| Year |
Citation |
Score |
| 2023 |
Defour JP, Leroy E, Dass S, Balligand T, Levy G, Brett IC, Papadopoulos N, Mouton C, Genet L, Pecquet C, Staerk J, Smith SO, Constantinescu SN. Constitutive activation and oncogenicity are mediated by loss of helical structure at the cytosolic boundary of thrombopoietin receptor mutant dimers. Elife. 12. PMID 37338955 DOI: 10.7554/eLife.81521 |
0.78 |
|
| 2021 |
Chandler B, Todd L, Smith SO. Magic angle spinning NMR of G protein-coupled receptors. Progress in Nuclear Magnetic Resonance Spectroscopy. 128: 25-43. PMID 35282868 DOI: 10.1016/j.pnmrs.2021.10.002 |
0.304 |
|
| 2020 |
Pope AL, Sanchez-Reyes OB, South K, Zaitseva E, Ziliox M, Vogel R, Reeves PJ, Smith SO. A Conserved Proline Hinge Mediates Helix Dynamics and Activation of Rhodopsin. Structure (London, England : 1993). PMID 32470317 DOI: 10.1016/J.Str.2020.05.004 |
0.418 |
|
| 2020 |
Crooks EJ, Irizarry BA, Ziliox M, Kawakami T, Victor TW, Xu F, Hojo H, Chiu K, Simmerling C, Van Nostrand WE, Smith SO, Miller LM. Copper stabilizes antiparallel β-sheet fibrils of the amyloid β40 (Aβ40)-Iowa variant. The Journal of Biological Chemistry. PMID 32376688 DOI: 10.1074/Jbc.Ra119.011955 |
0.302 |
|
| 2020 |
Levy G, Carillo S, Papoular B, Cassinat B, Zini JM, Leroy E, Varghese LN, Chachoua I, Defour JP, Smith SO, Constantinescu S. MPL Mutations in Essential Thrombocythemia Uncover A Common Path of Activation with Eltrombopag Dependent on W491. Blood. PMID 31978223 DOI: 10.1182/Blood.2019003240 |
0.354 |
|
| 2019 |
Tang TC, Kienlen-Campard P, Hu Y, Perrin F, Opsomer R, Octave JN, Constantinescu SN, Smith SO. Influence of the familial Alzheimer's disease-associated T43I mutation on the transmembrane structure and γ-secretase processing of the C99 peptide. The Journal of Biological Chemistry. PMID 30755484 DOI: 10.1074/Jbc.Ra118.006061 |
0.798 |
|
| 2019 |
Smith S, Tang T, Hu Y, Kienlen-Campard P, Constantinescu S, Octave J, Perrin F, Opsomer R. C55 13C Chemical Shifts Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27639 |
0.773 |
|
| 2018 |
Chung H, Crooks EJ, Ziliox M, Smith SO. Disaggregation of Aβ42 for Structural and Biochemical Studies. Methods in Molecular Biology (Clifton, N.J.). 1777: 321-330. PMID 29744845 DOI: 10.1007/978-1-4939-7811-3_20 |
0.338 |
|
| 2017 |
Hu Y, Kienlen-Campard P, Tang TC, Perrin F, Opsomer R, Decock M, Pan X, Octave JN, Constantinescu SN, Smith SO. β-Sheet Structure within the Extracellular Domain of C99 Regulates Amyloidogenic Processing. Scientific Reports. 7: 17159. PMID 29215043 DOI: 10.1038/S41598-017-17144-0 |
0.801 |
|
| 2017 |
Sanchez-Reyes OB, Cooke ALG, Tranter DB, Rashid D, Eilers M, Reeves PJ, Smith SO. G Protein-Coupled Receptors Contain Two Conserved Packing Clusters. Biophysical Journal. 112: 2315-2326. PMID 28591604 DOI: 10.1016/J.Bpj.2017.04.051 |
0.397 |
|
| 2016 |
Kimata N, Pope A, Eilers M, Opefi CA, Ziliox M, Hirshfeld A, Zaitseva E, Vogel R, Sheves M, Reeves PJ, Smith SO. Retinal orientation and interactions in rhodopsin reveal a two-stage trigger mechanism for activation. Nature Communications. 7: 12683. PMID 27585742 DOI: 10.1038/Ncomms12683 |
0.45 |
|
| 2016 |
Kimata N, Pope A, Sanchez-Reyes OB, Eilers M, Opefi CA, Ziliox M, Reeves PJ, Smith SO. Free backbone carbonyls mediate rhodopsin activation. Nature Structural & Molecular Biology. PMID 27376589 DOI: 10.1038/Nsmb.3257 |
0.463 |
|
| 2016 |
Decock M, Stanga S, Octave JN, Dewachter I, Smith SO, Constantinescu SN, Kienlen-Campard P. Glycines from the APP GXXXG/GXXXA Transmembrane Motifs Promote Formation of Pathogenic Aβ Oligomers in Cells. Frontiers in Aging Neuroscience. 8: 107. PMID 27242518 DOI: 10.3389/Fnagi.2016.00107 |
0.372 |
|
| 2016 |
Kimata N, Pope A, Eilers M, Opefi C, Ziliox M, Hirschfeld A, Zaitseva E, Vogel R, Sheves M, Reeves P, Smith S. 13C Chemical Shifts - Metarhodopsin II Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26813 |
0.312 |
|
| 2016 |
Kimata N, Pope A, Eilers M, Opefi C, Ziliox M, Hirschfeld A, Zaitseva E, Vogel R, Sheves M, Reeves P, Smith S. 13C Chemical Shifts rhodopsion Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26812 |
0.323 |
|
| 2016 |
Kimata N, Pope A, Sanchez-Reyes O, Eilers M, Opefi C, Ziliox M, Reeves P, Smith S. 13C Chemical shifts of free backbone carbonyls in bovine rhodopsin and Meta II Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26811 |
0.343 |
|
| 2015 |
Leroy E, Defour JP, Sato T, Dass S, Gryshkova V, Myat Marlar S, Staerk J, Constantinescu SN, Smith SO. His499 Regulates Dimerization and Prevents Oncogenic Activation by Asparagine Mutations of the Human Thrombopoietin Receptor. The Journal of Biological Chemistry. PMID 26627830 DOI: 10.1074/Jbc.M115.696534 |
0.392 |
|
| 2015 |
Decock M, El Haylani L, Stanga S, Dewachter I, Octave JN, Smith SO, Constantinescu SN, Kienlen-Campard P. Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing. Febs Open Bio. 5: 763-73. PMID 26500837 DOI: 10.1016/J.Fob.2015.09.002 |
0.368 |
|
| 2015 |
Fu Z, Aucoin D, Davis J, Van Nostrand WE, Smith SO. Mechanism of Nucleated Conformational Conversion of Aβ42. Biochemistry. 54: 4197-207. PMID 26069943 DOI: 10.1021/Acs.Biochem.5B00467 |
0.352 |
|
| 2015 |
Kimata N, Reeves PJ, Smith SO. Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 253: 111-8. PMID 25797010 DOI: 10.1016/J.Jmr.2014.12.014 |
0.434 |
|
| 2015 |
Kimata N, Pope A, Rashid D, Reeves PJ, Smith SO. Sequential structural changes in rhodopsin occurring upon photoactivation. Methods in Molecular Biology (Clifton, N.J.). 1271: 159-71. PMID 25697523 DOI: 10.1007/978-1-4939-2330-4_11 |
0.395 |
|
| 2015 |
Marinangeli C, Tasiaux B, Opsomer R, Hage S, Sodero AO, Dewachter I, Octave JN, Smith SO, Constantinescu SN, Kienlen-Campard P. Presenilin transmembrane domain 8 conserved AXXXAXXXG motifs are required for the activity of the γ-secretase complex. The Journal of Biological Chemistry. 290: 7169-84. PMID 25614624 DOI: 10.1074/Jbc.M114.601286 |
0.365 |
|
| 2014 |
Fu Z, Aucoin D, Ahmed M, Ziliox M, Van Nostrand WE, Smith SO. Capping of aβ42 oligomers by small molecule inhibitors. Biochemistry. 53: 7893-903. PMID 25422864 DOI: 10.1021/Bi500910B |
0.325 |
|
| 2014 |
Tamagaki H, Furukawa Y, Yamaguchi R, Hojo H, Aimoto S, Smith SO, Sato T. Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3. Biochemistry. 53: 5000-7. PMID 25010350 DOI: 10.1021/Bi500327Q |
0.416 |
|
| 2014 |
Tang TC, Hu Y, Kienlen-Campard P, El Haylani L, Decock M, Van Hees J, Fu Z, Octave JN, Constantinescu SN, Smith SO. Conformational changes induced by the A21G Flemish mutation in the amyloid precursor protein lead to increased Aβ production. Structure (London, England : 1993). 22: 387-96. PMID 24462250 DOI: 10.1016/J.Str.2013.12.012 |
0.795 |
|
| 2014 |
Pope A, Eilers M, Reeves PJ, Smith SO. Amino acid conservation and interactions in rhodopsin: probing receptor activation by NMR spectroscopy. Biochimica Et Biophysica Acta. 1837: 683-93. PMID 24183693 DOI: 10.1016/J.Bbabio.2013.10.007 |
0.417 |
|
| 2013 |
Opefi CA, South K, Reynolds CA, Smith SO, Reeves PJ. Retinitis pigmentosa mutants provide insight into the role of the N-terminal cap in rhodopsin folding, structure, and function. The Journal of Biological Chemistry. 288: 33912-26. PMID 24106275 DOI: 10.1074/Jbc.M113.483032 |
0.383 |
|
| 2013 |
Xu B, Chakraborty R, Eilers M, Dakshinamurti S, O'Neil JD, Smith SO, Bhullar RP, Chelikani P. High-level expression, purification and characterization of a constitutively active thromboxane A2 receptor polymorphic variant. Plos One. 8: e76481. PMID 24086743 DOI: 10.1371/Journal.Pone.0076481 |
0.366 |
|
| 2013 |
Kotarba AE, Aucoin D, Hoos MD, Smith SO, Van Nostrand WE. Fine mapping of the amyloid β-protein binding site on myelin basic protein. Biochemistry. 52: 2565-73. PMID 23510371 DOI: 10.1021/Bi4001936 |
0.368 |
|
| 2013 |
Goncalves J, Eilers M, South K, Opefi CA, Laissue P, Reeves PJ, Smith SO. Magic angle spinning nuclear magnetic resonance spectroscopy of G protein-coupled receptors. Methods in Enzymology. 522: 365-89. PMID 23374193 DOI: 10.1016/B978-0-12-407865-9.00017-0 |
0.417 |
|
| 2013 |
Defour JP, Itaya M, Gryshkova V, Brett IC, Pecquet C, Sato T, Smith SO, Constantinescu SN. Tryptophan at the transmembrane-cytosolic junction modulates thrombopoietin receptor dimerization and activation. Proceedings of the National Academy of Sciences of the United States of America. 110: 2540-5. PMID 23359689 DOI: 10.1073/Pnas.1211560110 |
0.81 |
|
| 2013 |
Matsushita C, Tamagaki H, Miyazawa Y, Aimoto S, Smith SO, Sato T. Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides. Proceedings of the National Academy of Sciences of the United States of America. 110: 1646-51. PMID 23319611 DOI: 10.1073/Pnas.1215207110 |
0.424 |
|
| 2012 |
Eilers M, Goncalves JA, Ahuja S, Kirkup C, Hirshfeld A, Simmerling C, Reeves PJ, Sheves M, Smith SO. Structural transitions of transmembrane helix 6 in the formation of metarhodopsin I. The Journal of Physical Chemistry. B. 116: 10477-89. PMID 22564141 DOI: 10.1021/Jp3019183 |
0.762 |
|
| 2012 |
Ladiwala AR, Litt J, Kane RS, Aucoin DS, Smith SO, Ranjan S, Davis J, Van Nostrand WE, Tessier PM. Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity. The Journal of Biological Chemistry. 287: 24765-73. PMID 22547072 DOI: 10.1074/Jbc.M111.329763 |
0.366 |
|
| 2012 |
Smith SO. Insights into the activation mechanism of the visual receptor rhodopsin. Biochemical Society Transactions. 40: 389-93. PMID 22435817 DOI: 10.1042/Bst20110751 |
0.356 |
|
| 2012 |
Itaya M, Brett IC, Smith SO. Synthesis, purification, and characterization of single helix membrane peptides and proteins for NMR spectroscopy. Methods in Molecular Biology (Clifton, N.J.). 831: 333-57. PMID 22167682 DOI: 10.1007/978-1-61779-480-3_18 |
0.802 |
|
| 2012 |
Defour J, Itaya M, Gryshkova V, Brett I, Pecquet C, Sato T, Smith SO, Constantinescu SN. Controlling Thrombopoietin Receptor Dimerization, Orientation and Activation Via Tryptophan 515 Blood. 120: 3449-3449. DOI: 10.1182/Blood.V120.21.3449.3449 |
0.807 |
|
| 2012 |
Hu Y, Smith SO. Structural Studies on the Similarity and Potential Interaction Between Aβ42 and Prion Peptides Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.1386 |
0.382 |
|
| 2011 |
Staerk J, Defour JP, Pecquet C, Leroy E, Antoine-Poirel H, Brett I, Itaya M, Smith SO, Vainchenker W, Constantinescu SN. Orientation-specific signalling by thrombopoietin receptor dimers. The Embo Journal. 30: 4398-413. PMID 21892137 DOI: 10.1038/Emboj.2011.315 |
0.791 |
|
| 2011 |
Arakawa M, Chakraborty R, Upadhyaya J, Eilers M, Reeves PJ, Smith SO, Chelikani P. Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β(2)-adrenergic receptor. Biochimica Et Biophysica Acta. 1808: 1170-8. PMID 21262196 DOI: 10.1016/J.Bbamem.2011.01.012 |
0.425 |
|
| 2010 |
Goncalves JA, South K, Ahuja S, Zaitseva E, Opefi CA, Eilers M, Vogel R, Reeves PJ, Smith SO. Highly conserved tyrosine stabilizes the active state of rhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 107: 19861-6. PMID 21041664 DOI: 10.1073/Pnas.1009405107 |
0.76 |
|
| 2010 |
Liao MC, Hoos MD, Aucoin D, Ahmed M, Davis J, Smith SO, Van Nostrand WE. N-terminal domain of myelin basic protein inhibits amyloid beta-protein fibril assembly. The Journal of Biological Chemistry. 285: 35590-8. PMID 20807757 DOI: 10.1074/Jbc.M110.169599 |
0.347 |
|
| 2010 |
Goncalves JA, Ahuja S, Erfani S, Eilers M, Smith SO. Structure and function of G protein-coupled receptors using NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy. 57: 159-80. PMID 20633362 DOI: 10.1016/J.Pnmrs.2010.04.004 |
0.759 |
|
| 2010 |
Khalifa NB, Van Hees J, Tasiaux B, Huysseune S, Smith SO, Constantinescu SN, Octave JN, Kienlen-Campard P. What is the role of amyloid precursor protein dimerization? Cell Adhesion & Migration. 4: 268-72. PMID 20400860 DOI: 10.4161/Cam.4.2.11476 |
0.369 |
|
| 2010 |
Ahmed M, Davis J, Aucoin D, Sato T, Ahuja S, Aimoto S, Elliott JI, Van Nostrand WE, Smith SO. Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils. Nature Structural & Molecular Biology. 17: 561-7. PMID 20383142 DOI: 10.1038/Nsmb.1799 |
0.73 |
|
| 2010 |
Smith SO. Structure and activation of the visual pigment rhodopsin. Annual Review of Biophysics. 39: 309-28. PMID 20192770 DOI: 10.1146/Annurev-Biophys-101209-104901 |
0.438 |
|
| 2010 |
Hornak V, Ahuja S, Eilers M, Goncalves JA, Sheves M, Reeves PJ, Smith SO. Light activation of rhodopsin: insights from molecular dynamics simulations guided by solid-state NMR distance restraints. Journal of Molecular Biology. 396: 510-27. PMID 20004206 DOI: 10.1016/J.Jmb.2009.12.003 |
0.759 |
|
| 2009 |
Ahuja S, Eilers M, Hirshfeld A, Yan ECY, Ziliox M, Sakmar TP, Sheves M, Smith SO. 6-s-cis conformation and polar binding pocket of the retinal chromophore in the photoactivated state of rhodopsin Journal of the American Chemical Society. 131: 15160-15169. PMID 19795853 DOI: 10.1021/Ja9034768 |
0.782 |
|
| 2009 |
Ahuja S, Smith SO. Multiple switches in G protein-coupled receptor activation. Trends in Pharmacological Sciences. 30: 494-502. PMID 19732972 DOI: 10.1016/J.Tips.2009.06.003 |
0.752 |
|
| 2009 |
Konno H, Aimoto S, Smith SO, Nosaka K, Akaji K. Synthesis of [19, 35, 36-(13)C(3)]-labeled TAK779 as a molecular probe. Bioorganic & Medicinal Chemistry. 17: 5769-74. PMID 19640721 DOI: 10.1016/J.Bmc.2009.07.026 |
0.357 |
|
| 2009 |
Plo I, Zhang Y, Le Couédic JP, Nakatake M, Boulet JM, Itaya M, Smith SO, Debili N, Constantinescu SN, Vainchenker W, Louache F, de Botton S. An activating mutation in the CSF3R gene induces a hereditary chronic neutrophilia. The Journal of Experimental Medicine. 206: 1701-7. PMID 19620628 DOI: 10.1084/Jem.20090693 |
0.604 |
|
| 2009 |
Ahuja S, Hornak V, Yan ECY, Syrett N, Goncalves JA, Hirshfeld A, Ziliox M, Sakmar TP, Sheves M, Reeves PJ, Smith SO, Eilers M. Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation Nature Structural and Molecular Biology. 16: 168-175. PMID 19182802 DOI: 10.1038/Nsmb.1549 |
0.774 |
|
| 2009 |
Ahuja S, Crocker E, Eilers M, Hornak V, Hirshfeld A, Ziliox M, Syrett N, Reeves PJ, Khorana HG, Sheves M, Smith SO. Location of the retinal chromophore in the activated state of rhodopsin*. The Journal of Biological Chemistry. 284: 10190-201. PMID 19176531 DOI: 10.1074/Jbc.M805725200 |
0.8 |
|
| 2009 |
Sato T, Tang TC, Reubins G, Fei JZ, Fujimoto T, Kienlen-Campard P, Constantinescu SN, Octave JN, Aimoto S, Smith SO. A helix-to-coil transition at the epsilon-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis. Proceedings of the National Academy of Sciences of the United States of America. 106: 1421-6. PMID 19164538 DOI: 10.1073/Pnas.0812261106 |
0.798 |
|
| 2009 |
Aucoin D, Camenares D, Zhao X, Jung J, Sato T, Smith SO. High-resolution 1H MAS RFDR NMR of biological membranes Journal of Magnetic Resonance. 197: 77-86. PMID 19121592 DOI: 10.1016/J.Jmr.2008.12.009 |
0.35 |
|
| 2009 |
Itaya M, Brett IC, Liu W, Constantinescu SN, Smith S. Structure of the Transmembrane Dimer of gp55-P of the Spleen Focus Forming Virus and its Interaction with the Erythropoietin Receptor Biophysical Journal. 96: 336a. DOI: 10.1016/J.Bpj.2008.12.3811 |
0.8 |
|
| 2009 |
Tang T, Sato T, Kienlen-Campard P, Constantinescu SN, Octave J, Smith SO. A Helix-to-Coil Transition in the Transmembrane Dimer of the Amyloid Precursor Protein is Required for Proteolysis by γ-Secretase Biophysical Journal. 96: 335a. DOI: 10.1016/J.Bpj.2008.12.3806 |
0.803 |
|
| 2009 |
Smith SO. Molecular Mechanism of Rhodopsin Photoactivation Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.3587 |
0.452 |
|
| 2009 |
Aucoin D, Camenares D, Smith S. Penetration of Aromatic Residues into Membrane Bilayers: A New Approach Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.2331 |
0.388 |
|
| 2008 |
Kienlen-Campard P, Tasiaux B, Van Hees J, Li M, Huysseune S, Sato T, Fei JZ, Aimoto S, Courtoy PJ, Smith SO, Constantinescu SN, Octave JN. Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs. The Journal of Biological Chemistry. 283: 7733-44. PMID 18201969 DOI: 10.1074/Jbc.M707142200 |
0.381 |
|
| 2007 |
Liu W, Fei JZ, Kawakami T, Smith SO. Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52. Biochimica Et Biophysica Acta. 1768: 2971-8. PMID 17996192 DOI: 10.1016/J.Bbamem.2007.10.011 |
0.366 |
|
| 2007 |
Chelikani P, Hornak V, Eilers M, Reeves PJ, Smith SO, RajBhandary UL, Khorana HG. Role of group-conserved residues in the helical core of beta2-adrenergic receptor. Proceedings of the National Academy of Sciences of the United States of America. 104: 7027-32. PMID 17438264 DOI: 10.1073/Pnas.0702024104 |
0.423 |
|
| 2006 |
Sato T, Pallavi P, Golebiewska U, McLaughlin S, Smith SO. Structure of the membrane reconstituted transmembrane-juxtamembrane peptide EGFR(622-660) and its interaction with Ca2+/calmodulin. Biochemistry. 45: 12704-14. PMID 17042488 DOI: 10.1021/Bi061264M |
0.404 |
|
| 2006 |
Sato T, Kienlen-Campard P, Ahmed M, Liu W, Li H, Elliott JI, Aimoto S, Constantinescu SN, Octave JN, Smith SO. Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42. Biochemistry. 45: 5503-16. PMID 16634632 DOI: 10.1021/Bi052485F |
0.347 |
|
| 2006 |
Mastrangelo IA, Ahmed M, Sato T, Liu W, Wang C, Hough P, Smith SO. High-resolution atomic force microscopy of soluble Abeta42 oligomers. Journal of Molecular Biology. 358: 106-19. PMID 16499926 DOI: 10.1016/J.Jmb.2006.01.042 |
0.303 |
|
| 2006 |
Crocker E, Eilers M, Ahuja S, Hornak V, Hirshfeld A, Sheves M, Smith SO. Location of Trp265 in metarhodopsin II: implications for the activation mechanism of the visual receptor rhodopsin. Journal of Molecular Biology. 357: 163-72. PMID 16414074 DOI: 10.1016/J.Jmb.2005.12.046 |
0.804 |
|
| 2006 |
Staerk J, Lacout C, Sato T, Smith SO, Vainchenker W, Constantinescu SN. An amphipathic motif at the transmembrane-cytoplasmic junction prevents autonomous activation of the thrombopoietin receptor. Blood. 107: 1864-71. PMID 16249382 DOI: 10.1182/Blood-2005-06-2600 |
0.385 |
|
| 2006 |
Smith SO. GPCR dimerization, a handbook Trends in Endocrinology and Metabolism. 17: 176. DOI: 10.1016/J.Tem.2006.05.002 |
0.366 |
|
| 2006 |
Zhang W, Sato T, Smith SO. NMR spectroscopy of basic/aromatic amino acid clusters in membrane proteins Progress in Nuclear Magnetic Resonance Spectroscopy. 48: 183-199. DOI: 10.1016/J.Pnmrs.2006.04.002 |
0.317 |
|
| 2005 |
Zhang W, Smith SO. Mechanism of penetration of Antp(43-58) into membrane bilayers. Biochemistry. 44: 10110-8. PMID 16042388 DOI: 10.1021/Bi050341V |
0.378 |
|
| 2005 |
Anderson LL, Marshall GR, Crocker E, Smith SO, Baranski TJ. Motion of carboxyl terminus of Galpha is restricted upon G protein activation. A solution NMR study using semisynthetic Galpha subunits. The Journal of Biological Chemistry. 280: 31019-26. PMID 15983037 DOI: 10.1074/Jbc.M503690200 |
0.809 |
|
| 2005 |
Eilers M, Hornak V, Smith SO, Konopka JB. Comparison of class A and D G protein-coupled receptors: common features in structure and activation. Biochemistry. 44: 8959-75. PMID 15966721 DOI: 10.1021/Bi047316U |
0.402 |
|
| 2005 |
McLaughlin S, Smith SO, Hayman MJ, Murray D. An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. The Journal of General Physiology. 126: 41-53. PMID 15955874 DOI: 10.1085/Jgp.200509274 |
0.366 |
|
| 2005 |
Liu W, Crocker E, Constantinescu SN, Smith SO. Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus. Biophysical Journal. 89: 1194-202. PMID 15894629 DOI: 10.1529/Biophysj.104.057844 |
0.788 |
|
| 2005 |
Patel AB, Crocker E, Reeves PJ, Getmanova EV, Eilers M, Khorana HG, Smith SO. Changes in interhelical hydrogen bonding upon rhodopsin activation. Journal of Molecular Biology. 347: 803-12. PMID 15769471 DOI: 10.1016/J.Jmb.2005.01.069 |
0.78 |
|
| 2005 |
Howard KP, Liu W, Crocker E, Nanda V, Lear J, Degrado WF, Smith SO. Rotational orientation of monomers within a designed homo-oligomer transmembrane helical bundle. Protein Science : a Publication of the Protein Society. 14: 1019-24. PMID 15741331 DOI: 10.1110/Ps.041110605 |
0.803 |
|
| 2005 |
Liu W, Crocker E, Zhang W, Elliott JI, Luy B, Li H, Aimoto S, Smith SO. Structural role of glycine in amyloid fibrils formed from transmembrane α-helices Biochemistry. 44: 3591-3597. PMID 15736968 DOI: 10.1021/Bi047827G |
0.798 |
|
| 2005 |
Kubatzky KF, Liu W, Goldgraben K, Simmerling C, Smith SO, Constantinescu SN. Structural requirements of the extracellular to transmembrane domain junction for erythropoietin receptor function. The Journal of Biological Chemistry. 280: 14844-54. PMID 15657048 DOI: 10.1074/Jbc.M411251200 |
0.418 |
|
| 2004 |
Patel AB, Crocker E, Eilers M, Hirshfeld A, Sheves M, Smith SO. Coupling of retinal isomerization to the activation of rhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 101: 10048-53. PMID 15220479 DOI: 10.1073/Pnas.0402848101 |
0.81 |
|
| 2004 |
Gambhir A, Hangyás-Mihályné G, Zaitseva I, Cafiso DS, Wang J, Murray D, Pentyala SN, Smith SO, McLaughlin S. Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins. Biophysical Journal. 86: 2188-207. PMID 15041659 DOI: 10.1016/S0006-3495(04)74278-2 |
0.383 |
|
| 2004 |
Liu W, Eilers M, Patel AB, Smith SO. Helix Packing Moments Reveal Diversity and Conservation in Membrane Protein Structure Journal of Molecular Biology. 337: 713-729. PMID 15019789 DOI: 10.1016/J.Jmb.2004.02.001 |
0.632 |
|
| 2004 |
Crocker E, Patel AB, Eilers M, Jayaraman S, Getmanova E, Reeves PJ, Ziliox M, Khorana HG, Sheves M, Smith SO. Dipolar assisted rotational resonance NMR of tryptophan and tyrosine in rhodopsin. Journal of Biomolecular Nmr. 29: 11-20. PMID 15017136 DOI: 10.1023/B:Jnmr.0000019521.79321.3C |
0.805 |
|
| 2004 |
Getmanova E, Patel AB, Klein-Seetharaman J, Loewen MC, Reeves PJ, Friedman N, Sheves M, Smith SO, Khorana HG. NMR spectroscopy of phosphorylated wild-type rhodopsin: mobility of the phosphorylated C-terminus of rhodopsin in the dark and upon light activation. Biochemistry. 43: 1126-33. PMID 14744159 DOI: 10.1021/Bi030120U |
0.619 |
|
| 2003 |
Seubert N, Royer Y, Staerk J, Kubatzky KF, Moucadel V, Krishnakumar S, Smith SO, Constantinescu SN. Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer. Molecular Cell. 12: 1239-50. PMID 14636581 DOI: 10.1016/S1097-2765(03)00389-7 |
0.41 |
|
| 2003 |
Zhang W, Crocker E, McLaughlin S, Smith SO. Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. The Journal of Biological Chemistry. 278: 21459-66. PMID 12670959 DOI: 10.1074/Jbc.M301652200 |
0.805 |
|
| 2003 |
Liu W, Crocker E, Siminovitch DJ, Smith SO. Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A. Biophysical Journal. 84: 1263-71. PMID 12547806 DOI: 10.1016/S0006-3495(03)74941-8 |
0.808 |
|
| 2003 |
Lin JC, Parrish W, Eilers M, Smith SO, Konopka JB. Aromatic residues at the extracellular ends of transmembrane domains 5 and 6 promote ligand activation of the G protein-coupled alpha-factor receptor. Biochemistry. 42: 293-301. PMID 12525156 DOI: 10.1021/Bi026766O |
0.402 |
|
| 2002 |
Schobert B, Cupp-Vickery J, Hornak V, Smith S, Lanyi J. Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. Journal of Molecular Biology. 321: 715-26. PMID 12206785 DOI: 10.1016/S0022-2836(02)00681-2 |
0.371 |
|
| 2002 |
Irusta PM, Luo Y, Bakht O, Lai CC, Smith SO, DiMaio D. Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor beta receptor. The Journal of Biological Chemistry. 277: 38627-34. PMID 12181311 DOI: 10.1074/Jbc.M204890200 |
0.379 |
|
| 2002 |
Smith SO, Smith C, Shekar S, Peersen O, Ziliox M, Aimoto S. Transmembrane interactions in the activation of the Neu receptor tyrosine kinase Biochemistry. 41: 9321-9332. PMID 12135353 DOI: 10.1021/Bi012117L |
0.486 |
|
| 2002 |
Eilers M, Patel AB, Liu W, Smith SO. Comparison of helix interactions in membrane and soluble alpha-bundle proteins. Biophysical Journal. 82: 2720-36. PMID 11964258 DOI: 10.1016/S0006-3495(02)75613-0 |
0.614 |
|
| 2002 |
Smith SO, Eilers M, Song D, Crocker E, Ying W, Groesbeek M, Metz G, Ziliox M, Aimoto S. Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer. Biophysical Journal. 82: 2476-86. PMID 11964235 DOI: 10.1016/S0006-3495(02)75590-2 |
0.814 |
|
| 2002 |
Eilers M, Ying W, Reeves PJ, Khorana HG, Smith SO. Magic angle spinning nuclear magnetic resonance of isotopically labeled rhodopsin. Methods in Enzymology. 343: 212-22. PMID 11675791 DOI: 10.1016/S0076-6879(02)43137-0 |
0.4 |
|
| 2001 |
Smith SO, Kawakami T, Liu W, Ziliox M, Aimoto S. Helical structure of phospholamban in membrane bilayers. Journal of Molecular Biology. 313: 1139-1148. PMID 11700069 DOI: 10.1006/Jmbi.2001.5101 |
0.431 |
|
| 2001 |
Smith SO, Song D, Shekar S, Groesbeek M, Ziliox M, Aimoto S. Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers. Biochemistry. 40: 6553-6558. PMID 11380249 DOI: 10.1021/Bi010357V |
0.415 |
|
| 2000 |
Eilers M, Shekar SC, Shieh T, Smith SO, Fleming PJ. Internal packing of helical membrane proteins. Proceedings of the National Academy of Sciences of the United States of America. 97: 5796-801. PMID 10823938 DOI: 10.1073/Pnas.97.11.5796 |
0.349 |
|
| 2000 |
Ying W, Irvine SE, Beekman RA, Siminovitch aDJ, Smith SO. Deuterium NMR Reveals Helix Packing Interactions in Phospholamban Journal of the American Chemical Society. 122: 11125-11128. DOI: 10.1021/Ja994111D |
0.403 |
|
| 1999 |
Javadpour MM, Eilers M, Groesbeek M, Smith SO. Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophysical Journal. 77: 1609-18. PMID 10465772 DOI: 10.1016/S0006-3495(99)77009-8 |
0.417 |
|
| 1999 |
Constantinescu SN, Liu X, Beyer W, Fallon A, Shekar S, Henis YI, Smith SO, Lodish HF. Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domain Embo Journal. 18: 3334-3347. PMID 10369674 DOI: 10.1093/Emboj/18.12.3334 |
0.349 |
|
| 1999 |
Klein O, Kegler-Ebo D, Su J, Smith S, DiMaio D. The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells Journal of Virology. 73: 3264-3272. PMID 10074180 DOI: 10.1128/Jvi.73.4.3264-3272.1999 |
0.365 |
|
| 1999 |
Eilers M, Reeves PJ, Ying W, Khorana HG, Smith SO. Magic angle spinning NMR of the protonated retinylidene Schiff base nitrogen in rhodopsin: expression of 15N-lysine- and 13C-glycine-labeled opsin in a stable cell line. Proceedings of the National Academy of Sciences of the United States of America. 96: 487-92. PMID 9892660 DOI: 10.1073/Pnas.96.2.487 |
0.413 |
|
| 1998 |
Surti T, Klein O, Aschheim K, DiMaio D, Smith SO. Structural models of the bovine papillomavirus E5 protein Proteins: Structure, Function and Genetics. 33: 601-612. PMID 9849943 DOI: 10.1002/(Sici)1097-0134(19981201)33:4<601::Aid-Prot12>3.0.Co;2-I |
0.364 |
|
| 1998 |
Klein O, Polack GW, Surti T, Kegler-Ebo D, Smith SO, Dimaio D. Role of glutamine 17 of the bovine papillomavirus E5 protein in platelet-derived growth factor receptor activation and cell transformation Journal of Virology. 72: 8921-8932. PMID 9765437 DOI: 10.1128/Jvi.72.11.8921-8932.1998 |
0.371 |
|
| 1998 |
Han M, Smith SO, Sakmar TP. Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6 Biochemistry. 37: 8253-8261. PMID 9609722 DOI: 10.1021/Bi980147R |
0.442 |
|
| 1998 |
Han M, Groesbeek M, Smith SO, Sakmar TP. Role of the C9 methyl group in rhodopsin activation: Characterization of mutant opsins with the artificial chromophore 11-cis-9-demethylretinal Biochemistry. 37: 538-545. PMID 9425074 DOI: 10.1021/Bi972060W |
0.432 |
|
| 1997 |
Sansom MS, Smith GR, Smart OS, Smith SO. Channels formed by the transmembrane helix of phospholamban: a simulation study. Biophysical Chemistry. 69: 269-81. PMID 9474759 DOI: 10.1016/S0301-4622(97)00109-9 |
0.301 |
|
| 1997 |
Han M, Groesbeek M, Sakmar TP, Smith SO. The C9 methyl group of retinal interacts with glycine-121 in rhodopsin Proceedings of the National Academy of Sciences of the United States of America. 94: 13442-13447. PMID 9391044 DOI: 10.1073/Pnas.94.25.13442 |
0.427 |
|
| 1997 |
Petti LM, Reddy V, Smith SO, Dimaio D. Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein. Journal of Virology. 71: 7318-7327. PMID 9311809 DOI: 10.1128/Jvi.71.10.7318-7327.1997 |
0.384 |
|
| 1997 |
Han M, Lou J, Nakanishi K, Sakmar TP, Smith SO. Partial agonist activity of 11-cis-retinal in rhodopsin mutants Journal of Biological Chemistry. 272: 23081-23085. PMID 9287308 DOI: 10.1074/Jbc.272.37.23081 |
0.396 |
|
| 1997 |
Arkin IT, Adams PD, Brünger AT, Smith SO, Engelman DM. Structural perspectives of phospholamban, a helical transmembrane pentamer. Annual Review of Biophysics and Biomolecular Structure. 26: 157-79. PMID 9241417 DOI: 10.1146/Annurev.Biophys.26.1.157 |
0.334 |
|
| 1997 |
Shieh T, Han M, Sakmar TP, Smith SO. The steric trigger in rhodopsin activation Journal of Molecular Biology. 269: 373-384. PMID 9199406 DOI: 10.1006/Jmbi.1997.1035 |
0.431 |
|
| 1997 |
Arkin IT, Adams PD, Brünger AT, Aimoto S, Engelman DM, Smith SO. Structure of the transmembrane cysteine residues in phospholamban. The Journal of Membrane Biology. 155: 199-206. PMID 9050443 DOI: 10.1007/S002329900172 |
0.419 |
|
| 1997 |
Metz G, Ziliox M, Smith SO. Towards quantitative CP-MAS NMR. Solid State Nuclear Magnetic Resonance. 7: 155-60. PMID 9050152 DOI: 10.1016/S0926-2040(96)01257-X |
0.304 |
|
| 1996 |
Smith SO, Aschheim K, Groesbeek M. Magic angle spinning NMR spectroscopy of membrane proteins. Quarterly Reviews of Biophysics. 29: 395-449. PMID 9080549 DOI: 10.1017/S0033583500005898 |
0.34 |
|
| 1996 |
Han M, Lin SW, Minkova M, Smith SO, Sakmar TP. Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant Journal of Biological Chemistry. 271: 32337-32342. PMID 8943296 DOI: 10.1074/Jbc.271.50.32337 |
0.418 |
|
| 1996 |
Han M, Lin SW, Smith SO, Sakmar TP. The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin Journal of Biological Chemistry. 271: 32330-32336. PMID 8943295 DOI: 10.1074/Jbc.271.50.32330 |
0.418 |
|
| 1996 |
Sanders CR, Czerski L, Vinogradova O, Badola P, Song D, Smith SO. Escherichia coli diacylglycerol kinase is an α-helical polytopic membrane protein and can spontaneously insert into preformed lipid vesicles Biochemistry. 35: 8610-8618. PMID 8679623 DOI: 10.1021/Bi9604892 |
0.363 |
|
| 1996 |
Smith SO, Smith CS, Bormann BJ. Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor. Nature Structural & Molecular Biology. 3: 252-258. PMID 8605627 DOI: 10.1038/Nsb0396-252 |
0.425 |
|
| 1996 |
Arkin IT, MacKenzie KR, Fisher L, Aimoto S, Engelman DM, Smith SO. Mapping the lipid-exposed surfaces of membrane proteins. Nature Structural Biology. 3: 240-3. PMID 8605625 DOI: 10.1038/Nsb0396-240 |
0.382 |
|
| 1995 |
Smith SO, Bormann BJ. Determination of helix-helix interactions in membranes by rotational resonance NMR. Proceedings of the National Academy of Sciences of the United States of America. 92: 488-491. PMID 7831316 DOI: 10.1073/Pnas.92.2.488 |
0.427 |
|
| 1995 |
Han M, Smith SO. NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin. Biochemistry. 34: 1425-32. PMID 7827090 DOI: 10.1021/Bi00004A037 |
0.432 |
|
| 1995 |
Arkin IT, Rothman M, Ludlam CF, Aimoto S, Engelman DM, Rothschild KJ, Smith SO. Structural model of the phospholamban ion channel complex in phospholipid membranes. Journal of Molecular Biology. 248: 824-34. PMID 7752243 DOI: 10.1006/Jmbi.1995.0263 |
0.385 |
|
| 1995 |
Han M, Smith SO. High-resolution structural studies of the retinal--Glu113 interaction in rhodopsin. Biophysical Chemistry. 56: 23-9. PMID 7662866 DOI: 10.1016/0301-4622(95)00011-L |
0.413 |
|
| 1995 |
Smith SO. Nuclear magnetic resonance studies on the structure and function of rhodopsin Behavioral and Brain Sciences. 18: 488. DOI: 10.1017/S0140525X00039467 |
0.347 |
|
| 1994 |
Smith SO, Jonas R, Braiman M, Bormann BJ. Structure and orientation of the transmembrane domain of glycophorin A in lipid bilayers. Biochemistry. 33: 6334-41. PMID 8193149 DOI: 10.1021/Bi00186A037 |
0.697 |
|
| 1994 |
Smith SO, Hamilton J, Salmon A, Bormann BJ. Rotational resonance NMR determination of intra- and intermolecular distance constraints in dipalmitoylphosphatidylcholine bilayers. Biochemistry. 33: 6327-6333. PMID 8193148 DOI: 10.1021/Bi00186A036 |
0.417 |
|
| 1993 |
Han M, DeDecker BS, Smith SO. Localization of the retinal protonated Schiff base counterion in rhodopsin. Biophysical Journal. 65: 899-906. PMID 8105993 DOI: 10.1016/S0006-3495(93)81117-2 |
0.391 |
|
| 1993 |
Tycko R, Smith SO. Symmetry principles in the design of pulse sequences for structural measurements in magic angle spinning nuclear magnetic resonance The Journal of Chemical Physics. 98: 932-943. DOI: 10.1063/1.465078 |
0.318 |
|
| 1993 |
Smith SO. Magic angle spinning NMR methods for internuclear distance measurements Current Opinion in Structural Biology. 3: 755-759. DOI: 10.1016/0959-440X(93)90060-X |
0.346 |
|
| 1993 |
Peersen OB, Smith SO. Rotational resonance NMR of biological membranes Concepts in Magnetic Resonance. 5: 303-317. DOI: 10.1002/Cmr.1820050403 |
0.413 |
|
| 1992 |
Smith SO, Peersen OB. Solid-state NMR approaches for studying membrane protein structure. Annual Review of Biophysics and Biomolecular Structure. 21: 25-47. PMID 1525470 DOI: 10.1146/Annurev.Bb.21.060192.000325 |
0.354 |
|
| 1992 |
Smith SO, Kustanovich I, Bhamidipati S, Salmon A, Hamilton JA. Interfacial conformation of dipalmitoylglycerol and dipalmitoylphosphatidylcholine in phospholipid bilayers. Biochemistry. 31: 11660-4. PMID 1445903 DOI: 10.1021/Bi00161A054 |
0.412 |
|
| 1992 |
Smith SO, de Groot H, Gebhard R, Lugtenburg J. Magic angle spinning NMR studies on the metarhodopsin II intermediate of bovine rhodopsin: evidence for an unprotonated Schiff base. Photochemistry and Photobiology. 56: 1035-9. PMID 1337211 DOI: 10.1111/J.1751-1097.1992.Tb09726.X |
0.399 |
|
| 1992 |
Peersen OB, Yoshimura S, Hojo H, Aimoto S, Smith SO. Rotational resonance NMR measurements of internuclear distances in an .alpha.-helical peptide Journal of the American Chemical Society. 114: 4332-4335. DOI: 10.1021/Ja00037A044 |
0.379 |
|
| 1991 |
Smith SO, Courtin J, de Groot H, Gebhard R, Lugtenburg J. 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin. Biochemistry. 30: 7409-15. PMID 1649627 DOI: 10.1021/Bi00244A007 |
0.387 |
|
| 1990 |
Smith SO, Palings I, Miley ME, Courtin J, de Groot H, Lugtenburg J, Mathies RA, Griffin RG. Solid-state NMR studies of the mechanism of the opsin shift in the visual pigment rhodopsin. Biochemistry. 29: 8158-64. PMID 2261469 DOI: 10.1021/Bi00487A025 |
0.517 |
|
| 1990 |
de Groot HJ, Smith SO, Courtin J, van den Berg E, Winkel C, Lugtenburg J, Griffin RG, Herzfeld J. Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin. Biochemistry. 29: 6873-83. PMID 2168744 DOI: 10.1021/Bi00481A017 |
0.366 |
|
| 1990 |
Herzfeld J, Das Gupta SK, Farrar MR, Harbison GS, McDermott AE, Pelletier SL, Raleigh DP, Smith SO, Winkel C, Lugtenburg J. Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin. Biochemistry. 29: 5567-74. PMID 2167129 DOI: 10.1021/Bi00475A022 |
0.349 |
|
| 1989 |
Farr-Jones S, Smith SO, Kettner CA, Griffin RG, Bachovchin WW. Crystal versus solution structure of enzymes: NMR spectroscopy of a peptide boronic acid-serine protease complex in the crystalline state Proceedings of the National Academy of Sciences of the United States of America. 86: 6922-6924. PMID 2780549 DOI: 10.1073/Pnas.86.18.6922 |
0.334 |
|
| 1989 |
Smith SO, de Groot HJ, Gebhard R, Courtin JM, Lugtenburg J, Herzfeld J, Griffin RG. Structure and protein environment of the retinal chromophore in light- and dark-adapted bacteriorhodopsin studied by solid-state NMR. Biochemistry. 28: 8897-904. PMID 2605231 DOI: 10.1021/bi00448a032 |
0.307 |
|
| 1987 |
Smith SO, Palings I, Copié V, Raleigh DP, Courtin J, Pardoen JA, Lugtenburg J, Mathies RA, Griffin RG. Low-temperature solid-state 13C NMR studies of the retinal chromophore in rhodopsin. Biochemistry. 26: 1606-11. PMID 3593680 DOI: 10.1021/Bi00380A018 |
0.567 |
|
| 1987 |
Smith SO, Braiman MS, Myers AB, Pardoen JA, Courtin JML, Winkel C, Lugtenburg J, Mathies RA. Vibrational analysis of the all-trans-retinal chromophore in light-adapted bacteriorhodopsin Journal of the American Chemical Society. 109: 3108-3125. DOI: 10.1021/Ja00244A038 |
0.691 |
|
| 1987 |
Smith SO, Pardoen JA, Lugtenburg J, Mathies RA. Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin The Journal of Physical Chemistry. 91: 804-819. DOI: 10.1021/J100288A011 |
0.48 |
|
| 1987 |
SMITH SO, BRAIMAN MS, MYERS AB, PARDOEN JA, COURTIN JML, WINKEL C, LUGTENBURG J, MATHIES RA. ChemInform Abstract: Vibrational Analysis of the all-trans-Retinal Chromophore in Light-Adapted Bacteriorhodopsin Cheminform. 18. DOI: 10.1002/chin.198738046 |
0.672 |
|
| 1987 |
SMITH SO, PARDOEN JA, LUGTENBURG J, MATHIES RA. ChemInform Abstract: Vibrational Analysis of the 13-cis-Retinal Chromophore in Dark-Adapted Bacteriorhodopsin Cheminform. 18. DOI: 10.1002/chin.198725036 |
0.413 |
|
| 1986 |
Smith SO, Hornung I, van der Steen R, Pardoen JA, Braiman MS, Lugtenburg J, Mathies RA. Are C14-C15 single bond isomerizations of the retinal chromophore involved in the proton-pumping mechanism of bacteriorhodopsin? Proceedings of the National Academy of Sciences of the United States of America. 83: 967-71. PMID 3006035 DOI: 10.1073/Pnas.83.4.967 |
0.706 |
|
| 1986 |
Schmidt A, Smith SO, Raleigh DP, Roberts JE, Griffin RG, Vega S. Chemical exchange effects in the NMR spectra of rotating solids The Journal of Chemical Physics. 85: 4248-4253. DOI: 10.1063/1.451796 |
0.3 |
|
| 1986 |
LUGTENBURG J, MURADIN-SZWEYKOWSKA M, HEEREMANS C, PARDOEN JA, HARBISON GS, HERZFELD J, GRIFFIN RG, SMITH SO, MATHIES RA. ChemInform Abstract: Mechanism for the Opsin Shift of Retinal′s Absorption in Bacteriorhodopsin. Chemischer Informationsdienst. 17. DOI: 10.1002/Chin.198640067 |
0.454 |
|
| 1985 |
Harbison GS, Smith SO, Pardoen JA, Courtin JM, Lugtenburg J, Herzfeld J, Mathies RA, Griffin RG. Solid-state 13C NMR detection of a perturbed 6-s-trans chromophore in bacteriorhodopsin. Biochemistry. 24: 6955-62. PMID 4074732 DOI: 10.1021/Bi00345A031 |
0.564 |
|
| 1985 |
Smith SO, Myers AB, Mathies RA, Pardoen JA, Winkel C, van den Berg EM, Lugtenburg J. Vibrational analysis of the all-trans retinal protonated Schiff base. Biophysical Journal. 47: 653-64. PMID 4016185 DOI: 10.1016/S0006-3495(85)83961-8 |
0.542 |
|
| 1985 |
Smith SO, Lugtenburg J, Mathies RA. Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy. The Journal of Membrane Biology. 85: 95-109. PMID 4009698 DOI: 10.1007/Bf01871263 |
0.568 |
|
| 1985 |
Smith SO, Mathies RA. Resonance Raman spectra of the acidified and deionized forms of bacteriorhodopsin. Biophysical Journal. 47: 251-4. PMID 3978203 DOI: 10.1016/S0006-3495(85)83899-6 |
0.525 |
|
| 1984 |
Smith SO, Myers AB, Pardoen JA, Winkel C, Mulder PP, Lugtenburg J, Mathies R. Determination of retinal Schiff base configuration in bacteriorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 81: 2055-9. PMID 16593445 DOI: 10.1073/Pnas.81.7.2055 |
0.559 |
|
| 1984 |
Harbison GS, Smith SO, Pardoen JA, Winkel C, Lugtenburg J, Herzfeld J, Mathies R, Griffin RG. Dark-adapted bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal Schiff bases. Proceedings of the National Academy of Sciences of the United States of America. 81: 1706-9. PMID 6584904 DOI: 10.1073/Pnas.81.6.1706 |
0.553 |
|
| 1984 |
Harbison GS, Smith SO, Pardoen JA, Mulder PP, Lugtenburg J, Herzfeld J, Mathies R, Griffin RG. Solid-state 13C NMR studies of retinal in bacteriorhodopsin. Biochemistry. 23: 2662-7. PMID 6466605 DOI: 10.1021/Bi00307A019 |
0.578 |
|
| 1983 |
Smith SO, Pardoen JA, Mulder PPJ, Curry B, Lugtenburg J, Mathies R. Chromophore structure in bacteriorhodopsin's O640 photointermediate Biochemistry. 22: 6141-6148. DOI: 10.1021/Bi00295A016 |
0.444 |
|
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