hacohen S, et al. Identifying a common molecular mechanism for inhibition of MITF and STAT3 by PIAS3. Blood [Internet]. 2006;107(7):2839–45. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33645500772&doi=10.1182%252fblood-2005-08-3325&partnerID=40&md5=3ca37bf57f5eb7ca0f83703a633e6c00

40.

Cohen-Saidon C, Carmi I, Keren A, Razin E. Antiapoptotic function of Bcl-2 in mast cells is dependent on its association with heat shock protein 90β. Blood [Internet]. 2006;107(4):1413–20. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-32644440045&doi=10.1182%252fblood-2005-07-2648&partnerID=40&md5=e7af0f9a95109f60ba803a8387b6104d

41.

Nechushtan H, Razin E. Mast cells: Must they always be different? Blood [Internet]. 2006;107(1):1–2. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-30144442234&doi=10.1182%252fblood-2005-10-3990&partnerID=40&md5=d08cd3aa73e73dc6575fcb22c487846c

42.

MacGlashan D, Galli SJ, Austen KF, Pecht I, Kawakami T, Brown M, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:89–94. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249147488&partnerID=40&md5=069cc2b83c3d2c03d7dac54f1c76231e

43.

Stevens R, Kitamura Y, Koyasu S, Rao A, Galli SJ, Ono SJ, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:11–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249137885&partnerID=40&md5=2d062b43cccdb493ed86927bf2d13a43

44.

Metcalfe DD, Oettgen H, Metzger H, Marshall JS, Rivera J, Galli SJ, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:24–38. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249125290&partnerID=40&md5=609e410aa6dae45bc3355769e279c4e7

45.

Pecht I, Razin E, Metcalfe DD, Koyasu S, Rivera J, Walls A, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:195–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249119199&partnerID=40&md5=f7b27b2d26a1186b7d6b41f1e3f93928

46.

Austen KF, Galli SJ, Rivera J, Oettgen H, Brown M, Koffer A, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:124–30. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249115914&partnerID=40&md5=2c3665d179efbf6c66e96776d9ac0949

47.

Ono SJ, Stevens R, Razin E, Kitamura Y, Austen KF, Rivera J, et al. General discussion I. Novartis Foundation Symposium [Internet]. 2005;271:95–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249111972&partnerID=40&md5=d6d49733aba5bfff2e1a86c3f17ee73e

48.

Rivera J, Stevens R, Metcalfe DD, Razin E, Rao A, Ono SJ, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:68–77. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249111654&partnerID=40&md5=dc6f97587d5266fab7cf5ee2e0150461

49.

Koffer A, Rivera J, Stevens R, Razin E, MacGlashan D, Koyasu S, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:47–53. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249106519&partnerID=40&md5=cfc985d66cfe1085c8fd22abe1d9e781

50.

Razin E, Monticelli S, Rao A, Rivera J, Stevens R, Brown M, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:187–90. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249100073&partnerID=40&md5=3d7b2c8a4510cb7c180fc73755ecba8b

51.

Razin E, Austen KF, Rivera J, Marshall JS, Koyasu S, Metcalfe DD, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:176–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249095830&partnerID=40&md5=0d02aefefdb613d91620143e0fd46cfe

52.

Pecht I, Kawakami T, Rivera J, Stevens R, MacDonald SM, Koyasu S, et al. Discussion. Novartis Foundation Symposium [Internet]. 2005;271:108–14. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-56249094518&partnerID=40&md5=020218c6ae3cf838d986e6d5307ff72e

53.

Cohen-Saidon C, Razin E. The involvement of Bcl-2 in mast cell apoptosis. Novartis Foundation Symposium [Internet]. 2005;271:191–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33745300487&partnerID=40&md5=a9f7122577d6d7948113573aff7f4b56

54.

Lee YN, Razin E. Nonconventional involvement of LysRS in the molecular mechanism of USF2 transcriptional activity in FcεRI-activated mast cells. Molecular and Cellular Biology [Internet]. 2005;25(20):8904–12. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-26444461483&doi=10.1128%252fMCB.25.20.8904-8912.2005&partnerID=40&md5=1dfaece2373c9ef6749b51213c1e82ca

55.

Sonnenblick A, Levy C, Razin E. Immunological trigger of mast cells by monomeric IgE: Effect on microphthalmia transcription factor, STAT3 network of interactions. Journal of Immunology [Internet]. 2005;175(3):1450–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-22544466958&doi=10.4049%252fjimmunol.175.3.1450&partnerID=40&md5=b3ea684faa915f6c7fe342fa23d87039

56.

Miller AJ, Levy C, Davis IJ, Razin E, Fisher DE. Sumoylation of MITF and its related family members TFE3 and TFEB. Journal of Biological Chemistry [Internet]. 2005;280(1):146–55. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-12844268574&doi=10.1074%252fjbc.M411757200&partnerID=40&md5=328d768c824d9c29fcc211e6d40a075f

57.

Sonnenblick A, Levy C, Razin E. Interplay between MITF, PIAS3, and STAT3 in mast cells and melanocytes. Molecular and Cellular Biology [Internet]. 2004;24(24):10584–92. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-10044251281&doi=10.1128%252fMCB.24.24.10584-10592.2004&partnerID=40&md5=196063991e153bd46a97fbc48c167f14

58.

Lee YN, Tuckerman J, Nechushtan H, Schutz G, Razin E, Angel P. c-Fos as a regulator of degranulation and cytokine production in FcεRI-activated mast cells. Journal of Immunology [Internet]. 2004;173(4):2571–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-4043176237&doi=10.4049%252fjimmunol.173.4.2571&partnerID=40&md5=ec491a5f2ebd46bef08afa71310d9829

59.

Lee YN, Nechushtan H, Figov N, Razin E. The Function of Lysyl-tRNA Synthetase and Ap4A as Signaling Regulators of MITF Activity in FcεRI-Activated Mast Cells. Immunity [Internet]. 2004;20(2):145–51. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-1342287127&doi=10.1016%2fS1074-7613%2804%2900020-2&partnerID=40&md5=4addcae670df8cba2ac0dc7d1bab4db9

60.

Levy C, Sonnenblick A, Razin E. Role Played by Microphthalmia Transcription Factor Phosphorylation and Its Zip Domain in Its Transcriptional Inhibition by PIAS3. Molecular and Cellular Biology [Internet]. 2003;23(24):9073–80. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344629660&doi=10.1128%252fMCB.23.24.9073-9080.2003&partnerID=40&md5=22223e4d8f2afc9bd7a82bace8a817ca

61.

Cohen-Saidon C, Nechushtan H, Kahlon S, Livni N, Nissim A, Razin E. A novel strategy using single-chain antibody to show the importance of Bcl-2 in mast cell survival. Blood [Internet]. 2003;102(7):2506–12. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141816702&doi=10.1182%252fblood-2002-12-3921&partnerID=40&md5=b28531226d74a0a6fb572e399d4ece02

62.

Nechushtan H, Razin E. The function of MITF and associated proteins in mast cells. Molecular Immunology [Internet]. 2002;38(16–18):1177–80. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036034250&doi=10.1016%2fS0161-5890%2802%2900059-7&partnerID=40&md5=5ab1e387c81a0557586d52b03e314026

63.

Levy C, Nechushtan H, Razin E. A new role for the STAT3 inhibitor, PIAS3: A repressor of microphthalmia transcription factor. Journal of Biological Chemistry [Internet]. 2002;277(3):1962–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037127318&doi=10.1074%252fjbc.M109236200&partnerID=40&md5=22ff24618e08ddfe4de0f9537b2d3fb9

64.

Nechushtan H, Razin E. Studies of different aspects of the role of protein kinase C in mast cells. International Archives of Allergy and Immunology [Internet]. 2001;124(1–3):130–2. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035044915&doi=10.1159%252f000053690&partnerID=40&md5=bdd2093e4c33821d182efda167a7b410

65.

Nechushtan H, Leitges M, Cohen C, Kay G, Razin E. Inhibition of degranulation and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ. Blood [Internet]. 2000;95(5):1752–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034161386&doi=10.1182%252fblood.v95.5.1752.005k18_1752_1757&partnerID=40&md5=d3d8b2d15309552994691114275bb687

66.

Bauer O, Razin E. Mast cell-nerve interactions. News in Physiological Sciences [Internet]. 2000;15(5):213–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034360657&doi=10.1152%252fphysiologyonline.2000.15.5.213&partnerID=40&md5=cbdad62efff64ca927864298fd1daa15

67.

Razin E, Zhang ZC, Nechushtan H, Frenkel S, Lee YN, Arudchandran R, et al. Suppression of microphthalmia transcriptional activity by its association with protein kinase C-interacting protein 1 in mast cells. Journal of Biological Chemistry [Internet]. 1999;274(48):34272–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0039613985&doi=10.1074%252fjbc.274.48.34272&partnerID=40&md5=c8c74931d66f05b0ba2290aefc1c5231

68.

Frenkel S, Kay G, Nechushtan H, Razin E. Nuclear translocation of upstream stimulating factor 2 (USF2) in activated mast cells: A possible role in their survival. Journal of Immunology [Internet]. 1998;161(6):2881–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032530948&partnerID=40&md5=a0d319b77e75c5f3f2155fab583f511d

69.

Zhang ZC, Nechushtan H, Jacob-Hirsch J, Avni D, Meyuhas O, Razin E. Growth-dependent and PKC-mediated translational regulation of the upstream stimulating factor-2 (USF2) mRNA in hematopoietic cells. Oncogene [Internet]. 1998;16(6):763–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0000500599&doi=10.1038%252fsj.onc.1201584&partnerID=40&md5=5342488f60e4a959f695e7e9937d27fc

70.

Nechushtan H, Razin E. Deciphering the early-response transcription factor networks in mast cells. Immunology Today [Internet]. 1998;19(10):441–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032188939&doi=10.1016%2fS0167-5699%2898%2901316-4&partnerID=40&md5=9106df6695c1406c0e3600ae5b12e2e8

71.

Ligumsky M, Kuperstein V, Nechushtan H, Zhang Z, Razin E. Analysis of cytokine profile in human colonic mucosal FcεRI-positive cells by single cell PCR: Inhibition of IL-3 expression in steroid-treated IBD patients. FEBS Letters [Internet]. 1997;413(3):436–40. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030768726&doi=10.1016%2fS0014-5793%2897%2900933-2&partnerID=40&md5=7ed31499234aa7f79caf2cb2954309c6

72.

Nechushtan H, Zhang Z, Razin E. Microphthalmia (mi) in murine mast cells: Regulation of its stimuli- mediated expression on the translational level. Blood [Internet]. 1997;89(8):2999–3008. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030903114&doi=10.1182%252fblood.v89.8.2999&partnerID=40&md5=4405d4d6981ff727c95f2aacdaf7c3ba

73.

Razin E, Lewin I, Zang ZC, Kupershtein V, Jacob-Hirsch J, Nechushtan H, et al. Translational regulation of mast cell USF-2 (fos-interacting protein) synthesis by cytokines and IgE-Ag: The dependency on PKC-β. FASEB Journal [Internet]. 1996;10(6):A1214. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33749113983&partnerID=40&md5=f34ddfa713a7e952a80c679c94bb7b45

74.

Necbushtan H, Soreq H, Kuperstein V, Tshoritf S, Razin E. Murine and human mast cells express acetylcholinesterase. FASEB Journal [Internet]. 1996;10(6):A1307. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33749098794&partnerID=40&md5=1954aaa3aefddd8b641743b5a189b5c6

75.

Nechushtan H, Soreq H, Kuperstein V, Tshori S, Razin E. Murine and human mast cell express acetylcholinesterase. FEBS Letters [Internet]. 1996;379(1):1–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030034629&doi=10.1016%2f0014-5793%2895%2901466-7&partnerID=40&md5=5a55b219acab03687ac63b12e9d65a90

76.

Lewin I, Jacob-Hirsch J, Zang ZC, Kupershtein V, Szallasi Z, Rivera J, et al. Aggregation of the FcεRI in mast cells induces the synthesis of Fos-interacting protein and increases its DNA binding activity: The dependence on protein kinase C-β. Journal of Biological Chemistry [Internet]. 1996;271(3):1514–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029664351&doi=10.1074%252fjbc.271.3.1514&partnerID=40&md5=f2e5f26c89af8b3a26510ed38c08f7fe

77.

Nechushtan H, Razin E. Regulation of mast cell growth and proliferation. Critical Reviews in Oncology/Hematology [Internet]. 1996;23(2):131–50. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030176084&doi=10.1016%2f1040-8428%2896%2900200-4&partnerID=40&md5=c7d24119ea65457cdffcb631f08f405d

78.

Chaikin E, Hakeem I, Razin E. The incapability of lnterleukin-4 to induce AP-1 activity in murine mast cells. International Archives of Allergy and Immunology [Internet]. 1995;107(1–3):57–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029049516&doi=10.1159%252f000236930&partnerID=40&md5=73239af527f1ea6994ee29e33dba1d33

79.

Cruz JR, Cano F, Razin E, Acheson DWK, Keusch GT. Fecal excretion of leukotriene C4 during human disease due to shigella dysenteriae. Journal of Pediatric Gastroenterology and Nutrition [Internet]. 1995;20(2):179–83. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028936488&doi=10.1097%252f00005176-199502000-00007&partnerID=40&md5=ee0c3643905e9896ce585912b149976c

80.

Razin E, Pecht I, Rivera J. Signal transduction in the activation of mast cells and basophils. Immunology Today [Internet]. 1995;16(8):370–3. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028887801&doi=10.1016%2f0167-5699%2895%2980003-4&partnerID=40&md5=27f7c1a18cb0e76ab75064182bc77a85

81.

Razin E, Szallasi Z, Kazanietz MG, Blumberg PM, Rivera J. Protein kinases C-β and C-ε link the mast cell high-affinity receptor for IgE to the expression of c-fos and c-jun. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1994;91(16):7722–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028169903&doi=10.1073%252fpnas.91.16.7722&partnerID=40&md5=a492006a14bb8c98c8ff1ebf4fdc35c7

82.

Chaikin E, Hakeem I, Razin E. Enhancement of interleukin-3-dependent mast cell proliferation by suppression of c-jun expression. Journal of Biological Chemistry [Internet]. 1994;269(11):8498–503. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028363974&partnerID=40&md5=c0d1fd177df767a080495d8f1fa90d9b

83.

Ophir A, Berenshtein E, Ziltener HJ, Razin E. 5-Fluorouracil and mast cell precursors in mice. Experimental Hematology [Internet]. 1993;21(12):1558–62. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027861031&partnerID=40&md5=442cd2c1890ca723afad809147a9aa72

84.

Baranes D, Lewin I, Razin E. Serum modulates mast cell responses to IgE antigen stimulation. European Journal of Immunology [Internet]. 1993;23(1):291–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027526051&doi=10.1002%252feji.1830230147&partnerID=40&md5=ddb452495368af547b1b9b5f71682265

85.

Lewin I, Nechushtan H, Ke Q, Razin E. Regulation of AP-1 expression and activity in antigen-stimulated mast cells: The role played by protein kinase C and the possible involvement of Fos interacting protein. Blood [Internet]. 1993;82(12):3745–51. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027144058&doi=10.1182%252fblood.v82.12.3745.bloodjournal82123745&partnerID=40&md5=cfbce823fad4dca19f00f8eb974151ca

86.

Razin E, Leslie KB, Schrader JW. Connective tissue mast cells in contact with fibroblasts express IL-3 mRNA. Analysis of single cells by polymerase chain reaction. Journal of Immunology [Internet]. 1991;146(3):981–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026087690&partnerID=40&md5=e41c2dc9e5959084803291108d2df159

87.

Baranes D, Razin E. Protein kinase C regulates proliferation of mast cells and the expression of the mRNAs of fos and jun proto-oncogenes during activation by IgE-Ag or calcium ionophore A23187. Blood [Internet]. 1991;78(9):2354–64. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026002444&doi=10.1182%252fblood.v78.9.2354.2354&partnerID=40&md5=4684c310d55bd69059b3d10663a3b7f4

88.

Chaikin E, Ziltener HJ, Razin E. Protein kinase C plays an inhibitory role in interleukin 3- and interleukin 4-mediated mast cell proliferation. Journal of Biological Chemistry [Internet]. 1990;265(36):22109–16. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025695871&partnerID=40&md5=5e3fa0562a86c51d4c1266d042909738

89.

Davidson S, Gilead L, Amira M, Ginsburg H, Razin E. Synthesis of chondroitin sulfate D and heparin proteoglycans in murine lymph node-derived mast cells. The dependence on fibroblasts. Journal of Biological Chemistry [Internet]. 1990;265(21):12324–30. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025324278&partnerID=40&md5=053617de1e25cf99142a89f6ab8a9d32

90.

Bashkin P, Razin E, Eldor A, Vlodavsky I. Degranulating mast cells secrete an endoglycosidase that degrades heparan sulfate in subendothelial extracellular matrix. Blood [Internet]. 1990;75(11):2204–12. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025370901&doi=10.1182%252fblood.v75.11.2204.2204&partnerID=40&md5=bb29fdb0fcc9d9f50b0ed3bd2ff4c5d3

91.

Gilead L, Bibi O, Razin E. Fibroblasts induce heparin synthesis in chondroitin sulfate E containing human bone marrow-derived mast cells. Blood [Internet]. 1990;76(6):1188–95. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025142229&doi=10.1182%252fblood.v76.6.1188.bloodjournal7661188&partnerID=40&md5=7ef570355b243e027eefb4bf33457684

92.

Razin E. Culture of bone marrow-derived mast cells: A model for studying oxidative metabolism of arachidonic acid and synthesis of other molecules derived from membrane phospholipids. Methods in Enzymology [Internet]. 1990;187(C):514–20. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024999197&doi=10.1016%2f0076-6879%2890%2987058-B&partnerID=40&md5=22fcfc35bf62de5e0dc001f7557065b5

93.

Matzner Y, Cohn M, Hyam E, Razin E, Fuks Z, Buchanan MR, et al. Generation of lipid neutrophil chemoattractant by irradiated bovine aortic endothelial cells. Journal of Immunology [Internet]. 1988;140(8):2681–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023942302&partnerID=40&md5=a9f9363d63e880a474dcc1983b100483

94.

Gilead L, Rahamim E, Ziv I, Or R, Razin E. Cultured human bone marrow-derived mast cells, their similarities to cultured murine E-mast cells. Immunology [Internet]. 1988;63(4):669–75. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023936180&partnerID=40&md5=e820652724aa67277b21ff7032620ced

95.

Eliakim R, Karmeli F, Razin E, Rachmilewitz D. Role of platelet-activating factor in ulcerative colitis. Enhanced production during active disease and inhibition by sulfasalazine and prednisolone. Gastroenterology [Internet]. 1988;95(5):1167–72. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023781719&doi=10.1016%2f0016-5085%2888%2990346-0&partnerID=40&md5=2d4349c4a306eec881633efee48c87e4

96.

Gilead L, Livni N, Eliakim R, Ligumsky M, Fich A, Okon E, et al. Human gastric mucosal mast cells are chondroitin sulphate E-containing mast cells. Immunology [Internet]. 1987;62(1):23–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023193143&partnerID=40&md5=a9665026f27e6c66d38df025f8ed7236

97.

Lerner M, Samuni A, Razin E. Stimulation of murine cultured mast cells under anaerobic conditions: inhibition of arachidonic acid release. Immunology Letters [Internet]. 1987;16(2):121–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023522691&doi=10.1016%2f0165-2478%2887%2990118-0&partnerID=40&md5=02499179a77ef1a7763e8d948a960298

98.

Baranes D, Matzner J, Razin E. Thrombin-induced calcium-independent degranulation of human neutrophils. Inflammation [Internet]. 1986;10(4):455–61. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023026568&doi=10.1007%252fBF00915829&partnerID=40&md5=810c0ed0f8f205f06e89ea46826921d8

99.

Razin E, Baranes D. Thrombin-induced lysozyme release from human neutrophils and phosphatidylinositol breakdown in cultured mouse E mast cells. Advances in prostaglandin, thromboxane, and leukotriene research [Internet]. 1986;16:135–40. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022989421&partnerID=40&md5=85cc10729a755796d19536444777affc

100.

Baranes D, Liu FT, Razin E. Thrombin and IgE antigen induce formation of inositol phosphates by mouse E-mast cells. FEBS Letters [Internet]. 1986;206(1):64–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022999155&doi=10.1016%2f0014-5793%2886%2981341-2&partnerID=40&md5=b7ade9e08e746f44c5f1ad197c7a7892

101.

Shalit M, Shoam H, Seno N, Razin E. New role for heparan sulfate: Regulator of leukotriene generation in mouse E-mast cells. Life Sciences [Internet]. 1986;39(10):903–10. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022495526&doi=10.1016%2f0024-3205%2886%2990372-3&partnerID=40&md5=a0859b1f47b363d9147290a3ee80d39b

102.

Eliakim R, Gilead L, Ligumsky M, Okon E, Rachmilewitz D, Razin E. Histamine and chondroitin sulfate E proteoglycan released by cultured human cell colonic mucosa: Indication for possible presence of E mast cells. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1986;83(2):461–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346632585&doi=10.1073%252fpnas.83.2.461&partnerID=40&md5=df759d4e18f138cb6458f392248f3186

103.

Baranes D, Liu FT, Marx G, Shalit M, Razin E. Regulation of thrombin-induced mast cell degranulation by zinc and manganese. Immunology Letters [Internet]. 1986;12(2–3):95–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022460520&doi=10.1016%2f0165-2478%2886%2990089-1&partnerID=40&md5=6ee0d8c73473f0e553830270e07c7483

104.

Pervin R, Kanner BI, Marx G, Razin E. Thrombin-induced degranulation of cultured bone marrow-derived mast cells: Effect on calcium uptake. Immunology [Internet]. 1985;56(4):667–72. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022354653&partnerID=40&md5=480ca77c5f5c2721888dbd659789c26b

105.

Shoam H, Razin E. BW755C inhibits the 5-lipoxygenase in E-mast cells without affecting degranulation. Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism [Internet]. 1985;837(1):1–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021998483&doi=10.1016%2f0005-2760%2885%2990078-5&partnerID=40&md5=9183b23052df83ceeb7a59451b0dcd05

106.

Razin E, Baranes D, Marx G. Thrombin-Mast cell interactions. Binding and cell activation. Experimental Cell Research [Internet]. 1985;160(2):380–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022205330&doi=10.1016%2f0014-4827%2885%2990184-3&partnerID=40&md5=cc567b7479e11c9dbea372fbfd7ce9aa

107.

Marx G, Barnes D, Razin E. Thrombin selective activation of mast cells. Federation Proceedings [Internet]. 1985;44(4):No. 5340. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021988265&partnerID=40&md5=c46a573431cee04db58dc35cb44fdf4d

108.

Razin E. Activation of the 5-lipoxygenase pathway in E-mast cells by peanut agglutinin. Journal of Immunology [Internet]. 1985;134(2):1142–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021908551&partnerID=40&md5=339f02fea59e731e2a8ad9c17cadcbe9

109.

Stevens RL, Bloes WF, Seldin DC, Razin E, Katz HR, Austen KF. Inhibition of proliferation of mouse T cell-dependent bone marrow-derived mast cells by rat serum does not change their unique phenotype. Journal of Immunology [Internet]. 1984;133(5):2674–80. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021747945&partnerID=40&md5=871e1d15d87cf42fa1e291740f4005b0

110.

Razin E, Marx G. Thrombin-induced degranulation of cultured bone marrow-derived mast cells. Journal of Immunology [Internet]. 1984;133(6):3282–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021745338&partnerID=40&md5=2929be23f8cb9ff69af00441802dca91

111.

Razin E, Romeo LC, Krilis S, Liu FT, Lewis RA, Corey EJ, et al. An analysis of the relationship between 5-lipoxygenase product generation and the secretion of preformed mediators from mouse bone marrow-derived mast cells. Journal of Immunology [Internet]. 1984;133(2):938–45. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021238253&partnerID=40&md5=965f6bee7e81e457cb73dd52c625c5d1

112.

Razin E, Stevens RL, Austen KF, Caulfield JP, Hein A, Liu FT, et al. Cloned mouse mast cells derived from immunized lymph node cells and from foetal liver cells exhibit characteristics of bone marrow-derived mast cells containing chondroitin sulphate E proteoglycan. Immunology [Internet]. 1984;52(3):563–75. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021269564&partnerID=40&md5=b220b91fd98e8031c08558813489797d

113.

Razin E, Ihle JN, Seldin D, Mencia-Huerta JM, Katz HR, LeBlanc PA, et al. Interleukin 3: A differentiation and growth factor for the mouse mast cell that contains chondroitin sulfate E proteoglycan. Journal of Immunology [Internet]. 1984;132(3):1479–86. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021350731&partnerID=40&md5=50926ee9f37a361113fa3d07897aa523

114.

Razin E, Lewis RA, Corey EJ, Austen KF. Separation of 5-lipoxygenase product generation and secretion of preformed mediators from mouse bone marrow-derived mast cells (BMMC). Federation Proceedings [Internet]. 1984;43(6):no. 1452. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021262931&partnerID=40&md5=41488ff3a1c7e1af90dc262172e0836c

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Razin E, Cordon-Cardo C, Good RA. Growth of a pure population of mouse mast cells in vitro with conditioned medium derived from concanavalin A-stimulated splenocytes. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1981;78(4 II):2559–61. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019403943&doi=10.1073%252fpnas.78.4.2559&partnerID=40&md5=bff89d21bc40a2cac68868f9f09f3675