Last updated September 2023 - School of Public Health
1.
Bulvik BE, Berenshtein E, Meyron-Holtz EG, Konijn AM, Chevion M. Cardiac Protection by Preconditioning Is Generated via an Iron-Signal Created by Proteasomal Degradation of Iron Proteins. PLoS ONE [Internet]. 2012;7(11). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84869098514&doi=10.1371%252fjournal.pone.0048947&partnerID=40&md5=1fbf986c0dbf9d3bc045b2288ac46078
2.
Bulvik BE, Berenshtein E, Konijn AM, Grinberg L, Vinokur V, Eliashar R, et al. Aging is an organ-specific process: Changes in homeostasis of iron and redox proteins in the rat. Age [Internet]. 2012;34(3):693–704. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84863713330&doi=10.1007%252fs11357-011-9268-7&partnerID=40&md5=31750e79dd424af9709090e472b7a246
3.
Chevion M, Leibowitz S, Aye NN, Novogrodsky O, Singer A, Avizemer O, et al. Heart protection by ischemic preconditioning: A novel pathway initiated by iron and mediated by ferritin. Journal of Molecular and Cellular Cardiology [Internet]. 2008;45(6):839–45. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-55649092852&doi=10.1016%252fj.yjmcc.2008.08.011&partnerID=40&md5=6cac435b42eb6e01d9cd12babfaf2207
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Obolensky A, Berenshtein E, Konijn AM, Banin E, Chevion M. Ischemic preconditioning of the rat retina: Protective role of ferritin. Free Radical Biology and Medicine [Internet]. 2008;44(7):1286–94. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-40949118141&doi=10.1016%252fj.freeradbiomed.2007.10.060&partnerID=40&md5=54d5216e3a01bb2fb36bfa2b2b190a9c
5.
Leimberg MJ, Prus E, Konijn AM, Fibach E. Macrophages function as a ferritin iron source for cultured human erythroid precursors. Journal of Cellular Biochemistry [Internet]. 2008;103(4):1211–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-40349103525&doi=10.1002%252fjcb.21499&partnerID=40&md5=82141ba41e86447f9a8a3a80fe240daf
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Leimberg JM, Prus E, Link G, Fibach E, Konijn AM. Iron-chelator complexes as iron sources for early developing human erythroid precursors. Translational Research [Internet]. 2008;151(2):88–96. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-38049017900&doi=10.1016%252fj.trsl.2007.12.002&partnerID=40&md5=98fe4b717b56abfc4f0b8a4ca95c1962
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Glickstein H, El RB, Link G, Breuer W, Konijn AM, Hershko C, et al. Action of chelators in iron-loaded cardiac cells: Accessibility to intracellular labile iron and functional consequences. Blood [Internet]. 2006;108(9):3195–203. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33750001927&doi=10.1182%252fblood-2006-05-020867&partnerID=40&md5=0344674a7b18118b516d5a2eea265275
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Hershko C, Link G, Konijn AM, Cabantchik ZI. Iron overload and chelation. Hematology [Internet]. 2005;10(SUPPL. 1):171–3. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-29244443379&doi=10.1080%252f10245330512331390294&partnerID=40&md5=e51d38f6e744be08f184dc8f540f11e5
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Leimberg JM, Konijn AM, Fibach E. Macrophages promote development of human erythroid precursors in transferrin-free culture medium. Hematology [Internet]. 2005;10(1):73–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-23244439589&doi=10.1080%252f10245330412331269876&partnerID=40&md5=e672b20a9daf340da5dbf9aafc71ac87
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Hershko C, Link G, Konijn AM, Cabantchik ZI. Objectives and mechanism of iron chelation therapy. Annals of the New York Academy of Sciences [Internet]. 2005;1054:124–35. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-29744458330&doi=10.1196%252fannals.1345.015&partnerID=40&md5=790ba93bbf73148d54346594ba7015f5
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Hershko CM, Link GM, Konijn AM, Cabantchik ZI. Iron chelation therapy. Current hematology reports [Internet]. 2005;4(2):110–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-24944457520&partnerID=40&md5=b33040d6f43972b7199ac1404faff33d
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Hershko C, Link G, Konijn AM. Cardioprotective effect of iron chelators. Advances in Experimental Medicine and Biology [Internet]. 2003;509:77–89. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042309616&partnerID=40&md5=74c74ef1fa776d85c89ef8402da04c4c
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Leimberg JM, Konijn AM, Fibach E. Developing human erythroid cells grown in transferrin-free medium utilize iron originating from extracellular ferritin. American Journal of Hematology [Internet]. 2003;73(3):211–2. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037969721&doi=10.1002%252fajh.10355&partnerID=40&md5=421e2d2a969131c9b6940082b020c790
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Link G, Ponka P, Konijn AM, Breuer W, Cabantchik ZI, Hershko C. Effects of combined chelation treatment with pyridoxal isonicotinoyl hydrazone analogs and deferoxamine in hypertransfused rats and in iron-loaded rat heart cells. Blood [Internet]. 2003;101(10):4172–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038603210&doi=10.1182%252fblood-2002-08-2382&partnerID=40&md5=92669db5bb05c67a1ff3c02a8d1c8b85
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Hershko C, Abrahamov A, Konijn AM, Breuer W, Cabantchik IZ, Pootrakul P, et al. Objectives and methods of iron chelation therapy. Bioinorganic Chemistry and Applications [Internet]. 2003;1(2):151–68. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-29844436963&doi=10.1155%252fS1565363303000128&partnerID=40&md5=739a5ea9bb7bb96a6b3ee19fc448603d
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Hirsh M, Konijn AM, Iancu TC. Acquisition, storage and release of iron by cultured human hepatoma cells. Journal of Hepatology [Internet]. 2002;36(1):30–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036129599&doi=10.1016%2fS0168-8278%2801%2900221-5&partnerID=40&md5=12f281971551c76222959cb8885ab517
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Berenshtein E, Vaisman B, Goldberg-Langerman C, Kitrossky N, Konijn AM, Chevion M. Roles of ferritin and iron in ischemic preconditioning of the heart. Molecular and Cellular Biochemistry [Internet]. 2002;234–235:283–92. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-4243248915&doi=10.1023%252fA%253a1015923202082&partnerID=40&md5=06be5096b7646f82e1fd54b8cb9380ea
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Zanninelli G, Loréal O, Brissot P, Konijn AM, Slotki IN, Hider RC, et al. The labile iron pool of hepatocytes in chronic and acute iron overload and chelator-induced iron deprivation. Journal of Hepatology [Internet]. 2002;36(1):39–46. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036128705&doi=10.1016%2fS0168-8278%2801%2900222-7&partnerID=40&md5=873e34cf9d0e3138097b62b84f5392f9
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Hershko C, Link G, Konijn AM, Huerta M, Rosenmann E, Reinus C. The iron-loaded gerbil model revisited: Effects of deferoxamine and deferiprone treatment. Journal of Laboratory and Clinical Medicine [Internet]. 2002;139(1):50–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036008996&doi=10.1067%252fmlc.2002.120364&partnerID=40&md5=5cfebf416406c200cbcfd9fd4b5e9869
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Seligmann H, Levi R, Konijn AM, Prokocimer M. Thiamine deficiency in patients with B-chronic lymphocytic leukaemia: A pilot study. Postgraduate Medical Journal [Internet]. 2001;77(911):582–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034845980&doi=10.1136%252fpmj.77.911.582&partnerID=40&md5=fb842d960ca0aee248b4fd27eb3f5799
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Hershko C, Konijn AM, Nick HP, Breuer W, Cabantchik ZI, Link G. ICL670A: A new synthetic oral chelator: Evaluation in hypertransfused rats with selective radioiron probes of hepatocellular and reticuloendothelial iron stores and in iron-loaded rat heart cells in culture. Blood [Internet]. 2001;97(4):1115–22. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035865702&doi=10.1182%252fblood.V97.4.1115&partnerID=40&md5=71bd1e3447a647da4bc36d09d5ff7495
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Link G, Konijn AM, Breuer W, Cabantchik ZI, Hershko C. Exploring the “iron shuttle” hypothesis in chelation therapy: Effects of combined deferoxamine and deferiprone treatment in hypertransfused rats with labeled iron stores and in iron-loaded rat heart cells in culture. Journal of Laboratory and Clinical Medicine [Internet]. 2001;138(2):130–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034928342&doi=10.1067%252fmlc.2001.116487&partnerID=40&md5=19560949c09b42c800f2f2ee340ab2f9
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El-Sharif N, Fischbein A, Konijn A, Gorodetsky R, El-Sharif H, Kaul B, et al. Re-emergence of lead poisoning from contaminated flour in a West Bank Palestinian village. International Journal of Occupational and Environmental Health [Internet]. 2000;6(3):183–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033846122&doi=10.1179%252foeh.2000.6.3.183&partnerID=40&md5=bcaec28b0294ad2e0a0d9a97a80b6f67
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Vaisman B, Meyron-Holtz EG, Fibach E, Krichevsky AM, Konijn AM. Ferritin expression in maturing normal human erythroid precursors. British Journal of Haematology [Internet]. 2000;110(2):394–401. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033840851&doi=10.1046%252fj.1365-2141.2000.02167.x&partnerID=40&md5=58ccff2fdc358e681b9f16f1aa2df5bb
25.
Meyron-Holtz EG, Vaisman B, Cabantchik ZI, Fibach E, Rouault TA, Hershko C, et al. Regulation of intracellular iron metabolism in human erythroid precursors by internalized extracellular ferritin. Blood [Internet]. 1999;94(9):3205–11. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033229699&doi=10.1182%252fblood.v94.9.3205.421k25_3205_3211&partnerID=40&md5=92573546cc6710f617d0097b4131e749
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Konijn AM, Glickstein H, Vaisman B, Meyron-Holtz EG, Slotki IN, Cabantchik ZI. The cellular labile iron pool and intracellular ferritin in K562 cells. Blood [Internet]. 1999;94(6):2128–34. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033568553&doi=10.1182%252fblood.v94.6.2128&partnerID=40&md5=7c91d2213ebcaab97896de984cb045a2
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Pountney DJ, Konijn AM, McKie AT, Peters TJ, Raja KB, Salisbury JR, et al. Iron proteins of duodenal enterocytes isolated from mice with genetically and experimentally altered iron metabolism. British Journal of Haematology [Internet]. 1999;105(4):1066–73. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033033374&doi=10.1046%252fj.1365-2141.1999.01441.x&partnerID=40&md5=ad12275ba2faffd079e6d5b5f3d72521
28.
Vaisman B, Konijn AM, Fibach E. Isolation of large and pure samples of human erythroid precursors at different stages of maturation using immunomagnetic separation of cells from liquid cultures. Acta Haematologica [Internet]. 1999;101(3):135–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032980169&doi=10.1159%252f000040939&partnerID=40&md5=d74250e794deb0225236306d2a5ee68f
29.
Link G, Konijn AM, Hershko C. Cardioprotective effect of α-tocopherol, ascorbate, deferoxamine, and deferiprone: Mitochondrial function in cultured, iron-loaded heart cells. Journal of Laboratory and Clinical Medicine [Internet]. 1999;133(2):179–88. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033082143&doi=10.1016%2fS0022-2143%2899%2990011-2&partnerID=40&md5=7cffb196a8c5081910a83acc5b7e7ce4
30.
Vaisman B, Santambrogio P, Arosio P, Fibach E, Konijn AM. An ELISA for the H-subunit of human ferritin which employs a combination of rabbit poly- and mice monoclonal antibodies and an enzyme labeled anti-mouse-IgG. Clinical Chemistry and Laboratory Medicine [Internet]. 1999;37(2):121–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032991343&doi=10.1515%252fCCLM.1999.022&partnerID=40&md5=d3636afe0dd9048e8f04cb2a72388772
31.
Hershko C, Konijn AM, Link G. Iron chelators for thalassaemia. British Journal of Haematology [Internet]. 1998;101(3):399–406. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031859181&doi=10.1046%252fj.1365-2141.1998.00726.x&partnerID=40&md5=e82142ca1adc47506c4f8608f623c9a1
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Link G, Saada A, Pinson A, Konijn AM, Hershko C. Mitochondrial respiratory enzymes are a major target of iron toxicity in rat heart cells. Journal of Laboratory and Clinical Medicine [Internet]. 1998;131(5):466–74. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032078224&doi=10.1016%2fS0022-2143%2898%2990148-2&partnerID=40&md5=7bb5a2a2db0e22e1ea0c21cb584a69b1
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Vaisman B, Fibach E, Konijn AM. Utilization of intracellular ferritin iron for hemoglobin synthesis in developing human erythroid precursors. Blood [Internet]. 1997;90(2):831–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030854921&doi=10.1182%252fblood.v90.2.831.831_831_838&partnerID=40&md5=56e7ce52315e05b3a6bd6de5cde048e8
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Zanninelli G, Glickstein H, Breuer W, Milgram P, Brissot P, Hider RC, et al. Chelation and mobilization of cellular iron by different classes of chelators. Molecular Pharmacology [Internet]. 1997;51(5):842–52. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-18344410299&doi=10.1124%252fmol.51.5.842&partnerID=40&md5=a5d1050b6ed2863e2a93f3c552efa7b2
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Ponka P, Richardson DR, Konijn AM, Gelvan D, Meyron-Holtz E, Fibach E. Can ferritin provide iron for hemoglobin synthesis? [2]. Blood [Internet]. 1997;89(7):2611–3. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030895693&doi=10.1182%252fblood.v89.7.2611&partnerID=40&md5=766eda120f62346cbdb00a3aceb8c18c
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Gelvan D, Fibach E, Meyron-Holtz EG, Konijn AM. Ferritin uptake by human erythroid precursors is a regulated iron uptake pathway. Blood [Internet]. 1996;88(8):3200–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029919416&doi=10.1182%252fblood.v88.8.3200.bloodjournal8883200&partnerID=40&md5=82573cb8e92b31b357f0be0b7ffbf751
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Glickstein H, Breuer W, Loyevsky M, Konijn AM, Libman J, Shanzer A, et al. Differential cytotoxicity of iron chelators on malaria-infected cells versus mammalian cells. Blood [Internet]. 1996;87(11):4871–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029945314&doi=10.1182%252fblood.v87.11.4871.bloodjournal87114871&partnerID=40&md5=6ff0f5c1e1ad9d83c68e9c0999e451d1
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Treffry A, Gelvan D, Konijn AM, Harrison PM. Ferritin does not accumulate iron oxidized by caeruloplasmin. Biochemical Journal [Internet]. 1995;305(1):21–3. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028814418&doi=10.1042%252fbj3050021&partnerID=40&md5=d396907e49b46f5cdfe18d0386999a22
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Konijn AM. 5 Iron metabolism in inflammation. Bailliere’s Clinical Haematology [Internet]. 1994;7(4):829–49. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028609224&doi=10.1016%2fS0950-3536%2805%2980127-1&partnerID=40&md5=ca216029c71da40fa32883201453c8b2
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Meyron-Holtz EG, Fibach E, Gelvan D, Konijn AM. Binding and uptake of exogenous isoferritins by cultured human erythroid precursor cells. British Journal of Haematology [Internet]. 1994;86(3):635–41. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028341609&doi=10.1111%252fj.1365-2141.1994.tb04797.x&partnerID=40&md5=85ee5ca0d1eec4e4b7210defe47d3115
41.
Hershko C, Konijn AM, Aisen P. Progress in iron research: Preface. Advances in Experimental Medicine and Biology [Internet]. 1994;356. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028007231&partnerID=40&md5=6988e4820574a9734424a1d50b940356
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Konijn AM, Meyron-Holtz EG, Fibach E, Gelvan D. Cellular ferritin uptake: A highly regulated pathway for iron assimilation in human erythroid precursor cells. Advances in Experimental Medicine and Biology [Internet]. 1994;356:189–97. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028000035&doi=10.1007%252f978-1-4615-2554-7_21&partnerID=40&md5=8baefd39da41c79be059dc19c42ffe81
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Simpson RJ, Konijn AM, Lombard M, Raja KB, Salisbury JR, Peters TJ. Tissue iron loading and histopathological changes in hypotransferrinaemic mice. The Journal of Pathology [Internet]. 1993;171(3):237–44. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027436546&doi=10.1002%252fpath.1711710313&partnerID=40&md5=08a551a65a125d28a9f4e7a75480aaf1
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Simpson RJ, Cooper CE, Raja KB, Halliwell B, Evans PJ, Arouma OI, et al. Non-transferrin-bound iron species in the serum of hypotransferrinaemic mice. BBA - General Subjects [Internet]. 1992;1156(1):19–26. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026678132&doi=10.1016%2f0304-4165%2892%2990090-H&partnerID=40&md5=70c330fa1e9aaff27be97f844d30201f
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Konijn AM, Kaplan R, Or R, Matzner Y. Glycosylated serum ferritin in patients with hematological malignancies before and after bone marrow transplantation. Leukemia and Lymphoma [Internet]. 1992;7(1–2):151–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026694214&doi=10.3109%252f10428199209053616&partnerID=40&md5=128f9b991c56ec6e8df1c7d417b5055a
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Bauminger ER, Fibach E, Konijn AM, Ofer S, Rachmilewitz EA. Mössbauer studies of iron uptake, ferritin and hemoglobin synthesis and denaturation in erythroid cell cultures. Hyperfine Interactions [Internet]. 1991;66(1–4):11–23. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0011237732&doi=10.1007%252fBF02395852&partnerID=40&md5=61884d014d906ce14d12d84712b18466
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Konijn AM, Meyron-Holtz EG, Levy R, Ben-Bassat H, Matzner Y. Specific binding of placental acidic isoferritin to cells of the T-cell line HD-MAR. FEBS Letters [Internet]. 1990;263(2):229–32. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025312109&doi=10.1016%2f0014-5793%2890%2981380-7&partnerID=40&md5=0feec8281316cd7504a9eb300894e391
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Yinnon A, Konijn AM, Link G, Moreb J, Hershko C. Diagnostic value of ferritin in malignant pleural and peritoneal effusions. Cancer [Internet]. 1988;62(12):2564–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024208086&doi=10.1002%2f1097-0142%2819881215%2962%3a12%3c2564%3a%3aAID-CNCR2820621219%3e3.0.CO%3b2-Q&partnerID=40&md5=2b7033cbccbec4eb09309ec37b72cbf5
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Holtz EG, Konijn AM. Stability of ferritin following solid-state enzymatic radioiodination. Clinica Chimica Acta [Internet]. 1988;178(1):113–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024118808&doi=10.1016%2f0009-8981%2888%2990277-X&partnerID=40&md5=b475b13a82dba32e1d91a19d1047ca68
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Arad I, Konijn AM, Linder N, Goldstein M, Kaufmann NA. Serum Ferritin Levels in Preterm Infants after Multiple Blood Transfusions. American Journal of Perinatology [Internet]. 1988;5(1):40–3. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023818673&doi=10.1055%252fs-2007-999651&partnerID=40&md5=1c9df8aad557abc3cde5dfb946422667
51.
Or R, Matzner Y, Konijn AM. Serum ferritin in patients undergoing bone marrow transplantation. Cancer [Internet]. 1987;60(5):1127–31. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023639526&doi=10.1002%2f1097-0142%2819870901%2960%3a5%3c1127%3a%3aAID-CNCR2820600535%3e3.0.CO%3b2-A&partnerID=40&md5=671e7118c128263666f1993741d25e70
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Fibach E, Konijn AM, Bauminger RE, Ofer S, Rachmilewitz EA. Effect of extracellular hemin on hemoglobin and ferritin content of erythroleukemia cells. Journal of Cellular Physiology [Internet]. 1987;130(3):460–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023099707&doi=10.1002%252fjcp.1041300321&partnerID=40&md5=3e2e4a1101abe57ffc2dc637d9a00922
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Zandman‐Goddard G, Matzner Y, Konijn AM, Hershko C. Cerebrospinal fluid ferritin in malignant CNS involvement. Cancer [Internet]. 1986;58(6):1346–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022525081&doi=10.1002%2f1097-0142%2819860915%2958%3a6%3c1346%3a%3aAID-CNCR2820580627%3e3.0.CO%3b2-W&partnerID=40&md5=88785ee92c95e8915bcd1f61d1cc69de
54.
Konijn AM, Tal R, Levy R, Matzner Y. Isolation and fractionation of ferritin from human term placenta-A source for human isoferritins. Analytical Biochemistry [Internet]. 1985;144(2):423–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021985474&doi=10.1016%2f0003-2697%2885%2990135-6&partnerID=40&md5=fda804e3599caab00ec15604ea4fe466
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Hershko C, Konijn AM, Link G, Moreb J, Grauer F, Weissenberg E. Combined use of zinc protoporphyrin (ZPP), mean corpuscular volume and haemoglobin measurements for classifying microcytic RBC disorders in children and young adults. Clinical & Laboratory Haematology [Internet]. 1985;7(3):259–69. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022353938&doi=10.1111%252fj.1365-2257.1985.tb00034.x&partnerID=40&md5=4c450eb4d110b6a73d6f4a8e69a2b0d2
56.
Matzner Y, Konijn AM, Shlomai Z, Ben‐Bassat H. Differential effect of isolated placental isoferritins on in vitro T‐lymphocyte function. British Journal of Haematology [Internet]. 1985;59(3):443–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021996239&doi=10.1111%252fj.1365-2141.1985.tb07331.x&partnerID=40&md5=3078e567f4be6eeae369da7d36b75a94
57.
Fibach E, Konijn AM, Rachmilewitz EA. Changes in cellular ferritin content during myeloid differentiation of human leukemic cell lines. American Journal of Hematology [Internet]. 1985;18(2):143–51. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021956005&doi=10.1002%252fajh.2830180205&partnerID=40&md5=4430fd9617e81151b119cdb350acbbe3
58.
Hershko C, Konijn AM, Moreb J, Link G, Grauer F, Weissenberg E. Iron depletion and blood lead levels in a population with endemic lead poisoning. Israel Journal of Medical Sciences [Internet]. 1984;20(11):1039–43. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021744322&partnerID=40&md5=1d7e1c7d1c927cdf52a9a2687efe54e3
59.
Treves AJ, Fuks Z, Voss R, Tal T, Barak V, Konijn AM, et al. Establishment of cell lines from somatic cell hybrids between human monocytes and mouse myeloma cells. Journal of Immunology [Internet]. 1984;132(2):690–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021357366&partnerID=40&md5=7880efbedc66cd7b50e1f8458315e475
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Hershko C, Abrahamov A, Moreb J, Hersh M, Shiffman R, Shahin A, et al. Lead Poisoning in a West Bank Arab Village. Archives of Internal Medicine [Internet]. 1984;144(10):1969–73. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84948722050&doi=10.1001%252farchinte.1984.04400010077015&partnerID=40&md5=3f4d85b0d2ff48650e27144d6e5886a9
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Hershko C, Yaffe Y, Richter ED, Konijn AM, Abrahamov A, Hersh M, et al. Lead poisoning. Harefuah [Internet]. 1983;105(10):303-306+348. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021045503&partnerID=40&md5=1d4c33cac7c3a143d018ba00dfae3956
62.
KAEMPFER R, KONIJN AM. Translational Competition by mRNA Species Encoding Albumin, Ferritin, Haemopexin and Globin. European Journal of Biochemistry [Internet]. 1983;131(3):545–50. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021095323&doi=10.1111%252fj.1432-1033.1983.tb07296.x&partnerID=40&md5=94882dee3423854e42ad90f337e12c92
63.
Fibach E, Bauminger ER, Konijn AM, Ofer S, Rachmilewitz EA. Iron storage in ferritin following intracellular hemoglobin denaturation in erythroleukemic cells. Blood [Internet]. 1983;62(4):928–30. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020636009&doi=10.1182%252fblood.v62.4.928.bloodjournal624928&partnerID=40&md5=7a5efdc7bdade7317b83721d74b454ea
64.
Moreb J, Popovtzer MM, Friedlaender MM, Konijn AM, Hershko C. Evaluation of iron status in patients on chronic hemodialysis: Relative usefulness of bone marrow hemosiderin, serum ferritin, transferrin saturation, mean corpuscular volume and red cell protoporphyrin. Nephron [Internet]. 1983;35(3):196–200. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020608604&doi=10.1159%252f000183074&partnerID=40&md5=bab779e180a3b1b5bfeabf18ca2feb7b
65.
Konijn AM, Levy R, Link G, Hershko C. A rapid and sensitive ELISA for serum ferritin employing a fluorogenic substrate. Journal of Immunological Methods [Internet]. 1982;54(3):297–307. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019994281&doi=10.1016%2f0022-1759%2882%2990314-3&partnerID=40&md5=d18e1672fffcc8edf7e327b53f3595d1
66.
Hershko C, Moreb J, Gaziel Y, Konijn AM, Rachmilewitz EA. Reduced Frequency of Iron Deficiency Anaemia in Sickle Cell Trait. Scandinavian Journal of Haematology [Internet]. 1982;29(4):304–10. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019949810&doi=10.1111%252fj.1600-0609.1982.tb00599.x&partnerID=40&md5=79d9394dd13142cfcab0aca3f6a2c438
67.
Hershko C, Bar-Or D, Gaziel Y, Naparstek E, Konijn AM, Grossowicz N, et al. Diagnosis of iron deficiency anemia in a rural population of children. Relative usefulness of serum ferritin, red cell protoporphyrin, red cell indices, and transferrin saturation determinations. American Journal of Clinical Nutrition [Internet]. 1981;34(8):1600–10. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019779274&doi=10.1093%252fajcn%252f34.8.1600&partnerID=40&md5=0a34824632aa52bd9e53acef16f49ba0
68.
Konijn AM, Carmel N, Levy R, Hershko C. Ferritin Synthesis in Inflammation: II. MECHANISM OF INCREASED FERRITIN SYNTHESIS. British Journal of Haematology [Internet]. 1981;49(3):361–70. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019439290&doi=10.1111%252fj.1365-2141.1981.tb07238.x&partnerID=40&md5=9584c8d6e64502e088d1e48952f20ffd
69.
Hershko C, Gaziel Y, Bar-Or D, Izak G, Naparstek E, Grossowicz N, et al. Anemia among Druze children in the Golan Heights. Israel Journal of Medical Sciences [Internet]. 1980;16(5):384–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018889514&partnerID=40&md5=e4b3a9f300d10a028e5669ec7e61ca83
70.
Alayoff A, Kapitulnik J, Konijn A, Kaufmann NA, Blondheim SH. Bilirubin binding capacity of albumin isolated from cord-blood serum is less than that from serum of adults. Clinical Chemistry [Internet]. 1980;26(6):738–40. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019311038&doi=10.1093%252fclinchem%252f26.6.0738&partnerID=40&md5=35ae229504778f1574d2cb8944e294ee
71.
Matzner Y, Konijn AM, Hershko C. Serum ferritin in hematologic malignancies. American Journal of Hematology [Internet]. 1980;9(1):13–22. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018946532&doi=10.1002%252fajh.2830090103&partnerID=40&md5=a8812066aa4a04796196b32e6f36c41f
72.
Matzner Y, Hershko C, Polliack A, Konijn AM, Izak G. Suppressive Effect of Ferritin on in Vitro Lymphocyte Function. British Journal of Haematology [Internet]. 1979;42(3):345–53. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018755795&doi=10.1111%252fj.1365-2141.1979.tb01142.x&partnerID=40&md5=16fc67cd7e228c619db994502821128b
73.
Loria A, Hershko C, Konijn AM. Serum ferritin in an elderly population. Journals of Gerontology [Internet]. 1979;34(4):521–4. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018749604&doi=10.1093%252fgeronj%252f34.4.521&partnerID=40&md5=a67be6c11949c020b1a956ac9790645b
74.
Hershko C, Konijn AM, Loria A. Serum ferritin and mean corpuscular volume measurement in the diagnosis of β-thalassaemia minor and iron deficiency. Acta Haematologica [Internet]. 1979;62(4):236–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018577218&doi=10.1159%252f000207578&partnerID=40&md5=b80dece1a7366013cfb0aa952e2ac2c8
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Konijn AM, Hershko C, Izak G. Ferritin synthesis and Iron uptake in developing erythroid cells. American Journal of Hematology [Internet]. 1979;6(4):373–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018570807&doi=10.1002%252fajh.2830060409&partnerID=40&md5=739b76cf43c84d33f657f7a0a0e93bf2
76.
Loria A, Konijn AM, Hershko C. Serum ferritin in β-thalassemia trait. Israel Journal of Medical Sciences [Internet]. 1978;14(11):1127–31. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018257813&partnerID=40&md5=ef113c62ec9bc3c0db8157aa0b0c99a0
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Konijn AM, Hershko C, Izak G. Ferritin synthesis in developing erythroid precursor cells. Israel Journal of Medical Sciences [Internet]. 1978;14(11):1181–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018224513&partnerID=40&md5=98ca1e2837cb9b815425e39e746896b5
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Carmel N, Konijn AM. Quantitative determination of ferritin by electroimmunoassay. Analytical Biochemistry [Internet]. 1978;85(2):499–505. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018199923&doi=10.1016%2f0003-2697%2878%2990247-6&partnerID=40&md5=4bf7f58a7d8a9314dd322ddea5c0ed4b
79.
Konijn AM, Hershko C. Ferritin Synthesis in Inflammation: I. PATHOGENESIS OF IMPAIRED IRON RELEASE. British Journal of Haematology [Internet]. 1977;37(1):7–16. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017703490&doi=10.1111%252fj.1365-2141.1977.tb08806.x&partnerID=40&md5=a5f1a6e2ec31725419267c3f3c984770
80.
Seban A, Konijn AM, Freier S. Chemical and immunological properties of a protein hydrolysate formula. American Journal of Clinical Nutrition [Internet]. 1977;30(6):840–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017398660&doi=10.1093%252fajcn%252f30.6.840&partnerID=40&md5=a082705e93b10727f600c0ad4558084b
81.
Konijn AM, Carmel N, Kaufmann NA. The redox state and the concentration of ketone bodies in tissues of rats fed carbohydrate free diets. Journal of Nutrition [Internet]. 1976;106(10):1507–14. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017097050&doi=10.1093%252fjn%252f106.10.1507&partnerID=40&md5=63fa9e3e3c560c7f7988be099ebdfae1
82.
Carmel N, Konijn AM, Kaufmann NA, Guggenheim K. Effects of carbohydrate free diets on the insulin carbohydrate relationships in rats. Journal of Nutrition [Internet]. 1975;105(9):1141–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0016747476&doi=10.1093%252fjn%252f105.9.1141&partnerID=40&md5=d5ec4f062d20e0ebb9e5e8316da222e1
83.
Konijn AM, Baliga BS, Munro HN. Synthesis of liver ferritin on free and membrane-bound polyribosomes of different sizes. FEBS Letters [Internet]. 1973;37(2):249–52. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015730130&doi=10.1016%2f0014-5793%2873%2980471-5&partnerID=40&md5=2b00d06a11cea2613e48348362638dfc
84.
Konijn AM, Guggenheim K. Characterization and mode of action of a goitrogen present in soya beans. Federation Proceedings [Internet]. 1973;32(3 (I)):28. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015874960&partnerID=40&md5=1fe8054aa8fe7f315641c2e0651bef32
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Konijn AM, Gershon B, Guggenheim K. Further purification and mode of action of a goitrogenic material from soybean flour. The Journal of nutrition [Internet]. 1973;103(3):378–83. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015594687&doi=10.1093%252fjn%252f103.3.378&partnerID=40&md5=75e27a1c480e69a0db33dcb56703679d
86.
Konijn AM, Eyal Z, Birnbaum D, Guggenheim K. Amylase secretion by rat pancreas following prolonged stimulation by unheated soybean flour. Digestion [Internet]. 1972;6(6):330–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015450086&doi=10.1159%252f000197251&partnerID=40&md5=982852ee271e1f198ffd85255ed99553
87.
Konijn AM, Edelstein S, Guggenheim K. Separation of a thyroid‐active fraction from unheated soya bean flour. Journal of the Science of Food and Agriculture [Internet]. 1972;23(5):549–55. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015344219&doi=10.1002%252fjsfa.2740230502&partnerID=40&md5=1f18743e251e288761a08572a5325de1
88.
Applebaum SW, Konijn AM, Menco B. Growth and biochemical adaptation of larvae of the beetle Dermestes maculatus to carbohydrate-free diets. Insect Biochemistry [Internet]. 1971;1(1):1–13. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-49649158385&doi=10.1016%2f0020-1790%2871%2990016-3&partnerID=40&md5=3a08cd957ea01f734c36a4f8cbc9d2dc
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Konijn AM, Muogbo DN, Guggenheim K. Metabolic effects of carbohydrate-free diets. Israel Journal of Medical Sciences [Internet]. 1970;6(4):498–505. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0014824755&partnerID=40&md5=11c04f6007ebd0e58516ed83880b1a5c
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Konijn AM, Guggenheim K. Effect of penicillin on growth and pancreatic amylase levels of rats fed soybean diets. Experientia [Internet]. 1970;26(7):727. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0014714777&doi=10.1007%252fBF02232508&partnerID=40&md5=77ba7cbca55ab7c2d160aca7d37070c6
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Konijn AM, Birk Y, Guggenheim K. In vitro synthesis of pancreatic enzymes: effect of soybean trypsin inhibitor. The American journal of physiology [Internet]. 1970;218(4):1113–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0014766151&doi=10.1152%252fajplegacy.1970.218.4.1113&partnerID=40&md5=7deb3c23e2aec957c4996ac9069acec6
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Konijn AM, Biek Y, Guggenheim K. Pancreatic enzyme pattern in rats as affected by dietary soybean flour. The Journal of nutrition [Internet]. 1970;100(3):361–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0014753273&doi=10.1093%252fjn%252f100.3.361&partnerID=40&md5=6b4611508c2e7861c85ceca908eb5051
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Konijn AM, Guggenheim K, Birk Y. Amylase synthesis in pancreas of rats fed soybean flour. The Journal of nutrition [Internet]. 1969;97(2):265–70. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0014468057&doi=10.1093%252fjn%252f97.2.265&partnerID=40&md5=1e0104d5b3f1c5cc467dd57f677fbb04
94.
Konijn AM, Guggenheim K. Effect of Raw Soybean Flour on the Composition of Rat Pancreas. Proceedings of the Society for Experimental Biology and Medicine [Internet]. 1967;126(1):65–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84971129763&doi=10.3181%252f00379727-126-32368&partnerID=40&md5=703ccbf83058ed04828819541b616cb8
95.
Applebaum SW, Konijn AM. Factors affecting the development of Tribolium castaneum (Herbst) on wheat. Journal of Stored Products Research [Internet]. 1967;2(4):323–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0009355637&doi=10.1016%2f0022-474X%2867%2990078-1&partnerID=40&md5=8988a9bd77e43f2ce0b9908aa6765eb9
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Konijn AM, Guggenheim K. Effect of raw soybean flour on the composition of rat pancreas. Rivista di patologia nervosa e mentale [Internet]. 1966;87(4):65–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0013938908&partnerID=40&md5=275429dbb89628f105daa4fa932a009d
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Applebaum SW, Konijn AM. The presence of a Tribolium-protease inhibitor in wheat. Journal of Insect Physiology [Internet]. 1966;12(6):665–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0009327482&doi=10.1016%2f0022-1910%2866%2990112-0&partnerID=40&md5=d597fec28e338e480c772454e6058263
98.
Applebaum SW, Konijn AM. THE UTILIZATION OF STARCH BY LARVAE OF THE FLOUR BEETLE, TRIBOLIUM CASTANEUM. The Journal of nutrition [Internet]. 1965;85(3):275–82. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0000775780&doi=10.1093%252fjn%252f85.3.275&partnerID=40&md5=d38d42d30200c56e06af20ccba3322d5