Publications

REFEREED ARTICLES

  1. Schusdziarra, C., Blamowska, M., Azem, A. and Hell, K. (in press) Methylation-controlled J-protein MCJ acts in the import of proteins into human mitochondria (in press). Human Molecular Genetics.
  2. Vitlin Gruber, A., Nisemblat, S., Zizelski, G., Parnas, P., Dzikowski, R., Azem, A. and Weiss, W. (in press) P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli. Plos ONE.
  3. Parnas, A., Nisemblat, S., Weiss, C., Levy-Rimler, G., Pri-Or, A., Zor, T., Lund, P., Bross, P., Azem, A. (2102) Identification of Elements that Dictate the Specificity of Mitochondrial Hsp60 for its Co-chaperonin. Plos ONE. Plos ONE. 7 (12), e50318.
  4. Kuo, W.Y., Huang, C.H., Liu, A.C.., Cheng, C.P., Li, S.H., Chang, W.C., Weiss, C., Azem, A., Jinn, T.L. (in press) Chaperonin 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts. New Phytol.
  5. Iosefson, O., Sharon, S., Goloubinoff, P., Azem, A. (2012). Reactivation of protein aggregates by mortalin and Tid1-the human mitochondrial Hsp70 chaperone system. Cell Stress & Chaperones. 17, 57-66.
  6. Marom, M., Azem, A. and Mokranjac, D. (2011) Understanding the molecular mechanism of protein translocation across the mitochondrial inner membrane: Still a long way to go. Biochem. Biophys. Acta (Biomembranes). 1808, 990-1001.
  7. Marom, M.†, Dayan, D.†, Demishtein-Zohary, K., Mokranjac, D., Neupert, W. and Azem, A. (2011) Direct interaction of mitochondrial targeting presequences with purified components of the TIM23 complex. J. Biol. Chem. 286, 43809-15438.
  8. Vitlin, A., Weiss, C., Demishtein-Zohary, K. Rasouly, A., Levin, D., Pisanty-Farchi, O., Breiman, A., Azem, A. (2011) Chloroplast β chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro. Plant Mol. Biol. 77, 105-115.
  9. Sharkia, R., Azem, A., Kaiya, Q., Zelnik, N. Mahajnah, M. (2010) Mental Retardation and Consanguinity in a Selected Region of the Israeli Arab Community. Cent. Eur. J. Med. 5, 91-96.
  10. Iosefson, O. and Azem, A. (2010) Reconstitution of the mitochondrial Hsp70 (mortalin)-p53 interaction using purified proteins - Identification of additional interacting regions. FEBS Lett. 584, 1080-1084.
  11. Azem, A., Tsfadia, Y., Hajouj, O., Shaked, I. and Daniel, E. (2010) Cross-linking with bifunctional reagents and its application to the study of the molecular symmetry and the arrangement of subunits in hexameric protein oligomers. Biochim. Biophys. Acta. 1804, 768-780.
  12. Weiss, C., Bonshtien, A., Farchi-Pisanty, O. ,Vitlin, A. and Azem, A. (2009) Cpn20: Siamese twins of the chaperonin world. Plant Mol. Biol (reviewed). 69, 227-238.
  13. Marom, M., Safonov, R., Amram, S., Avneon, Y., Nachliel, E., Gutman, G, Zohary, K., Azem, A. and Tsfadia, Y. (2009). The Interaction of Tim44 C-terminal Domain with Negatively-Charged Phospholipids. Biochemistry. 48, 11185-95.
  14. Parnas, A., Nadler, M., Nisemblat, S., Horovitz, A., Mandel, H., and Azem, A. (2009) The MitCHAP-60 Disease is due to Entropic Destabilization of the Human Mitochondrial Hsp60 oligomer. J. Biol. Chem. 284, 28198-28203.
  15. Elsner, S., Simian, D., Iosefson, O, Marom, M and Azem, A. (2009) The Mitochondrial Protein Translocation Motor: Structural Conservation between the Human and Yeast Tim14/Pam18-Tim16/Pam16 co-Chaperones. Int. J. Mol. Sci. 10, 2041-53.
  16. Bonshtien, A., Parnas, A., Sharkia, R., Niv, A., Mizrahi, I., Azem, A. and Weiss, C. (2009) Differential effects of co-chaperonin homologs on cpn60 oligomers. Cell Stress & Chaperones. 14, 509-519.
  17. Mokranjac, D. Sichting, M., Popov-Čeleketić, D., Mapa, K., Hell, K., Gevorkyan-Airapetov, L., Zohary, K., Azem, A. and Neupert (2009) Role of Tim50 in the Transfer of Precursor Proteins from the Outer to the Inner Membrane of Mitochondria. Mol. Biol. Cell 20, 1400-1407.
  18. Gevorkyan-Airapetov, L. , Zohary, L., Popov-Čeleketić, D., Mapa, K., Hell, K., Neupert, W., Azem, A., and Mokranjac, D. (2009). Interaction of Tim23 with Tim50 is essential for protein translocation by the mitochondrial TIM23 complex. J. Biol. Chem. 284, 4865-4872.
  19. Sharkia, R., Zaid, M., Athamna, A., Cohen, D., Azem, A. and Zalan, A. (2008) The changing pattern of consanguinity in a selected region of the Israeli Arab community. Amer. J. of Hum. Biol. 20, 72-77.
  20. Slutsky-Leiderman, O., Marom, M., Iosefson, O., Levy, R., Maoz, S. and Azem, A. (2007) The interplay between components of the mitochondrial protein translocation motor studied using purified components. J. Biol. Chem. 282, 33935-33942.
  21. Choresh, O., Azem, A. and Loya, Y. (2007) Over expression of highly conserved mitochondrial 70-kDa heat shock protein in the sea anemone Anemonia viridis. J. Therm. Biol. 32, 367-373.
  22. Bonshtien, AL., Weiss, C., Vitlin, A., Niv, A., Lorimer, GH. and Azem, A. (2007) Significance of the N-terminal domain for the function of chloroplast chaperonin. J. Biol. Chem. 282, 4463-4469.
  23. Iosefson, O., Levy, R., Marom, M., Slutsky-Leiderman, O. Azem, A. (2007) The Pam18/Tim14-Pam16/Tim16 complex of the mitochondrial translocation motor: the formation of a stable complex from marginally stable proteins. Protein Science. 16, 316-322.
  24. Blanga-Kanfi, S., Amitsur, M., Azem, A. And Kaufmann, G. (2006) PrrC-anticodon nuclease: functional organization of a prototypical bacterial restriction RNase. Nucleic Acids Res. 34, 3209-3219.
  25. De Los Rios, P., Ben-Zvi, A., Slutsky, O., Azem, A., Goloubinoff, P. (2006) Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc. Natl. Acad. Sci. USA. 103, 6166-6171.
  26. Moro, F., Fernandez-Saiz, V., Slutsky, O., Azem, A., Muga, A. (2005) Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70. Role of the divergent C-terminal alpha-helical subdomain. FEBS J. 272, 3184-3196.
  27. Sichting, M., Mokranjac, D., Azem, A., Neupert, W. and Hell, K. (2005) Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1. EMBO J. 24, 1046-1056.
  28. Choresh, O., Loya, Y., Müller, W.E.G., Wiedenmann, J., Azem, A. (2004). The mitochondrial 60-kDa heat shock protein in marine invertebrates: biochemical purification and molecular characterization. Cell Stress & Chaperones. 9, 38-48.
  29. Sharkia, R., Bonshtien, A.L., Mizrahi, I., Weiss, C., Niv, A., Lustig, A., Viitanen, P. and Azem, A. (2003) On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20. Biochim Biophys Acta. 1651, 76-84.
  30. Diamant, S., Rosental, D., Azem, A., Eliahu, N., Ben-Zvi, A. and Goloubinoff, P. (2003). Dicarboxylic amino-acids and Glycin-Betain regulate chaperone-mediated protein-disaggregation under stress. Mol. Microbiol. 49, 401-410.
  31. Weiss, C., Niv, A. and Azem, A. (2002) Two-step purification of mitochondrial hsp70, Ssc1p, using Mge1(His)6 immobilized on Ni-agarose. Protein Express. Purif. 24, 268-273.
  32. Kurek, I., Dulberger, R., Azem, A., Ben-Tzvi, B., Sudhakar, D., Christou, P., Breiman, A. (2002) Deletion of the C-terminal 138 amino acids of the wheat FKBP73 abrogates calmodulin binding, dimerisation and male fertility in transgenic rice. Plant Mol. Biol. 48, 369-381.
  33. Levy-Rimler, G., Bell, RE., Ben-Tal, N. and Azem, A. (2002) Type I chaperonins: Not all are created equal. FEBS Letters. 529, 1-5.
  34. Levy-Rimler, G., Viitanen, P., Weiss, C., Sharkia, R., Greenberg, A., Niv, A., Lustig, A., Delarea, Y and Azem, A. (2001) The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60. Eur. J. Biochem. 268, 3465-3472.
  35. Dickson, R., Weiss, C., Howard, R., Aldrich, S.P., Ellis, R.J., Lorimer, G., Azem, A. and Viitanen, P. (2000) Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding. J. Biol. Chem. 275, 11829-11835.
  36. Weiss, C., Oppliger, W., Vergères, G., Demel, R., Jenö, P., Horst, M., de Kruijff, B., Schatz, G., Azem, A. (1999) Domain structure and lipid interaction of recombinant yeast Tim44. Proc. Natl. Acad. Sci. USA 96, 8890-8894.
  37. Matouschek, A., Azem, A., Ratliff, K., Glick, BS., Schmid, K., and Schatz, G. (1997). Active unfolding of precursor proteins during mitochondrial protein import. EMBO J. 16, 6727-6736.
  38. Azem, A., Oppliger, W., Lustig, A., Jenö, P., Feifel, B., Schatz, G., and Horst, M. (1997) The mitochondrial hsp70 chaperone system. J Biol. Chem. 270, 28387-28391.
  39. Goloubinoff, P., Diamant, S., Weiss, C., and Azem, A. (1997) GroES binding regulates GroEL chaperonin activity under heat shock. FEBS Letters 407, 215-219.
  40. Horst, M., Oppliger, W., Rospert, S., Schonfeld, H.-J., Schatz, G., and Azem, A. (1997) Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J. 16, 1842-1849.
  41. Horst, M., Azem, A., Schatz, G., and Glick, BS. (1997) "What is the driving force for protein import into mitochondria?" Biochim. Biophys. Acta (reviewed). 1318, 71-78.
  42. Azem, A., Diamant, S., Kessel, M., Weiss, C., and Goloubinoff, P. (1995) The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 hetero-oligomer. Proc. Natl. Acad. Sci. USA 92, 12021-12025.
  43. Diamant, S., Azem, A., Weiss, C., and Goloubinoff, P. (1995) Increased efficiency of GroE-assisted protein folding by manganese ions. J. Biol. Chem. 270, 2837-28391.
  44. Diamant, S., Azem, A., Weiss, C. and Goloubinoff, P. (1995) Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of the GroEL chaperonin. Biochemistry 34,273-277.
  45. Azem, A., Shaked, I., Rosenbusch, J.-P. and Daniel, E (1995) Cross-linking of porin with glutardialdehyde: a test for the adequacy of permises of cross-linking theory. Biochim. Biophys. Acta. 1243, 151-156.
  46. Azem, A., Kessel, M. and Goloubinoff, P. (1994) Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. Science 265, 653-656.
  47. Azem, A., Diamant, S. and Goloubinoff, P. (1994) Effect of divalent cations on the molecular structure of the GroEL oligomer. Biochemistry 33, 6671-6675.
  48. Daniel, E. Azem, A., Shaked, I. and Mevarech, M. (1993) Subunit structure of halophilic malate dehydrogenase from Haloarcula marismortui. Comp. Biochem. Physiol. 106B, 401-405.
  49. Azem, A. and Daniel, E. (1992) Structure of extracellular hemoglobin from the brine shrimp Artemia salina. Comp. Biochem. Physiol. 101B, 185-188.
  50. Ilan, E., Azem, A. and Daniel, E. (1990) Structural characterization and oxygen binding properties of extracellular hemoglobin from the marine polychaete Eurythoe complanata. Comp. Biochem. Physiol. 96B, 783-786.

CHAPTERS IN BOOKS

  1. Marom, M. and Azem, A. (in press). The use of cardiolipin-containing liposomes as a model system to study the interaction between proteins and the inner mitochondrial membrane. Methods Mol. Biol.
  2. Iosefson, O. and Azem, A. (2012) The Many Faces of Mortalin and Tid1. In: Mortalin Biology: Life, Stress and Death (eds. Sunil C. Kaul, Renu Wadhwa), Springer, Dordrecht Heidelberg, London, New-York, ISBN 978-94-007-3026-7.
  3. Sharkia, R., Athamny, E., Khatib, M., Sheikh-Muhammad, A., Azem, A., Mahajnah, M. (2012). Consanguinity and Its Effect on Morbidity and Congenital disorders among Israeli Arab Society. In: Genetic Disease (ISBN: 978-953-307-409-2), InTech.
  4. Sharkia, R., Viitanen, P., Levy-Rimler, G., Weiss, C., Niv, A. and Azem, A. (2002) The higher plant chaperonins. In: The Annual Plant Reviews (eds. McManus, M., Laing, W. and Allan, A.), Sheffield Academic Press, Sheffield, UK. 8, 181-203.
  5. Azem, A., Weiss, C., and Goloubinoff, P. (1998) Chemical crosslinking as a method for the structural analysis of GroE chaperonin complexes. Methods Enzymol. 290, 253-268.
  6. Azem, A., Pinhasy, A., and Daniel, E. (1991). "Cross-linking with bifunctional reagents and its application to the determination of the quaternary structures of invertebrate extracellular hemoglobins". In : Structure and function of invertebrate dioxygen carriers (eds. Vinogradov, S. and Kapp, O.) pp 49-57. Springer-Verlag, New-York.
  7. Azem, A., Tsfadia, Y. and Daniel, E. (1990). Polypeptide chain structure of erythrocruorin from Lumbricus rubellus. In: Invertebrate dioxygen carriers (eds. Preaux, G. and Lontie, R.) pp 17-20. Louvain University Press, Louvain.
   
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