| Year |
Citation |
Score |
| 2022 |
Sanchez MLK, Wiley S, Reijerse E, Lubitz W, Birrell JA, Dyer RB. Time-Resolved Infrared Spectroscopy Reveals the pH-Independence of the First Electron Transfer Step in the [FeFe] Hydrogenase Catalytic Cycle. The Journal of Physical Chemistry Letters. 13: 5986-5990. PMID 35736652 DOI: 10.1021/acs.jpclett.2c01467 |
0.664 |
|
| 2021 |
Su H, Brockman JM, Duan Y, Sen N, Chhabra H, Bazrafshan A, Blanchard AT, Meyer T, Andrews B, Doye JPK, Ke Y, Dyer RB, Salaita K. Massively Parallelized Molecular Force Manipulation with On-Demand Thermal and Optical Control. Journal of the American Chemical Society. PMID 34762807 DOI: 10.1021/jacs.1c08796 |
0.529 |
|
| 2021 |
Eller MW, Siaw HMH, Dyer RB. Stability of HA2 Prefusion Structure and pH-Induced Conformational Changes in the HA2 Domain of H3N2 Hemagglutinin. Biochemistry. PMID 34435771 DOI: 10.1021/acs.biochem.1c00551 |
0.738 |
|
| 2021 |
Kozlowski R, Zhao J, Dyer RB. Acceleration of catalysis in dihydrofolate reductase by transient, site-specific photothermal excitation. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33468677 DOI: 10.1073/pnas.2014592118 |
0.316 |
|
| 2020 |
Vansuch GE, Wu CH, Haja DK, Blair SA, Chica B, Johnson MK, Adams MWW, Dyer RB. Metal-ligand cooperativity in the soluble hydrogenase-1 from . Chemical Science. 11: 8572-8581. PMID 34123117 DOI: 10.1039/d0sc00628a |
0.78 |
|
| 2020 |
Sanchez MLK, Konecny SE, Narehood SM, Reijerse EJ, Lubitz W, Birrell JA, Dyer RB. The Laser-Induced Potential-Jump: a Method for Rapid Electron Injection into Oxidoreductase Enzymes. The Journal of Physical Chemistry. B. PMID 32924491 DOI: 10.1021/Acs.Jpcb.0C05718 |
0.683 |
|
| 2020 |
Vaughn MB, Biren C, Li Q, Ragupathi A, Dyer RB. Site-Specific Tryptophan Labels Reveal Local Microsecond-Millisecond Motions of Dihydrofolate Reductase. Molecules (Basel, Switzerland). 25. PMID 32842574 DOI: 10.3390/Molecules25173819 |
0.798 |
|
| 2020 |
Yang W, Vansuch GE, Liu Y, Jin T, Liu Q, Ge A, Sanchez MLK, K Haja D, Adams MWW, Dyer RB, Lian T. Surface ligand "liquid" to "crystalline" phase transition modulates the solar H2 production quantum efficiency of CdS nanorod/mediator/hydrogenases assemblies. Acs Applied Materials & Interfaces. PMID 32662974 DOI: 10.1021/Acsami.0C07820 |
0.768 |
|
| 2020 |
Vansuch GE, Wu C, Haja DK, Blair SA, Chica B, Johnson MK, Adams MWW, Dyer RB. Metal–ligand cooperativity in the soluble hydrogenase-1 from Pyrococcus furiosus Chemical Science. 11: 8572-8581. DOI: 10.1039/D0Sc00628A |
0.754 |
|
| 2019 |
Sanchez MLK, Sommer C, Reijerse E, Birrell JA, Lubitz W, Dyer RB. Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-resolved Infrared Spectroscopy. Journal of the American Chemical Society. PMID 31509403 DOI: 10.1021/Jacs.9B08348 |
0.691 |
|
| 2019 |
Raghunath G, Dyer RB. Kinetics of histidine-tagged protein association to nickel-decorated liposome surfaces. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 31466440 DOI: 10.1021/Acs.Langmuir.9B01700 |
0.797 |
|
| 2019 |
Deng H, Dyer RB, Callender R. Active Site Glu165 Activation in Triosephosphate Isomerase and its Deprotonation Kinetics. The Journal of Physical Chemistry. B. PMID 31013084 DOI: 10.1021/Acs.Jpcb.9B02981 |
0.374 |
|
| 2019 |
Sanchez MLK, Wu CH, Adams MWW, Dyer RB. Optimizing electron transfer from CdSe QDs to hydrogenase for photocatalytic H production. Chemical Communications (Cambridge, England). PMID 30997456 DOI: 10.1039/C9Cc01150A |
0.657 |
|
| 2018 |
Davis CM, Zanetti-Polzi L, Gruebele M, Amadei A, Dyer RB, Daidone I. A quantitative connection of experimental and simulated folding landscapes by vibrational spectroscopy. Chemical Science. 9: 9002-9011. PMID 30647892 DOI: 10.1039/C8Sc03786H |
0.754 |
|
| 2018 |
Zhao J, Su H, Vansuch GE, Liu Z, Salaita K, Dyer RB. Localized Nanoscale Heating Leads to Ultrafast Hydrogel Volume-Phase Transition. Acs Nano. PMID 30574782 DOI: 10.1021/Acsnano.8B07150 |
0.76 |
|
| 2018 |
Andrews BA, Dyer RB. Small molecule cores demonstrate non-competitive inhibition of lactate dehydrogenase. Medchemcomm. 9: 1369-1376. PMID 30151092 DOI: 10.1039/C8Md00309B |
0.305 |
|
| 2018 |
Dyer RB, Eller MW. Dynamics of hemagglutinin-mediated membrane fusion. Proceedings of the National Academy of Sciences of the United States of America. PMID 30127027 DOI: 10.1073/Pnas.1811183115 |
0.766 |
|
| 2018 |
Nagarajan S, Xiao S, Raleigh DP, Dyer RB. Heterogeneity in the Folding of Villin Headpiece Subdomain HP36. The Journal of Physical Chemistry. B. PMID 30118232 DOI: 10.1021/Acs.Jpcb.8B07683 |
0.349 |
|
| 2018 |
Peters JW, Beratan DN, Bothner B, Dyer RB, Harwood CS, Heiden ZM, Hille R, Jones AK, King PW, Lu Y, Lubner CE, Minteer SD, Mulder DW, Raugei S, Schut GJ, et al. A new era for electron bifurcation. Current Opinion in Chemical Biology. 47: 32-38. PMID 30077080 DOI: 10.1016/J.Cbpa.2018.07.026 |
0.779 |
|
| 2018 |
Kozlowski R, Ragupathi A, Dyer RB. Characterizing the Surface Coverage of Protein-Gold Nanoparticle Bioconjugates. Bioconjugate Chemistry. PMID 30004227 DOI: 10.1021/Acs.Bioconjchem.8B00366 |
0.308 |
|
| 2018 |
Siaw HMH, Raghunath G, Dyer RB. Peripheral Protein Unfolding Drives Membrane Bending. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 29925237 DOI: 10.1021/Acs.Langmuir.8B01136 |
0.763 |
|
| 2018 |
Su H, Liu Z, Liu Y, Ma VP, Blanchard A, Zhao J, Galior K, Dyer RB, Salaita K. Light-Responsive Polymer Particles as Force Clamps for the Mechanical Unfolding of Target Molecules. Nano Letters. PMID 29589759 DOI: 10.1016/J.Bpj.2018.11.2406 |
0.586 |
|
| 2018 |
Vaughn MB, Zhang J, Spiro TG, Dyer RB, Klinman JP. Activity-Related Microsecond Dynamics Revealed by Temperature-Jump Förster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase. Journal of the American Chemical Society. PMID 29323490 DOI: 10.1021/Jacs.7B12369 |
0.793 |
|
| 2017 |
Greene BL, Vansuch GE, Chica BC, Adams MWW, Dyer RB. Applications of Photogating and Time Resolved Spectroscopy to Mechanistic Studies of Hydrogenases. Accounts of Chemical Research. PMID 29083854 DOI: 10.1021/Acs.Accounts.7B00356 |
0.788 |
|
| 2017 |
Zanetti-Polzi L, Davis CM, Gruebele M, Dyer RB, Amadei A, Daidone I. Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation. Febs Letters. PMID 28881468 DOI: 10.1002/1873-3468.12836 |
0.736 |
|
| 2017 |
Reddish MJ, Callender R, Dyer RB. Resolution of Submillisecond Kinetics of Multiple Reaction Pathways for Lactate Dehydrogenase. Biophysical Journal. 112: 1852-1862. PMID 28494956 DOI: 10.1016/J.Bpj.2017.03.031 |
0.777 |
|
| 2017 |
Jeong BS, Dyer RB. Proton Transport Mechanism of M2 Proton Channel Studied by Laser Induced pH-jump. Journal of the American Chemical Society. PMID 28467842 DOI: 10.1021/Jacs.7B00617 |
0.315 |
|
| 2017 |
Davis CM, Reddish MJ, Dyer RB. Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics. Spectrochimica Acta. Part a, Molecular and Biomolecular Spectroscopy. 178: 185-191. PMID 28189834 DOI: 10.1016/J.Saa.2017.01.069 |
0.786 |
|
| 2017 |
Chica B, Wu C, Liu Y, Adams MWW, Lian T, Dyer RB. Balancing electron transfer rate and driving force for efficient photocatalytic hydrogen production in CdSe/CdS nanorod–[NiFe] hydrogenase assemblies Energy & Environmental Science. 10: 2245-2255. DOI: 10.1039/C7Ee01738C |
0.759 |
|
| 2017 |
Greene BL, Schut GJ, Adams MWW, Dyer RB. Pre-Steady-State Kinetics of Catalytic Intermediates of an [FeFe]-Hydrogenase Acs Catalysis. 7: 2145-2150. DOI: 10.1021/Acscatal.6B03276 |
0.694 |
|
| 2017 |
Hew Ming Siaw H, Raghunath G, Dyer RB. Steric Pressure from Peripheral Protein Conformational Changes Drives Membrane Curvature Biophysical Journal. 112: 229a. DOI: 10.1016/J.Bpj.2016.11.1260 |
0.778 |
|
| 2016 |
Greene BL, Vansuch GE, Wu CH, Adams MW, Dyer RB. Glutamate Gated Proton-Coupled Electron Transfer Activity of a [NiFe]-Hydrogenase. Journal of the American Chemical Society. PMID 27617712 DOI: 10.1021/Jacs.6B07789 |
0.786 |
|
| 2016 |
Schuler EE, Nagarajan S, Dyer RB. Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes. The Journal of Physical Chemistry Letters. PMID 27513014 DOI: 10.1021/Acs.Jpclett.6B01512 |
0.791 |
|
| 2016 |
Greene BL, Wu CH, Vansuch GE, Adams MW, Dyer RB. Proton Inventory and Dynamics in the Nia-S to Nia-C Transition of a [NiFe]-Hydrogenase. Biochemistry. PMID 26956769 DOI: 10.1021/Acs.Biochem.5B01348 |
0.79 |
|
| 2016 |
Reddish MJ, Vaughn MB, Fu R, Dyer RB. Ligand-Dependent Conformational Dynamics of Dihydrofolate Reductase. Biochemistry. 55: 1485-93. PMID 26901612 DOI: 10.1021/Acs.Biochem.5B01364 |
0.797 |
|
| 2016 |
Karahalis GJ, Thangavel A, Chica B, Bacsa J, Dyer RB, Scarborough CC. Synthesis and Catalytic Reactivity of a Dicopper(II) μ-η(2):η(2)-Peroxo Species Supported by 1,4,7-Tri-tert-butyl-1,4,7-triazacyclononane. Inorganic Chemistry. PMID 26789550 DOI: 10.1021/Acs.Inorgchem.5B02205 |
0.766 |
|
| 2016 |
Davis CM, Dyer RB. The Role of Electrostatic Interactions in Folding of β-Proteins. Journal of the American Chemical Society. PMID 26750867 DOI: 10.1021/Jacs.5B13201 |
0.701 |
|
| 2015 |
Kise DP, Reddish MJ, Dyer RB. Sandwich-format 3D printed microfluidic mixers: a flexible platform for multi-probe analysis. Journal of Micromechanics and Microengineering : Structures, Devices, and Systems. 25. PMID 26855478 DOI: 10.1088/0960-1317/25/12/124002 |
0.752 |
|
| 2015 |
Greene BL, Wu CH, McTernan PM, Adams MW, Dyer RB. Proton-coupled electron transfer dynamics in the catalytic mechanism of a [NiFe]-hydrogenase. Journal of the American Chemical Society. 137: 4558-66. PMID 25790178 DOI: 10.1021/Jacs.5B01791 |
0.734 |
|
| 2015 |
Davis CM, Cooper AK, Dyer RB. Fast helix formation in the B domain of protein A revealed by site-specific infrared probes. Biochemistry. 54: 1758-66. PMID 25706439 DOI: 10.1021/Acs.Biochem.5B00037 |
0.717 |
|
| 2015 |
Callender R, Dyer RB. The dynamical nature of enzymatic catalysis. Accounts of Chemical Research. 48: 407-13. PMID 25539144 DOI: 10.1021/Ar5002928 |
0.427 |
|
| 2015 |
Einarsdóttir O, McDonald W, Funatogawa C, Szundi I, Woodruff WH, Dyer RB. The pathway of O₂to the active site in heme-copper oxidases. Biochimica Et Biophysica Acta. 1847: 109-18. PMID 24998308 DOI: 10.1016/J.Bbabio.2014.06.008 |
0.581 |
|
| 2014 |
Reddish MJ, Peng HL, Deng H, Panwar KS, Callender R, Dyer RB. Direct evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopy. The Journal of Physical Chemistry. B. 118: 10854-62. PMID 25149276 DOI: 10.1021/Jp5050546 |
0.793 |
|
| 2014 |
Davis CM, Dyer RB. WW domain folding complexity revealed by infrared spectroscopy. Biochemistry. 53: 5476-84. PMID 25121968 DOI: 10.1021/Bi500556H |
0.72 |
|
| 2014 |
Zhao C, Glass EN, Chica B, Musaev DG, Sumliner JM, Dyer RB, Lian T, Hill CL. All-inorganic networks and tetramer based on tin(II)-containing polyoxometalates: tuning structural and spectral properties with lone-pairs. Journal of the American Chemical Society. 136: 12085-91. PMID 25076405 DOI: 10.1021/Ja5060127 |
0.771 |
|
| 2014 |
Peng HL, Deng H, Dyer RB, Callender R. Energy landscape of the Michaelis complex of lactate dehydrogenase: relationship to catalytic mechanism. Biochemistry. 53: 1849-57. PMID 24576110 DOI: 10.1021/Bi500215A |
0.393 |
|
| 2014 |
Li G, Magana D, Dyer RB. Anisotropic energy flow and allosteric ligand binding in albumin. Nature Communications. 5: 3100. PMID 24445265 DOI: 10.1038/Ncomms4100 |
0.32 |
|
| 2014 |
Zheng W, Liu Y, West A, Schuler EE, Yehl K, Dyer RB, Kindt JT, Salaita K. Quantum dots encapsulated within phospholipid membranes: phase-dependent structure, photostability, and site-selective functionalization. Journal of the American Chemical Society. 136: 1992-9. PMID 24417287 DOI: 10.1021/Ja411339F |
0.777 |
|
| 2014 |
Kise DP, Magana D, Reddish MJ, Dyer RB. Submillisecond mixing in a continuous-flow, microfluidic mixer utilizing mid-infrared hyperspectral imaging detection. Lab On a Chip. 14: 584-91. PMID 24302515 DOI: 10.1039/C3Lc51171E |
0.763 |
|
| 2013 |
Davis CM, Dyer RB. Dynamics of an ultrafast folding subdomain in the context of a larger protein fold. Journal of the American Chemical Society. 135: 19260-7. PMID 24320936 DOI: 10.1021/Ja409608R |
0.691 |
|
| 2013 |
Burke KS, Parul D, Reddish MJ, Dyer RB. A simple three-dimensional-focusing, continuous-flow mixer for the study of fast protein dynamics. Lab On a Chip. 13: 2912-21. PMID 23760106 DOI: 10.1039/C3Lc50497B |
0.793 |
|
| 2013 |
Davis C, Kindt J, Dyer RB. Dynamics and Mechanism of Membrane-Induced Folding of a Small Beta-Hairpin Biophysical Journal. 104: 236a. DOI: 10.1016/J.Bpj.2012.11.1331 |
0.704 |
|
| 2012 |
Nagarajan S, Schuler EE, Ma K, Kindt JT, Dyer RB. Dynamics of the gel to fluid phase transformation in unilamellar DPPC vesicles. The Journal of Physical Chemistry. B. 116: 13749-56. PMID 23130986 DOI: 10.1021/Jp309832U |
0.783 |
|
| 2012 |
Vu DM, Brewer SH, Dyer RB. Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli. Biochemistry. 51: 9104-11. PMID 23098216 DOI: 10.1021/Bi301296Y |
0.372 |
|
| 2012 |
Li G, Magana D, Dyer RB. Direct observation and control of ultrafast photoinduced twisted intramolecular charge transfer (TICT) in triphenyl-methane dyes. The Journal of Physical Chemistry. B. 116: 12590-6. PMID 23009668 DOI: 10.1021/Jp307091F |
0.309 |
|
| 2012 |
Yehl K, Joshi JP, Greene BL, Dyer RB, Nahta R, Salaita K. Catalytic deoxyribozyme-modified nanoparticles for RNAi-independent gene regulation Acs Nano. 6: 9150-9157. PMID 22966955 DOI: 10.1021/Nn3034265 |
0.731 |
|
| 2012 |
Davis CM, Xiao S, Raleigh DP, Dyer RB. Raising the speed limit for β-hairpin formation. Journal of the American Chemical Society. 134: 14476-82. PMID 22873643 DOI: 10.1021/Ja3046734 |
0.712 |
|
| 2012 |
Greene BL, Joseph CA, Maroney MJ, Dyer RB. Direct evidence of active-site reduction and photodriven catalysis in sensitized hydrogenase assemblies. Journal of the American Chemical Society. 134: 11108-11. PMID 22716776 DOI: 10.1021/Ja3042367 |
0.666 |
|
| 2012 |
Brewer SH, Tang Y, Vu DM, Gnanakaran S, Raleigh DP, Dyer RB. Temperature dependence of water interactions with the amide carbonyls of α-helices. Biochemistry. 51: 5293-9. PMID 22680405 DOI: 10.1021/Bi3006434 |
0.335 |
|
| 2012 |
Li G, Magana D, Dyer RB. Photoinduced electron transfer in folic acid investigated by ultrafast infrared spectroscopy. The Journal of Physical Chemistry. B. 116: 3467-75. PMID 22364409 DOI: 10.1021/Jp300392A |
0.332 |
|
| 2011 |
Nagarajan S, Taskent-Sezgin H, Parul D, Carrico I, Raleigh DP, Dyer RB. Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes. Journal of the American Chemical Society. 133: 20335-40. PMID 22039909 DOI: 10.1021/Ja2071362 |
0.348 |
|
| 2011 |
Deng H, Vu DV, Clinch K, Desamero R, Dyer RB, Callender R. Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase. The Journal of Physical Chemistry. B. 115: 7670-8. PMID 21568287 DOI: 10.1021/Jp2015929 |
0.373 |
|
| 2011 |
Magana D, Parul D, Dyer RB, Shreve AP. Implementation of time-resolved step-scan fourier transform infrared (FT-IR) spectroscopy using a kHz repetition rate pump laser. Applied Spectroscopy. 65: 535-42. PMID 21513597 DOI: 10.1366/10-06179 |
0.329 |
|
| 2010 |
Taskent-Sezgin H, Chung J, Banerjee PS, Nagarajan S, Dyer RB, Carrico I, Raleigh DP. Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics. Angewandte Chemie (International Ed. in English). 49: 7473-5. PMID 20815000 DOI: 10.1002/Anie.201003325 |
0.388 |
|
| 2010 |
Dyer RB, Gai F, Woodruff WH, Gilmanshin R, Callender RH. ChemInform Abstract: Infrared Studies of Fast Events in Protein Folding Cheminform. 30: no-no. DOI: 10.1002/CHIN.199905298 |
0.528 |
|
| 2009 |
Dyer RB, Brauns EB. Laser-induced temperature jump infrared measurements of RNA folding. Methods in Enzymology. 469: 353-72. PMID 20946798 DOI: 10.1016/S0076-6879(09)69017-0 |
0.303 |
|
| 2008 |
Deng H, Brewer S, Vu DM, Clinch K, Callender R, Dyer RB. On the pathway of forming enzymatically productive ligand-protein complexes in lactate dehydrogenase. Biophysical Journal. 95: 804-13. PMID 18390601 DOI: 10.1529/Biophysj.108.128884 |
0.371 |
|
| 2007 |
Religa TL, Johnson CM, Vu DM, Brewer SH, Dyer RB, Fersht AR. The helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain Proceedings of the National Academy of Sciences of the United States of America. 104: 9272-9277. PMID 17517666 DOI: 10.1073/Pnas.0703434104 |
0.373 |
|
| 2007 |
Brewer SH, Song B, Raleigh DP, Dyer RB. Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy. Biochemistry. 46: 3279-85. PMID 17305369 DOI: 10.1021/Bi602372Y |
0.378 |
|
| 2007 |
Dyer RB. Ultrafast and downhill protein folding. Current Opinion in Structural Biology. 17: 38-47. PMID 17223539 DOI: 10.1016/J.Sbi.2007.01.001 |
0.341 |
|
| 2006 |
Werner JH, Joggerst R, Dyer RB, Goodwin PM. A two-dimensional view of the folding energy landscape of cytochrome c. Proceedings of the National Academy of Sciences of the United States of America. 103: 11130-5. PMID 16844777 DOI: 10.1073/Pnas.0604712103 |
0.381 |
|
| 2006 |
Barry BA, Cooper IB, De Riso A, Brewer SH, Vu DM, Dyer RB. Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle. Proceedings of the National Academy of Sciences of the United States of America. 103: 7288-91. PMID 16632606 DOI: 10.1073/Pnas.0600216103 |
0.333 |
|
| 2006 |
Causgrove TP, Dyer RB. Nonequilibrium protein folding dynamics : laser-induced pH-jump studies of the helix-coil transition Chemical Physics. 323: 2-10. DOI: 10.1016/J.Chemphys.2005.08.032 |
0.376 |
|
| 2005 |
Brewer SH, Vu DM, Tang Y, Li Y, Franzen S, Raleigh DP, Dyer RB. Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain. Proceedings of the National Academy of Sciences of the United States of America. 102: 16662-7. PMID 16269546 DOI: 10.1073/Pnas.0505432102 |
0.36 |
|
| 2005 |
Fesinmeyer RM, Peterson ES, Dyer RB, Andersen NH. Studies of helix fraying and solvation using 13C' isotopomers. Protein Science : a Publication of the Protein Society. 14: 2324-32. PMID 16131660 DOI: 10.1110/Ps.051510705 |
0.313 |
|
| 2005 |
Brauns EB, Dyer RB. Time-resolved infrared spectroscopy of RNA folding. Biophysical Journal. 89: 3523-30. PMID 16126826 DOI: 10.1529/Biophysj.105.061531 |
0.345 |
|
| 2005 |
Dyer RB, Maness SJ, Franzen S, Fesinmeyer RM, Olsen KA, Andersen NH. Hairpin folding dynamics: the cold-denatured state is predisposed for rapid refolding. Biochemistry. 44: 10406-15. PMID 16042418 DOI: 10.1021/Bi050698Z |
0.337 |
|
| 2005 |
McClendon S, Vu DM, Clinch K, Callender R, Dyer RB. Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase. Biophysical Journal. 89: L07-9. PMID 15879476 DOI: 10.1529/Biophysj.105.064675 |
0.398 |
|
| 2004 |
Vu DM, Peterson ES, Dyer RB. Experimental resolution of early steps in protein folding: testing molecular dynamics simulations. Journal of the American Chemical Society. 126: 6546-7. PMID 15161270 DOI: 10.1021/Ja048416Q |
0.379 |
|
| 2004 |
McMahon BH, Fabian M, Tomson F, Causgrove TP, Bailey JA, Rein FN, Dyer RB, Palmer G, Gennis RB, Woodruff WH. FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase. Biochimica Et Biophysica Acta. 1655: 321-31. PMID 15100047 DOI: 10.1016/J.Bbabio.2004.01.007 |
0.598 |
|
| 2004 |
Vu DM, Myers JK, Oas TG, Dyer RB. Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein. Biochemistry. 43: 3582-9. PMID 15035628 DOI: 10.1021/Bi036203S |
0.398 |
|
| 2003 |
Gillespie B, Vu DM, Shah PS, Marshall SA, Dyer RB, Mayo SL, Plaxco KW. NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics. Journal of Molecular Biology. 330: 813-9. PMID 12850149 DOI: 10.1016/S0022-2836(03)00616-8 |
0.336 |
|
| 2003 |
Maness SJ, Franzen S, Gibbs AC, Causgrove TP, Dyer RB. Nanosecond temperature jump relaxation dynamics of cyclic beta-hairpin peptides. Biophysical Journal. 84: 3874-82. PMID 12770893 DOI: 10.1016/S0006-3495(03)75115-7 |
0.321 |
|
| 2003 |
Gulotta M, Rogatsky E, Callender RH, Dyer RB. Primary folding dynamics of sperm whale apomyoglobin: core formation. Biophysical Journal. 84: 1909-18. PMID 12609893 DOI: 10.1016/S0006-3495(03)74999-6 |
0.38 |
|
| 2002 |
Callender R, Dyer RB. Probing protein dynamics using temperature jump relaxation spectroscopy. Current Opinion in Structural Biology. 12: 628-33. PMID 12464315 DOI: 10.1016/S0959-440X(02)00370-6 |
0.367 |
|
| 2002 |
Tomson F, Bailey JA, Gennis RB, Unkefer CJ, Li Z, Silks LA, Martinez RA, Donohoe RJ, Dyer RB, Woodruff WH. Direct infrared detection of the covalently ring linked His-Tyr structure in the active site of the heme-copper oxidases. Biochemistry. 41: 14383-90. PMID 12450405 DOI: 10.1021/Bi026370C |
0.574 |
|
| 2002 |
Gulotta M, Deng H, Deng H, Dyer RB, Callender RH. Toward an understanding of the role of dynamics on enzymatic catalysis in lactate dehydrogenase. Biochemistry. 41: 3353-63. PMID 11876643 DOI: 10.1021/Bi016009A |
0.39 |
|
| 2002 |
Bailey JA, Tomson FL, Mecklenburg SL, MacDonald GM, Katsonouri A, Puustinen A, Gennis RB, Woodruff WH, Dyer RB. Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli. Biochemistry. 41: 2675-83. PMID 11851414 DOI: 10.1021/Bi010823G |
0.611 |
|
| 2002 |
Werner JH, Dyer RB, Fesinmeyer RM, Andersen NH. Dynamics of the primary processes of protein folding: Helix nucleation Journal of Physical Chemistry B. 106: 487-494. DOI: 10.1021/Jp0125799 |
0.321 |
|
| 2001 |
Franzen S, Bailey J, Dyer RB, Woodruff WH, Hu RB, Thomas MR, Boxer SG. A photolysis-triggered heme ligand switch in H93G myoglobin. Biochemistry. 40: 5299-305. PMID 11318654 DOI: 10.1021/Bi0023403 |
0.597 |
|
| 2000 |
Leeson DT, Gai F, Rodriguez HM, Gregoret LM, Dyer RB. Protein folding and unfolding on a complex energy landscape. Proceedings of the National Academy of Sciences of the United States of America. 97: 2527-32. PMID 10681466 DOI: 10.1073/Pnas.040580397 |
0.574 |
|
| 2000 |
Franzen S, Boxer SG, Dyer RB, Woodruff WH. Resonance Raman studies of heme axial ligation in H93G myoglobin Journal of Physical Chemistry B. 104: 10359-10367. DOI: 10.1021/Jp001231V |
0.552 |
|
| 1999 |
Shreve AP, Franzen S, Simpson MC, Dyer RB. Dependence of NO recombination dynamics in horse myoglobin on solution glycerol content Journal of Physical Chemistry B. 103: 7969-7975. DOI: 10.1021/Jp991163G |
0.302 |
|
| 1999 |
Andersen NH, Dyer RB, Fesinmeyer RM, Gai F, Liu Z, Neidigh JW, Tong H. Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation [5] Journal of the American Chemical Society. 121: 9879-9880. DOI: 10.1021/Ja991829K |
0.47 |
|
| 1998 |
Omberg KM, Schoonover JR, Bernhard S, Moss JA, Treadway JA, Kober EM, Dyer RB, Meyer TJ. Mid-Infrared Spectrum of [Ru(phen)(3)](2+). Inorganic Chemistry. 37: 3505-3508. PMID 11670434 DOI: 10.1021/Ic971554E |
0.324 |
|
| 1998 |
Callender RH, Dyer RB, Gilmanshin R, Woodruff WH. Fast events in protein folding: the time evolution of primary processes. Annual Review of Physical Chemistry. 49: 173-202. PMID 9933907 DOI: 10.1146/Annurev.Physchem.49.1.173 |
0.591 |
|
| 1998 |
Gilmanshin R, Callender RH, Dyer RB. The core of apomyoglobin E-form folds at the diffusion limit. Nature Structural Biology. 5: 363-5. PMID 9586997 DOI: 10.1038/Nsb0598-363 |
0.321 |
|
| 1998 |
Kim Y, Babcock GT, Surerus KK, Fee JA, Dyer RB, Woodruff WH, Oertling WA. Cyanide binding and active site structure in heme-copper oxidases: normal coordinate analysis of iron-cyanide vibrations of a3(2+)CN- complexes of cytochromes ba3 and aa3. Biospectroscopy. 4: 1-15. PMID 9547010 DOI: 10.1002/(Sici)1520-6343(1998)4:1<1::Aid-Bspy1>3.0.Co;2-A |
0.577 |
|
| 1998 |
Franzen S, Roach MP, Chen YP, Dyer RB, Woodruff WH, Dawson JH. The unusual reactivities of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase do not arise from a histidine imidazolate proximal heme iron ligand Journal of the American Chemical Society. 120: 4658-4661. DOI: 10.1021/Ja973212D |
0.363 |
|
| 1998 |
Schoonover JR, Shreve AP, Dyer RB, Cleary RL, Ward MD, Bignozzi CA. Time-Resolved Infrared Studies on Two Isomeric Ruthenium(II)/Rhenium(I) Complexes Containing a Nonsymmetric Quaterpyridine Bridging Ligand Inorganic Chemistry. 37: 2598-2601. DOI: 10.1021/Ic9705305 |
0.342 |
|
| 1998 |
Dyer RB, Gai F, Woodruff WH, Gilmanshin R, Callender RH. Infrared Studies of Fast Events in Protein Folding Accounts of Chemical Research. 31: 709-716. DOI: 10.1021/Ar970343A |
0.669 |
|
| 1997 |
Gilmanshin R, Williams S, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: relaxation dynamics and structure of the I form of apomyoglobin. Biochemistry. 36: 15006-12. PMID 9398226 DOI: 10.1021/bi970634r |
0.567 |
|
| 1997 |
Puustinen A, Bailey JA, Dyer RB, Mecklenburg SL, Wikström M, Woodruff WH. Fourier transform infrared evidence for connectivity between CuB and glutamic acid 286 in cytochrome bo3 from Escherichia coli. Biochemistry. 36: 13195-200. PMID 9341207 DOI: 10.1021/bi971091o |
0.507 |
|
| 1997 |
Gilmanshin R, Dyer RB, Callender RH. Structural heterogeneity of the various forms of apomyoglobin: implications for protein folding. Protein Science : a Publication of the Protein Society. 6: 2134-42. PMID 9336836 DOI: 10.1002/Pro.5560061008 |
0.378 |
|
| 1997 |
Riistama S, Hummer G, Puustinen A, Dyer RB, Woodruff WH, Wikström M. Bound water in the proton translocation mechanism of the haem-copper oxidases. Febs Letters. 414: 275-80. PMID 9315701 DOI: 10.1016/S0014-5793(97)01003-X |
0.574 |
|
| 1997 |
Gilmanshin R, Williams S, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proceedings of the National Academy of Sciences of the United States of America. 94: 3709-13. PMID 9108042 DOI: 10.1073/Pnas.94.8.3709 |
0.613 |
|
| 1996 |
Schoonover JR, Strouse GF, Dyer RB, Bates WD, Chen P, Meyer TJ. Application of Time-Resolved, Step-Scan Fourier Transform Infrared Spectroscopy to Excited-State Electronic Structure in Polypyridyl Complexes of Rhenium(I). Inorganic Chemistry. 35: 273-274. PMID 11666202 DOI: 10.1021/Ic950905R |
0.348 |
|
| 1996 |
Decatur SM, Franzen S, DePillis GD, Dyer RB, Woodruff WH, Boxer SG. Trans effects in nitric oxide binding to myoglobin cavity mutant H93G. Biochemistry. 35: 4939-44. PMID 8664286 DOI: 10.1021/bi951661p |
0.542 |
|
| 1996 |
Williams S, Causgrove TP, Gilmanshin R, Fang KS, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry. 35: 691-7. PMID 8547249 DOI: 10.1021/bi952217p |
0.564 |
|
| 1996 |
Schoonover JR, Strouse GF, Omberg KM, Dyer RB. Time-resolved, step-scan ftir spectroscopy of excited states of transition metal complexes Comments On Inorganic Chemistry. 18: 165-188. DOI: 10.1080/02603599608032720 |
0.359 |
|
| 1996 |
Bignozzi CA, Schoonover JR, Dyer RB. Application of time-resolved vibrational spectroscopy to the study of excited-state intercomponent processes in supramolecular systems Comments On Inorganic Chemistry. 18: 77-100. DOI: 10.1080/02603599608032715 |
0.319 |
|
| 1996 |
Causgrove TP, Dyer RB. Picosecond Structural Dynamics of Myoglobin following Photolysis of Carbon Monoxide The Journal of Physical Chemistry. 100: 3273-3277. DOI: 10.1021/Jp952483C |
0.347 |
|
| 1994 |
Dyer RB, Peterson KA, Stoutland PO, Woodruff WH. Picosecond infrared study of the photodynamics of carbonmonoxy-cytochrome c oxidase. Biochemistry. 33: 500-7. PMID 8286380 DOI: 10.1021/bi00168a015 |
0.557 |
|
| 1994 |
Oertling WA, Surerus KK, Einarsdóttir O, Fee JA, Dyer RB, Woodruff WH. Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: comparison of the a3/CuB site to that of bovine cytochrome aa3. Biochemistry. 33: 3128-41. PMID 8130228 DOI: 10.1021/bi00176a048 |
0.557 |
|
| 1993 |
Einarsdóttir O, Dyer RB, Lemon DD, Killough PM, Hubig SM, Atherton SJ, López-Garriga JJ, Palmer G, Woodruff WH. Photodissociation and recombination of carbonmonoxy cytochrome oxidase: Dynamics from picoseconds to kiloseconds Biochemistry. 32: 12013-12024. PMID 8218278 |
0.54 |
|
| 1993 |
Schoonover JR, Gordon KC, Argazzi R, Woodruff WH, Peterson KA, Bignozzi CA, Dyer RB, Meyer TJ. Application of transient infrared spectroscopy to intramolecular energy transfer in [(phen)(CO)3ReI(NC)RuII(CN)(bpy) 2]+ Journal of the American Chemical Society. 115: 10996-10997. DOI: 10.1021/Ja00076A070 |
0.345 |
|
| 1993 |
Doorn SK, Dyer RB, Stoutland PO, Woodruff WH. Ultrafast electron transfer and coupled vibrational dynamics in cyanide bridged mixed-valence transition-metal dimers Journal of the American Chemical Society. 115: 6398-6405. DOI: 10.1021/Ja00067A065 |
0.573 |
|
| 1992 |
Stoutland PO, Dyer RB, Woodruff WH. Ultrafast infrared spectroscopy. Science (New York, N.Y.). 257: 1913-7. PMID 1329200 DOI: 10.1126/science.1329200 |
0.508 |
|
| 1992 |
Surerus KK, Oertling WA, Fan C, Gurbiel RJ, Einarsdóttir O, Antholine WE, Dyer RB, Hoffman BM, Woodruff WH, Fee JA. Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B-CN complex suggests four 14N atoms are coordinated to CuB. Proceedings of the National Academy of Sciences of the United States of America. 89: 3195-9. PMID 1314380 DOI: 10.1073/pnas.89.8.3195 |
0.518 |
|
| 1992 |
Kuila D, Schoonover JR, Dyer RB, Batie CJ, Ballou DP, Fee JA, Woodruff WH. Resonance Raman studies of Rieske-type proteins. Biochimica Et Biophysica Acta. 1140: 175-83. PMID 1280165 DOI: 10.1016/0005-2728(92)90007-O |
0.57 |
|
| 1992 |
Doorn SK, Stoutland PO, Dyer RB, Woodruff WH. Picosecond infrared study of ultrafast electron transfer and vibrational energy relaxation in a mixed-valent ruthenium dimer Journal of the American Chemical Society. 114: 3133-3134. DOI: 10.1021/Ja00034A067 |
0.555 |
|
| 1992 |
Bignozzi CA, Argazzi R, Schoonover JR, Gordon KC, Dyer RB, Scandola F. Electronic coupling in cyano-bridged ruthenium polypyridine complexes and role of electronic effects on cyanide stretching frequencies Inorganic Chemistry. 31: 5260-5267. DOI: 10.1021/Ic00051A018 |
0.335 |
|
| 1992 |
Doorn SK, Gordon KC, Dyer RB, Woodruff WH. Time-resolved infrared spectroscopy of tetrakis(1,3-diisocyanopropane)dirhodium(2+) tetraphenylborate Inorganic Chemistry. 31: 2284-2285. DOI: 10.1021/IC00037A054 |
0.514 |
|
| 1991 |
Woodruff WH, Einarsdóttir O, Dyer RB, Bagley KA, Palmer G, Atherton SJ, Goldbeck RA, Dawes TD, Kliger DS. Nature and functional implications of the cytochrome a3 transients after photodissociation of CO-cytochrome oxidase. Proceedings of the National Academy of Sciences of the United States of America. 88: 2588-92. PMID 1848709 |
0.552 |
|
| 1991 |
Dyer RB, Peterson KA, Stoutland PO, Woodruff WH. Ultrafast photoinduced ligand transfer in carbonmonoxy cytochrome c oxidase. Observation by picosecond infrared spectroscopy Journal of the American Chemical Society. 113: 6276-6277. DOI: 10.1021/Ja00016A057 |
0.581 |
|
| 1991 |
K. Surerus K, Oertling W, Fan C, Einarsdóttir Ó, Dyer R, Antholine WE, Hoffman BM, Woodruff WH, Fee JA. Spectroscopic characterization of the Fe(II)a·CN complex of Thermus thermophilus cytochrome ba3: A novel reaction of a terminal oxidase with cyanide Journal of Inorganic Biochemistry. 43: 352. DOI: 10.1016/0162-0134(91)84339-B |
0.545 |
|
| 1991 |
Woodruff WH, Dyer R, Peterson K, Stoutland P, Bagley K, Einarsdóttir Ó, Kliger DS, Goldbeck R, Dawes T, Martin J, Lambry J, Palmer G, Atherton SJ, Hubig SM. Ultrafast and not-so-fast dynamics of cytochrome oxidase: The ligand shuttle and its possible relevance to proton translocation Journal of Inorganic Biochemistry. 43: 351. DOI: 10.1016/0162-0134(91)84338-A |
0.588 |
|
| 1990 |
Donohoe RJ, Dyer RB, Swanson BI, Violette CA, Frank HA, Bocian DF. Near-infrared-excitation resonance Raman spectra of the primary electron donor in photosynthetic reaction centers from Rhodobacter sphaeroides Journal of the American Chemical Society. 112: 6716-6718. DOI: 10.1021/Ja00174A044 |
0.332 |
|
| 1989 |
Dyer RB, Lopez-Garriga JJ, Einarsdottir O, Woodruff WH. The orientation of carbonyl in carbonmonoxy cytochrome oxidase and its transient photoproducts. Direct evidence from time-resolved infrared linear dichroism Journal of the American Chemical Society. 111: 8962-8963. DOI: 10.1021/Ja00206A053 |
0.532 |
|
| 1989 |
Dyer RB, Einarsdottir O, Killough PM, Lopez-Garriga JJ, Woodruff WH. Transient binding of photodissociated carbon monoxide to CuB+ of eukaryotic cytochrome oxidase at ambient temperature. Direct evidence from time-resolved infrared spectroscopy Journal of the American Chemical Society. 111: 7657-7659. DOI: 10.1021/Ja00201A080 |
0.495 |
|
| 1989 |
Einarsdóttir O, Killough P, Dyer R, López-Garriga J, Atherton S, Hubig S, Palmer G, Woodruff W. Photodissociation and recombination dynamics of carbonmonoxy cytochrome oxidase Journal of Inorganic Biochemistry. 36: 267. DOI: 10.1016/0162-0134(89)84356-9 |
0.507 |
|
| 1989 |
Woodruff W, Dyer R, López-Garriga J, Einarsdóttir ', Killough P. Time-resolved infrared linear dichroism studies of the orientation of CO in carbonmonoxy cytochrome oxidase Journal of Inorganic Biochemistry. 36: 267. DOI: 10.1016/0162-0134(89)84355-7 |
0.494 |
|
| 1988 |
Schoonover JR, Dyer RB, Woodruff WH, Baker GM, Noguchi M, Palmer G. A comparison of the resonance Raman properties of the fast and slow forms of cytochrome oxidase Biochemistry. 27: 5433-5440. PMID 2846036 DOI: 10.1021/Bi00415A008 |
0.527 |
|
| 1987 |
Dyer RB, Palmer RA, Ghirardelli RG, Bradshaw JS, Jones BA. Circular dichroism studies of the solution structure of chiral pyridine substituted crowns and their complexes Journal of the American Chemical Society. 109: 4780-4786. DOI: 10.1021/Ja00250A004 |
0.489 |
|
| 1986 |
Dyer RB, Metcalf DH, Ghirardelli RG, Palmer RA, Holt EM. Circular dichroism studies of crown complexed ion pairs: A comparison of the alkali and alkaline earth nitrate complexes of chiral crown ethers Journal of the American Chemical Society. 108: 3621-3629. DOI: 10.1021/Ja00273A013 |
0.474 |
|
| 1986 |
Dyer RB, Ghirardelli RG, Palmer RA, Holt EM. Crown ether complexed ion pairs: Solution and solid-state structures of the (2S,6S)-2,6-dimethyl-1,4,7,10,13,16-hexaoxacyclooctadecane complex of potassium nitrate Inorganic Chemistry. 25: 3184-3188. DOI: 10.1021/Ic00238A019 |
0.486 |
|
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