Stuart J. Edelstein - Publications

Affiliations: 
1986 Biochemistry, Molecular and Cell Biology Cornell University, Ithaca, NY, United States 
 1986- Biochemistry Université de Genève, Genève, Genève, Switzerland 
Area:
hemoglobin
Website:
http://www.unige.ch/sciences/biochimie/Edelstein/cv.html

59 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2017 Menny A, Lefebvre SN, Schmidpeter PA, Drège E, Fourati Z, Delarue M, Edelstein SJ, Nimigean CM, Joseph D, Corringer PJ. Identification of a pre-active conformation of a pentameric channel receptor. Elife. 6. PMID 28294942 DOI: 10.7554/Elife.23955  0.301
2016 Edelstein SJ, Changeux JP. Biased Allostery. Biophysical Journal. 111: 902-8. PMID 27602718 DOI: 10.1016/j.bpj.2016.07.044  0.382
2015 Dutta-Roy R, Rosenmund C, Edelstein SJ, Le Novère N. Ligand-dependent opening of the multiple AMPA receptor conductance states: a concerted model. Plos One. 10: e0116616. PMID 25629405 DOI: 10.1371/Journal.Pone.0116616  0.32
2013 Prevost MS, Moraga-Cid G, Van Renterghem C, Edelstein SJ, Changeux JP, Corringer PJ. Intermediate closed state for glycine receptor function revealed by cysteine cross-linking. Proceedings of the National Academy of Sciences of the United States of America. 110: 17113-8. PMID 24085847 DOI: 10.1073/Pnas.1317009110  0.511
2013 Edelstein SJ, Le Novère N. Cooperativity of allosteric receptors. Journal of Molecular Biology. 425: 1424-32. PMID 23523898 DOI: 10.1016/J.Jmb.2013.03.011  0.347
2011 Changeux JP, Edelstein S. Conformational selection or induced fit? 50 years of debate resolved. F1000 Biology Reports. 3: 19. PMID 21941598 DOI: 10.3410/B3-19  0.496
2010 Edelstein SJ, Changeux JP. Relationships between structural dynamics and functional kinetics in oligomeric membrane receptors. Biophysical Journal. 98: 2045-52. PMID 20483311 DOI: 10.1016/J.Bpj.2010.01.050  0.502
2010 Edelstein SJ, Stefan MI, Le Novère N. Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction. Plos One. 5: e8449. PMID 20052284 DOI: 10.1371/Journal.Pone.0008449  0.307
2010 Edelstein SJ, Stefan M, Le Novère N. Ligand Depletion in vivo Modulates the Dynamic Range of Cooperative Signal Transduction Biophysical Journal. 98: 45a. DOI: 10.1016/J.Bpj.2009.12.261  0.31
2006 Changeux JP, Edelstein SJ. Allosteric receptors after 30 years Rendiconti Lincei. 17: 59-96. DOI: 10.1007/BF02904502  0.371
2005 Grutter T, de Carvalho LP, Dufresne V, Taly A, Edelstein SJ, Changeux JP. Molecular tuning of fast gating in pentameric ligand-gated ion channels. Proceedings of the National Academy of Sciences of the United States of America. 102: 18207-12. PMID 16319224 DOI: 10.1073/Pnas.0509024102  0.509
2005 Jacob F, Perrin D, Sánchez C, Monod J, Edelstein S. [The operon: a group of genes with expression coordinated by an operator. C.R.Acad. Sci. Paris 250 (1960) 1727-1729]. Comptes Rendus Biologies. 328: 514-20. PMID 15999435 DOI: 10.1016/j.crvi.2005.04.005  0.586
2005 Changeux JP, Edelstein SJ. Allosteric mechanisms of signal transduction. Science (New York, N.Y.). 308: 1424-8. PMID 15933191 DOI: 10.1126/Science.1108595  0.426
2003 Grutter T, Prado de Carvalho L, Le Novère N, Corringer PJ, Edelstein S, Changeux JP. An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors. The Embo Journal. 22: 1990-2003. PMID 12727867 DOI: 10.1093/Emboj/Cdg197  0.508
2001 Palanche T, Ilien B, Zoffmann S, Reck MP, Bucher B, Edelstein SJ, Galzi JL. The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states. The Journal of Biological Chemistry. 276: 34853-61. PMID 11459843 DOI: 10.1074/Jbc.M104363200  0.306
2001 Changeux JP, Edelstein SJ. Allosteric mechanisms in normal and pathological nicotinic acetylcholine receptors Current Opinion in Neurobiology. 11: 369-377. PMID 11399437 DOI: 10.1016/S0959-4388(00)00221-X  0.491
2001 Bohler S, Gay S, Bertrand S, Corringer PJ, Edelstein SJ, Changeux JP, Bertrand D. Desensitization of neuronal nicotinic acetylcholine receptors conferred by N-terminal segments of the beta 2 subunit. Biochemistry. 40: 2066-74. PMID 11329274 DOI: 10.1021/Bi0020022  0.475
2000 Martinez KL, Corringer PJ, Edelstein SJ, Changeux JP, Mérola F. Structural differences in the two agonist binding sites of the Torpedo nicotinic acetylcholine receptor revealed by time-resolved fluorescence spectroscopy. Biochemistry. 39: 6979-90. PMID 10841780 DOI: 10.1021/bi992811p  0.405
1998 Marden MC, Kiger L, Poyart C, Edelstein SJ. Identifying the conformational state of bi-liganded haemoglobin Cellular and Molecular Life Sciences. 54: 1365-1384. PMID 9893711 DOI: 10.1007/S000180050260  0.313
1998 Changeux JP, Edelstein SJ. Allosteric receptors after 30 years. Neuron. 21: 959-80. PMID 9856454 DOI: 10.1016/S0896-6273(00)80616-9  0.511
1998 Changeux JP, Bertrand D, Corringer PJ, Dehaene S, Edelstein S, Léna C, Le Novère N, Marubio L, Picciotto M, Zoli M. Brain nicotinic receptors: structure and regulation, role in learning and reinforcement. Brain Research. Brain Research Reviews. 26: 198-216. PMID 9651527 DOI: 10.1016/S0165-0173(97)00040-4  0.466
1998 Edelstein SJ, Changeux JP. Allosteric transitions of the acetylcholine receptor. Advances in Protein Chemistry. 51: 121-84. PMID 9615170 DOI: 10.1016/S0065-3233(08)60652-X  0.452
1998 Corringer PJ, Bertrand S, Bohler S, Edelstein SJ, Changeux JP, Bertrand D. Critical elements determining diversity in agonist binding and desensitization of neuronal nicotinic acetylcholine receptors. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 18: 648-57. PMID 9425007 DOI: 10.1523/Jneurosci.18-02-00648.1998  0.503
1997 Edelstein SJ, Schaad O, Changeux JP. Myasthenic nicotinic receptor mutant interpreted in terms of the allosteric model. Comptes Rendus De L'Acadã©Mie Des Sciences. Sã©Rie Iii, Sciences De La Vie. 320: 953-61. PMID 9587473 DOI: 10.1016/S0764-4469(97)82468-7  0.484
1997 Bertrand S, Devillers-Thiéry A, Palma E, Buisson B, Edelstein SJ, Corringer PJ, Changeux JP, Bertrand D. Paradoxical allosteric effects of competitive inhibitors on neuronal alpha7 nicotinic receptor mutants. Neuroreport. 8: 3591-6. PMID 9427332 DOI: 10.1097/00001756-199711100-00034  0.461
1997 Edelstein SJ, Schaad O, Changeux JP. Single binding versus single channel recordings: a new approach to study ionotropic receptors. Biochemistry. 36: 13755-60. PMID 9374851 DOI: 10.1021/Bi9718301  0.495
1996 Edelstein SJ, Changeux JP. Allosteric proteins after thirty years: the binding and state functions of the neuronal alpha 7 nicotinic acetylcholine receptors. Experientia. 52: 1083-90. PMID 8988250 DOI: 10.1007/Bf01952106  0.502
1996 Edelstein SJ, Schaad O, Henry E, Bertrand D, Changeux JP. A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions. Biological Cybernetics. 75: 361-79. PMID 8983160 DOI: 10.1007/S004220050302  0.491
1996 Galzi JL, Edelstein SJ, Changeux J. The multiple phenotypes of allosteric receptor mutants. Proceedings of the National Academy of Sciences of the United States of America. 93: 1853-8. PMID 8700848 DOI: 10.1073/Pnas.93.5.1853  0.501
1994 Changeux JP, Edelstein SJ. On allosteric mechanisms and acetylcholine receptors. Trends in Biochemical Sciences. 19: 399-400. PMID 7817393 DOI: 10.1016/0968-0004(94)90084-1  0.457
1990 Baudin-Chich V, Pagnier J, Marden M, Bohn B, Lacaze N, Kister J, Schaad O, Edelstein SJ, Poyart C. Enhanced polymerization of recombinant human deoxyhemoglobin β6 Glu→Ile Proceedings of the National Academy of Sciences of the United States of America. 87: 1845-1849. PMID 1968639 DOI: 10.1073/Pnas.87.5.1845  0.304
1987 Akey CW, Crepeau RH, Edelstein SJ. The innermost chorionic layer of Drosophila. II. Three-dimensional structure determination of the 90 ° crystal form by electron microscopy Journal of Molecular Biology. 193: 685-692. PMID 3112411 DOI: 10.1016/0022-2836(87)90351-2  0.672
1987 Akey CW, Edelstein SJ. The innermost chorionic layer of Drosophila. I. The role of chorin octamers in the formation of a family of interdigitating crystalline plates Journal of Molecular Biology. 193: 673-683. PMID 3112410 DOI: 10.1016/0022-2836(87)90350-0  0.661
1986 Edelstein SJ, Edsall JT. Linkage between ligand binding and the dimer-tetramer equilibrium in the Monod-Wyman-Changeux model of hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 83: 3796-800. PMID 3459157 DOI: 10.1073/Pnas.83.11.3796  0.326
1986 Akey CW, Dunn SD, Spitsberg V, Edelstein SJ. Electron microscopy of single molecules and crystals of F1-ATPases Methods in Enzymology. 434-446. PMID 2908457 DOI: 10.1016/S0076-6879(86)26043-7  0.647
1984 Akey CW, Szalay M, Edelstein SJ. Trigonal catalase crystals: a new molecular packing assignment obtained from sections preserved with tannic acid. Ultramicroscopy. 13: 103-11. PMID 6474594 DOI: 10.1016/0304-3991(84)90061-5  0.669
1984 Akey CW, Szalay M, Edelstein SJ. Trigonal catalase crystals: A new molecular packing assignment obtained from sections preserved with tannic acid Ultramicroscopy. 13: 103-111. DOI: 10.1016/0304-3991(84)90061-5  0.624
1983 Akey CW, Crepeau RH, Dunn SD, McCarty RE, Edelstein SJ. Electron microscopy and single molecule averaging of subunit-deficient F1-ATPases from Escherichia coli and spinach chloroplasts. Embo Journal. 2: 1409-1415. PMID 10872338 DOI: 10.1002/J.1460-2075.1983.Tb01599.X  0.658
1983 Akey CW, Edelstein SJ. Equivalence of the projected structure of thin catalase crystals preserved for electron microscopy by negative stain, glucose or embedding in the presence of tannic acid Journal of Molecular Biology. 163: 575-612. PMID 6842587 DOI: 10.1016/0022-2836(83)90113-4  0.659
1983 Akey CW, Spitsberg V, Edelstein SJ. Electron microscopy of beef heart F1-ATPase crystals. Journal of Biological Chemistry. 258: 3222-3229. PMID 6219110  0.64
1981 Edelstein SJ. Molecular topology in crystals and fibers of hemoglobin S Journal of Molecular Biology. 150: 557-575. PMID 7328645 DOI: 10.1016/0022-2836(81)90381-8  0.305
1981 Crepeau RH, Edelstein SJ, Szalay M, Benesch RE, Benesch R, Kwong S, Edalji R. Sickle cell hemoglobin fiber structure altered by alpha-chain mutation. Proceedings of the National Academy of Sciences of the United States of America. 78: 1406-10. PMID 6940165 DOI: 10.1073/Pnas.78.3.1406  0.302
1980 McEwen B, Edelstein SJ. Evidence for a mixed lattice in microtubules reassembled in vitro Journal of Molecular Biology. 139: 123-143. PMID 7411629 DOI: 10.1016/0022-2836(80)90300-9  0.301
1980 Akey CW, Moffat K, Wharton DC, Edelstein SJ. Characterization of crystals of a cytochrome oxidase (nitrite reductase) from Pseudomonas aeruginosa by X-ray diffraction and electron microscopy Journal of Molecular Biology. 136: 19-43. PMID 6245219 DOI: 10.1016/0022-2836(80)90364-2  0.669
1979 Tamm LK, Crepeau RH, Edelstein SJ. Three-dimensional reconstruction of tubulin in zinc-induced sheets. Journal of Molecular Biology. 130: 473-92. PMID 480360 DOI: 10.1016/0022-2836(79)90435-2  0.31
1979 Dykes GW, Crepeau RH, Edelstein SJ. Three-dimensional reconstruction of the 14-filament fibers of hemoglobin S Journal of Molecular Biology. 130: 451-472. PMID 480359 DOI: 10.1016/0022-2836(79)90434-0  0.313
1979 Garrell RL, Crepeau RH, Edelstein SJ. Cross-sectional views of hemoglobin S fibers by electron microscopy and computer modeling. Proceedings of the National Academy of Sciences of the United States of America. 76: 1140-4. PMID 286299 DOI: 10.1073/Pnas.76.3.1140  0.601
1978 Dykes G, Crepeau RH, Edelstein SJ. Three-dimensional reconstruction of the fibres of sickle cell haemoglobin Nature. 272: 506-510. PMID 692655 DOI: 10.1038/272506A0  0.311
1978 Crepeau RH, Dykes G, Garrell R, Edelstein SJ. Diameter of haemoglobin S fibres in sickled cells Nature. 274: 616-617. PMID 672997 DOI: 10.1038/274616A0  0.605
1978 Crepeau RH, McEwen B, Edelstein SJ. Differences in α and β polypeptide chains of tubulin resolved by electron microscopy with image reconstruction Proceedings of the National Academy of Sciences of the United States of America. 75: 5006-5010. PMID 283410 DOI: 10.1073/Pnas.75.10.5006  0.32
1977 Crepeau RH, McEwen B, Dykes G, Edelstein SJ. Structural studies on porcine brain tubulin in extended sheets Journal of Molecular Biology. 116: 301-315. PMID 599559 DOI: 10.1016/0022-2836(77)90218-2  0.301
1976 Gibson RE, O'Brien RD, Edelstein SJ, Thompson WR. Acetylcholine receptor oligomers from electroplax of Torpedo species Biochemistry. 15: 2377-2383. PMID 1276144 DOI: 10.1021/Bi00656A020  0.314
1973 Edelstein SJ, Schachman HK. Measurement of partial specific volume by sedimentation equilibrium in H2O-D2O solutions. Methods in Enzymology. 27: 82-98. PMID 4797942 DOI: 10.1016/S0076-6879(73)27006-4  0.517
1973 Carroll RC, Eldefrawi ME, Edelstein SJ. Studies on the structure of the acetylcholine receptor from Torpedo marmorata. Biochemical and Biophysical Research Communications. 55: 864-72. PMID 4761088 DOI: 10.1016/0006-291X(73)91224-2  0.304
1973 Schachman HK, Edelstein SJ. Ultracentrifugal studies with absorption optics and a split-beam photoelectric scanner. Methods in Enzymology. 27: 3-59. PMID 4359237 DOI: 10.1016/S0076-6879(73)27003-9  0.515
1973 Schachman HK, Edelstein SJ. [1] Ultracentrifugal studies with absorption optics and a split-beam photoelectric scanner Methods in Enzymology. 27: 3-59. DOI: 10.1016/S0076-6879(73)27003-9  0.434
1972 Edelstein SJ. An allosteric mechanism for the acetylcholine receptor Biochemical and Biophysical Research Communications. 48: 1160-1165. PMID 5066285 DOI: 10.1016/0006-291X(72)90832-7  0.307
1967 Edelstein SJ, Schachman HK. The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. The Journal of Biological Chemistry. 242: 306-11. PMID 6016615  0.452
1966 Schachman HK, Edelstein SJ. Ultracentrifuge studies with absorption optics. IV. Molecular weight determinations at the microgram level. Biochemistry. 5: 2681-705. PMID 5968578  0.455
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