| 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 |
0.38 |
|
| 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 |
0.51 |
|
| 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 |
0.495 |
|
| 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 |
0.501 |
|
| 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 |
0.37 |
|
| 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 |
0.508 |
|
| 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 |
0.425 |
|
| 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 |
0.507 |
|
| 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 |
0.49 |
|
| 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 |
0.474 |
|
| 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 |
0.404 |
|
| 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 |
0.51 |
|
| 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 |
0.465 |
|
| 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 |
0.451 |
|
| 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 |
0.502 |
|
| 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 |
0.483 |
|
| 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 |
0.46 |
|
| 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 |
0.494 |
|
| 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 |
0.501 |
|
| 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 |
0.49 |
|
| 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 |
0.5 |
|
| 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 |
0.456 |
|
| 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 |
0.67 |
|
| 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 |
0.659 |
|
| 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 |
0.646 |
|
| 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 |
0.668 |
|
| 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 |
0.622 |
|
| 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 |
0.656 |
|
| 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 |
0.657 |
|
| 1983 |
Akey CW, Spitsberg V, Edelstein SJ. Electron microscopy of beef heart F1-ATPase crystals. Journal of Biological Chemistry. 258: 3222-3229. PMID 6219110 |
0.638 |
|
| 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 |
0.667 |
|
| 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 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 1990 |
Poyart C, Schaad O, Kister J, Galacteros F, Edelstein SJ, Blouquit Y, Arous N. Hemoglobin Saint Mande [β102 (G4) Asn→Tyr]. Functional studies and structrual modeling reveal an altered T state European Journal of Biochemistry. 194: 343-348. PMID 2269272 DOI: 10.1111/J.1432-1033.1990.Tb15624.X |
0.297 |
|
| 2014 |
Edelstein SJ. A novel equation for cooperativity of the allosteric state function. Journal of Molecular Biology. 426: 39-42. PMID 24051418 DOI: 10.1016/J.Jmb.2013.09.010 |
0.296 |
|
| 1969 |
Goldberg ME, Edelstein SJ. Sedimentation equilibrium of paucidisperse systems. Subunit structure of complemented β-galactosidase Journal of Molecular Biology. 46: 431-436,IN5,437-440. PMID 4904100 DOI: 10.1016/0022-2836(69)90186-7 |
0.295 |
|
| 1983 |
McEwen BF, Ceska TA, Crepeau RH, Edelstein SJ. Structural changes in tubulin sheets upon removal of microtubule-associated proteins Journal of Molecular Biology. 166: 119-140. PMID 6854640 DOI: 10.1016/S0022-2836(83)80002-3 |
0.294 |
|
| 1993 |
Cretegny I, Edelstein SJ. Double strand packing in hemoglobin S fibers Journal of Molecular Biology. 230: 733-738. PMID 8478930 DOI: 10.1006/Jmbi.1993.1195 |
0.292 |
|
| 1992 |
Craescu C, Schaad O, Garel M, Rosa R, Edelstein S. Structural modeling of the human erythrocyte bisphosphoglycerate mutase Biochimie. 74: 519-526. PMID 1387804 DOI: 10.1016/0300-9084(92)90149-9 |
0.289 |
|
| 1971 |
Edelstein SJ. Extensions of the allosteric model for haemoglobin Nature. 230: 224-227. PMID 4926711 DOI: 10.1038/230224A0 |
0.287 |
|
| 1997 |
Edelstein SJ, Bardsley WG. Contributions of individual molecular species to the Hill coefficient for ligand binding by an oligomeric protein Journal of Molecular Biology. 267: 10-16. PMID 9096203 DOI: 10.1006/Jmbi.1996.0861 |
0.286 |
|
| 1992 |
Bellocq C, Andrey-Tornare I, Paunier Doret AM, Maeder B, Paturle L, Job D, Haiech J, Edelstein SJ. Purification of assembly-competent tubulin from Saccharomyces cerevisiae European Journal of Biochemistry. 210: 343-349. PMID 1446683 DOI: 10.1111/J.1432-1033.1992.Tb17427.X |
0.286 |
|
| 1989 |
Marden MC, Kister J, Poyart C, Edelstein SJ. Analysis of hemoglobin oxygen equilibrium curves are unique solutions possible? Journal of Molecular Biology. 208: 341-345. PMID 2769761 DOI: 10.1016/0022-2836(89)90393-8 |
0.285 |
|
| 2017 |
Menny A, Lefebvre SN, Schmidpeter PA, Drège E, Fourati Z, Delarue M, Edelstein SJ, Nimigean CM, Joseph D, Corringer P. Author response: Identification of a pre-active conformation of a pentameric channel receptor Elife. DOI: 10.7554/Elife.23955.029 |
0.282 |
|
| 2003 |
Edelstein SJ. John Edsall and ligand-linked subunit interactions in hemoglobin Biophysical Chemistry. 100: 117-121. PMID 12646357 DOI: 10.1016/S0301-4622(02)00270-3 |
0.281 |
|
| 1975 |
Edelstein SJ. Cooperative interactions of hemoglobin. Annual Review of Biochemistry. 44: 209-32. PMID 237460 DOI: 10.1146/Annurev.Bi.44.070175.001233 |
0.279 |
|
| 1973 |
Edelstein SJ, Telford JN, Crepeau RH. Structure of fibers of sickle cell hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 70: 1104-7. PMID 4123929 DOI: 10.1073/Pnas.70.4.1104 |
0.277 |
|
| 1988 |
Rozycki MD, Stetzkowski-Marden F, Edelstein SJ. Conservation of tubulin α-β differences in zinc-induced sheets with variations in pH and microtubule-associated protein content Journal of Ultrastructure Research and Molecular Structure Research. 98: 48-59. PMID 3351354 DOI: 10.1016/S0889-1605(88)80933-9 |
0.275 |
|
| 2015 |
Lai M, Brun D, Edelstein SJ, Le Novère N. Modulation of calmodulin lobes by different targets: an allosteric model with hemiconcerted conformational transitions. Plos Computational Biology. 11: e1004063. PMID 25611683 DOI: 10.1371/Journal.Pcbi.1004063 |
0.274 |
|
| 1984 |
Crepeau RH, Edelstein SJ. Polarity of the 14-strand fibers of sickle cell hemoglobin determined by cross-correlation methods Ultramicroscopy. 13: 11-18. PMID 6474595 DOI: 10.1016/0304-3991(84)90052-4 |
0.273 |
|
| 1987 |
Rodgers DW, Crepeau RH, Edelstein SJ. Pairings and polarities of the 14 strands in sickle cell hemoglobin fibers Proceedings of the National Academy of Sciences of the United States of America. 84: 6157-6161. PMID 3476937 DOI: 10.1073/Pnas.84.17.6157 |
0.272 |
|
| 1979 |
Edelstein SJ, Crepeau RH. Oblique alignment of hemoglobin S fibers in sickled cells Journal of Molecular Biology. 134: 851-855. PMID 537079 DOI: 10.1016/0022-2836(79)90491-1 |
0.271 |
|
| 1984 |
Ceska TA, Edelstein SJ. Three-dimensional reconstruction of tubulin in zinc-induced sheets. II. Consequences of removal of microtubule associated proteins Journal of Molecular Biology. 175: 349-370. PMID 6726813 DOI: 10.1016/0022-2836(84)90353-X |
0.269 |
|
| 1996 |
Edelstein SJ. An allosteric theory for hemoglobin incorporating asymmetric states to test the putative molecular code for cooperativity Journal of Molecular Biology. 257: 737-744. PMID 8636978 DOI: 10.1006/Jmbi.1996.0198 |
0.267 |
|
| 1974 |
Edelstein SJ. Extensions of the allosteric model for hemoglobin. II. Consequences of functional nonequivalence of the alpha and beta chains. Biochemistry. 13: 4998-5002. PMID 4433533 DOI: 10.1021/Bi00721A020 |
0.263 |
|
| 2005 |
Caburet S, Conti C, Schurra C, Lebofsky R, Edelstein SJ, Bensimon A. Human ribosomal RNA gene arrays display a broad range of palindromic structures Genome Research. 15: 1079-1085. PMID 16024823 DOI: 10.1101/Gr.3970105 |
0.262 |
|
| 1974 |
Gibson QH, Hoffman BM, Grepeau RH, Edelstein SJ, Bull C. Manganese hemoglobin: allosteric effects in stopped flow flash photolysis and sedimentation measurements. Biochemical and Biophysical Research Communications. 59: 146-51. PMID 4842296 DOI: 10.1016/S0006-291X(74)80186-5 |
0.258 |
|
| 1971 |
Edelstein SJ, Ellis GH. Observations on the labeling of fringes for ultracentrifugation with interference optics Analytical Biochemistry. 43: 89-98. PMID 5167094 DOI: 10.1016/0003-2697(71)90111-4 |
0.257 |
|
| 1998 |
Corringer P, Bertrand S, Bohler S, Edelstein S, Bertrand D, Changeux J. 25 Critical elements determining diversity in agonist binding and desensitization of neuronal nAChR Journal of Physiology-Paris. 92: 424-425. DOI: 10.1016/S0928-4257(99)80037-0 |
0.256 |
|
| 1996 |
Irminger-Finger I, Hurt E, Roebuck A, Collart MA, Edelstein SJ. MHP1, an essential gene in Saccharomyces cerevisiae required for microtubule function Journal of Cell Biology. 135: 1323-1339. PMID 8947554 DOI: 10.1083/Jcb.135.5.1323 |
0.252 |
|
| 2013 |
Poitevin F, Edelstein SJ. Corrigendum to “Derivation of the Crick–Wyman Equation for Allosteric Proteins Defining the Difference between the Number of Binding Sites and the Hill Coefficient” [J. Mol. Biol. 425 (2013) 1497–1499] Journal of Molecular Biology. 425: 3024. DOI: 10.1016/J.Jmb.2013.06.001 |
0.251 |
|
| 1985 |
Edelstein SJ. Chapter 25. Sickle Cell Anemia Annual Reports in Medicinal Chemistry. 20: 247-255. DOI: 10.1016/S0065-7743(08)61051-9 |
0.25 |
|
| 2008 |
Stefan MI, Edelstein SJ, Le Novère N. An allosteric model of calmodulin explains differential activation of PP2B and CaMKII. Proceedings of the National Academy of Sciences of the United States of America. 105: 10768-73. PMID 18669651 DOI: 10.1073/Pnas.0804672105 |
0.249 |
|
| 2013 |
Poitevin F, Edelstein SJ. Derivation of the Crick-Wyman equation for allosteric proteins defining the difference between the number of binding sites and the hill coefficient Journal of Molecular Biology. 425: 1497-1499. PMID 23518232 DOI: 10.1016/J.Jmb.2013.03.014 |
0.248 |
|
| 1998 |
Bohler S, Corringer P, Changeux J, Bertrand S, Bertrand D, Edelstein S. Regulation of desensitization by beta subunit in neuronal nAchR Journal of Physiology-Paris. 92: 414. DOI: 10.1016/S0928-4257(99)80026-6 |
0.245 |
|
| 1974 |
Crepeau RH, Hensley CP, Edelstein SJ. Analytical ultracentrifugation with absorption optics and a scanner-computer system. Applications to molecular weight measurements on interacting systems. Biochemistry. 13: 4860-5. PMID 4429669 DOI: 10.1021/Bi00720A027 |
0.241 |
|
| 2020 |
Li L, Lai M, Cole S, Le Novère N, Edelstein SJ. Neurogranin stimulates Ca2+/calmodulin-dependent kinase II by suppressing calcineurin activity at specific calcium spike frequencies. Plos Computational Biology. 16: e1006991. PMID 32049957 DOI: 10.1371/Journal.Pcbi.1006991 |
0.24 |
|
| 1976 |
Crepeau RH, Conrad RH, Edelstein SJ. UV laser scanning and fluorescence monitoring of analytical ultracentrifugation with an on-line computer system Biophysical Chemistry. 5: 27-39. PMID 963221 DOI: 10.1016/0301-4622(76)80024-5 |
0.234 |
|
| 1972 |
Hamilton MN, Edelstein SJ. Cat hemoglobin: PH-dependent cooperativity of oxygen binding Science. 178: 1104-1106. PMID 5086838 DOI: 10.1126/Science.178.4065.1104 |
0.23 |
|
| 1971 |
Thomas JO, Edelstein SJ. Molecular weights and volumes from density perturbation ultracentrifugation. application to aldolase and deoxyribonucleic acid polymerase in solutions of guanidine hydrochloride Biochemistry. 10: 477-482. PMID 5543978 DOI: 10.1021/Bi00779A020 |
0.224 |
|
| 1984 |
Alston K, Park CM, Rodgers DW, Edelstein SJ, Nagel RL. The polymerization of nickel (II) hemoglobin S under aerobic conditions Blood. 64: 556-558. PMID 6743829 DOI: 10.1182/Blood.V64.2.556.Bloodjournal642556 |
0.216 |
|
| 1973 |
Tainsky M, Edelstein SJ. Enhanced quaternary stability of beta hemoglobin in 2 M-sodium chloride. Journal of Molecular Biology. 75: 735-9. PMID 4732071 DOI: 10.1016/0022-2836(73)90304-5 |
0.211 |
|
| 2013 |
Edelstein SJ. Allosteric interactions after 50 years Journal of Molecular Biology. 425: 1391-1395. PMID 23524132 DOI: 10.1016/J.Jmb.2013.03.026 |
0.203 |
|
| 1994 |
Dumoulin A, Baudin V, Kiger L, Edelstein SJ, Marden M, Poyart C, Pagnier J. Chimeric hemoglobin subunits: Functional properties of a recombinant β/α hemoglobin Artificial Cells, Blood Substitutes, and Immobilization Biotechnology. 22: 733-738. PMID 7994395 |
0.2 |
|
| 1998 |
Kiger L, Dumoulin A, Edelstein SJ, Abraham DJ, Promé D, Poyart C, Marden MC, Pagnier J. Chimeric β-EF3-α hemoglobin (Ψ): Energetics of subunit interaction and ligand binding Biochemistry. 37: 7328-7339. PMID 9585547 DOI: 10.1021/bi972689z |
0.195 |
|
| 1975 |
Hoffman BM, Gibson QH, Bull C, Crepeau RH, Edelstein SJ, Fisher RG, McDonald MJ. Manganese-substituted hemoglobin and myoglobin. Annals of the New York Academy of Sciences. 244: 174-86. PMID 1056162 DOI: 10.1111/J.1749-6632.1975.Tb41530.X |
0.194 |
|
| 1976 |
Edelstein SJ. Sickle cell disease Nature. 260: 98-100. DOI: 10.1038/260098A0 |
0.191 |
|
| 1975 |
Edelstein SJ, Beyer WB, Eldefrawi AT, Eldefrawi ME. Molecular weight of the acetylcholine receptors of electric organs and the effect of Triton X 100 Journal of Biological Chemistry. 250: 6101-6106. PMID 1150674 |
0.19 |
|
| 1983 |
Edelstein SJ. Molecular architecture of the fibers of sickle (SS) hemoglobin. The American Journal of Pediatric Hematology/Oncology. 5: 386-9. PMID 6670718 |
0.185 |
|
| 1993 |
Baudin V, Pagnier J, Kiger L, Kister J, Schaad O, Bihoreau MT, Lacaze N, Marden MC, Edelstein SJ, Poyart C. Functional consequences of mutations at the allosteric interface in hetero- and homo-hemoglobin tetramers Protein Science. 2: 1320-1330. PMID 8401217 |
0.18 |
|
| 1987 |
Gibson QH, Edelstein SJ. Oxygen binding and subunit interaction of hemoglobin in relation to the two-state model. The Journal of Biological Chemistry. 262: 516-9. PMID 3804994 |
0.172 |
|
| 1980 |
Edelstein SJ. Structure of the fibers of hemoglobin S Texas Reports On Biology and Medicine. 221-232. PMID 7034270 |
0.171 |
|
| 1990 |
Bollag DM, Tornare I, Stalder R, Doret AMP, Rozycki MD, Edelstein SJ. Overexpression of tubulin in yeast: Differences in subunit association European Journal of Cell Biology. 51: 295-302. PMID 2190834 |
0.17 |
|
| 1987 |
Kister J, Poyart C, Edelstein SJ. An expanded two-state allosteric model for interactions of human hemoglobin a with nonsaturating concentrations of 2,3-diphosphoglycerate Journal of Biological Chemistry. 262: 12085-12091. PMID 3624249 |
0.163 |
|
| 1982 |
Crepeau RH, Fram EK, McEwen B, Akey CW, Pantaloni D, Szalay M, Edelstein SJ. IMAGE PROCESSING OF IMPERFECT PROTEIN ARRAYS: SECTIONED CRYSTALS AND TUBULIN SHEETS AND RINGS Proceedings - Electron Microscopy Society of America. 84-87. |
0.157 |
|
| 1975 |
Hensley P, Edelstein SJ, Wharton DC, Gibson QH. Conformation and spin state in methemoglobin. The Journal of Biological Chemistry. 250: 952-60. PMID 234444 |
0.15 |
|
| 1992 |
Bihoreau MT, Baudin V, Marden M, Lacaze N, Bohn B, Kister J, Schaad O, Dumoulin A, Edelstein SJ, Poyart C, Pagnier J. Steric and hydrophobic determinants of the solubilities of recombinant sickle cell hemoglobins Protein Science. 1: 145-150. PMID 1363932 |
0.142 |
|
| 1993 |
Schaad O, Vallone B, Edelstein SJ. Critical residues responsible for self-association differences of hemoglobin α and β chains: Analysis by molecular modeling Comptes Rendus De L'Academie Des Sciences - Series Iii. 316: 564-571. PMID 8019877 |
0.14 |
|
| 1976 |
Josephs R, Jarosch HS, Edelstein SJ. Polymorphism of sickle cell hemoglobin fibers. Journal of Molecular Biology. 102: 409-26. PMID 1271468 DOI: 10.1016/0022-2836(76)90324-7 |
0.134 |
|
| 1983 |
Rhoda MD, Martin J, Blouquit Y, Garel MC, Edelstein SJ, Rosa J. Sickle cell hemoglobin fiber formation strongly inhibited by the stanleyville II mutation (α78 Asn → Lys) Biochemical and Biophysical Research Communications. 111: 8-13. PMID 6681956 DOI: 10.1016/S0006-291X(83)80109-0 |
0.131 |
|
| 1970 |
Forrest G, Edelstein SJ. On the subunit structure of the cold labile adenosine triphosphatase of mitochondria Journal of Biological Chemistry. 245: 6468-6470. PMID 4249558 |
0.127 |
|
| 1980 |
Edelstein SJ. Patterns in the quinary structures of proteins. Plasticity and inequivalence of individual molecules in helical arrays of sickle cell hemoglobin and tubulin. Biophysical Journal. 32: 347-360. PMID 7248453 |
0.124 |
|
| 2009 |
Stefan MI, Edelstein SJ, Le Novère N. Computing phenomenologic Adair-Klotz constants from microscopic MWC parameters. Bmc Systems Biology. 3: 68. PMID 19602261 DOI: 10.1186/1752-0509-3-68 |
0.124 |
|
| 1987 |
Kister J, Poyart C, Edelstein SJ. Oxygen-organophosphate linkage in hemoglobin A. The double hump effect. Biophysical Journal. 52: 527-535. PMID 3676434 |
0.124 |
|
| 1986 |
Edelstein SJ, Poyart C, Blouquit Y, Kister J. Self-association of haemoglobin olympia (α2β2 20 (B2) Val → Met). A human haemoglobin bearing a substitution at the surface of the molecule Journal of Molecular Biology. 187: 277-289. PMID 3701868 DOI: 10.1016/0022-2836(86)90234-2 |
0.123 |
|
| 1975 |
Edelstein SJ, Gibson QH. The effect of functional differences in the α and β chains on the cooperativity of the oxidation reduction reaction of hemoglobin Journal of Biological Chemistry. 250: 961-965. PMID 234445 |
0.121 |
|
| 1985 |
Fullmer CS, Edelstein S, Wasserman RH. Lead-binding properties of intestinal calcium-binding proteins. The Journal of Biological Chemistry. 260: 6816-9. PMID 3997849 |
0.12 |
|
| 1975 |
Hensley P, Moffat K, Edelstein SJ. Influence of inositol hexaphosphate binding on subunit dissociation in methemoglobin Journal of Biological Chemistry. 250: 9391-9396. PMID 1194291 |
0.12 |
|
| 1993 |
Pagnier J, Bihoreau MT, Baudin V, Edelstein SJ, Poyart C. Polymerization and solubility of recombinant hemoglobins α2β2 6 Glu → Ala (Hb Makassar) and α2β2 6 Glu → Ala, 23 Val → Ile | POLYMERISATION ET SOLUBILITE DES HEMOGLOBINES RECOMBINANTES α2β2 6 GLU → ALA (HB MAKASSAR) ET α2β2 6 GLU → ALA, 23 VAL → ILE Comptes Rendus De L'Academie Des Sciences - Series Iii. 316: 431-436. PMID 8402272 |
0.116 |
|
| 1973 |
Tu SC, Edelstein SJ, McCormick DB. A modified purification method and properties of pure porcine d-amino acid oxidase Archives of Biochemistry and Biophysics. 159: 889-896. DOI: 10.1016/0003-9861(73)90532-8 |
0.114 |
|
| 1995 |
Interthal H, Bellocq C, Bähler J, Bashkirov VI, Edelstein S, Heyer WD. A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae. The Embo Journal. 14: 1057-66. PMID 7720696 DOI: 10.1002/J.1460-2075.1995.Tb07088.X |
0.113 |
|
| 1974 |
Hamilton MN, Edelstein SJ. Cat hemoglobin. pH dependence of cooperativity and ligand binding. The Journal of Biological Chemistry. 249: 1323-9. PMID 4817749 |
0.112 |
|
| 2023 |
Komatsu J, Cico A, Poncin R, Le Bohec M, Morf J, Lipin S, Graindorge A, Eckert H, Saffarian A, Cathaly L, Guérin F, Majello S, Ulveling D, Vayaboury A, Fernandez N, ... ... Edelstein S, et al. RevGel-seq: instrument-free single-cell RNA sequencing using a reversible hydrogel for cell-specific barcoding. Scientific Reports. 13: 4866. PMID 36964177 DOI: 10.1038/s41598-023-31915-y |
0.111 |
|
| 1976 |
Edelstein SJ, McEwen B, Gibson QH. Subunit dissociation in fish hemoglobins. The Journal of Biological Chemistry. 251: 7632-7. PMID 1002703 |
0.109 |
|
| 1977 |
Crepeau RH, Dykes G, Edelstein SJ. Structure of the fibers of sickle cell hemoglobin in the presence of 2,3-diphosphoglycerate. Biochemical and Biophysical Research Communications. 75: 496-502. PMID 851451 DOI: 10.1016/0006-291X(77)91069-5 |
0.099 |
|
| 1970 |
Edelstein SJ, Rehmar MJ, Olson JS, Gibson QH. Functional aspects of the subunit association-dissociation equilibria of hemoglobin. The Journal of Biological Chemistry. 245: 4372-81. PMID 5498425 |
0.096 |
|
| 2008 |
Stefan MI, Edelstein SJ, Le Novère N. An allosteric model of calmodulin explains differential activation of PP2B and CaMKII (Proceedings of the National Academy of Sciences of the United States of America (2008) 105, 31, (10768-10773) DOI: 10.1073/pnas.0804672105) Proceedings of the National Academy of Sciences of the United States of America. 105: 19024. DOI: 10.1073/pnas.0810309105 |
0.095 |
|
| 1988 |
Roberts DF, Edelstein SJ. The Sickled Cell: From Myths to Molecules. Man. 23: 563. DOI: 10.2307/2803269 |
0.088 |
|
| 1986 |
Wodak SJ, de Coen JL, Edelstein SJ, Demarne H, Beuzard Y. Modification of human hemoglobin by glutathione. III. Perturbations of hemoglobin conformation analyzed by computer modeling Journal of Biological Chemistry. 261: 14717-14724. PMID 3771549 |
0.085 |
|
| 2005 |
Edelstein SJ. Structures of the lac operon proteins | Structures des protéines de l'opéron lac Comptes Rendus - Biologies. 328: 511-513. PMID 15950159 DOI: 10.1016/j.crvi.2005.04.003 |
0.084 |
|
| 1988 |
Acquaye C, Blanchette-Mackie EJ, Reindorf C, Edelstein S, Schechter AN. Electron microscopic studies of the intracellular polymerization of sickle hemoglobin Blood Cells. 13: 359-372. PMID 3382746 |
0.076 |
|
| 1983 |
Edelstein S. Properties of the fibers of hemoglobin S Clinical Respiratory Physiology. 19: 368-369. |
0.066 |
|
| 1984 |
Fullmer CS, Brindak ME, Edelstein S, Wasserman RH. Early and direct effect of 1,25-dihydroxycholecalciferol on calcium uptake by duodena of rachitic chicks. Proceedings of the Society For Experimental Biology and Medicine. Society For Experimental Biology and Medicine (New York, N.Y.). 177: 455-8. PMID 6334856 |
0.06 |
|
| 2014 |
Edelstein SJ. A novel equation for cooperativity of the allosteric state function Journal of Molecular Biology. 426: 39-42. DOI: 10.1016/j.jmb.2013.09.010 |
0.058 |
|
| 1987 |
Lee YS, Taylor AN, Reimers TJ, Edelstein S, Fullmer CS, Wasserman RH. Calbindin-D in peripheral nerve cells is vitamin D and calcium dependent. Proceedings of the National Academy of Sciences of the United States of America. 84: 7344-8. PMID 3478696 |
0.051 |
|
| 1983 |
Edelstein SJ, Stevenson I. Sickle cell anaemia and reincarnation beliefs in Nigeria. Lancet. 2: 1140. PMID 6138668 |
0.05 |
|
| 1973 |
Thomas JO, Edelstein SJ. Observation of the dissociation of unliganded hemoglobin. II. Effect of pH, salt, and dioxane. The Journal of Biological Chemistry. 248: 2901-5. PMID 4697399 |
0.049 |
|
| 1984 |
Edelstein S, Fullmer CS, Wasserman RH. Gastrointestinal absorption of lead in chicks: involvement of the cholecalciferol endocrine system. The Journal of Nutrition. 114: 692-700. PMID 6325646 |
0.046 |
|
| 1987 |
Edelstein SJ. An alternative paradigm for hominoid evolution Human Evolution. 2: 169-174. DOI: 10.1007/BF02436404 |
0.019 |
|
| 2008 |
Edelstein SJ. The quest for acceptance Journal of Scientific Exploration. 22: 95-99. |
0.017 |
|
| 2014 |
Edelstein SJ. Of mice and men New York Review of Books. 61. |
0.01 |
|
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