| Year |
Citation |
Score |
| 2023 |
Ishigami I, Sierra RG, Su Z, Peck A, Wang C, Poitevin F, Lisova S, Hayes B, Moss FR, Boutet S, Sublett RE, Yoon CH, Yeh SR, Rousseau DL. Structural insights into functional properties of the oxidized form of cytochrome c oxidase. Nature Communications. 14: 5752. PMID 37717031 DOI: 10.1038/s41467-023-41533-x |
0.804 |
|
| 2023 |
Ishigami I, Carbajo S, Zatsepin N, Hikita M, Conrad CE, Nelson G, Coe J, Basu S, Grant T, Seaberg MH, Sierra RG, Hunter MS, Fromme P, Fromme R, Rousseau DL, ... Yeh SR, et al. Detection of a Geminate Photoproduct of Bovine Cytochrome Oxidase by Time-Resolved Serial Femtosecond Crystallography. Journal of the American Chemical Society. PMID 37695261 DOI: 10.1021/jacs.3c07803 |
0.8 |
|
| 2023 |
Ishigami I, Carbajo S, Zatsepin N, Hikita M, Conrad CE, Nelson G, Coe J, Basu S, Grant T, Seaberg MH, Sierra RG, Hunter MS, Fromme P, Fromme R, Rousseau DL, ... Yeh SR, et al. Detection of a geminate photoproduct of bovine cytochrome c oxidase by time-resolved serial femtosecond crystallography. Biorxiv : the Preprint Server For Biology. PMID 37214971 DOI: 10.1101/2023.05.08.539888 |
0.804 |
|
| 2023 |
Ishigami I, Sierra RG, Su Z, Peck A, Wang C, Poitevin F, Lisova S, Hayes B, Moss FR, Boutet S, Sublett RE, Yoon CH, Yeh SR, Rousseau DL. Structural basis for functional properties of cytochrome oxidase. Biorxiv : the Preprint Server For Biology. PMID 36993562 DOI: 10.1101/2023.03.20.530986 |
0.816 |
|
| 2022 |
Mondal P, Ishigami I, Yeh SR, Wijeratne GB. The Role of Heme Peroxo Oxidants in the Rational Mechanistic Modeling of Nitric Oxide Synthase: Characterization of Key Intermediates and Elucidation of the Mechanism. Angewandte Chemie (International Ed. in English). PMID 36169890 DOI: 10.1002/anie.202211521 |
0.771 |
|
| 2022 |
Ishigami I, Russi S, Cohen A, Yeh SR, Rousseau DL. Temperature-dependent structural transition following X-ray-induced metal center reduction in oxidized cytochrome c oxidase. The Journal of Biological Chemistry. 101799. PMID 35257742 DOI: 10.1016/j.jbc.2022.101799 |
0.802 |
|
| 2021 |
Mondal P, Ishigami I, Gérard EF, Lim C, Yeh SR, de Visser SP, Wijeratne GB. Proton-coupled electron transfer reactivities of electronically divergent heme superoxide intermediates: a kinetic, thermodynamic, and theoretical study. Chemical Science. 12: 8872-8883. PMID 34257888 DOI: 10.1039/d1sc01952j |
0.753 |
|
| 2020 |
Pham KN, Lewis-Ballester A, Yeh SR. Conformational Plasticity in Human Heme-Based Dioxygenases. Journal of the American Chemical Society. PMID 33373218 DOI: 10.1021/jacs.0c09970 |
0.302 |
|
| 2019 |
Ishigami I, Lewis-Ballester A, Echelmeier A, Brehm G, Zatsepin NA, Grant TD, Coe JD, Lisova S, Nelson G, Zhang S, Dobson ZF, Boutet S, Sierra RG, Batyuk A, Fromme P, ... ... Yeh SR, et al. Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome oxidase. Proceedings of the National Academy of Sciences of the United States of America. 116: 3572-3577. PMID 30808749 DOI: 10.1073/Pnas.1814526116 |
0.811 |
|
| 2018 |
Lewis-Ballester A, Karkashon S, Batabyal D, Poulos TL, Yeh SR. Inhibition Mechanisms of Human Indoleamine 2,3 Dioxygenase 1. Journal of the American Chemical Society. PMID 29897749 DOI: 10.1021/Jacs.8B03691 |
0.733 |
|
| 2017 |
Lewis-Ballester A, Pham KN, Batabyal D, Karkashon S, Bonanno JB, Poulos TL, Yeh SR. Structural insights into substrate and inhibitor binding sites in human indoleamine 2,3-dioxygenase 1. Nature Communications. 8: 1693. PMID 29167421 DOI: 10.1038/S41467-017-01725-8 |
0.72 |
|
| 2017 |
Ishigami I, Zatsepin NA, Hikita M, Conrad CE, Nelson G, Coe JD, Basu S, Grant TD, Seaberg MH, Sierra RG, Hunter MS, Fromme P, Fromme R, Yeh SR, Rousseau DL. Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature. Proceedings of the National Academy of Sciences of the United States of America. PMID 28698372 DOI: 10.1073/Pnas.1705628114 |
0.799 |
|
| 2017 |
Uchida T, Sekine Y, Dojun N, Lewis-Ballester A, Ishigami I, Matsui T, Yeh SR, Ishimori K. Reaction intermediates in the heme degradation reaction by HutZ from Vibrio cholerae. Dalton Transactions (Cambridge, England : 2003). PMID 28607990 DOI: 10.1039/C7Dt01562C |
0.787 |
|
| 2016 |
Batabyal D, Lewis-Ballester A, Yeh SR, Poulos TL. A Comparative Analysis on the Effector Role of Redox Partner Binding in Bacterial P450s. Biochemistry. PMID 27808504 DOI: 10.1021/Acs.Biochem.6B00913 |
0.725 |
|
| 2016 |
Lewis-Ballester A, Forouhar F, Kim SM, Lew S, Wang Y, Karkashon S, Seetharaman J, Batabyal D, Chiang BY, Hussain M, Correia MA, Yeh SR, Tong L. Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase. Scientific Reports. 6: 35169. PMID 27762317 DOI: 10.1038/Srep35169 |
0.739 |
|
| 2016 |
Nelson G, Kirian RA, Weierstall U, Zatsepin NA, Faragó T, Baumbach T, Wilde F, Niesler FB, Zimmer B, Ishigami I, Hikita M, Bajt S, Yeh SR, Rousseau DL, Chapman HN, et al. Three-dimensional-printed gas dynamic virtual nozzles for x-ray laser sample delivery. Optics Express. 24: 11515-30. PMID 27410079 DOI: 10.1364/Oe.24.011515 |
0.75 |
|
| 2016 |
Alvarez L, Lewis Ballester A, Roitberg AE, Estrin DA, Yeh SR, Marti MA, Capece L. Structural study of a flexible active site loop in human indoleamine 2,3-dioxygenase and its functional implications. Biochemistry. PMID 27112409 DOI: 10.1021/Acs.Biochem.6B00077 |
0.4 |
|
| 2015 |
Hayden EY, Kaur P, Williams TL, Matsui H, Yeh SR, Rousseau DL. Heme Stabilization of α-Synuclein Oligomers during Amyloid Fibril Formation. Biochemistry. 54: 4599-610. PMID 26161848 DOI: 10.1021/Acs.Biochem.5B00280 |
0.473 |
|
| 2015 |
Ahn YO, Lee HJ, Kaluka D, Yeh SR, Rousseau DL, Ädelroth P, Gennis RB. The two transmembrane helices of CcoP are sufficient for assembly of the cbb3-type heme-copper oxygen reductase from Vibrio cholerae. Biochimica Et Biophysica Acta. PMID 26116881 DOI: 10.1016/J.Bbabio.2015.06.013 |
0.564 |
|
| 2015 |
Egawa T, Haber J, Fee JA, Yeh SR, Rousseau DL. Interactions of Cu(B) with Carbon Monoxide in Cytochrome c Oxidase: Origin of the Anomalous Correlation between the Fe-CO and C-O Stretching Frequencies. The Journal of Physical Chemistry. B. 119: 8509-20. PMID 26056844 DOI: 10.1021/Acs.Jpcb.5B04444 |
0.526 |
|
| 2015 |
Kaluka D, Batabyal D, Chiang BY, Poulos TL, Yeh SR. Spectroscopic and mutagenesis studies of human PGRMC1. Biochemistry. 54: 1638-47. PMID 25675345 DOI: 10.1021/Bi501177E |
0.713 |
|
| 2015 |
Ishigami I, Hikita M, Egawa T, Yeh SR, Rousseau DL. Proton translocation in cytochrome c oxidase: insights from proton exchange kinetics and vibrational spectroscopy. Biochimica Et Biophysica Acta. 1847: 98-108. PMID 25268561 DOI: 10.1016/J.Bbabio.2014.09.008 |
0.791 |
|
| 2015 |
Egawa T, Haber J, Fee JA, Yeh SR, Rousseau DL. Interactions of CuB with Carbon Monoxide in Cytochrome c Oxidase: Origin of the Anomalous Correlation between the Fe-CO and C-O Stretching Frequencies Journal of Physical Chemistry B. 119: 8509-8520. DOI: 10.1021/acs.jpcb.5b04444 |
0.486 |
|
| 2015 |
Hayden EY, Kaur P, Williams TL, Matsui H, Yeh SR, Rousseau DL. Heme Stabilization of α-Synuclein Oligomers during Amyloid Fibril Formation Biochemistry. 54: 4599-4610. DOI: 10.1021/acs.biochem.5b00280 |
0.423 |
|
| 2014 |
Ahn YO, Mahinthichaichan P, Lee HJ, Ouyang H, Kaluka D, Yeh SR, Arjona D, Rousseau DL, Tajkhorshid E, Adelroth P, Gennis RB. Conformational coupling between the active site and residues within the K(C)-channel of the Vibrio cholerae cbb3-type (C-family) oxygen reductase. Proceedings of the National Academy of Sciences of the United States of America. 111: E4419-28. PMID 25288772 DOI: 10.1073/Pnas.1411676111 |
0.513 |
|
| 2013 |
Egawa T, Yeh SR, Rousseau DL. Redox-controlled proton gating in bovine cytochrome c oxidase. Plos One. 8: e63669. PMID 23696843 DOI: 10.1016/J.Bpj.2012.11.3105 |
0.591 |
|
| 2013 |
Li W, Chen L, Lu C, Elmore BO, Astashkin AV, Rousseau DL, Yeh SR, Feng C. Regulatory role of Glu546 in flavin mononucleotide-heme electron transfer in human inducible nitric oxide synthase. Inorganic Chemistry. 52: 4795-801. PMID 23570607 DOI: 10.1021/Ic3020892 |
0.541 |
|
| 2013 |
Sabat J, Egawa T, Lu C, Stuehr DJ, Gerfen GJ, Rousseau DL, Yeh SR. Catalytic intermediates of inducible nitric-oxide synthase stabilized by the W188H mutation. The Journal of Biological Chemistry. 288: 6095-106. PMID 23269673 DOI: 10.1074/Jbc.M112.403238 |
0.547 |
|
| 2012 |
Yu MA, Egawa T, Shinzawa-Itoh K, Yoshikawa S, Guallar V, Yeh SR, Rousseau DL, Gerfen GJ. Two tyrosyl radicals stabilize high oxidation states in cytochrome C oxidase for efficient energy conservation and proton translocation. Journal of the American Chemical Society. 134: 4753-61. PMID 22296274 DOI: 10.1021/Ja210535W |
0.585 |
|
| 2012 |
Capece L, Lewis-Ballester A, Yeh SR, Estrin DA, Marti MA. Complete reaction mechanism of indoleamine 2,3-dioxygenase as revealed by QM/MM simulations. The Journal of Physical Chemistry. B. 116: 1401-13. PMID 22196056 DOI: 10.1021/Jp2082825 |
0.334 |
|
| 2012 |
Egawa T, Chen Y, Fee JA, Yeh SR, Rousseau DL. The rate-limiting step in O(2) reduction by cytochrome ba(3) from Thermus thermophilus. Biochimica Et Biophysica Acta. 1817: 666-71. PMID 22138627 DOI: 10.1016/J.Bbabio.2011.11.010 |
0.584 |
|
| 2012 |
Maza WA, Vetromile C, Lewis-Ballester A, Yeh S, Larsen RW. Time-Resolved Enthalpy and Volume Changes for Co-Photorelease from Indoleamine 2,3-Dioxygenase Biophysical Journal. 102: 467a. DOI: 10.1016/J.Bpj.2011.11.2561 |
0.369 |
|
| 2012 |
Yeh S, Lewis-Ballester A, Karkashon S. Comparative Studies of Human Indoleamine 2,3-Dioxygenase (IDO) and Tryptophan Dioxygenase (TDO) Biophysical Journal. 102: 467a. DOI: 10.1016/J.Bpj.2011.11.2560 |
0.401 |
|
| 2011 |
Yu MA, Egawa T, Shinzawa-Itoh K, Yoshikawa S, Yeh SR, Rousseau DL, Gerfen GJ. Radical formation in cytochrome c oxidase. Biochimica Et Biophysica Acta. 1807: 1295-304. PMID 21718686 DOI: 10.1016/J.Bbabio.2011.06.012 |
0.568 |
|
| 2011 |
Egawa T, Ganesan K, Lin MT, Yu MA, Hosler JP, Yeh SR, Rousseau DL, Gennis RB. Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli. Biochimica Et Biophysica Acta. 1807: 1342-8. PMID 21684251 DOI: 10.1016/J.Bbabio.2011.06.001 |
0.521 |
|
| 2011 |
Yeh S, Lu C, Lin Y. Interplay Between Ligand and Substrate Binding in Human Indoleamine 2,3-Dioxygenase Biophysical Journal. 100: 222a. DOI: 10.1016/J.Bpj.2010.12.1427 |
0.392 |
|
| 2011 |
Lewis-Ballester A, Batabyal D, Egawa T, Lu C, Lin Y, Capece L, Martí M, Estrin D, Yeh S. Reaction Mechanism of Heme-Based Dioxygenases Biophysical Journal. 100: 221a. DOI: 10.1016/J.Bpj.2010.12.1419 |
0.755 |
|
| 2010 |
Capece L, Lewis-Ballester A, Batabyal D, Di Russo N, Yeh SR, Estrin DA, Marti MA. The first step of the dioxygenation reaction carried out by tryptophan dioxygenase and indoleamine 2,3-dioxygenase as revealed by quantum mechanical/molecular mechanical studies. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 811-23. PMID 20361220 DOI: 10.1007/S00775-010-0646-X |
0.743 |
|
| 2010 |
Sudhamsu J, Kabir M, Airola MV, Patel BA, Yeh SR, Rousseau DL, Crane BR. Co-expression of ferrochelatase allows for complete heme incorporation into recombinant proteins produced in E. coli. Protein Expression and Purification. 73: 78-82. PMID 20303407 DOI: 10.1016/J.Pep.2010.03.010 |
0.54 |
|
| 2010 |
Lu C, Zhao X, Lu Y, Rousseau DL, Yeh SR. Role of copper ion in regulating ligand binding in a myoglobin-based cytochrome C oxidase model. Journal of the American Chemical Society. 132: 1598-605. PMID 20070118 DOI: 10.1021/Ja907777F |
0.497 |
|
| 2010 |
Yu MA, Egawa T, Yeh SR, Rousseau DL, Gerfen GJ. EPR characterization of ascorbyl and sulfur dioxide anion radicals trapped during the reaction of bovine Cytochrome c Oxidase with molecular oxygen. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 203: 213-9. PMID 20056464 DOI: 10.1016/J.Jmr.2009.12.017 |
0.475 |
|
| 2010 |
Ji H, Das TK, Puustinen A, Wikström M, Yeh SR, Rousseau DL. Modulation of the active site conformation by site-directed mutagenesis in cytochrome c oxidase from Paracoccus denitrificans. Journal of Inorganic Biochemistry. 104: 318-23. PMID 20056281 DOI: 10.1016/J.Jinorgbio.2009.11.011 |
0.54 |
|
| 2010 |
Rousseau D, Ji H, Das T, Puustinen A, Wikstrom M, Yeh S. Modulation of the Conformation of Cytochrome c Oxidase from paracoccus Denitrificans by Active-Site Mutations Biophysical Journal. 98: 640a-641a. DOI: 10.1016/J.Bpj.2009.12.3510 |
0.564 |
|
| 2010 |
Yeh S, Lewis-Ballester A, Batabyal D, Egawa T, Lu C, Lin Y, Marti MA, Capece L, Estrin DA. Ferryl Intermediates in Heme-Based Dioxygenases Biophysical Journal. 98: 640a. DOI: 10.1016/J.Bpj.2009.12.3509 |
0.752 |
|
| 2010 |
Yeh S, Han S, Rousseau DL. ChemInform Abstract: Cytochrome c Folding and Unfolding: A Biphasic Mechanism Cheminform. 30: no-no. DOI: 10.1002/chin.199905299 |
0.497 |
|
| 2009 |
Egawa T, Lin MT, Hosler JP, Gennis RB, Yeh SR, Rousseau DL. Communication between R481 and Cu(B) in cytochrome bo(3) ubiquinol oxidase from Escherichia coli. Biochemistry. 48: 12113-24. PMID 19928831 DOI: 10.1021/Bi901187U |
0.609 |
|
| 2009 |
Lewis-Ballester A, Batabyal D, Egawa T, Lu C, Lin Y, Marti MA, Capece L, Estrin DA, Yeh SR. Evidence for a ferryl intermediate in a heme-based dioxygenase. Proceedings of the National Academy of Sciences of the United States of America. 106: 17371-6. PMID 19805032 DOI: 10.1073/Pnas.0906655106 |
0.736 |
|
| 2009 |
Sabat J, Stuehr DJ, Yeh SR, Rousseau DL. Characterization of the proximal ligand in the P420 form of inducible nitric oxide synthase. Journal of the American Chemical Society. 131: 12186-92. PMID 19658411 DOI: 10.1021/Ja901016A |
0.543 |
|
| 2009 |
Egawa T, Lee HJ, Ji H, Gennis RB, Yeh SR, Rousseau DL. Identification of heme propionate vibrational modes in the resonance Raman spectra of cytochrome c oxidase. Analytical Biochemistry. 394: 141-3. PMID 19563766 DOI: 10.1016/J.Ab.2009.06.035 |
0.512 |
|
| 2009 |
Egawa T, Lee HJ, Gennis RB, Yeh SR, Rousseau DL. Critical structural role of R481 in cytochrome c oxidase from Rhodobacter sphaeroides. Biochimica Et Biophysica Acta. 1787: 1272-5. PMID 19463779 DOI: 10.1016/J.Bbabio.2009.05.006 |
0.525 |
|
| 2009 |
Batabyal D, Yeh SR. Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76. Journal of the American Chemical Society. 131: 3260-70. PMID 19209904 DOI: 10.1021/Ja807969A |
0.737 |
|
| 2009 |
Egawa T, Durand JL, Hayden EY, Rousseau DL, Yeh SR. Design and evaluation of a passive alcove-based microfluidic mixer. Analytical Chemistry. 81: 1622-7. PMID 19140669 DOI: 10.1021/Ac802410G |
0.427 |
|
| 2009 |
Yu MA, Gerfen GJ, Yeh S, Rousseau DL. Rapid Freeze-quench Trapping Of Intermediates In The Reaction Of Cytochrome c Oxidase With Hydrogen Peroxide Biophysical Journal. 96: 565a. DOI: 10.1016/J.Bpj.2008.12.3708 |
0.588 |
|
| 2009 |
Yeh S, Lu C, Egawa T, Lin Y, Mukai M, Wu G, Shepherd M, Poole RK. The Single Domain Hemoglobin From Campylobactor Jejuni: The Unique Structural Features Underlying Its NO Dioxygenase Activity Biophysical Journal. 96: 557a. DOI: 10.1016/J.Bpj.2008.12.3659 |
0.364 |
|
| 2009 |
Batabyal D, Yeh S. Substrate-Protein Interaction in Human Tryptophan dioxygenase Biophysical Journal. 96: 438a. DOI: 10.1016/J.Bpj.2008.12.2249 |
0.758 |
|
| 2009 |
Lu C, Lin Y, Yeh S. The Unique Dioxygen Activation Mechanism of Human Indoleamine 2,3-Dioxygenase Biophysical Journal. 96: 438a. DOI: 10.1016/J.Bpj.2008.12.2247 |
0.353 |
|
| 2009 |
Egawa T, Lee H, Gennis RB, Yeh S, Rousseau DL. Resonance Raman Investigation of the R481 Mutants of Cytochrome c Oxidase from R. sphaeroides Biophysical Journal. 96: 435a. DOI: 10.1016/J.Bpj.2008.12.2231 |
0.567 |
|
| 2009 |
Sabat J, Rousseau DL, Yeh S. Proximal Ligand Switch Triggered by Carbon Monoxide in Inducible Nitric Oxide Synthase Biophysical Journal. 96: 435a. DOI: 10.1016/J.Bpj.2008.12.2230 |
0.588 |
|
| 2009 |
Hayden EY, Yeh S, Rousseau DL, Das BC. Investigations of Amyloid Fiber Formation of Alpha-Synuclein and Amyloid-beta Using Newly Synthesized Small Molecules Biophysical Journal. 96: 218a. DOI: 10.1016/J.Bpj.2008.12.1908 |
0.488 |
|
| 2008 |
Kabir M, Sudhamsu J, Crane BR, Yeh SR, Rousseau DL. Substrate-ligand interactions in Geobacillus stearothermophilus nitric oxide synthase. Biochemistry. 47: 12389-97. PMID 18956884 DOI: 10.1021/Bi801491E |
0.583 |
|
| 2008 |
Ji H, Rousseau DL, Yeh SR. Heme-heme communication during the alkaline-induced structural transition in cytochrome c oxidase. Journal of Inorganic Biochemistry. 102: 414-26. PMID 18187199 DOI: 10.1016/J.Jinorgbio.2007.11.004 |
0.569 |
|
| 2008 |
Rousseau DL, Li D, Hayden EY, Deng H, Yeh SR. Ligand-protein interactions in mammalian nitric oxide synthase The Smallest Biomolecules: Diatomics and Their Interactions With Heme Proteins. 465-497. DOI: 10.1016/B978-044452839-1.50018-8 |
0.487 |
|
| 2008 |
Lu C, Egawa T, Batabyal D, Mukai M, Yeh SR. Microbial hemoglobins. structure, function, and folding The Smallest Biomolecules: Diatomics and Their Interactions With Heme Proteins. 235-266. DOI: 10.1016/B978-044452839-1.50011-5 |
0.678 |
|
| 2007 |
Batabyal D, Yeh SR. Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase. Journal of the American Chemical Society. 129: 15690-701. PMID 18027945 DOI: 10.1021/Ja076186K |
0.758 |
|
| 2007 |
Lu C, Mukai M, Lin Y, Wu G, Poole RK, Yeh SR. Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni. The Journal of Biological Chemistry. 282: 25917-28. PMID 17606611 DOI: 10.1074/Jbc.M704415200 |
0.406 |
|
| 2007 |
Li D, Kabir M, Stuehr DJ, Rousseau DL, Yeh SR. Substrate- and isoform-specific dioxygen complexes of nitric oxide synthase. Journal of the American Chemical Society. 129: 6943-51. PMID 17488012 DOI: 10.1021/Ja070683J |
0.584 |
|
| 2006 |
Samelson-Jones BJ, Yeh SR. Interactions between nitric oxide and indoleamine 2,3-dioxygenase. Biochemistry. 45: 8527-38. PMID 16834326 DOI: 10.1021/bi060143j |
0.733 |
|
| 2006 |
Wainwright LM, Wang Y, Park SF, Yeh SR, Poole RK. Purification and spectroscopic characterization of Ctb, a group III truncated hemoglobin implicated in oxygen metabolism in the food-borne pathogen Campylobacter jejuni. Biochemistry. 45: 6003-11. PMID 16681372 DOI: 10.1021/Bi052247K |
0.365 |
|
| 2006 |
Li D, Hayden EY, Panda K, Stuehr DJ, Deng H, Rousseau DL, Yeh SR. Regulation of the monomer-dimer equilibrium in inducible nitric-oxide synthase by nitric oxide. The Journal of Biological Chemistry. 281: 8197-204. PMID 16421101 DOI: 10.1074/Jbc.M507328200 |
0.578 |
|
| 2005 |
Ji H, Yeh SR, Rousseau DL. Structural characterization of the [Pco/o(2)] compound of cytochrome c oxidase. Febs Letters. 579: 6361-4. PMID 16263119 DOI: 10.1016/J.Febslet.2005.10.018 |
0.514 |
|
| 2005 |
Rousseau DL, Li D, Couture M, Yeh SR. Ligand-protein interactions in nitric oxide synthase. Journal of Inorganic Biochemistry. 99: 306-23. PMID 15598509 DOI: 10.1016/J.Jinorgbio.2004.11.007 |
0.598 |
|
| 2004 |
Zhong S, Rousseau DL, Yeh SR. Modulation of the folding energy landscape of cytochrome C with salt. Journal of the American Chemical Society. 126: 13934-5. PMID 15506749 DOI: 10.1021/Ja0459431 |
0.541 |
|
| 2004 |
Li D, Stuehr DJ, Yeh SR, Rousseau DL. Heme distortion modulated by ligand-protein interactions in inducible nitric-oxide synthase. The Journal of Biological Chemistry. 279: 26489-99. PMID 15066989 DOI: 10.1074/Jbc.M400968200 |
0.633 |
|
| 2004 |
Ji H, Yeh SR, Rousseau DL. Modulation of the electron redistribution in mixed valence cytochrome C oxidase by protein conformational changes. The Journal of Biological Chemistry. 279: 9392-9. PMID 14660573 DOI: 10.1074/Jbc.M310729200 |
0.506 |
|
| 2004 |
Adar F, Jelicks L, Naudin C, Rousseau D, Whitley A, Yeh S. Use of Vibrational Spectroscopy to Elucidate the Atherosclerotic Disease Process in the Apo E Knock-out Mouse Model Microscopy and Microanalysis. 10: 1300-1301. DOI: 10.1017/S1431927604887592 |
0.425 |
|
| 2003 |
Lin Y, Gerfen GJ, Rousseau DL, Yeh SR. Ultrafast microfluidic mixer and freeze-quenching device. Analytical Chemistry. 75: 5381-6. PMID 14710815 DOI: 10.1021/Ac0346205 |
0.527 |
|
| 2003 |
Mukai M, Yeh S, Rousseau D. Resonance Raman Study of the reaction site of Flavohemoglobin Seibutsu Butsuri. 43: S85. DOI: 10.2142/Biophys.43.S85_3 |
0.539 |
|
| 2002 |
Chattopadhyay K, Zhong S, Yeh SR, Rousseau DL, Frieden C. The intestinal fatty acid binding protein: the role of turns in fast and slow folding processes. Biochemistry. 41: 4040-7. PMID 11900547 DOI: 10.1021/Bi012042L |
0.516 |
|
| 2002 |
Terentis AC, Thomas SR, Takikawa O, Littlejohn TK, Truscott RJ, Armstrong RS, Yeh SR, Stocker R. The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions. The Journal of Biological Chemistry. 277: 15788-94. PMID 11867636 DOI: 10.1074/Jbc.M200457200 |
0.379 |
|
| 2001 |
Yeh SR, Ropson IJ, Rousseau DL. Hierarchical folding of intestinal fatty acid binding protein. Biochemistry. 40: 4205-10. PMID 11284675 DOI: 10.1021/Bi0155044 |
0.543 |
|
| 2001 |
Mukai M, Mills CE, Poole RK, Yeh SR. Flavohemoglobin, a globin with a peroxidase-like catalytic site. The Journal of Biological Chemistry. 276: 7272-7. PMID 11092893 DOI: 10.1074/Jbc.M009280200 |
0.427 |
|
| 2000 |
Yeh SR, Rousseau DL. Hierarchical folding of cytochrome c. Nature Structural Biology. 7: 443-5. PMID 10881185 DOI: 10.1038/75831 |
0.56 |
|
| 2000 |
Marinkovic NS, Adzic AR, Sullivan M, Kovacs K, Miller LM, Rousseau DL, Yeh S, Chance MR. Design and implementation of a rapid-mixer flow cell for time-resolved infrared microspectroscopy Review of Scientific Instruments. 71: 4057. DOI: 10.1063/1.1319342 |
0.476 |
|
| 1999 |
Jamin M, Yeh SR, Rousseau DL, Baldwin RL. Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate. Journal of Molecular Biology. 292: 731-40. PMID 10497035 DOI: 10.1006/Jmbi.1999.3074 |
0.541 |
|
| 1999 |
Yeh SR, Rousseau DL. Ligand exchange during unfolding of cytochrome c. The Journal of Biological Chemistry. 274: 17853-9. PMID 10364230 DOI: 10.1074/Jbc.274.25.17853 |
0.622 |
|
| 1998 |
Yeh SR, Rousseau DL. Folding intermediates in cytochrome c. Nature Structural Biology. 5: 222-8. PMID 9501916 DOI: 10.1038/Nsb0398-222 |
0.583 |
|
| 1998 |
Yeh S, Han S, Rousseau DL. CytochromecFolding and Unfolding: A Biphasic Mechanism Accounts of Chemical Research. 31: 727-736. DOI: 10.1021/ar970084p |
0.452 |
|
| 1997 |
Yeh SR, Takahashi S, Fan B, Rousseau DL. Ligand exchange during cytochrome c folding. Nature Structural Biology. 4: 51-6. PMID 8989324 DOI: 10.1038/Nsb0197-51 |
0.544 |
|
| 1997 |
Takahashi S, Yeh SR, Das TK, Chan CK, Gottfried DS, Rousseau DL. Folding of cytochrome c initiated by submillisecond mixing. Nature Structural Biology. 4: 44-50. PMID 8989323 DOI: 10.1038/Nsb0197-44 |
0.551 |
|
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