Dr. Ofer Yifrach: Publications
1.
E. Magidovich, S. J. Fleishman and O. Yifrach (2006). Intrinsically
disordered C-terminal segments of voltage-activated potassium channels: a
possible fishing rod-like mechanism for channel binding to scaffold proteins. Bioinformatics,
22, 1546-1550. 2.
E. Magidovich and O. Yifrach (2004). Conserved
gating hinge in ligand- and voltage-dependent K+ channels. Biochemistry, 43, 13242-13247. 3.
S. J. Fleishman, O. Yifrach and N. Ben-Tal
(2004). Evolutionary conserved network of amino acids mediates
gating in voltage-dependent potassium channels. J. Mol. Biol. 340,
307-318. 4.
O. Yifrach (2004). Hill coefficient for estimating the magnitude of
cooperativity in gating transitions of voltage-dependent ion channels. Biophys. J. 87,
822-830.
5.
O. Yifrach and R. MacKinnon (2002).
Energetics of pore opening in a voltage-gated K+ channel.
Cell, 111, 231-239. 6.
A. Horovitz, G. Kafri, Y. Fridman and O. Yifrach (2001).
Allostery in Chaperonins.
J. Struct. Biol. 135, 104-114. 7.
O. Yifrach and A. Horovitz (2000). Coupling between protein folding and cooperative ATP
binding in the GroEL chaperonin.
Proc. Natl. Acad. Sci., 8.
A. Horovitz and O. Yifrach (2000). On the relationship between the Hill coefficients for
steady-state and transient kinetic data: a criterion for concerted transitions
in allosteric proteins.
Bull. Math. Biol., 62,
241-246. 9.
A. Erbse, O. Yifrach, S. Jones and P. A. Lund (1999). Chaperone activity of a GroEL protein that can exist in
a single or double ring forms. J. Biol.
Chem. 274, 20351-20357. 10.
O. Yifrach and A. Horovitz (1998). Mapping the transition state of the allosteric pathway
of GroEL by protein engineering.
J. Am. Chem. Soc. 120, 13262-13263. 11.
O. Yifrach and A. Horovitz (1998). Transient kinetic analysis of ATP binding-induced
conformational changes in the allosteric chaperonin GroEL.
Biochemistry
37, 7083-7088. 12.
H. E. White, S. Chen, A. M. Roseman, O. Yifrach, A. Horovitz and
H. R. Saibil (1997). Structural
basis of allosteric changes in the GroEL mutant Arg197®
Ala.
Nat. Struct. Biol. 4, 690-694. 13.
O. Yifrach and A. Horovitz (1996).
Allosteric control of non-folded protein binding to GroEL.
J. Mol. Biol.
255, 356-361. 14.
O. Yifrach and A. Horovitz (1995).
Nested cooperativity in the ATPase activity of the oligomeric chaperonin
GroEL.
Biochemistry 34, 5303-5308. 15.
O. Kovalenko, O. Yifrach and A. Horovitz (1994).
Residue Lys-
Biochemistry 33, 14974-14978. 16.
O. Yifrach and A.
Horovitz (1994). Two lines of allosteric communication in the oligomeric
chaperonin GroEL are revealed by the single mutation Arg-196®
Ala.
J. Mol. Biol. 243, 397-401. 17.
A. Horovitz, E.S.
Bochkareva, O. Yifrach and A.S. Girshovich (1994). Prediction of an inter-residue interaction in the
chaperonin GroEL from multiple sequence alignment is confirmed by double mutant
cycle analysis.
J. Mol. Biol. 233, 133-138. |
Last Updated: 19/03/2007 |