Peer-reviewed publications

  1. Samson, A.O.; Chill, J.H.; Rodriguez, E.; Scherf, T.; Anglister, J. NMR mapping and secondary structure determination of the major acetylcholine receptor alpha-subunit determinant interacting with alpha-bungarotoxin. Biochemistry 2001, 40(18), 5464-5473.

  2. Chill, J.H.; Nivasch, R.; Levy, R.; Albeck, S.; Schreiber, G.; Anglister, J. The human interferon receptor: NMR-based modeling, mapping of the IFN-α2 binding site, and observed ligand-induced tightening. Biochemistry. 2002, 41(11), 3575-3585.

  3. Yao, Y.; Wang, J.; Viroonchatapan, N.; Samson, A.O.; Chill, J.H.; Rothe, E.; Anglister, J.; Wang, Z.Z. The human interferon receptor: Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic acetylcholine receptor alpha subunit. J. Biol. Chem. 2002, 277(15), 12613-12621.

  4. Samson, A.O.; Scherf, T.; Eisenstein, M.; Chill, J.H.; Anglister J. The mechanism for acetylcholine receptor inhibition by α-neurotoxins and species-specific resistance to a-bungarotoxin revealed by NMR. Neuron, 2002, 35(2), 319-332.        

  5. Chill, J.H.; Quadt, S.R.; Levy, R.; Schreiber, G.; Anglister J. The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding.  Structure (Camb.), 2003, 11(7), 791-802.

  6. Chill, J.H.*; Quadt, S.R.; Anglister J. Backbone dynamics of the human type I interferon receptor, a representative α-helical cytokine receptor. Biochemistry, 2004, 43(31), 10127-10137. (*Corresponding author).

  7. Rozen, O.; Chill, J.H.; Kessler, N.; Mester, B.; Sharon, M.; Zolla-Pazner, S.; Anglister J. Induced fit in HIV-neutralizing antibody complexes: evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization. Biochemistry, 2005, 44(19), 7250-7258.

  8. Samson, A.O.; Chill, J.H.; Anglister J. 2D-measurement of proton T1ρ relaxation in unlabeled proteins: Mobility changes in α-bungarotoxin upon binding of an acetylcholine receptor peptide. Biochemistry, 2005, 44(32), 10926-10934. 

  9. Chill, J.H.; Louis, J.M.; Miller, C.; Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci, 2006, 15(4), 684-698.

  10. Chill, J.H.; Louis, J.M.; Baber, J.L.; Bax A. Measurement of 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel. J. Biomol NMR, 2006, 36(2), 123-136.

  11. Quadt-Akabayov, S.R.; Chill, J.H.; Levy, R.; Kessler, N.; Anglister J. Determination of the human type I interferon receptor binding site on human interferon α2 by cross saturation and an NMR-based model of the complex. Protein Sci., 2006, 15(11), 2656-2668.

  12. Ying, J.; Chill, J.H.; Louis, J.M.; Bax A. Mixed-time parallel evolution and multiple quantum NMR experiments: sensitivity and resolution enhancement in heteronuclear NMR. J. Biomol. NMR, 2007, 37(3), 195-204.

  13. Chill, J.H.; Louis, J.M.; Delaglio, F.; Bax A. Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR. Biochim. Biophys. Acta  2007, 1768(12), 3260-3270.

  14. Chill, J.H.*; Naider, F.N. A solution NMR view of protein dynamics in the biological membrane. Curr. Opin. Struc. Biol. 2011, 21, 627-633. (*Corresponding author)

  15. Kamnesky, G.; Shaked, H.; Chill, J.H.*; The distal C-terminal region of the KcsA potassium channel is a pH-dependent tetramerization domain. J. Mol. Biol. 2012, 418(3-4), 237-247. (*Corresponding author)

  16. Novacek, J.; Haba, N.; Chill, J.H.; Zidek, L.; Sklenar, V.; 4D non-uniformly sampled HabCabCON/intra-HabCabNCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins. J. Biomol. NMR 2012, 53(2), 139-148.

  17. Bermel, W.; Bertini, I.; Chill, J.H.; Felli, I.C.; Haba, N.Y.; Kumar, M.V.; Pierattelli, R. 13C-direct detection amino acid selective NMR experiments to simplify the assignment of IDPs. ChemBioChem, 2012, 13(16), 2425-2432.

  18. Guttman, C.; Davidov, G.; Shaked, H.; Ganguly, A.; Miller, J.F.; Chill, J.H.*.; Zarivach, R.* Characterization of the N-terminal domain of BteA: a Bordatella Type III secreted cytotoxic effector. PLoS One, 2013, 8(1):e55650. (*Corresponding authors).

  19. Haba, N.Y.; Gross, R.; Novacek, J.; Shaked, H.; Zidek, L,; Barda-Saad, M.; Chill, J.H.* NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. Biophyiscal J. 2013, 105(2), 481-493. (*Corresponding author)

  20. Shapira, R.; Rudnick, S.; Daniel, B.; Viskind, O.; Aisha, V.; Richman, M.; Ayasolla, K.R.; Perelman, A.; Chill, J.H.; Gruzman, A.; Rahimipour, S. Multifunctional cyclic D,L-α-peptide architectures stimulate non-insulin dependent glucose uptake in skeletal muscle cells and protect them against oxidative stress. J. Med. Chem. 2013, 56(17), 6709-6718.

  21. Zazrin, H.; Shaked, H.; Chill, J.H.* Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR. BBA-Biomembranes, BBA-Biomembranes, 2014, 1838, 784-792. (*Corresponding author)

  22. Guttman, C.; Davidov, G.; Yahalom, A.; Shaked, H.; Kolusheva, S.; Bitton, R.; Chill, J.H.*; Zarivach, R.* BtcA, a class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism. PLoS One, 2013, 8(12), e81557. (*Corresponding authors)

  23. Fried, S.; Eliyaho, S.; Pauker, H.M.; Noy, E.; Reicher, B.; Chill, J.H. and Mira Barda-Saad. Triple color-FRET analysis reveals a dynamic conformational change within the actin regulating WIP:WASp complex. Science Signaling, 2014, 7(331):ra60. doi: 10.1126/scisignal.2005198.

  24. Kamnesky, G.; Hirschhorn, O.; Shaked, H.; Chen, J.; Yao, L.; Chill, J.H.* Molecular determinants of tetramerization in the KcsA cytoplasmic domain. Protein Science, 2014, 23(10):1403-1416. (*Corresponding author)

  25. Elazari-Shalom, H.; Zazrin-Grynspan, H.; Shaked, H.; Chill, J.H.* An NMR study of the transmembrane domain of hepatitis C virus E2 glycoprotein. BBA Biomembranes, 2014, 1838(11):2919-2128. (*Corresponding author)

  26. Sher, I.; Chang, S.-C.; Li, Y.; Chhabra, S.; Palmer III, A.G.;.Norton, R.S. and Chill, J.H.* Conformational flexibility in the binding surface of the potassium channel blocker ShK. ChemBioChem, 2014, 15(16):2402-2410. Featured on cover. (*Corresponding author)

  27. Elazari-Shalom, H.; Shaked, H.; Esteban-Martin, S.; Salvatella, X.; Barda-Saad, M.; Chill, J.H.* New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization. FEBS J., 2015, 282(4), 700-714. 

  28. Reytblat, I.; Keinan-Adamsky, K.; Chill, J.H.; Gottlieb, H.; Gedanken, A.; Goobes, G. NMR studies of DNA microcapsules prepared using sonochemical methods. Phys. Chem. Chem. Phys. 2015, 17(3), 2235-2240.

  29. Chill, J.H.; NMR of proteins: Eavesdropping on molecular events. Isr. Chem. Eng. 2015, 1, 13-21

  30. Meirovitch, E.: Tchaicheeyan, O.; Sher, I.; Norton, R.S.; Chill, J.H. Structural dynamics of the potassium channel blocker ShK: SRLS analysis of 15N relaxation. J. Phys. Chem. B 2015, 119, 15130-15137.

  31. Zhao, R.; Dai, H.; Mendelman, N.; Cuello, L.; Chill, J.H.; Goldstein, S. Designer and natural peptide toxin blockers of the KcsA potassium channel identified by phage-display. Proc. Natl. Acad. Sci. 2015, 112(50), E7013-7021.

  32. Chemerovski-Glikman, M.; Rozentur-Shkop, E.; Richman, M.; Grupi, A.; Getler, A.; Cohen, H.Y.; Shaked, H.; Wallin, C.; Wärmländer, S.K.; Haas, E.; Gräslund, A.; Chill, J.H.; Rahimipour, S. Self-assembled cyclic D,L-a-peptides as generic conformational inhibitors of a-synuclein aggregation and toxicity. Chemistry 2016, 22(40), 14236-14246.

  33. Barber-Zucker, S.; Uebe, R.; Davidov, G.; Navon, Y.; Sherf, D.; Chill, J.H.; Kass, I.; Bitton, R.; Schüler, D.; Zarivach R. Disease-homologous mutation in the cation diffusion facilitator protein MamM causes single-domain structural loss and signifies its importance. Sci. Rep. 2016, 6, 31933.

  34. Rozentur-Shkop, E.; Goobes, G.; Chill, J.H. A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP. J. Biomol NMR 2016, 66(4), 243-257s.

  35. Levy, A.R.; Nissim, M.; Mendelman, N.; Chill, J.H.; Ruthstein, S. The Ctr1 intracellular loop is involved in the copper transfer mechanism to the Atox1 metallochaperone. J. Phys. Chem. B. 2016, 120(48), 12334-12345.

  36. Halle-Bikovski, A.; Fried, S.; Biber, G.; Rozentur-Shkop, E.; Joseph, N.; Shaked, H.; Barda-Saad, M.† Chill, J.H.† New structural insights into formation of the key actin regulating WIP-WASp complex determined by NMR and molecular imaging. ACS Chem. Biol. 2018, 13(1), 100-109.

  37. Belostozky, A.; Richman, M.; Lisiansky, E.; Tovchygrechko, A.; Chill, J.H.; Rahimipour, S. Inhibition of tau-derived hexapeptide aggregation and toxicity by a self-assembled cyclic D,L-α-peptide conformational inhibitor. Chem Commun (Camb) 2018, 54(47), 5890-5893.

  38. Halle-Bikovski, A.; Rozentur-Shkop, E.; Shaked, H.; Barda-Saad, M.† Chill, J.H.† From disordered polypeptide to functional regulator: a structural view of WASp-interacting protein and its complex with WASp in human T-cells. Biophysical J. 2018, 114(3), 26a.

  39. Baskin, M.; Zhu, H.; Qu, Z.-W.; Chill, J.H.; Grimme, S.; Maayan, G. Folding of unstructured peptoids and heterobimetallic peptoid complexes formation upon side chains-to-metal coordination. Chem. Sci. 2019, doi: 10.1039/c8sc03616k.

  40. Qasim. A.; Sher, I.; Hirschhorn, O.; Shaked, H.; Qasim, Z.; Ruthstein, S.; Chill, J.H. A KcsA cytoplasmic pH-gate investigated in lipoprotein nanodiscs. ChemBioChem, 2019, doi: 10.1002/cbic.201800627

  41. Sasson, E.; Kolitz-Domb, M.; Chill, J.H.; Margel, S. Engineering of durable antifog thin coatings on plastic films by UV-curing of proteinoid prepolymers with PEG-diacrylate monomers. ACS Omega 2019, 4(5), 9352-9360.

  42. Yahalom, A.; Davidov, G.; Kolusheva, S.; Shaked, H.; Barber-Zucker, S.; Zarivach, R.† Chill, J.H.† Structure and membrane-targeting of a Bordetella pertussis effector N-terminal domain. BBA-Biomembranes, 2019, 1861(12):183054 (†Co-corresponding author).

  43. Chill, J.H.*; Qasim, A.; Sher, I.; Gross, R. NMR perspectives of the KcsA potassium channel in the membrane environment. Isr J. Chem., 2019, 59(11-12), 1001-1013. (*Corresponding author)

  44. Zhao, R.; Dai, H.; Mendelman, N.; Chill, J.H.†; Goldstein, S.A.N†. Tethered peptide neurotoxins display two blocking mechanisms in the K+ channel pore as do their untethered analogues. Sci. Adv. 2020, 6(10), eaaz3439. (†Co-corresponding author)

  45. Sokolik, C.G.; Qassem, N.; Chill, J.H. The disordered cellular multi-tasker WIP and its protein-protein interactions: a structural view. Biomolecules 2020, 10(7), 1084-1093.

  46. Hadad, E.; Rudnick-Glick, S.; Grinberg, I.; Kolitz-Domb, M.; Chill, J.H.; Margel, S. Synthesis and characterization of poly-(RGD) proteinoid polymers and NIR fluorescent nanoparticles of optimal d,l-configuration for drug-delivery applications - in vitro study. ACS Omega 2020, 5(37), 23568-23577.



Book chapters


  1. Samson, A.O.; Scherf, T.; Eisenstein, M.; Chill, J.H.; Anglister J. The mechanism for acetylcholine receptor inhibition by α-neurotoxins and species specific resistance to α-bungarotoxin revealed by NMR. Cholinergic mechanisms, function and dysfunction, 2004, eds. Silman I., Soreq H., Anglister L., Michaelson D., Fisher A., p.45-54, Taylor & Francis group, UK.

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