Prof. Ada Yonath RIBOSOME GROUP

LIST OF PUBLICATIONS

· Rajan KS, Aryal S, Hiregange DG, Bashan A, Madmoni H, Olami M, Doniger T, Cohen-Chalamish S, Pescher P, Taoka M, Nobe Y, Fedorenko A, Bose T, Zimermann E, Prina E, Aharon-Hefetz N, Pilpel Y, Isobe T, Unger R, Späth GF, Yonath A, Michaeli S. (2024). Structural and mechanistic insights into the function of Leishmania ribosome lacking a single pseudouridine modification. Cell Rep. 43(5),114203; PMID: 38722744.

· Rivalta, A., Hiregange, D.G., Bose, T., Fridkin, G., Rajan, K.S., Yonath, A., Zimmerman, E., Bashan, A. and Yonath, H. (2023). Medical Implications of Functional and Destructive Cellular Motions: Curiosity-Driven Open Issues. In Curious Future Insight: Science for a Better Tomorrow (pp. 65-82). Cham: Springer International Publishing.

· Rajan KS, Madmoni H, Bashan A, Taoka M, Aryal S, Nobe Y, Doniger T, Galili Kostin B, Blumberg A, Cohen-Chalamish S, Schwartz S, Rivalta A, Zimmerman E, Unger R, Isobe T, Yonath A, Michaeli S. (2023). A single pseudouridine on rRNA regulates ribosome structure and function in the mammalian parasite Trypanosoma brucei. Nat Commun. 14(1):7462; PMID: 37985661.

· Nguyen A. M. T., Shalev-Benami M., Rosa-Teijeiro C., Ibarra-Meneses A. V., Yonath A., Bashan A., Jaffe C. L., Olivier M., Fernandez-Prada C., William D. L. (2023). Systematic Exploration of Functional Group Relevance for Anti-Leishmanial Activity of Anisomycin. Biomedicines, 11, 2541

· Hiregange D. G., Rivalta A., Yonath A., Zimmerman E., Bashan A., and Yonath H. (2022). Mutations in RPS19 may affect ribosome function and biogenesis in Diamond Blackfan anemia. FEBS Open Bio. 12, 1419-1434; PMID: 35583751.

· Cimicata, G., Fridkin, G., Bose, T., Eyal, Z., Halfon, Y., Breiner-Goldstein, E., Fox, T., Zimmerman, E., Bashan, A., de Val, N., Wlodawer, A., and Yonath, A. (2022). Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis. mBio 13, e0030622; PMID: 35348349.

· Bose, T., Fridkin, G., Davidovich, C., Krupkin, M., Dinger, N., Falkovich, A.H., Peleg, Y., Agmon, I., Bashan, A., and Yonath, A. (2022). Origin of life: protoribosome forms peptide bonds and links RNA and protein dominated worlds. Nucleic Acids Res 50, 1815-1828; PMID: 35137169.

· Hiregange, D.G., Rivalta, A., Bose, T., Breiner-Goldstein, E., Samiya, S., Cimicata, G., Kulakova, L., Zimmerman, E., Bashan, A., Herzberg, O., and Yonath, A. (2022). Cryo-EM structure of the ancient eukaryotic ribosome from the human parasite Giardia lamblia. Nucleic Acids Res 50, 1770-1782; PMID: 35100413.

· Bose T, Fridkin G, Bashan A, Yonath A. (2021). Origin of Life: Chiral Short RNA Chains Capable of Non-Enzymatic Peptide Bond Formation , Isr. J. Chem., 61, 863 – 872.

· König G, Sokkar P, Pryk N, Heinrich S, Möller D, Cimicata G, Matzov D, Dietze P, Thiel W, Bashan A, Bandow JE, Zuegg J, Yonath A, Schulz F, Sanchez-Garcia E. (2021). Rational prioritization strategy allows the design of macrolide derivatives that overcome antibiotic resistance. Proc Natl Acad Sci U S A. 118(46):e2113632118; PMID: 34750269.

· Breiner-Goldstein, E., Eyal, Z., Matzov, D., Halfon, Y., Cimicata, G., Baum, M., Rokney, A., Ezernitchi, A.V., Lowell, A.N., Schmidt, J.J., Rozenberg, H., Zimmerman, E., Bashan, A., Valinsky, L., Anzai, Y., Sherman, D. H., Yonath, A. (2021). Ribosome-binding and anti-microbial studies of the mycinamicins, 16-membered macrolide antibiotics from Micromonospora griseorubida. Nucleic Acids Res 49, 9560-9573.; PMID: 34417608

· Matzov, D., Taoka, M., Nobe, Y., Yamauchi, Y., Halfon, Y., Asis, N., Zimermann, E., Rozenberg, H., Bashan, A., Bhushan, S. Isobe, T., Gray, M. W.,Yonath, A., Shalev-Benami, M. (2020). Cryo-EM structure of the highly atypical cytoplasmic ribosome of Euglena gracilis. Nucleic Acids Res, 18; 48 (20): 11750-11761; PMID: 33091122.

· Halfon, Y., Matzov, D., Eyal, Z., Bashan, A., Zimmerman, E., Kjeldgaard, J., Ingmer, H., and Yonath, A. (2020). Modulation in the exit tunnel of the S. aureus ribosome leads to erythromycin resistance. In European Synchrotron Radiation Facility (ESRF) (Spotlights on Science).

· Halfon, Y., Jimenez-Fernandez, A., La Rosa, R., Espinosa Portero, R., Krogh Johansen, H., Matzov, D., Eyal, Z., Bashan, A., Zimmerman, E., Belousoff, M., Molin, S., and Yonath, A. (2019). Structure of Pseudomonas aeruginosa ribosomes from an aminoglycoside-resistant clinical isolate. Proc Natl Acad Sci U S A, 116, 22275-22281; PMID: 31611393.

· Matzov, D., Bashan, A., Yap, M.F., and Yonath, A. (2019). Stress response as implemented by hibernating ribosomes: a structural overview. Febs J 286, 3558-3565.; PMID: 31230411

· Halfon, Y., Matzov, D., Eyal, Z., Bashan, A., Zimmerman, E., Kjeldgaard, J., Ingmer, H., and Yonath, A. (2019). Exit tunnel modulation as resistance mechanism of S. aureus erythromycin resistant mutant. Sci Rep 9, 11460; PMID: 31391518

· Yonath, A. (2019). Could a bright outlook for antibiotics usage emerge from colossal health issue? In Bacterial resistance to antibiotics: from molecules to man, B.B. Bonev, and N.M. Brown, eds. (UK: John Wiley & Sons).

· Cimicata, G., Bose, T., Fridkin, G., Rivalta, A., Peretz, M., Bashan, A., and Yonath, A. (2018). Contemporary challenges in medical usage of antibiotics. In Pontificiae Academiae Scientiarvm Acta 25, J. von Braun, Sorondo, MS., ed. (Vatican City: Transformative Roles of Science in Society: From Emerging Basic Science Toward Solutions for People's Wellbeing), pp. 97-101.

· Shalev-Benami, M., Zhang, Y., Rozenberg, H., Nobe, Y., Taoka, M., Matzov, D., Zimmerman, E., Bashan, A., Isobe, T., Jaffe, C.L., Yonath, A. and Skiniotis, G. (2017). Atomic resolution snapshot of Leishmania ribosome inhibition by the aminoglycoside paromomycin. Nat Commun 8, 1589; PMID: 29150609

· Matzov, D., Aibara, S., Basu, A., Zimmerman, E., Bashan, A., Yap, M.F., Amunts, A., and Yonath, A.E. (2017). The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus. Nat Commun 8, 723; PMID: 28959035

· Matzov D., Eyal Z., Benhamou R.I., Shalev-Benami M., Halfon Y., Krupkin M., Zimmerman E., Rozenberg H., Bashan A., Fridman M. and Yonath, A. (2017). Structural insights of lincosamides targeting the ribosome of Staphylococcus aureus. Nucleic Acids Res, 45, 10284-10292; PMID: 28973455

· Wekselman, I., Zimmerman, E., Davidovich, C., Belousoff, M., Matzov, D., Krupkin, M., Rozenberg, H., Bashan, A., Friedlander, G., Kjeldgaard, J., Ingmer, H., Lindahl, L., Zengel, M. J., and Yonath, A. (2017). The Ribosomal Protein uL22 Modulates the Shape of the Protein Exit Tunnel. Structure 25, 1233-1241; PMID: 28689968

· Yonath, A. (2017). Quantum mechanic glimpse into peptide bond formation within the ribosome shed light on origin of life. Struct Chem, Springer 28, 1285-1291

· Belousoff, M.J., Eyal, Z., Radjainia, M., Ahmed, T., Bamert, R.S., Matzov, D., Bashan, A., Zimmerman, E., Mishra, S., Cameron, D., Elmlund, H., Peleg, A. Y., Bhushan, S., Lithgow, T., and Yonath, A. (2017). Structural basis for linezolid binding site rearrangement in the Staphylococcus aureus ribosome. mBio 8 (3); PMID: 28487427

· Matzov, D., Bashan, A., and Yonath, A. (2017). A Bright Future for Antibiotics? Annu Rev Biochem 86, 567-583; PMID: 28654325

· Eyal, Z., Matzov, D., Krupkin, M., Paukner, S., Riedl, R., Rozenberg, H., Zimmerman, E., Bashan, A., and Yonath, A. (2016). A novel pleuromutilin antibacterial compound, its binding mode and selectivity mechanism. Sci Rep 6, 39004; PMID: 27958389

· Zaccai, G., Natali, F., Peters, J., Rihova, M., Zimmerman, E., Ollivier, J., Combet, J., Maurel, M.C., Bashan, A., and Yonath, A. (2016). The fluctuating ribosome: thermal molecular dynamics characterized by neutron scattering.Sci Rep 6, 37138; PMID: 27849042

· Krupkin, M., Wekselman, I., Matzov, D., Eyal, Z., Diskin Posner, Y., Rozenberg, H., Zimmerman, E., Bashan, A., and Yonath, A. (2016). Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding. Proc Natl Acad Sci U S A 113, E6796-E6805; PMID: 27791159

· Shalev-Benami, M., Zhang, Y., Matzov, D., Halfon, Y., Zackay, A., Rozenberg, H., Zimmerman, E., Bashan, A., Jaffe, C.L., Yonath, A., and Skiniotis, G. (2016). 2.8 Angstrom cryo-EM structure of the large ribosomal subunit from the eukaryotic parasite, Leishmania Cell Rep 16, 288-294; PMID: 27373148

· Auerbach-Nevo, T., Baram, D., Bashan, A., Belousoff, M., Breiner, E., Davidovich, C., Cimicata, G., Eyal, Z., Halfon, Y., Krupkin, M., Matzov, M, Metz, M., Mruwat, R., Peretz, M., Pick, O., Pyetan, E., Rozenberg, H., Shalev-Benami, M., Wekselman, I. , Zarivach, R., Zimmerman, E., Assis, N., Bloch, J., Israeli, H., Kalaora, R., Lim, L., Sade-Falk, O., Shapira, T., Taha-Salaime, L., Tang, H. and Yonath, A. (2016). Ribosomal Antibiotics: Contemporary Challenges. Antibiotics (Basel, Switzerland) 5, 24 1-11; PMID: 27367739

·Eyal, Z., Matzov, D., Krupkin, M., Wekselman, I., Paukner, S., Zimmerman, E., Rozenberg, H., Bashan, A., and Yonath, A. (2015). Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus. Proc Natl Acad Sci U S A, 112(43): E5805-14; PMCID: PMC4629319

·Sun, L., Xiong, Y., Bashan, A., Zimmerman, E., Shulman Daube, S., Peleg, Y., Albeck, S., Unger, T., Yonath, H., Krupkin, M., Matzov, D.,Yonath, A.(2015) A Recombinant Collagen-mRNA Platform for Controllable Protein Synthesis. ChemBioChem 16, 1415-1419; PMCID: PMC4517095

·Krupkin, M., Bashan, A., and Yonath, A. (2014). Glimpse into the Origin of Life: What was First, the Genetic Code or its Products, the Proteins? In Why does Evolution Matter? The Importance of Understanding Evolution, G. Trueba, ed. (Cambridge Scholars Publishing). pp. 87-100

· Ban, N., Beckmann, R., Cate, J.H., Dinman, J.D., Dragon, F., Ellis, S.R., Lafontaine, D.L., Lindahl, L., Liljas, A., Lipton, J.M., McAlear, M. A., Moore, P. B., Noller, H. F., Ortega, J., Panse, V. G., Ramakrishnan, V., Spahn, C. M., Steitz, T. A., Tchorzewski, M., Tollervey, D., Warren, A. J., Williamson, J. R., Wilson, D., Yonath, A. & Yusupov, M. (2014). A new system for naming ribosomal proteins. Curr Opin Struct Biol 24C,165-169; PMCID: PMC2946966

· Zimmerman, E., Bashan, A., and Yonath, A. (2014). Antibiotics at the Ribosomal Exit Tunnel–Selected Structural Aspects. In Antibiotics: Targets, Mechanisms and Resistance, C.O. Gualerzi, L. Brandi, A. Fabbretti, and C.L. Pon, eds. (Weinheim, Germany: Wiley-VCH), pp. 509-524; NLM ID:101623838

· Huang, L., Krupkin, M., Bashan, A., Yonath, A. and Massa, L. (2013). Protoribosome by quantum kernel energy method, Proc Natl Acad Sci U S A 110, 37, 14900-5; PMCID: PMC3773780

· Yonath, A. (2012). Ribosomes: Ribozymes that Survived Evolution Pressures but Is Paralyzed by Tiny Antibiotics. M.A. Carrondo, and P. Spadon, eds. In: NATO Science for Peace and Security Series A: Chemistry and Biology, Macromolecular Crystallography pp. 195-208.

· Fox, G. E., Tran, Q. and Yonath, A. (2012). An exit cavity was crucial to the polymerase activity of the early ribosome. Astrobiology 12, 57-60; PMID:22191510

· Rozenberg, H. and Yonath, A. (2011). Le rayonnement synchrotron et le ribosome. L'Actualité Chimique 356-357

· Yonath, A. (2011). Merging disciplines: chemical bases of life processes are revealed by X-ray crystallography. Sci China Chem 54, 2021-2023

· Krupkin, M., Matzov, D., Tang, H., Metz, M., Kalaora, R., Belousoff, M. J., Zimmerman, E., Bashan A. and Yonath, A. (2011). A vestige of a prebiotic bonding machine is functioning within the contemporary ribosome. Philos Trans R Soc Lond B Biol Sci 366, 2972-2978; PMID:21930590

· Bashan A. and Yonath, A. (2011). Ribosome crystallography: From early evolution to contemporary medical Insights. In Ribosomes Structure, Function, and Dynamics, M.V. Rodnina, W. Wintermeyer, and R. Green, eds. New York, Springer, pp. 3-18

· Yonath, A. (2011). X-ray crystallography at the heart of life science. Curr Opin Struct Biol 21, 622-626; PMID:21824762

· Belousoff, M. J., Shapira, T., Bashan, A., Zimmerman, E., Rozenberg, H., Arakawa, K., Kinashi H. and Yonath, A. (2011). Crystal structure of the synergistic antibiotic pair, lankamycin and lankacidin, in complex with the large ribosomal subunit. Proc Natl Acad Sci U S A, (2011) 108, 2717-2722; PMID:21282615

· Davidovich, C. (2010). Targeting Functional Centers of the Ribosome, Doctoral Thesis, Weizmann Institute of Science, Rehovot, Israel

· Belousoff, M.J., Davidovich, C., Bashan A. and A. Yonath. (2010). On the development towards the modern world: A plausible role of uncoded peptides in the RNA world. In Origins of life and evolution of biospheres K. Ruiz-Mirazo, and P.L. Luisi, eds. (Springer) pp. 415-419; PMID:20571915

· Bashan, A., Zimmerman, E., Belousoff, M. J., Rozenberg, H., Davidovich, C., Wekselman, I., Shapira, T., Krupkin, M. and A. Yonath (2010). The ribosome as drug target: lessons from 3D structures. Isr Chem Soc, 25, 10-18

· Bashan, A., Belousoff, M. J., Davidovich C. and A. Yonath, (2010). Linking the RNA world to modern life: The proto-ribosome conception. Orig Life Evol Biosph, 40, 425-429; PMID:20571915

· Yonath, A. (2010). Hibernating bears, antibiotics, and the evolving ribosome (Nobel Lecture). Angew Chem Int Ed Engl, 49, 4341-4354

· Davidovich, C., Belousoff, M. J, Wekselman, I., Shapira, T., Krupkin, M., Zimmerman, E., Bashan, A. and A. Yonath (2010). The proto-ribosome: an ancient nano-machine for peptide bond formation. Isr J Chem 50, 29-35

· Belousoff, M. J., Davidovich, C., Zimmerman, E., Caspi, Y., Wekselman, I., Rozenszajn, L., Shapira, T., Sade-Falk, O., Taha, L., Bashan, A., Weiss M. S. and A. Yonath, (2010). Ancient machinery embedded in the contemporary ribosome, Biochem Soc Trans, 38, 422-427; PMID:20298195

· Auerbach, T., Mermershtain, I., Davidovich, C., Bashan, A., Belousoff, M., Wekselman, I., Zimmerman, E., Xiong, L., Klepacki, D., Arakawa, K., Kinashi,, H., Mankin, A. S. and Yonath, A. (2010). The structure of ribosome-lankacidin complex reveals ribosomal sites for synergistic antibiotics. Proc Natl Acad Sci U S A, 107, 1983-1988; PMID:20080686

· Massa, L., Matta, C.F., Yonath A. and Karle, J. (2010). Quantum Transition State for Peptide Bond Formation in the Ribosome. In Quantum Biochemistry, C.F. Matta, ed. (Weinheim Germany, Wiley-VCH Verlag GmbH & Co. KGaA), pp. 16, 501-515

· Davidovich, C., Belousoff, M., Bashan, A. and A. Yonath, (2009). The evolving ribosome: from non-coded peptide bond formation to sophisticated translation machinery. Res Microbiol 160, 487-492; PMID:19619641

· Yonath, A. (2009). Large facilities and the evolving ribosome, the cellular machine for genetic-code translation. J R Soc Interface 6 Suppl 5, S575-585; PMID:19656820

· Yonath, A. (2009). Can structures lead to better drugs? Lessons from ribosome research. In: NATO Science for Peace and Security Series A: Chemistry and Biology, From Molecules to Medicines, Sussman, J. L. and Spadon, P. eds. (Springer), pp. 231-251

· Yonath, A. (2009) Ribosome: an ancient cellular nano-machine for genetic code translation In Biophysics and the challenges of emerging threats, In: NATO Science for Peace and Security Series B: Physics and Biophysics, Biophysics and the challenges of emerging threats, J. D. Puglisi, ed. (Springer) pp. 121-155

· Auerbach, T., Mermershtain, I., Bashan, A., Davidovich, C., Rosenberg, H., Sherman, D. H. and A. Yonath, (2009). Structural basis for the antibacterial activity of the 12-membered-ring mono-sugar macrolide methymycin, Biotechnolog, 84, 24-35

· Zimmerman E. and Yonath, A. (2009). Biological Implications of the Ribosome's Stunning Stereochemistry, ChemBioChem 10, 63-72; PMID:19089882

· Agmon I., Davidovich C., Bashan A. and Yonath, A. (2009). Identification of the prebiotic translation apparatus within the contemporary ribosome, Nature Precedings

· Davidovich, C., Bashan A. and Yonath, A. (2008). Structural basis for cross-resistance to ribosomal PTC antibiotics, Proc Natl Acad Sci U S A 105, 20665-70; PMID:19098107

· Wekselman, I., Davidovich, C., Agmon, I. Zimmerman, E., Rosenberg, H., Bashan, A., Berisio, R. and Yonath, A. (2008). Ribosome's mode of function: myths, facts and recent results, J Pept Sci 15, 122-130; PMID:19053078

· Bashan, A. and Yonath, A. (2008). The linkage between ribosomal crystallography, metal ions,heteropolytungstates and functional flexibility, J Mol Struct, 890, 289-294; PMID:19915655

· Bashan, A. and Yonath, A. (2008). Correlating ribosome function with high-resolution structures, Trends Microbiol, 16, 326-335; PMID:18547810

· Pyetan, E., Baram, D., Auerbach-Nevo T. and Yonath, A. (2007). Chemical parameters influencing fine-tuning in the binding of macrolide antibiotics to the ribosomal tunnel, Pure Appl Chem, 79, 955-968

· Davidovich, C., Bashan, A., Auerbach-Nevo, T., Yaggie, R.D., Gontarek R.R. and Yonath, A. (2007). Induced-fit tightens pleuromutilins binding to ribosomes and remote interactions enable their selectivity, Proc Natl Acad Sci USA, 104, 4291-4296; PMID:17360517

· Yonath, A. (2007). Ribosomal crystallography: peptide bond formation, chaperone assistance, and antibiotics inactivation. In: NATO Security through Science Series, Structure and Biophysics, New Technologies for Current Challenges in Biology and Beyond, J. D. Puglisi, ed. (Springer) 127–153

· Agmon, I., Bashan A. and Yonath, A. (2006). On ribosome conservation and evolution, Isr J Ecol Evol, 52, 359-74

· Yonath, A. (2006). Triggering positive competition, Nature, 444, 435-36; PMID:17122845

· Berisio, R., Corti, N., Pfister, P., Yonath A. and Bottger, E. C. (2006). 23S rRNA 2058A->G alteration mediates ketolide resistance in combination with deletion in L22, Antimicrob Agents Chemother 50, 3816-23; PMID:16923950

· Sato, N. S., Hirabayashi, N., Agmon, I., Yonath, A. and Suzuki, T. (2006). Comprehensive genetic selection revealed essential bases in the peptidyl-transferase center, Proc Natl Acad Acad Sci U S A 103, 15386-91; PMID:17032763

· Gindulyte, A., Bashan, A., Agmon, I., Massa, L., Yonath A. and Karle, J. (2006). The transition state for formation of the peptide bond in the ribosome, Proc Natl Acad Sci U S A 103, 13327-32; PMID:16938893

· Agmon, I., Bashan, A., Zarivach, R. and Yonath, A. (2005). Symmetry at the active site of the ribosome: structure and functional implications, Biol Chem 386, 833-44; PMID:16164408

· Yonath, A. (2005). Ribosomal crystallography: peptide bond formation, chaperone assistance and antibiotics activity, Mol Cells, 20, 1-16; PMID:16258236

· Baram, D, Pyetan, E., Sittner, A., Auerbach-Nevo, T., Bashan A. and Yonath, A. (2005). Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome revealed its chaperone action, Proc Natl Acad Sci USA, 102, 12017-22; PMID:16091460

· Yonath, A. (2005). Antibiotics targeting ribosomes: resistance, selectivity, synergism, and cellular regulation, Annu Rev Biochem, 74, 649-79; PMID:16180279

· Amit, M., Berisio, R., Baram, D., Harms, J., Bashan A. and Yonath, A. (2005). A crevice adjoining the ribosome tunnel: hints for cotranslational folding, FEBS Lett, 579, 3207-13; PMID:15943964

· Bashan A. and Yonath, A. (2005). Ribosome crystallography: catalysis and evolution of peptide bond formation, nascent chain elongation and its cotranslational folding, Biochem Soc Trans, 33, 488-92; PMID:15916549

· Auerbach-Nevo, T., Zarivach, R., Peretz M. and Yonath, A. (2005). Reproducible growth of well diffracting ribosomal crystals, Acta Crystallogr, D61 Biol Crystallogr, 713-9

· Pfister, P., Corti, N., Hobbie, S., Bruell, C., Zarivach, R. Yonath, A. and Boettger, E. C. (2005). 23S rRNA base pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A->G, Proc Natl Acad Sci USA, 102, 5180-5; PMID:15930627

· Baram D. and Yonath, A. (2005). From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects, FEBS Lett, 579, 948-54; PMID:15680980

· Schluenzen, F., Pyetan, E., Fucini, P., Yonath A. and Harms, J. M. (2004). Inhibition of peptide bond formation by Pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin, Mol Microbiol, 54, 1287-94; PMID:15554968

· Auerbach, T., Bashan, A. and Yonath, A. (2004). Ribosomal antibiotics: structural basis for resistance, synergism and selectivity, Trends Biotechnol, 22, 570-6; PMID:15491801

· Zarivach, R., Bashan, A., Berisio, R., Harms, J., Auerbach, T., Schluenzen, F., Bartels, H., Baram, D., Pyetan, E., Sittner, A., Amit, M., Hansen, H.A.S., Kessler, M., Liebe, C., Wolff, A., Agmon, I. and Yonath, A. (2004). Functional aspects of ribosomal architecture: symmetry, chirality and regulation, J Phys Org Chem, 17, 901-12

· Yonath A. and Bashan, A. (2004). Ribosomal crystallography: Initiation, peptide bond formation and amino acid polymerization are hampered by antibiotics, Annu Rev Microbiol, 58, 233-51; PMID:15487937

· Yonath A. (2004). Ribosomal crystallography: dynamics, flexibility and peptide bond formation, In: “Conformational proteomics of macromolecular architecture” ( Cheng, R.H. and Hammar, L. Eds) World Scientific Publishing, New Jersey, 12, 245-90

· Harms, J., Schluenzen, F., Fucini, P., Bartels, H. and Yonath, A. (2004). Alterations at the peptidyl transferase center of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin, BMC Biol, 2, 4;1-10; PMID:15059283

· Agmon, I., Amit, M., Auerbach, T., Bashan, A., Baram, D., Bartels, H., Berisio, R., Greenberg, I., Harms, J. Hansen, H. A.S, Kessler, M., Pyetan, E., Schluenzen, F., Sittner, A., Yonath A. and Zarivach, R. (2004). Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism, FEBS Lett, 567, 20-6; PMID:15165888

· Yonath, A. (2004). Ribosomes, the machines of life, In: "Life science for the 21st century" (E. Keinan, I. Schechter and M. Sela Eds) Wiley-VCV Press, Weinheim, Germany,1, 1-47

*· Yonath, A. (2003). David and Goliath: how do small antibiotics paralyze the giant ribosome? Keriat Benium, 1-9

· Yonath, A. (2003). Ribosomal tolerance and peptide bond formation, BioChem, 384, 1411-9; PMID:14669983

· Yonath, A. (2003). Structural insight into functional aspects of ribosomal RNA targeting, ChemBioChem, 4, 1008-17; PMID:14523918

· Bashan, A., Zarivach, R., Schluenzen, F., Agmon, I., Harms, J., Auerbach, T., Baram, D., Berisio, R., Bartels, H., Hansen, H.A.S., Fucini, P., Wilson, D., Peretz, M., Kessler M. and Yonath, A. (2003). Ribosomal crystallography: peptide bond formation and its inhibition, Biopolymers, 70,19-41; PMID:12925991

· Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H.A.S., Fucini P. and Yonath, A. (2003). Structural insight into the antibiotic action of telithromycin on resistant mutants, J. Bacteriol, 185, 4276-9; PMID:12837804

· Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., Fucini, P., Hansen, H.A.S., Harms, J., Kessler, M., Peretz, M., Schluenzen, F., Yonath A. and Zarivach, R. (2003). On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes, Eur J Biochem, 270, 2543-56; PMID:12787020

· Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram D. and Yonath, A. (2003). Structural insight into the role of the ribosomal tunnel in cellular regulation, Nat Struct Biol, 10, 366-70; PMID:12665853

· Ben-Zeev, E., Zarivach, R., Shoham, M., Yonath A. and Eisenstein, M. (2003). Prediction of the structure of the complex between the 30S ribosomal subunit and colicin E3 via weighted-geometric docking, J Biomol Struct Dyn, 20, 669-76; PMID:12643769

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· Yonath, A. and Wittmann, H.G. (1988). Crystallographic and image reconstruction studies on ribosomal particles from bacterial sources, Methods Enzymol, 164, 95-117.; PMID: 3071693

· Yonath, A. and Wittmann, H.G. (1987). Towards a molecular model for the large ribosomal prticales, In: "Mol structure, Chemical Reactivity and Biological Activity" (J. Stezowski Ed) Oxford Press, B11, 137-42.

· Arad, T., Piefke, J., Gewitz, H.S., Romberg, B., Glotz, C., Muessig, J., Yonath, A. and Wittmann, H.G. (1987). The growth of ordered two-dimensional sheets of ribosomal particles from salt-alcohol mixtures, Anal Biochem, 167, 113-7; PMID: 3434787

· Gewitz, H.S., Glotz, C., Goischke, P., Romberg, B., Muessig, J., Yonath, A. and Wittmann, H.G. (1987). Reconstitution and crystallization experiments with isolated split proteins from Bacillus stearothermophilus ribosomes, Biochem Int, 15, 887-95; PMID: 3435552

· Glotz, C., Muessig, J., Gewitz, H.S., Makowski, I., Arad, T., Yonath, A. and Wittmann, H.G. (1987). Three-dimensional crystals of ribosomes and their subunits from eu- and archaebacteria, Biochem Int, 15, 953-60; PMID:3124853

· Arad, T., Piefke, J., Weinstein, S., Gewitz, H.S., Yonath, A. and Wittmann, H.G. (1987). Three-dimensional image reconstruction from ordered arrays of 70S ribosomes, Biochimie, 69, 1001-6.

· Yonath, A., Leonard, K.R. and Wittmann, H.G.(1987). A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction, Science, 236, 813-6.

· Makowski, I., Frolow, F., Saper, M.A., Shoham, M., Wittmann, H.G. and Yonath, A. (1987). Single crystals of large ribosomal particles from Halobacterium marismortui diffract to 6 A, J Mol Biol, 193, 819-22.

· Yonath, A., Leonard, K.R., Weinstein, S. and Wittmann, H.G. (1987). Approaches to the determination of the three-dimensional architecture of ribosomal particles, Cold Spring Harb Symp Quant Biol, 52, 729-41.

· Piefke, J., Arad, T., Gewitz, H.S., Yonath, A. and Wittmann, H.G. (1986). The growth of ordered two-dimensional sheets of 70S ribosomes from Bacillus stearothermophilus, FEBS Lett, 209, 104-6.

· Yonath, A., Saper, M.A., Makowski, I., Muessig, J., Piefke, J., Bartunik, H.D., Bartels K.S. and Wittmann, H.G. (1986). Characterization of single crystals of the large ribosomal particles from Bacillus stearothermophilus, J Mol Biol, 187, 633-6.

·Yonath, A., Saper, M.A., Frolow, F., Makowski I. and Wittmann, H.G. (1986). Characterization of single crystals of the large ribosomal particles from a mutant of B. stearothermophilus, J Mol Biol, 192, 161-2.

· Yonath, A., Saper M.A. and Wittmann, H.G. (1986). Studies on crystals of intact bacterial ribosomal particles, In: "Structure, Function and Genetics of Ribosomes" (B. Hardesty and G. Kramer Eds) Springer-Verlag, NY,112-127.

· Shoham, M., Muessig, J., Shevack, A., Arad, T., Wittmann H.G. and Yonath, A. (1986). A new crystal form of large ribosomal subunits from Halobacterium marismortui, FEBS Lett, 208, 321-4

· Shevack, A., Gewitz, H.S., Hennemann, B., Yonath A. and Wittmann, H.G. (1985). Characterization and crystallization of ribosomal particles from Halobacterium marismortui, FEBS Lett, 184, 68-71.

· Wittmann, H.G. and Yonath, A. (1985). Diffraction studies on crystals of ribosomal particles, In: "The Structure and Function of the Genetic Apparatus" (C. Nicollini and P. Ts'o Eds) Plenum Press, 177-89.

· Yonath, A. (1984). Three-dimensional crystals of ribosomal particles, TIBS, 9, 227-30.

· Yonath, A., Bartunik, H.D., Bartels, K.S. and Wittmann, H.G. (1984). Some X-ray diffraction patterns from single crystals of the large ribosomal subunit from Bacillus stearothermophilus, J Mol Biol, 177, 201-6.

· Shaanan, B., Shoham, M., Yonath, A., Lis, H. and Sharon, M. (1984). Crystallization and preliminary X-ray diffraction studies of soybean agglutinin, J Mol Biol, 174, 723-5.

· Arad, T., Leonard, K., Wittmann, H.G. and A. Yonath, Two-dimensional crystalline sheets of Bacillus stearothermophilus 50S ribosomal particles, EMBO J, 3, 127-31 (1984)

· Yonath, A., Piefke, J., Muessig, J., Gewitz, H.S. and Wittmann, H.G. (1983). A compact three-dimensional crystal form of the large ribosomal subunit from Bacillus stearothermophilus, FEBS Lett, 163, 69-72.

· Talmon, J., Ranghino, G., Yonath, A.and Cohen, I.R. (1983). Structural analysis of insulin determinants seen by T cells directed by H-2 genes, Immunogenetics, 18, 79-89.

· A. Yonath, B. Tesche, S. Lorenz, J. Muessig, V.A. Erdmann and H.G. Wittmann, (1983). Several crystal forms of the Bacillus stearothermophilus 50S ribosomal particles, FEBS Lett, 154, 15-20.

· Yonath, A., Khavitch, G., Tesche, B., Muessig, J., Lorenz, S., Erdmann, V.A. and Wittmann, H.G. (1982). The nucleation of crystals of the large ribosomal subunits from Bacillus stearothermophilus, Biochem Int, 5, 629-36.

· Wittmann, H.G, Muessig, .J., Piefke, J., Gewitz, H.S., Rheinberger, H.J. and Yonath, A. (1982). Crystallization of Escherichia coli ribosomes, FEBS Lett, 146, 217-20.

· Yonath, A., Muessig, J. and Wittmann, H.G. (1982). Parameters for crystal growth of ribosomal subunits, J Cell Biochem, 19, 145-55

· Leonard, K.R, . Arad, T., Tesche, B., Erdmann, V.A., Wittmann, H.G. and Yonath, A. (1982). Crystallization, electron microscopy and three-dimensional reconstruction studies of ribosomal subunits, In: "Electron Microscopy 1982", Offizin Paul Hartung, Hamburg, 3, 9-15.

· K. Appelt, J. Dijk, R. Reinhardt, S. Sanhuesa, S.W. White, K.S. Wilson and A. Yonath, (1981). The crystallization of ribosomal proteins from the 50S subunit of the Escherichia coli and Bacillus stearothermophilus ribosome, J Biol Chem, 256, 11787-90.

· Ranghino, G., Talmon, J., Yonath, A.and Cohen, I.R. (1981). The conformation of antigenic determinants of insulin and H-2 gene control of the immune response of T lymphocytes, In: "Structural Aspects of Recognition and Assembly in Biological Macromolecules" (M. Balaban Ed) Balaban ISS, Rehovot and Philadelphia, 1, 263-79.

· A. Yonath, J. Muessig, B. Tesche, S. Lorenz, V.A. Erdmann and H.G. Wittmann, (1980). Crystallization of the large ribosomal subunit from B. stearothermophilus, Biochem Int, 1, 428-35.

· Sielecki, A. and Yonath, A. (1980). Conformational adjustment to substrate binding in crystals of triclinic lysozyme, In: "Biomolecular Structure, Conformation, Function and Evolution" (R. Srinivasan Ed) Pergamon Press, Oxford, NY, 1, 201-4.

· Keith, C., Feldmann, D., Jones, E.O., Deganello, S., Yonath, A. and Sigler P.B. (1979). Crystallographic structure analysis of a dimeric phospholipase at 2.5 A resolution, J Supramol Structure, S3, 118.

· Yonath, A. (1979). Some structural aspects of subunit interactions in proteins, J de Chimie Physique, 76, 827-29.

· Sussman, J.L., Zipori, P., Harel, M., Yonath, A. and Werber, M.M. (1979). Preliminary X-ray diffraction studies on 2 Fe-ferredoxin from Halobacterium of the Dead Sea, J Mol Biol, 134, 375-7.

· M. Shoham, A. Yonath, J.L. Sussman, J. Moult, W. Traub and A.J. Kalb, (1979). Crystal structure of demetallized concanavalin A: the metal-binding region, J Mol Biol, 131, 137-55.

· Zelano, J.A., Westbrook, E. Yonath, A., Druyan, M.E. and Sigler, P.B. (1979). Crystalline cholera toxin shows five-fold molecular symmetry, In: "Molecular Mechanisms of Biological Recognition" (M. Balaban Ed) Elsevier/North Holland, 157-63.

· . Sigler, P.B, Druyan, M.E., Zelano, J., Yonath, A., Kiefer, H.C. and Finkelstein, R.A. (1978). Cholera toxin crystals suitable for X-ray diffraction, J Supramol Structure, S2, 342.

· Shoham, M., Sussman, J.L. Yonath, A., Moult, J., Traub, W. and Kalb, A.J. (1978). The effect of binding of metal ions on the 3-dimensional structure of demetallized concanavalin A, FEBS Lett, 95, 54-6.

· Yonath, A., Podjarny, A., Honig, B., Traub, W., Sielecki, A., Herzberg, O. and Moult, J. (1978). Structural analysis of denaturant-protein interactions: comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme, Biophys Struct Mech, 4, 27-36.

· Traub, W., Yonath, A., Podjarny, A., Sielecki, A., Honig, B. and Moult, J. (1977). Crystallographic studies of protein folding, J Biophys 17, 134a.

· Podjarny, A.D. and Yonath, A. (1977). Use of matrix direct methods for low resolution phase extension for t-RNA, Acta Crystallogr A33, 655-661.

· Yonath, A., Sielecki, A., Moult, J., Podjarny, A. and Traub, W. (1977). Crystallographic studies of protein denaturation and renaturation. 1. Effects of denaturants on volume and X-ray pattern of cross-linked triclinic lysozyme crystals, Biochemistry, 16, 1413-7.

· Yonath, A., Podjarny, A, Honig, B., Sielecki, A. and Traub, W. (1977). Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme, Biochemistry, 16, 1418-24.

· Podjarny, A., Yonath, A. and Traub, W. (1976). Application of multivariate distribution theory to phase extension for crystalline proteins, Acta Crystallogr. A, 32, 281.

· Moult, J., Yonath, A., Traub, W., Smilansky, A., Podjarny, A., Rabinovich, D. and Saya, A. (1976). The structure of triclinic lysozyme at 2-5 A resolution, J Mol Biol, 100, 179-95.

· Yonath, A., Traub, W. and Miller, E.J. (1975). Crystallization of cyanogen bromide peptides from chick cartilage collagen, FEBS Lett, 57, 93-5

· Yonath, A., Smilansky, A. and Sharon, N. (1974). X-ray crystallographic study of binding of cobalt ion to hen egg-white lysozyme, FEBS Lett, 49, 178-80.

· Teichberg, V.I., Sharon, N., Moult, J., Smilansky, A. and Yonath, A. (1974). Binding of divalent copper ions to aspartic acid residue 52 in hen egg- white lysozyme, J Mol Biol, 87, 357-68.

· Yonath, A. (1971). Low-angle x-ray studies on striated muscle at low ionic strength, Isr J Chem 9, 4

· Arnone, A., Bier, C.J., Cotton, F.A., Day, V.W., Hazen, Jr. E.E., Richardson, D.C., Richardson, J.S. and Yonath, A. (1971). A high resolution structure of an inhibitor complex of extracellular nuclease of Staphylococcus aureus. I. Experimental procedures and chain tracing, J Biol Chem, 246, 2302-16

· Traub, W., Yonath, A. and Segal, D.M. (1969). Molecular structure of collagen, Acta Crystallogr A, 25, S199

· Segal, D.M., Traub, W. and Yonath, A. (1969). Polymers of tripeptides as collagen models. 8. X-ray studies of four polyhexapeptides, J Mol Biol, 43, 519-27.

· Yonath A. and Traub, W. (1969). Polymers of tripeptides as collagen models. IV. Structure analysis of poly(L-proly-glycyl-L-proline), J Mol Biol, 43, 461-77.

· Traub, W., Yonath, A. and Segal, D.M. (1969). On the molecular structure of collagen, Nature, 221, 914-7.

· Blauer, G. and Yonath, A. (1967). Macromolecular hemochromes: the system ferroprotoporphyrin IX- polylysine in aqueous medium, Arch Biochem Biophys, 121, 587-95.

· Traub, W. and Yonath, A. (1967). Polymers of tripeptides as collagen models. 3. Structural relationship between two forms of poly(L-prolyl-L-alanyl-glycine), J Mol Biol, 25, 351-5.

· Traub, W., Shmueli, U., Suwalsky, M. and Yonath, A. (1967). Some X-ray studies concerning the influence of solvent on polypeptide structures, In: “Conformation of Biopolymers” (G.N. Ramachandran Ed) Elsevier Madras 449-67.

· Traub, W. and Yonath, A. (1966). Structural studies of some polypeptides related to collagen, Acta Crystallogr, S21 A166.

· Traub, W. and Yonath, A. (1966). Polymers of tripeptides as collagen models. I. X-ray studies of poly(L- prolyl-glycyl-L-proline) and related polytripeptides, J Mol Biol, 16, 404-14; PMID: 5954171

· Yonath, A.,Yonath, J. and Traub, W. (1966). An x-ray investigation of the mechanochemical melting of collagen, Israel J Chem, 3, 246.

· Traub, W. and Yonath, A. (1965). X-ray studies of polypeptides of ordered amino-acid sequence related to collagen, Proc. Israel crystallography society, 3, 43.

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* Hebrew