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William A. Eaton - Publications

Affiliations: 
Biophysical Chemistry National Institutes of Health, Bethesda, MD 
Area:
Kinetics, dynamics, and mechanisms of protein folding
Website:
http://www.niddk.nih.gov/about-niddk/staff-directory/intramural/william-eaton/pages/research-summary.aspx

125 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
2021 Henry ER, Metaferia B, Li Q, Harper J, Best RB, Glass KE, Cellmer T, Dunkelberger EB, Conrey A, Thein SL, Bunn HF, Eaton WA. Treatment of sickle cell disease by increasing oxygen affinity of hemoglobin. Blood. PMID 34197597 DOI: 10.1182/blood.2021012070  0.478
2017 Eaton WA, Wolynes PG. Theory, simulations, and experiments show that proteins fold by multiple pathways. Proceedings of the National Academy of Sciences of the United States of America. PMID 29087352 DOI: 10.1073/Pnas.1716444114  0.359
2017 Chung HS, Eaton WA. Protein folding transition path times from single molecule FRET. Current Opinion in Structural Biology. 48: 30-39. PMID 29080467 DOI: 10.1016/J.Sbi.2017.10.007  0.435
2016 Cellmer T, Ferrone FA, Eaton WA. Universality of supersaturation in protein-fiber formation. Nature Structural & Molecular Biology. PMID 27018803 DOI: 10.1038/Nsmb.3197  0.6
2016 Truex K, Sung Chung H, Louis JM, Eaton WA. Single Molecule Fluorescence Studies of Transition Paths in DNA Hairpin Folding Biophysical Journal. 110: 635a. DOI: 10.1016/J.Bpj.2015.11.3398  0.786
2015 Chung HS, Piana-Agostinetti S, Shaw DE, Eaton WA. Structural origin of slow diffusion in protein folding. Science (New York, N.Y.). 349: 1504-10. PMID 26404828 DOI: 10.1126/Science.Aab1369  0.438
2015 Truex K, Chung HS, Louis JM, Eaton WA. Testing Landscape Theory for Biomolecular Processes with Single Molecule Fluorescence Spectroscopy. Physical Review Letters. 115: 018101. PMID 26182121 DOI: 10.1103/Physrevlett.115.018101  0.766
2015 Henry ER, Mozzarelli A, Viappiani C, Abbruzzetti S, Bettati S, Ronda L, Bruno S, Eaton WA. Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models. Biophysical Journal. 109: 1264-72. PMID 26038112 DOI: 10.1016/J.Bpj.2015.04.037  0.324
2015 Chung HS, Piana-Agostinetti S, Shaw DE, Eaton WA. Structural Origin of Landscape Roughness in Protein Folding from Single-Molecule FRET and All-Atom Molecular Dynamics Simulations Biophysical Journal. 108: 347a. DOI: 10.1016/J.Bpj.2014.11.1901  0.436
2014 Viappiani C, Abbruzzetti S, Ronda L, Bettati S, Henry ER, Mozzarelli A, Eaton WA. Experimental basis for a new allosteric model for multisubunit proteins Proceedings of the National Academy of Sciences of the United States of America. 111: 12758-12763. PMID 25139985 DOI: 10.1073/Pnas.1413566111  0.367
2014 Truex K, Chung HS, Eaton WA, Louis J. Single Molecule FRET Studies of DNA Hairpin Folding Biophysical Journal. 106: 439a. DOI: 10.1016/J.Bpj.2013.11.2475  0.787
2013 Chung HS, Cellmer T, Louis JM, Eaton WA. Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories. Chemical Physics. 422: 229-237. PMID 24443626 DOI: 10.1016/J.Chemphys.2012.08.005  0.39
2013 Chung HS, Eaton WA. Single-molecule fluorescence probes dynamics of barrier crossing Nature. 502: 685-688. PMID 24153185 DOI: 10.1038/Nature12649  0.428
2013 Henry ER, Best RB, Eaton WA. Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations Proceedings of the National Academy of Sciences of the United States of America. 110: 17880-17885. PMID 24128764 DOI: 10.1073/Pnas.1317105110  0.598
2013 Best RB, Hummer G, Eaton WA. Native contacts determine protein folding mechanisms in atomistic simulations Proceedings of the National Academy of Sciences of the United States of America. 110: 17874-17879. PMID 24128758 DOI: 10.1073/Pnas.1311599110  0.696
2013 Chung HS, Louis JM, Eaton WA. Single-Molecule FRET Shows Folding Transition Path Time for All-Alpha Protein Slowed by Internal Friction Biophysical Journal. 104: 188a. DOI: 10.1016/J.Bpj.2012.11.1060  0.453
2012 Wolynes PG, Eaton WA, Fersht AR. Chemical physics of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 109: 17770-1. PMID 23112193 DOI: 10.1073/Pnas.1215733109  0.349
2012 Boura E, Różycki B, Chung HS, Herrick DZ, Canagarajah B, Cafiso DS, Eaton WA, Hummer G, Hurley JH. Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission. Structure (London, England : 1993). 20: 874-86. PMID 22579254 DOI: 10.1016/J.Str.2012.03.008  0.482
2012 Chung HS, McHale K, Louis JM, Eaton WA. Single-molecule fluorescence experiments determine protein folding transition path times Science. 335: 981-984. PMID 22363011 DOI: 10.1126/Science.1215768  0.455
2012 Hummer G, Eaton W. Transition Path Times for DNA and RNA Folding from Force Spectroscopy Physics. 5. DOI: 10.1103/Physics.5.87  0.537
2012 Sung Chung H, Gopich IV, McHale K, Louis JM, Eaton WA. Measurement of Average Transition-Path Time for Protein Folding in Single Molecule FRET Experiments Biophysical Journal. 102: 217a-218a. DOI: 10.1016/J.Bpj.2011.11.1192  0.449
2011 Boura E, Rózycki B, Herrick DZ, Chung HS, Vecer J, Eaton WA, Cafiso DS, Hummer G, Hurley JH. Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 108: 9437-42. PMID 21596998 DOI: 10.1073/Pnas.1101763108  0.524
2011 Cellmer T, Buscaglia M, Henry ER, Hofrichter J, Eaton WA. Making connections between ultrafast protein folding kinetics and molecular dynamics simulations Proceedings of the National Academy of Sciences of the United States of America. 108: 6103-6108. PMID 21441105 DOI: 10.1073/Pnas.1019552108  0.438
2011 Chung HS, Gopich IV, McHale K, Cellmer T, Louis JM, Eaton WA. Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein Journal of Physical Chemistry A. 115: 3642-3656. PMID 20509636 DOI: 10.1021/Jp1009669  0.395
2011 Cellmer T, Buscaglia M, Henry E, Hofrichter J, Eaton W. Measuring Sub-Microsceond Protein Folding Kinetics with Independent Probes Biophysical Journal. 100: 400a. DOI: 10.1016/J.Bpj.2010.12.2378  0.439
2011 Chung HS, Gopich IV, McHale K, Louis JM, Eaton WA. Photon-By-Photon Analysis of Single Molecule Fluorescence Trajectories Determines an Upper Bound for the Transition Path Time in Protein Folding Biophysical Journal. 100: 349a. DOI: 10.1016/J.Bpj.2010.12.2104  0.447
2010 Chung HS, Louis JM, Eaton WA. Distinguishing between protein dynamics and dye photophysics in single-molecule FRET experiments Biophysical Journal. 98: 696-706. PMID 20159166 DOI: 10.1016/J.Bpj.2009.12.4322  0.393
2010 Chung HS, Gopich IV, Louis JM, McHale K, Cellmer T, Eaton WA. Photon-By-Photon Analysis of Single Molecule Fluorescence Trajectories of a Fast Folding Protein Biophysical Journal. 98: 29a-30a. DOI: 10.1016/J.Bpj.2009.12.174  0.419
2009 Vaiana SM, Best RB, Yau WM, Eaton WA, Hofrichter J. Evidence for a partially structured state of the amylin monomer Biophysical Journal. 97: 2948-2957. PMID 19948124 DOI: 10.1016/J.Bpj.2009.08.041  0.585
2009 Hoi SC, Louis JM, Eaton WA. Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories Proceedings of the National Academy of Sciences of the United States of America. 106: 11837-11844. PMID 19584244 DOI: 10.1073/Pnas.0901178106  0.454
2009 Chung HS, Louis JM, Eaton WA. Measurement of Single Molecule Folding/unfolding Trajectories Biophysical Journal. 96: 388a-389a. DOI: 10.1016/J.Bpj.2008.12.2903  0.444
2009 Vaiana SM, Best RB, Yau W, Eaton WA, Hofrichter J. Collapse Of Rat And Human Amylin From Nanosecond-resolved Intramolecular Contact Formation Biophysical Journal. 96: 319a. DOI: 10.1016/J.Bpj.2008.12.1601  0.319
2008 Kubelka J, Henry ER, Cellmer T, Hofrichter J, Eaton WA. Chemical, physical, and theoretical kinetics of an ultrafast folding protein Proceedings of the National Academy of Sciences of the United States of America. 105: 18655-18662. PMID 19033473 DOI: 10.1073/Pnas.0808600105  0.394
2008 Cellmer T, Henry ER, Hofrichter J, Eaton WA. Measuring internal friction of an ultrafast-folding protein Proceedings of the National Academy of Sciences of the United States of America. 105: 18320-18325. PMID 19020085 DOI: 10.1073/Pnas.0806154105  0.417
2008 Eaton WA, Hummer G, Zwanzig RW. A tribute to Attila Szabo. The Journal of Physical Chemistry. B. 112: 5881-91. PMID 18461907 DOI: 10.1021/Jp801687S  0.416
2008 Godoy-Ruiz R, Henry ER, Kubelka J, Hofrichter J, Muñoz V, Sanchez-Ruiz JM, Eaton WA. Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data Journal of Physical Chemistry B. 112: 5938-5949. PMID 18278894 DOI: 10.1021/Jp0757715  0.626
2008 Schuler B, Eaton WA. Protein folding studied by single-molecule FRET Current Opinion in Structural Biology. 18: 16-26. PMID 18221865 DOI: 10.1016/J.Sbi.2007.12.003  0.65
2007 Best RB, Merchant KA, Gopich IV, Schuler B, Bax A, Eaton WA. Effect of flexibility and cis residues in single-molecule FRET studies of polyproline. Proceedings of the National Academy of Sciences of the United States of America. 104: 18964-9. PMID 18029448 DOI: 10.1073/Pnas.0709567104  0.705
2007 Cellmer T, Henry ER, Kubelka J, Hofrichter J, Eaton WA. Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration Journal of the American Chemical Society. 129: 14564-14565. PMID 17983235 DOI: 10.1021/Ja0761939  0.419
2007 Eaton WA, Henry ER, Hofrichter J, Bettati S, Viappiani C, Mozzarelli A. Evolution of allosteric models for hemoglobin Iubmb Life. 59: 586-599. PMID 17701554 DOI: 10.1080/15216540701272380  0.311
2007 Merchant KA, Best RB, Louis JM, Gopich IV, Eaton WA. Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy any molecular simulations Proceedings of the National Academy of Sciences of the United States of America. 104: 1528-1533. PMID 17251351 DOI: 10.1073/Pnas.0607097104  0.628
2006 Muñoz V, Ghirlando R, Blanco FJ, Jas GS, Hofrichter J, Eaton WA. Folding and aggregation kinetics of a β-hairpin Biochemistry. 45: 7023-7035. PMID 16752893 DOI: 10.1021/Bi052556A  0.625
2006 Kubelka J, Chiu TK, Davies DR, Eaton WA, Hofrichter J. Sub-microsecond protein folding. Journal of Molecular Biology. 359: 546-53. PMID 16643946 DOI: 10.1016/J.Jmb.2006.03.034  0.421
2006 Buscaglia M, Lapidus LJ, Eaton WA, Hofrichter J. Effects of denaturants on the dynamics of loop formation in polypeptides. Biophysical Journal. 91: 276-88. PMID 16617069 DOI: 10.1529/Biophysj.105.071167  0.361
2005 Chiu TK, Kubelka J, Herbst-Irmer R, Eaton WA, Hofrichter J, Davies DR. High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein. Proceedings of the National Academy of Sciences of the United States of America. 102: 7517-22. PMID 15894611 DOI: 10.1073/Pnas.0502495102  0.348
2005 Buscaglia M, Kubelka J, Eaton WA, Hofrichter J. Determination of ultrafast protein folding rates from loop formation dynamics Journal of Molecular Biology. 347: 657-664. PMID 15755457 DOI: 10.1016/J.Jmb.2005.01.057  0.439
2005 Schuler B, Lipman EA, Steinbach PJ, Kumkell M, Eaton WA. Polyproline and the "spectroscopic ruler" revisited with single-molecule flourescence Proceedings of the National Academy of Sciences of the United States of America. 102: 2754-2759. PMID 15699337 DOI: 10.1073/Pnas.0408164102  0.614
2004 Viappiani C, Bettati S, Bruno S, Ronda L, Abbruzzetti S, Mozzarelli A, Eaton WA. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels Proceedings of the National Academy of Sciences of the United States of America. 101: 14414-14419. PMID 15385676 DOI: 10.1073/Pnas.0405987101  0.362
2004 Kubelka J, Hofrichter J, Eaton WA. The protein folding 'speed limit' Current Opinion in Structural Biology. 14: 76-88. PMID 15102453 DOI: 10.1016/J.Sbi.2004.01.013  0.391
2004 Henry ER, Eaton WA. Combinatorial modeling of protein folding kinetics: Free energy profiles and rates Chemical Physics. 307: 163-185. DOI: 10.1016/J.Chemphys.2004.06.064  0.415
2003 Lipman EA, Schuler B, Bakajin O, Eaton WA. Single-molecule measurement of protein folding kinetics Science. 301: 1233-1235. PMID 12947198 DOI: 10.1126/Science.1085399  0.636
2003 Buscaglia M, Schuler B, Lapidus LJ, Eaton WA, Hofrichter J. Kinetics of intramolecular contact formation in a denatured protein. Journal of Molecular Biology. 332: 9-12. PMID 12946342 DOI: 10.1016/S0022-2836(03)00891-X  0.63
2003 Kubelka J, Eaton WA, Hofrichter J. Experimental tests of villin subdomain folding simulations Journal of Molecular Biology. 329: 625-630. PMID 12787664 DOI: 10.1016/S0022-2836(03)00519-9  0.421
2003 Schuler B, Lipman EA, Eaton WA. Erratum: corrigendum: Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy Nature. 421: 94-94. DOI: 10.1038/Nature01291  0.592
2002 Schuler B, Lipman EA, Eaton WA. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy Nature. 419: 743-747. PMID 12384704 DOI: 10.1038/Nature01060  0.649
2002 Henry ER, Bettati S, Hofrichter J, Eaton WA. A tertiary two-state allosteric model for hemoglobin Biophysical Chemistry. 98: 149-164. PMID 12128196 DOI: 10.1016/S0301-4622(02)00091-1  0.38
2002 Lapidus LJ, Eaton WA, Hofrichter J. Measuring dynamic flexibility of the coil state of a helix-forming peptide. Journal of Molecular Biology. 319: 19-25. PMID 12051933 DOI: 10.1016/S0022-2836(02)00193-6  0.345
2002 Lapidus LJ, Steinbach PJ, Eaton WA, Szabo A, Hofrichter J. Effects of chain stiffness on the dynamics of loop formation in polypeptides. Appendix: Testing a 1-dimensional diffusion model for peptide dynamics Journal of Physical Chemistry B. 106: 11628-11640. DOI: 10.1021/Jp020829V  0.342
2001 Lapidus LJ, Eaton WA, Hofrichter J. Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass. Physical Review Letters. 87: 258101. PMID 11736610 DOI: 10.1103/Physrevlett.87.258101  0.352
2000 Hagen SJ, Eaton WA. Two-state expansion and collapse of a polypeptide Journal of Molecular Biology. 301: 1019-1027. PMID 10966803 DOI: 10.1006/Jmbi.2000.3969  0.439
2000 Eaton WA, Muñoz V, Hagen SJ, Jas GS, Lapidus LJ, Henry ER, Hofrichter J. Fast kinetics and mechanisms in protein folding. Annual Review of Biophysics and Biomolecular Structure. 29: 327-59. PMID 10940252 DOI: 10.1146/Annurev.Biophys.29.1.327  0.647
2000 Lapidus LJ, Eaton WA, Hofrichter J. Measuring the rate of intramolecular contact formation in polypeptides. Proceedings of the National Academy of Sciences of the United States of America. 97: 7220-5. PMID 10860987 DOI: 10.1073/Pnas.97.13.7220  0.326
2000 Hagen SJ, Eaton WA. Two-state expansion and collapse of a polypeptide. Journal of Molecular Biology. 297: 781-9. PMID 10731428 DOI: 10.1006/Jmbi.2000.3508  0.441
2000 Thompson PA, Muñoz V, Jas GS, Henry ER, Eaton WA, Hofrichter J. The Helix-Coil Kinetics of a Heteropeptide Journal of Physical Chemistry B. 104: 378-389.  0.554
1999 Muñoz V, Eaton WA. A simple model for calculating the kinetics of protein folding from three-dimensional structures Proceedings of the National Academy of Sciences of the United States of America. 96: 11311-11316. PMID 10500173 DOI: 10.1073/Pnas.96.20.11311  0.644
1999 Pollack L, Tate MW, Darnton NC, Knight JB, Gruner SM, Eaton WA, Austin RH. Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proceedings of the National Academy of Sciences of the United States of America. 96: 10115-7. PMID 10468571 DOI: 10.1073/Pnas.96.18.10115  0.332
1999 Eaton WA. Searching for 'downhill scenarios' in protein folding Proceedings of the National Academy of Sciences of the United States of America. 96: 5897-5899. PMID 10339514 DOI: 10.1073/Pnas.96.11.5897  0.326
1999 Eaton WA, Henry ER, Hofrichter J, Mozzarelli A. Is cooperative oxygen binding by hemoglobin really understood? Nature Structural Biology. 6: 351-8. PMID 10201404 DOI: 10.1038/7586  0.328
1999 Manoj N, Srinivas VR, Surolia A, Vijayan M, Suguna K, Ravishankar R, Schwarzenbacher R, Zeth K, Diederichs, Kostner GM, Gries A, Laggner P, Prassl R, Madhusudan, Akamine P, ... ... Eaton WA, et al. Contributory presentations/posters Journal of Biosciences. 24: 33-198. DOI: 10.1007/Bf02989373  0.568
1998 Muñoz V, Henry ER, Hofrichter J, Eaton WA. A statistical mechanical model for β-hairpin kinetics Proceedings of the National Academy of Sciences of the United States of America. 95: 5872-5879. PMID 9600886 DOI: 10.1073/Pnas.95.11.5872  0.612
1998 Eaton WA, Muñoz V, Thompson PA, Henry ER, Hofrichter J. Kinetics and Dynamics of Loops, α-Helices, β-Hairpins, and Fast-Folding Proteins Accounts of Chemical Research. 31: 745-753. DOI: 10.1021/Ar9700825  0.571
1997 Muñoz V, Thompson PA, Hofrichter J, Eaton WA. Folding dynamics and mechanism of β-hairpin formation Nature. 390: 196-199. PMID 9367160 DOI: 10.1038/36626  0.596
1997 Thompson PA, Eaton WA, Hofrichter J. Laser temperature jump study of the helix⇆coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model Biochemistry. 36: 9200-9210. PMID 9230053 DOI: 10.1021/Bi9704764  0.436
1997 Henry ER, Jones CM, Hofrichter J, Eaton WA. Can a two-state MWC allosteric model explain hemoglobin kinetics? Biochemistry. 36: 6511-6528. PMID 9174369 DOI: 10.1021/Bi9619177  0.386
1997 Chan CK, Hu Y, Takahashi S, Rousseau DL, Eaton WA, Hofrichter J. Submillisecond protein folding kinetics studied by ultrarapid mixing Proceedings of the National Academy of Sciences of the United States of America. 94: 1779-1784. PMID 9050855 DOI: 10.1073/Pnas.94.5.1779  0.419
1997 Mozzarelli A, Rivetti C, Rossi GL, Eaton WA, Henry ER. Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals Protein Science. 6: 484-489. PMID 9041656 DOI: 10.1002/Pro.5560060230  0.333
1997 Eaton WA, Muñoz V, Thompson PA, Chan CK, Hofrichter J. Submillisecond kinetics of protein folding Current Opinion in Structural Biology. 7: 10-14. PMID 9032067 DOI: 10.1016/S0959-440X(97)80003-6  0.621
1997 Hagen SJ, Hofrichter J, Eaton WA. Rate of intrachain diffusion of unfolded cytochrome c Journal of Physical Chemistry B. 101: 2352-2365. DOI: 10.1021/Jp9622997  0.361
1996 Eaton WA, Thompson PA, Chan CK, Hagen SJ, Hofrichter J. Fast events in protein folding Structure. 4: 1133-1139. PMID 8939749 DOI: 10.1016/S0969-2126(96)00121-9  0.398
1996 Chan CK, Hofrichter J, Eaton WA, Winkler JR, Gray HB. Optical triggers of protein folding Science. 274: 628-629. PMID 8928010 DOI: 10.1126/Science.274.5287.628  0.404
1996 Hagen SJ, Hofrichter J, Szabo A, Eaton WA. Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding Proceedings of the National Academy of Sciences of the United States of America. 93: 11615-11617. PMID 8876184 DOI: 10.1073/Pnas.93.21.11615  0.36
1996 Hagen SJ, Eaton WA. Nonexponential structural relaxations in proteins Journal of Chemical Physics. 104: 3395-3398. DOI: 10.1063/1.471044  0.437
1996 Hagen SJ, Hofrichter J, Eaton WA. Geminate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature Journal of Physical Chemistry. 100: 12008-12021. DOI: 10.1021/Jp960219T  0.368
1995 Hagen SJ, Hofrichter J, Eaton WA. Protein reaction kinetics in a room-temperature glass Science. 269: 959-962. PMID 7638618 DOI: 10.1126/Science.7638618  0.342
1994 Ansari A, Jones CM, Henry ER, Hofrichter J, Eaton WA. Conformational relaxation and ligand binding in myoglobin Biochemistry. 33: 5128-5145. PMID 8172888 DOI: 10.1021/Bi00183A017  0.708
1993 Ansari A, Jones CM, Henry ER, Hofrichter J, Eaton WA. Photoselection in polarized photolysis experiments on heme proteins. Biophysical Journal. 64: 852-68. PMID 8471730 DOI: 10.1016/S0006-3495(93)81446-2  0.677
1993 Rivetti C, Mozzarelli A, Rossi GL, Henry ER, Eaton WA. Oxygen binding by single crystals of hemoglobin. Biochemistry. 32: 2888-906. PMID 8457555 DOI: 10.1021/Bi00062A021  0.307
1993 Schaad O, Zhou HX, Szabo A, Eaton WA, Henry ER. Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin. Proceedings of the National Academy of Sciences of the United States of America. 90: 9547-51. PMID 8415739 DOI: 10.1073/Pnas.90.20.9547  0.366
1993 Jones CM, Henry ER, Hu Y, Chan CK, Luck SD, Bhuyan A, Roder H, Hofrichter J, Eaton WA. Fast events in protein folding initiated by nanosecond laser photolysis. Proceedings of the National Academy of Sciences of the United States of America. 90: 11860-4. PMID 8265638 DOI: 10.1073/Pnas.90.24.11860  0.38
1992 Jones CM, Ansari A, Henry ER, Christoph GW, Hofrichter J, Eaton WA. Speed of intersubunit communication in proteins. Biochemistry. 31: 6692-702. PMID 1637808 DOI: 10.1021/Bi00144A008  0.692
1992 Ansari A, Jones CM, Henry ER, Hofrichter J, Eaton WA. The role of solvent viscosity in the dynamics of protein conformational changes. Science (New York, N.Y.). 256: 1796-8. PMID 1615323 DOI: 10.1126/Science.1615323  0.673
1991 Hofrichter J, Henry ER, Szabo A, Murray LP, Ansari A, Jones CM, Coletta M, Falcioni G, Brunori M, Eaton WA. Dynamics of the quaternary conformational change in trout hemoglobin. Biochemistry. 30: 6583-98. PMID 2054357 DOI: 10.1021/Bi00240A031  0.67
1991 Eaton WA, Henry ER, Hofrichter J. Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 88: 4472-5. PMID 2034685 DOI: 10.1073/Pnas.88.10.4472  0.386
1990 Eaton WA, Hofrichter J. Sickle cell hemoglobin polymerization. Advances in Protein Chemistry. 40: 63-279. PMID 2195851 DOI: 10.1016/S0065-3233(08)60287-9  0.306
1988 Murray LP, Hofrichter J, Henry ER, Ikeda-Saito M, Kitagishi K, Yonetani T, Eaton WA. The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 85: 2151-5. PMID 3353372 DOI: 10.1073/Pnas.85.7.2151  0.35
1988 Murray LP, Hofrichter J, Henry ER, Eaton WA. Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin. Biophysical Chemistry. 29: 63-76. PMID 3282562 DOI: 10.1016/0301-4622(88)87025-X  0.395
1988 Janes SM, Dalickas GA, Eaton WA, Hochstrasser RM. Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin. Biophysical Journal. 54: 545-9. PMID 3207839 DOI: 10.1016/S0006-3495(88)82987-4  0.414
1987 Mozzarelli A, Hofrichter J, Eaton WA. Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo. Science (New York, N.Y.). 237: 500-6. PMID 3603036 DOI: 10.1126/Science.3603036  0.313
1986 Henry ER, Eaton WA, Hochstrasser RM. Molecular dynamics simulations of cooling in laser-excited heme proteins. Proceedings of the National Academy of Sciences of the United States of America. 83: 8982-6. PMID 3024159 DOI: 10.1073/Pnas.83.23.8982  0.514
1985 Hofrichter J, Henry ER, Sommer JH, Deutsch R, Ikeda-Saito M, Yonetani T, Eaton WA. Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. Biochemistry. 24: 2667-79. PMID 4027219 DOI: 10.1021/Bi00332A012  0.307
1985 Ferrone FA, Hofrichter J, Eaton WA. Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. Journal of Molecular Biology. 183: 611-31. PMID 4020873 DOI: 10.1016/0022-2836(85)90175-5  0.619
1985 Ferrone FA, Hofrichter J, Eaton WA. Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques. Journal of Molecular Biology. 183: 591-610. PMID 4020872 DOI: 10.1016/0022-2836(85)90174-3  0.612
1983 Henry ER, Sommer JH, Hofrichter J, Eaton WA. Geminate recombination of carbon monoxide to myoglobin. Journal of Molecular Biology. 166: 443-51. PMID 6854651 DOI: 10.1016/S0022-2836(83)80094-1  0.356
1983 Hofrichter J, Sommer JH, Henry ER, Eaton WA. Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity. Proceedings of the National Academy of Sciences of the United States of America. 80: 2235-9. PMID 6572974 DOI: 10.1073/Pnas.80.8.2235  0.398
1982 Coletta M, Hofrichter J, Ferrone FA, Eaton WA. Kinetics of sickle haemoglobin polymerization in single red cells. Nature. 300: 194-7. PMID 7133139 DOI: 10.1038/300194A0  0.608
1982 Sunshine HR, Hofrichter J, Ferrone FA, Eaton WA. Oxygen binding by sickle cell hemoglobin polymers. Journal of Molecular Biology. 158: 251-73. PMID 7120411 DOI: 10.1016/0022-2836(82)90432-6  0.588
1981 Eaton WA, Hofrichter J. Polarized absorption and linear dichroism spectroscopy of hemoglobin. Methods in Enzymology. 76: 175-261. PMID 7035792 DOI: 10.1016/0076-6879(81)76126-3  0.307
1980 Ferrone FA, Hofrichter J, Sunshine HR, Eaton WA. Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. Biophysical Journal. 32: 361-80. PMID 7248455 DOI: 10.1016/S0006-3495(80)84962-9  0.617
1979 Sunshine HR, Hofrichter J, Eaton WA. Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins. Journal of Molecular Biology. 133: 435-67. PMID 94101 DOI: 10.1016/0022-2836(79)90402-9  0.303
1978 Sunshine HR, Hofrichter J, Eaton WA. Requirements for therapeutic inhibition of sickle haemoglobin gelation Nature. 275: 238-240. PMID 692700 DOI: 10.1038/275238A0  0.319
1978 Greene BI, Hochstrasser RM, Weisman RB, Eaton WA. Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation. Proceedings of the National Academy of Sciences of the United States of America. 75: 5255-9. PMID 281677 DOI: 10.1073/Pnas.75.11.5255  0.609
1977 Ross PD, Hofrichter J, Eaton WA. Thermodynamics of gelation of sickle cell deoxyhemoglobin Journal of Molecular Biology. 115: 111-134. PMID 22759 DOI: 10.1016/0022-2836(77)90093-6  0.312
1976 Eaton WA, Hofrichter J, Ross PD, Tschudin RG, Becker ED. Comparison of sickle cell hemoglobin gelation kinetics measured by NMR and optical methods. Biochemical and Biophysical Research Communications. 69: 538-47. PMID 1267801 DOI: 10.1016/0006-291X(76)90554-4  0.337
1976 Hofrichter J, Ross PD, Eaton WA. Supersaturation in sickle cell hemoglobin solutions Proceedings of the National Academy of Sciences of the United States of America. 73: 3035-3039. PMID 9640 DOI: 10.1073/Pnas.73.9.3035  0.305
1975 Eaton WA, Hofrichter J, Makinen MW, Andersen RD, Ludwig ML. Optical spectra and electronic structure of flavine mononucleotide in flavodoxin crystals. Biochemistry. 14: 2146-51. PMID 1148163 DOI: 10.1021/Bi00681A016  0.628
1974 Makinen MW, Eaton WA. Optically detected conformational changes in haemoglobin single crystals. Nature. 247: 62-4. PMID 4808946 DOI: 10.1038/247062A0  0.632
1974 Hofrichter J, Ross PD, Eaton WA. Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease Proceedings of the National Academy of Sciences of the United States of America. 71: 4864-4868. PMID 4531026 DOI: 10.1073/Pnas.71.12.4864  0.35
1973 Hofrichter J, Hendricker DG, Eaton WA. Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes Proceedings of the National Academy of Sciences of the United States of America. 70: I. PMID 4519649 DOI: 10.1073/Pnas.70.12.3604  0.313
1973 Makinen MW, Eaton WA. Polarized single crystal absorption spectra of carboxy- and oxyhemoglobin. Annals of the New York Academy of Sciences. 206: 210-22. PMID 4356180 DOI: 10.1111/J.1749-6632.1973.Tb43213.X  0.629
1970 Eaton WA, Lewis TP. Polarized single-crystal absorption spectrum of 1-methyluracil The Journal of Chemical Physics. 53: 2164-2172. PMID 5449969 DOI: 10.1063/1.1674310  0.324
1969 Eaton WA, Charney E. Near-infrared absorption and circular dichroism spectra of ferrocytochrome c: d-d transitions. The Journal of Chemical Physics. 51: 4502-5. PMID 5361549 DOI: 10.1063/1.1671818  0.569
1968 Eaton WA, Hochstrasser RM. Single-crystal spectra of ferrimyoglobin complexes in polarized light. The Journal of Chemical Physics. 49: 985-95. PMID 5679525 DOI: 10.1063/1.1670263  0.479
1967 Hanania GI, Irvine DH, Eaton WA, George P. Thermodynamic aspects of the potassium hexacyanoferrate(3)-(2) system. II. Reduction potential. The Journal of Physical Chemistry. 71: 2022-30. PMID 6047411 DOI: 10.1021/J100866A008  0.469
1967 Eaton WA, George P, Hanania GI. Thermodynamic aspects of the potassium hexacyanoferrate(III)-(II) system. I. Ion association. The Journal of Physical Chemistry. 71: 2016-21. PMID 6047410 DOI: 10.1021/J100866A007  0.459
1967 Eaton WA, Hochstrasser RM. Electronic spectrum of single crystals of ferricytochrome-c. The Journal of Chemical Physics. 46: 2533-9. PMID 6039380 DOI: 10.1063/1.1841081  0.471
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