REFEREED ARTICLES

1)  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.

2)  Azem, A. and Daniel, E. (1992)  Structure of extracellular hemoglobin from the brine shrimp Artemia salina.  Comp. Biochem. Physiol.  101B, 185-188.

3)  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.

4)  Azem, A., Diamant, S. and Goloubinoff, P. (1994)  Effect of divalent cations on the molecular structure of the GroEL oligomer.  Biochemistry  33, 6671-6675.

5)  Azem, A., Kessel, M. and Goloubinoff, P. (1994)  Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.  Science  265, 653-656.

6)  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.

7)  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.

8)  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.

9)  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.

10)  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.

11)  Goloubinoff, P., Diamant, S., Weiss, C., and Azem, A. (1997)  GroES binding regulates GroEL chaperonin activity under heat shock.  FEBS Letters 407, 215-219.

12)  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.

13)  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.

14)  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.

15)  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.

16)  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.

17)  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.

18)  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.

19)  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.

20)  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.

21)  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.

22)  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.

23)  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.

24)  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.

25)  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.

26)  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.

27)  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.

28)  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.

29)  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.

30)  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.

31)  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.

32)  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.

33)  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.

34)  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.

35)  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.

36)  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.

37)  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.

38)  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.

39)  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.

40)  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.

41)  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, 43809-43815

42)  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.

CHAPTERS IN BOOKS

1)  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.

2)  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.

3)  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.

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) Sharkia, R., Athamny, E., Khatib, M., Sheikh-Muhammad, A., Azem, A.,  Mahajnah, M. (2011). Consanguinity and Its Effect on Morbidity and Congenital disorders among Israeli Arab Society. In: Genetic Disease (ISBN: 978-953-307-409-2), InTech.

REVIEWES

1)  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.

2)  Levy-Rimler, G., Bell, RE., Ben-Tal, N. and Azem, A. (2002) Type I chaperonins: Not all are created equal.  FEBS Letters (invited).  529, 1-5.

3)  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