Shahar Nisemblat

Experienced Team Lead with a proven record of successfully guiding R&D teams, specializing in protein purification methods and strategies

Eager to leverage my expertise in a dynamic role where I can drive innovative solutions and lead impactful projects

• Gomez-Llorente, Y., Jebara, F., Patra, M., Malik, R., Nisemblat, S., Chomsky-Hecht, O., Parnas, A., Azem, A., J.A., Hirsch and Ubarretxena-Belandia, I., Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin, Nat Commun 11, 1916, 2020.
• Weiss, C., Jebara, F., Nisemblat, S. & Azem, A. Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle, Front. Mol. Biosci., 2016, Dec 08.
• Nisemblat, S., Yaniv, O., Parnas, A., Frolow, F. & Azem, A. Crystal structure of the human mitochondrial chaperonin symmetrical football complex.Proc Natl Acad Sci U S A, 2015 May 27;112(19):6044-9.
• Nisemblat, S., Parnas, A., Yaniv, O., Azem, A. & Frolow, F. Crystallization and structure determination of a symmetrical 'football' complex of the mammalian mitochondrial Hsp60-Hsp10 chaperonins. Acta Crystallogr F Struct Biol Commun, 2014 Jan 24;70(Pt 1):116-9.
• Vitlin Gruber, A., Nisemblat, S., Azem, A. & Weiss, C. The complexity of chloroplast chaperonins. Trends Plant Sci, 2013 Dec 12;18(12):688-94.
• Vitlin-Gruber, A., Nisemblat, S., Zizelski, G., Parnas, A., Dzikowski, R., Azem, A., Weiss, C., P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli., PLoS One, 2013 10;8(1):e53909.
• Parnas, A.*, Nisemblat, S.*, Weiss, C., Levy-Rimler, G., Pri-Or, A., Zor, T., Lund, P.A., Bross, P., Azem, A., Identification of elements that dictate the specificity of mitochondrial Hsp60 for its Co-chaperonin. PLoS One, 2012 4;7(12):e50318.

*Equal contribution

• Parnas, A., Nadler, M., Nisemblat, S., Horovitz, A., Mandel, H. and Azem, A., The mitchap-60 disease is due to entropic destabilization of the human mitochondrial Hspp60 oligomer. J Biol Chem, 2009 Oct 25;284(41):28198-203.