| Year |
Citation |
Score |
| 2020 |
Samuel PP, White MA, Ou WC, Case DA, Phillips GN, Olson JS. The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly. Biophysical Journal. PMID 32075750 DOI: 10.1016/J.Bpj.2020.01.031 |
0.791 |
|
| 2020 |
Samuel Mohan Dass PP, Phillips GN, Olson JS, Case DA. Molten Globules and Metallocofactor Disassociation Steer Human Hemoglobin Disassembly Biophysical Journal. 118: 338a. DOI: 10.1016/J.Bpj.2019.11.1884 |
0.373 |
|
| 2019 |
Olson JS. Lessons Learned from 50 Years of Hemoglobin Research: Unstirred and Cell-Free Layers, Electrostatics, Baseball Gloves, and Molten Globules. Antioxidants & Redox Signaling. PMID 31530172 DOI: 10.1089/Ars.2019.7876 |
0.477 |
|
| 2019 |
Meng F, Kassa T, Strader MB, Soman J, Olson JS, Alayash AI. Substitutions in the β subunits of sickle-cell hemoglobin improve oxidative stability and increase the delay time of sickle-cell fiber formation. The Journal of Biological Chemistry. PMID 30630954 DOI: 10.1074/Jbc.Ra118.006452 |
0.394 |
|
| 2019 |
Samuel Mohan Dass PP, Phillips GN, Olson JS, Case DA. Resolving the Transition States of Human Hemoglobin Assembly through a Combination of Spectroscopic Studies and All-Atom Molecular Dynamics Simulations Biophysical Journal. 116: 63a-64a. DOI: 10.1016/J.Bpj.2018.11.388 |
0.386 |
|
| 2018 |
Sjodt M, Macdonald R, Marshall JD, Clayton J, Olson JS, Phillips ML, Gell DA, Wereszczynski J, Clubb RT. Energetics Underlying Hemin Extraction from Human Hemoglobin by. The Journal of Biological Chemistry. PMID 29540481 DOI: 10.1074/Jbc.Ra117.000803 |
0.403 |
|
| 2017 |
Cardenas ASB, Samuel PP, Olson JS. 2017 Military Supplement: Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering. Shock (Augusta, Ga.). PMID 29112633 DOI: 10.1097/Shk.0000000000001053 |
0.805 |
|
| 2017 |
Strader MB, Bangle R, Parker Siburt CJ, Varnado CL, Soman J, Benitez Cardenas AS, Samuel PS, Singleton EW, Crumbliss AL, Olson JS, Alayash AI. Engineering Oxidative Stability in Human Hemoglobin based on the Hb Providence (βK82D) mutation and Genetic Crosslinking. The Biochemical Journal. PMID 29070524 DOI: 10.1042/Bcj20170491 |
0.378 |
|
| 2017 |
Samuel PP, Ou WC, Phillips GN, Olson JS. The Mechanism of Human Apohemoglobin Unfolding. Biochemistry. PMID 28218841 DOI: 10.1021/Acs.Biochem.6B01235 |
0.812 |
|
| 2017 |
Benitez Cardenas AS, Olson JS. Factors Governing Autooxidation of Human Hemoglobin Biophysical Journal. 112: 66a. DOI: 10.1016/J.Bpj.2016.11.395 |
0.391 |
|
| 2017 |
Samuel PP, Ou W, Phillips GN, Olson JS. In Vitro Studies of the Folding and Assembly Mechanism of Hemoglobin Biophysical Journal. 112: 59a. DOI: 10.1016/J.Bpj.2016.11.358 |
0.826 |
|
| 2016 |
Bissé E, Schaeffer-Reiss C, Van Dorsselaer A, Alayi TD, Epting T, Winkler K, Benitez Cardenas AS, Soman J, Birukou I, Samuel PP, Olson JS. Hemoglobin Kirklareli (α H58L), a New Variant Associated with Fe Deficiency and Increased CO Binding. The Journal of Biological Chemistry. PMID 28011635 DOI: 10.1074/Jbc.M116.764274 |
0.802 |
|
| 2016 |
Esquerra RM, Bibi BM, Tipgunlakant P, Birukou I, Soman J, Olson JS, Kliger DS, Goldbeck RA. The Role of Heme Pocket Water in Allosteric Regulation of Ligand Reactivity in Human Hemoglobin. Biochemistry. PMID 27355904 DOI: 10.1021/Acs.Biochem.6B00081 |
0.801 |
|
| 2016 |
Samuel PP, Ou W, Phillips GN, Olson JS. An in Vitro Investigation of Globin Folding and Expression Biophysical Journal. 110: 209a-210a. DOI: 10.1016/J.Bpj.2015.11.1166 |
0.791 |
|
| 2015 |
Samuel PP, Smith LP, Phillips GN, Olson JS. Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin. The Journal of Biological Chemistry. 290: 23479-95. PMID 26205820 DOI: 10.1074/Jbc.M115.672204 |
0.8 |
|
| 2015 |
Sjodt M, Macdonald R, Spirig T, Chan AH, Dickson CF, Fabian M, Olson JS, Gell DA, Clubb RT. The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin. Journal of Molecular Biology. PMID 25687963 DOI: 10.1016/J.Jmb.2015.02.008 |
0.353 |
|
| 2014 |
Strader MB, Hicks WA, Kassa T, Singleton E, Soman J, Olson JS, Weiss MJ, Mollan TL, Wilson MT, Alayash AI. Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: a novel subunit-specific mechanism in hemoglobin. The Journal of Biological Chemistry. 289: 22342-57. PMID 24939847 DOI: 10.1074/Jbc.M114.568980 |
0.801 |
|
| 2014 |
Mollan TL, Jia Y, Banerjee S, Wu G, Kreulen RT, Tsai AL, Olson JS, Crumbliss AL, Alayash AI. Redox properties of human hemoglobin in complex with fractionated dimeric and polymeric human haptoglobin. Free Radical Biology & Medicine. 69: 265-77. PMID 24486321 DOI: 10.1016/J.Freeradbiomed.2014.01.030 |
0.811 |
|
| 2014 |
Soman J, Strader M, Hicks W, Kassa T, Singleton E, Olson J, Weiss M, Mollan T, Wilson M, Alayash A. Crystallographic evidence for oxidative Met→Asp conversion in human hemoglobin Acta Crystallographica Section a Foundations and Advances. 70: C310-C310. DOI: 10.1107/S2053273314096892 |
0.799 |
|
| 2014 |
Olson JS, Gutfreund H. Quentin Howieson Gibson. 9 December 1918 — 16 March 2011 Biographical Memoirs of Fellows of the Royal Society. 60: 169-210. DOI: 10.1098/Rsbm.2013.0018 |
0.401 |
|
| 2013 |
Schotte F, Cho HS, Soman J, Wulff M, Olson JS, Anfinrud PA. Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallography. Chemical Physics. 422: 98-106. PMID 24839343 DOI: 10.1016/J.Chemphys.2012.12.030 |
0.349 |
|
| 2013 |
Dickson CF, Rich AM, D'Avigdor WM, Collins DA, Lowry JA, Mollan TL, Khandros E, Olson JS, Weiss MJ, Mackay JP, Lay PA, Gell DA. α-Hemoglobin-stabilizing protein (AHSP) perturbs the proximal heme pocket of oxy-α-hemoglobin and weakens the iron-oxygen bond. The Journal of Biological Chemistry. 288: 19986-20001. PMID 23696640 DOI: 10.1074/Jbc.M112.437509 |
0.824 |
|
| 2013 |
Nienhaus K, Olson JS, Nienhaus GU. An engineered heme-copper center in myoglobin: CO migration and binding. Biochimica Et Biophysica Acta. 1834: 1824-31. PMID 23459127 DOI: 10.1016/J.Bbapap.2013.02.031 |
0.399 |
|
| 2013 |
Boechi L, Arrar M, Martà MA, Olson JS, Roitberg AE, Estrin DA. Hydrophobic effect drives oxygen uptake in myoglobin via histidine E7. The Journal of Biological Chemistry. 288: 6754-62. PMID 23297402 DOI: 10.1074/Jbc.M112.426056 |
0.423 |
|
| 2013 |
Mollan TL, Banerjee S, Wu G, Parker Siburt CJ, Tsai AL, Olson JS, Weiss MJ, Crumbliss AL, Alayash AI. α-Hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of α-subunits of human HbA with hydrogen peroxide. The Journal of Biological Chemistry. 288: 4288-98. PMID 23264625 DOI: 10.1074/Jbc.M112.412064 |
0.805 |
|
| 2013 |
Varnado CL, Mollan TL, Birukou I, Smith BJ, Henderson DP, Olson JS. Development of recombinant hemoglobin-based oxygen carriers. Antioxidants & Redox Signaling. 18: 2314-28. PMID 23025383 DOI: 10.1089/Ars.2012.4917 |
0.805 |
|
| 2012 |
Salter MD, Blouin GC, Soman J, Singleton EW, Dewilde S, Moens L, Pesce A, Nardini M, Bolognesi M, Olson JS. Determination of ligand pathways in globins: apolar tunnels versus polar gates. The Journal of Biological Chemistry. 287: 33163-78. PMID 22859299 DOI: 10.1074/Jbc.M112.392258 |
0.798 |
|
| 2012 |
Mollan TL, Abraham B, Strader MB, Jia Y, Lozier JN, Olson JS, Alayash AI. Familial secondary erythrocytosis due to increased oxygen affinity is caused by destabilization of the T state of hemoglobin Brigham (α₂β₂(Pro100Leu)). Protein Science : a Publication of the Protein Society. 21: 1444-55. PMID 22821886 DOI: 10.1002/Pro.2130 |
0.809 |
|
| 2012 |
Ekworomadu MT, Poor CB, Owens CP, Balderas MA, Fabian M, Olson JS, Murphy F, Bakkalbasi E, Balkabasi E, Honsa ES, He C, Goulding CW, Maresso AW. Differential function of lip residues in the mechanism and biology of an anthrax hemophore. Plos Pathogens. 8: e1002559. PMID 22412371 DOI: 10.1371/Journal.Ppat.1002559 |
0.415 |
|
| 2012 |
Tsai AL, Martin E, Berka V, Olson JS. How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase. Antioxidants & Redox Signaling. 17: 1246-63. PMID 22356101 DOI: 10.1089/Ars.2012.4564 |
0.443 |
|
| 2012 |
Mollan TL, Khandros E, Weiss MJ, Olson JS. Kinetics of α-globin binding to α-hemoglobin stabilizing protein (AHSP) indicate preferential stabilization of hemichrome folding intermediate. The Journal of Biological Chemistry. 287: 11338-50. PMID 22298770 DOI: 10.1074/Jbc.M111.313247 |
0.815 |
|
| 2012 |
Khandros E, Mollan TL, Yu X, Wang X, Yao Y, D'Souza J, Gell DA, Olson JS, Weiss MJ. Insights into hemoglobin assembly through in vivo mutagenesis of α-hemoglobin stabilizing protein. The Journal of Biological Chemistry. 287: 11325-37. PMID 22287545 DOI: 10.1074/Jbc.M111.313205 |
0.814 |
|
| 2012 |
Tsai AL, Berka V, Martin E, Olson JS. A "sliding scale rule" for selectivity among NO, CO, and O₂ by heme protein sensors. Biochemistry. 51: 172-86. PMID 22111978 DOI: 10.1021/Bi2015629 |
0.412 |
|
| 2011 |
Honsa ES, Fabian M, Cardenas AM, Olson JS, Maresso AW. The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC. The Journal of Biological Chemistry. 286: 33652-60. PMID 21808055 DOI: 10.1074/Jbc.M111.241687 |
0.325 |
|
| 2011 |
Birukou I, Maillett DH, Birukova A, Olson JS. Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway. Biochemistry. 50: 7361-74. PMID 21793487 DOI: 10.1021/Bi200923K |
0.832 |
|
| 2011 |
Crowley MA, Mollan TL, Abdulmalik OY, Butler AD, Goodwin EF, Sarkar A, Stolle CA, Gow AJ, Olson JS, Weiss MJ. A hemoglobin variant associated with neonatal cyanosis and anemia. The New England Journal of Medicine. 364: 1837-43. PMID 21561349 DOI: 10.1056/Nejmoa1013579 |
0.794 |
|
| 2011 |
Birukou I, Soman J, Olson JS. Blocking the gate to ligand entry in human hemoglobin. The Journal of Biological Chemistry. 286: 10515-29. PMID 21193395 DOI: 10.1074/Jbc.M110.176271 |
0.807 |
|
| 2011 |
Pesce A, Nardini M, Dewilde S, Capece L, Martà MA, Congia S, Salter MD, Blouin GC, Estrin DA, Ascenzi P, Moens L, Bolognesi M, Olson JS. Ligand migration in the apolar tunnel of Cerebratulus lacteus mini-hemoglobin. The Journal of Biological Chemistry. 286: 5347-58. PMID 21147768 DOI: 10.1074/Jbc.M110.169045 |
0.816 |
|
| 2010 |
Esquerra RM, López-Peña I, Tipgunlakant P, Birukou I, Nguyen RL, Soman J, Olson JS, Kliger DS, Goldbeck RA. Kinetic spectroscopy of heme hydration and ligand binding in myoglobin and isolated hemoglobin chains: an optical window into heme pocket water dynamics. Physical Chemistry Chemical Physics : Pccp. 12: 10270-8. PMID 20668762 DOI: 10.1039/C003606B |
0.8 |
|
| 2010 |
Peña MI, Davlieva M, Bennett MR, Olson JS, Shamoo Y. Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection. Molecular Systems Biology. 6: 387. PMID 20631681 DOI: 10.1038/Msb.2010.43 |
0.327 |
|
| 2010 |
Tsai AL, Berka V, Martin F, Ma X, van den Akker F, Fabian M, Olson JS. Is Nostoc H-NOX a NO sensor or redox switch? Biochemistry. 49: 6587-99. PMID 20572679 DOI: 10.1021/Bi1002234 |
0.384 |
|
| 2010 |
Culbertson DS, Olson JS. Role of heme in the unfolding and assembly of myoglobin. Biochemistry. 49: 6052-63. PMID 20540498 DOI: 10.1021/Bi1006942 |
0.802 |
|
| 2010 |
Smith RD, Blouin GC, Johnson KA, Phillips GN, Olson JS. Straight-chain alkyl isocyanides open the distal histidine gate in crystal structures of myoglobin . Biochemistry. 49: 4977-86. PMID 20481504 DOI: 10.1021/Bi1001739 |
0.816 |
|
| 2010 |
Blouin GC, Schweers RL, Olson JS. Alkyl isocyanides serve as transition state analogues for ligand entry and exit in myoglobin. Biochemistry. 49: 4987-97. PMID 20476741 DOI: 10.1021/Bi1001745 |
0.811 |
|
| 2010 |
Blouin GC, Olson JS. The stretching frequencies of bound alkyl isocyanides indicate two distinct ligand orientations within the distal pocket of myoglobin. Biochemistry. 49: 4968-76. PMID 20476740 DOI: 10.1016/J.Bpj.2010.12.2263 |
0.811 |
|
| 2010 |
Tarlovsky Y, Fabian M, Solomaha E, Honsa E, Olson JS, Maresso AW. A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC. Journal of Bacteriology. 192: 3503-11. PMID 20435727 DOI: 10.1128/Jb.00054-10 |
0.344 |
|
| 2010 |
Soldatova AV, Ibrahim M, Olson JS, Czernuszewicz RS, Spiro TG. New light on NO bonding in Fe(III) heme proteins from resonance Raman spectroscopy and DFT modeling. Journal of the American Chemical Society. 132: 4614-25. PMID 20218710 DOI: 10.1021/Ja906233M |
0.352 |
|
| 2010 |
Birukou I, Schweers RL, Olson JS. Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin. The Journal of Biological Chemistry. 285: 8840-54. PMID 20080971 DOI: 10.1074/Jbc.M109.053934 |
0.82 |
|
| 2010 |
Bianchetti CM, Blouin GC, Bitto E, Olson JS, Phillips GN. The structure and NO binding properties of the nitrophorin-like heme-binding protein from Arabidopsis thaliana gene locus At1g79260.1. Proteins. 78: 917-31. PMID 19938152 DOI: 10.1002/Prot.22617 |
0.815 |
|
| 2010 |
Mollan TL, Yu X, Weiss MJ, Olson JS. The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly. Antioxidants & Redox Signaling. 12: 219-31. PMID 19659437 DOI: 10.1089/Ars.2009.2780 |
0.766 |
|
| 2010 |
Birukou I, Schweers RL, Olson JS. Role of His(E7) in Regulating Ligand Binding to the Subunits of Human HbA Biophysical Journal. 98: 642a. DOI: 10.1016/J.Bpj.2009.12.3516 |
0.823 |
|
| 2010 |
Nguyen RL, Lintner BW, Pena IL, Tipgunlakant P, Soman J, Birukou I, Olson JS, Asarnow DE, Kliger DS, Goldbeck RA, Esquerra RM. The Effect of Non-Coordinated Water in the Heme Pocket on the Ligand Binding Dynamics of Heme Proteins Biophysical Journal. 98: 639a-640a. DOI: 10.1016/J.Bpj.2009.12.3505 |
0.788 |
|
| 2010 |
Culbertson DS, Olson JS. General Mechanisms for the Folding and Assembly of Myoglobins and Hemoglobins Biophysical Journal. 98: 639a. DOI: 10.1016/J.Bpj.2009.12.3501 |
0.809 |
|
| 2009 |
Fabian M, Solomaha E, Olson JS, Maresso AW. Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis. The Journal of Biological Chemistry. 284: 32138-46. PMID 19759022 DOI: 10.1074/Jbc.M109.040915 |
0.315 |
|
| 2009 |
Goldbeck RA, Pillsbury ML, Jensen RA, Mendoza JL, Nguyen RL, Olson JS, Soman J, Kliger DS, Esquerra RM. Optical detection of disordered water within a protein cavity. Journal of the American Chemical Society. 131: 12265-72. PMID 19655795 DOI: 10.1021/Ja903409J |
0.35 |
|
| 2009 |
Smagghe BJ, Hoy JA, Percifield R, Kundu S, Hargrove MS, Sarath G, Hilbert JL, Watts RA, Dennis ES, Peacock WJ, Dewilde S, Moens L, Blouin GC, Olson JS, Appleby CA. Review: correlations between oxygen affinity and sequence classifications of plant hemoglobins. Biopolymers. 91: 1083-96. PMID 19441024 DOI: 10.1002/Bip.21256 |
0.795 |
|
| 2009 |
Asmundson AL, Taber AM, van der Walde A, Lin DH, Olson JS, Anthony-Cahill SJ. Coexpression of human alpha- and circularly permuted beta-globins yields a hemoglobin with normal R state but modified T state properties. Biochemistry. 48: 5456-65. PMID 19397368 DOI: 10.1021/Bi900216P |
0.78 |
|
| 2009 |
Yu X, Mollan TL, Butler A, Gow AJ, Olson JS, Weiss MJ. Analysis of human alpha globin gene mutations that impair binding to the alpha hemoglobin stabilizing protein. Blood. 113: 5961-9. PMID 19349619 DOI: 10.1182/Blood-2008-12-196030 |
0.785 |
|
| 2009 |
Aranda R, Cai H, Worley CE, Levin EJ, Li R, Olson JS, Phillips GN, Richards MP. Structural analysis of fish versus mammalian hemoglobins: effect of the heme pocket environment on autooxidation and hemin loss. Proteins. 75: 217-30. PMID 18831041 DOI: 10.1002/Prot.22236 |
0.533 |
|
| 2008 |
Salter MD, Nienhaus K, Nienhaus GU, Dewilde S, Moens L, Pesce A, Nardini M, Bolognesi M, Olson JS. The apolar channel in Cerebratulus lacteus hemoglobin is the route for O2 entry and exit. The Journal of Biological Chemistry. 283: 35689-702. PMID 18840607 DOI: 10.1074/Jbc.M805727200 |
0.815 |
|
| 2008 |
Maillett DH, Simplaceanu V, Shen TJ, Ho NT, Olson JS, Ho C. Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin. Biochemistry. 47: 10551-63. PMID 18788751 DOI: 10.1021/Bi800816V |
0.825 |
|
| 2008 |
Villarreal DM, Phillips CL, Kelley AM, Villarreal S, Villaloboz A, Hernandez P, Olson JS, Henderson DP. Enhancement of recombinant hemoglobin production in Escherichia coli BL21(DE3) containing the Plesiomonas shigelloides heme transport system. Applied and Environmental Microbiology. 74: 5854-6. PMID 18676700 DOI: 10.1128/Aem.01291-08 |
0.333 |
|
| 2008 |
Graves PE, Henderson DP, Horstman MJ, Solomon BJ, Olson JS. Enhancing stability and expression of recombinant human hemoglobin in E. coli: Progress in the development of a recombinant HBOC source. Biochimica Et Biophysica Acta. 1784: 1471-9. PMID 18489914 DOI: 10.1016/J.Bbapap.2008.04.012 |
0.397 |
|
| 2008 |
Zhu H, Xie G, Liu M, Olson JS, Fabian M, Dooley DM, Lei B. Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus. The Journal of Biological Chemistry. 283: 18450-60. PMID 18467329 DOI: 10.1074/Jbc.M801466200 |
0.314 |
|
| 2007 |
Aranda R, Worley CE, Liu M, Bitto E, Cates MS, Olson JS, Lei B, Phillips GN. Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp. Journal of Molecular Biology. 374: 374-83. PMID 17920629 DOI: 10.1016/J.Jmb.2007.08.058 |
0.526 |
|
| 2007 |
Olson JS, Soman J, Phillips GN. Ligand pathways in myoglobin: a review of Trp cavity mutations. Iubmb Life. 59: 552-62. PMID 17701550 DOI: 10.1080/15216540701230495 |
0.601 |
|
| 2007 |
Ran Y, Zhu H, Liu M, Fabian M, Olson JS, Aranda R, Phillips GN, Dooley DM, Lei B. Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter. The Journal of Biological Chemistry. 282: 31380-8. PMID 17699155 DOI: 10.1074/Jbc.M705967200 |
0.544 |
|
| 2007 |
Mocny JC, Olson JS, Connell TD. Passively released heme from hemoglobin and myoglobin is a potential source of nutrient iron for Bordetella bronchiseptica. Infection and Immunity. 75: 4857-66. PMID 17664260 DOI: 10.1128/Iai.00407-07 |
0.324 |
|
| 2007 |
Deng P, Nienhaus K, Palladino P, Olson JS, Blouin G, Moens L, Dewilde S, Geuens E, Nienhaus GU. Transient ligand docking sites in Cerebratulus lacteus mini-hemoglobin. Gene. 398: 208-23. PMID 17531406 DOI: 10.1016/J.Gene.2007.01.037 |
0.801 |
|
| 2006 |
Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ. Biochemical fates of alpha hemoglobin bound to alpha hemoglobin-stabilizing protein AHSP. The Journal of Biological Chemistry. 281: 32611-8. PMID 16901899 DOI: 10.1074/Jbc.M607311200 |
0.386 |
|
| 2006 |
Nygaard TK, Blouin GC, Liu M, Fukumura M, Olson JS, Fabian M, Dooley DM, Lei B. The mechanism of direct heme transfer from the streptococcal cell surface protein Shp to HtsA of the HtsABC transporter. The Journal of Biological Chemistry. 281: 20761-71. PMID 16717094 DOI: 10.1074/Jbc.M601832200 |
0.78 |
|
| 2006 |
Gardner PR, Gardner AM, Brashear WT, Suzuki T, Hvitved AN, Setchell KD, Olson JS. Hemoglobins dioxygenate nitric oxide with high fidelity. Journal of Inorganic Biochemistry. 100: 542-50. PMID 16439024 DOI: 10.1016/J.Jinorgbio.2005.12.012 |
0.605 |
|
| 2006 |
Goldbeck RA, Bhaskaran S, Ortega C, Mendoza JL, Olson JS, Soman J, Kliger DS, Esquerra RM. Water and ligand entry in myoglobin: assessing the speed and extent of heme pocket hydration after CO photodissociation. Proceedings of the National Academy of Sciences of the United States of America. 103: 1254-9. PMID 16432219 DOI: 10.1073/Pnas.0507840103 |
0.422 |
|
| 2005 |
Ionascu D, Gruia F, Ye X, Yu A, Rosca F, Beck C, Demidov A, Olson JS, Champion PM. Temperature-dependent studies of NO recombination to heme and heme proteins. Journal of the American Chemical Society. 127: 16921-34. PMID 16316238 DOI: 10.1021/Ja054249Y |
0.428 |
|
| 2005 |
Dantsker D, Roche C, Samuni U, Blouin G, Olson JS, Friedman JM. The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities. The Journal of Biological Chemistry. 280: 38740-55. PMID 16155005 DOI: 10.1074/Jbc.M506333200 |
0.812 |
|
| 2005 |
Miranda JJ, Maillett DH, Soman J, Olson JS. Thermoglobin, oxygen-avid hemoglobin in a bacterial hyperthermophile. The Journal of Biological Chemistry. 280: 36754-61. PMID 16135523 DOI: 10.1074/Jbc.M505918200 |
0.798 |
|
| 2005 |
Zhang W, Olson JS, Phillips GN. Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis. Biophysical Journal. 88: 2801-14. PMID 15653746 DOI: 10.1529/Biophysj.104.047936 |
0.564 |
|
| 2005 |
Nienhaus K, Olson JS, Franzen S, Nienhaus GU. The origin of stark splitting in the initial photoproduct state of MbCO. Journal of the American Chemical Society. 127: 40-1. PMID 15631438 DOI: 10.1021/Ja0466917 |
0.356 |
|
| 2004 |
Geuens E, Dewilde S, Hoogewijs D, Pesce A, Nienhaus K, Nienhaus GU, Olson J, Vanfleteren J, Bolognesi M, Moens L. Nerve globins in invertebrates Iubmb Life. 56: 653-656. PMID 15804828 DOI: 10.1080/15216540500037471 |
0.365 |
|
| 2004 |
Schotte F, Soman J, Olson JS, Wulff M, Anfinrud PA. Picosecond time-resolved X-ray crystallography: probing protein function in real time. Journal of Structural Biology. 147: 235-46. PMID 15450293 DOI: 10.1016/J.Jsb.2004.06.009 |
0.332 |
|
| 2004 |
Pesce A, Nardini M, Ascenzi P, Geuens E, Dewilde S, Moens L, Bolognesi M, Riggs AF, Hale A, Deng P, Nienhaus GU, Olson JS, Nienhaus K. Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin. The Journal of Biological Chemistry. 279: 33662-72. PMID 15161908 DOI: 10.1074/Jbc.M403597200 |
0.465 |
|
| 2004 |
Kundu S, Blouin GC, Premer SA, Sarath G, Olson JS, Hargrove MS. Tyrosine B10 inhibits stabilization of bound carbon monoxide and oxygen in soybean leghemoglobin. Biochemistry. 43: 6241-52. PMID 15147208 DOI: 10.1021/Bi049848G |
0.806 |
|
| 2004 |
Puranik M, Nielsen SB, Youn H, Hvitved AN, Bourassa JL, Case MA, Tengroth C, Balakrishnan G, Thorsteinsson MV, Groves JT, McLendon GL, Roberts GP, Olson JS, Spiro TG. Dynamics of carbon monoxide binding to CooA. The Journal of Biological Chemistry. 279: 21096-108. PMID 14990568 DOI: 10.1074/Jbc.M400613200 |
0.45 |
|
| 2004 |
Olson JS, Foley EW, Rogge C, Tsai AL, Doyle MP, Lemon DD. No scavenging and the hypertensive effect of hemoglobin-based blood substitutes. Free Radical Biology & Medicine. 36: 685-97. PMID 14990349 DOI: 10.1016/J.Freeradbiomed.2003.11.030 |
0.795 |
|
| 2004 |
Unno M, Matsui T, Chu GC, Couture M, Yoshida T, Rousseau DL, Olson JS, Ikeda-Saito M. Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function. The Journal of Biological Chemistry. 279: 21055-61. PMID 14966119 DOI: 10.1074/Jbc.M400491200 |
0.413 |
|
| 2003 |
Nienhaus K, Deng P, Olson JS, Warren JJ, Nienhaus GU. Structural dynamics of myoglobin: ligand migration and binding in valine 68 mutants. The Journal of Biological Chemistry. 278: 42532-44. PMID 12907676 DOI: 10.1074/Jbc.M306888200 |
0.409 |
|
| 2003 |
Schotte F, Lim M, Jackson TA, Smirnov AV, Soman J, Olson JS, Phillips GN, Wulff M, Anfinrud PA. Watching a protein as it functions with 150-ps time-resolved x-ray crystallography. Science (New York, N.Y.). 300: 1944-7. PMID 12817148 DOI: 10.1126/Science.1078797 |
0.438 |
|
| 2003 |
Coyle CM, Vogel KM, Rush TS, Kozlowski PM, Williams R, Spiro TG, Dou Y, Ikeda-Saito M, Olson JS, Zgierski MZ. FeNO structure in distal pocket mutants of myoglobin based on resonance Raman spectroscopy. Biochemistry. 42: 4896-903. PMID 12718530 DOI: 10.1021/Bi026395B |
0.361 |
|
| 2003 |
Olson JS, Foley EW, Maillett DH, Paster EV. Measurement of rate constants for reactions of O2, CO, and NO with hemoglobin. Methods in Molecular Medicine. 82: 65-91. PMID 12669638 DOI: 10.1385/1-59259-373-9:065 |
0.773 |
|
| 2002 |
Dou Y, Maillett DH, Eich RF, Olson JS. Myoglobin as a model system for designing heme protein based blood substitutes. Biophysical Chemistry. 98: 127-48. PMID 12128195 DOI: 10.1016/S0301-4622(02)00090-X |
0.827 |
|
| 2002 |
Draghi F, Miele AE, Travaglini-Allocatelli C, Vallone B, Brunori M, Gibson QH, Olson JS. Controlling ligand binding in myoglobin by mutagenesis. The Journal of Biological Chemistry. 277: 7509-19. PMID 11744723 DOI: 10.1074/Jbc.M109206200 |
0.649 |
|
| 2001 |
Liong EC, Dou Y, Scott EE, Olson JS, Phillips GN. Waterproofing the heme pocket. Role of proximal amino acid side chains in preventing hemin loss from myoglobin. The Journal of Biological Chemistry. 276: 9093-100. PMID 11084036 DOI: 10.1074/Jbc.M008593200 |
0.662 |
|
| 2001 |
Scott EE, Gibson QH, Olson JS. Mapping the pathways for O2 entry into and exit from myoglobin. The Journal of Biological Chemistry. 276: 5177-88. PMID 11018046 DOI: 10.1074/Jbc.M008282200 |
0.744 |
|
| 2000 |
Hargrove MS, Brucker EA, Stec B, Sarath G, Arredondo-Peter R, Klucas RV, Olson JS, Phillips GN. Crystal structure of a nonsymbiotic plant hemoglobin. Structure (London, England : 1993). 8: 1005-14. PMID 10986467 DOI: 10.1016/S0969-2126(00)00194-5 |
0.556 |
|
| 2000 |
Gardner PR, Gardner AM, Martin LA, Dou Y, Li T, Olson JS, Zhu H, Riggs AF. Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon monoxide inhibition. The Journal of Biological Chemistry. 275: 31581-7. PMID 10922365 DOI: 10.1074/Jbc.M004141200 |
0.616 |
|
| 2000 |
Scott EE, Paster EV, Olson JS. The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis. The Journal of Biological Chemistry. 275: 27129-36. PMID 10852902 DOI: 10.1074/Jbc.M000452200 |
0.629 |
|
| 2000 |
Qiu Y, Maillett DH, Knapp J, Olson JS, Riggs AF. Lamprey hemoglobin. Structural basis of the bohr effect. The Journal of Biological Chemistry. 275: 13517-28. PMID 10788466 DOI: 10.1074/Jbc.275.18.13517 |
0.825 |
|
| 2000 |
Gardner AM, Martin LA, Gardner PR, Dou Y, Olson JS. Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis. The Journal of Biological Chemistry. 275: 12581-9. PMID 10777548 DOI: 10.1074/Jbc.275.17.12581 |
0.653 |
|
| 2000 |
Gardner AM, Martin LA, Gardner PR, Dou Y, Olson JS, Kurtz D.M. J. Steady-state and transient kinetics of Escherichia coli nitric oxide dioxygenase (Flavohemoglobin) Chemtracts. 13: 534-538. |
0.503 |
|
| 1999 |
Thorsteinsson MV, Bevan DR, Potts M, Dou Y, Eich RF, Hargrove MS, Gibson QH, Olson JS. A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties. Biochemistry. 38: 2117-26. PMID 10026295 DOI: 10.1021/Bi9819172 |
0.632 |
|
| 1999 |
Alayash AI, Ryan BA, Eich RF, Olson JS, Cashon RE. Reactions of sperm whale myoglobin with hydrogen peroxide. Effects of distal pocket mutations on the formation and stability of the ferryl intermediate. The Journal of Biological Chemistry. 274: 2029-37. PMID 9890961 DOI: 10.1074/Jbc.274.4.2029 |
0.414 |
|
| 1999 |
Phillips GN, Teodora ML, Li T, Smith B, Olson JS. Bound CO Is a Molecular Probe of Electrostatic Potential in the Distal Pocket of Myoglobin Journal of Physical Chemistry B. 103: 8817-8829. DOI: 10.1021/Jp9918205 |
0.444 |
|
| 1999 |
Tomita T, Hirota S, Ogura T, Olson JS, Kitagawa T. Resonance Raman investigation of Fe-N-O structure of nitrosylheme in myoglobin and its mutants Journal of Physical Chemistry B. 103: 7044-7054. DOI: 10.1021/Jp991106N |
0.308 |
|
| 1998 |
Krzywda S, Murshudov GN, Brzozowski AM, Jaskolski M, Scott EE, Klizas SA, Gibson QH, Olson JS, Wilkinson AJ. Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution. Biochemistry. 37: 15896-907. PMID 9843395 DOI: 10.1021/Bi9812470 |
0.771 |
|
| 1998 |
Mansy SS, Olson JS, Gonzalez G, Gilles-Gonzalez MA. Imidazole is a sensitive probe of steric hindrance in the distal pockets of oxygen-binding heme proteins. Biochemistry. 37: 12452-7. PMID 9730817 DOI: 10.1021/Bi980516J |
0.492 |
|
| 1998 |
Unzai S, Eich R, Shibayama N, Olson JS, Morimoto H. Rate constants for O2 and CO binding to the alpha and beta subunits within the R and T states of human hemoglobin. The Journal of Biological Chemistry. 273: 23150-9. PMID 9722544 DOI: 10.1074/Jbc.273.36.23150 |
0.347 |
|
| 1998 |
Tang Q, Kalsbeck WA, Olson JS, Bocian DF. Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin. Biochemistry. 37: 7047-56. PMID 9578593 DOI: 10.1021/Bi9729413 |
0.396 |
|
| 1998 |
Nguyen BD, Zhao X, Vyas K, La Mar GN, Lile RA, Brucker EA, Phillips GN, Olson JS, Wittenberg JB. Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata. The Journal of Biological Chemistry. 273: 9517-26. PMID 9545280 DOI: 10.1074/Jbc.273.16.9517 |
0.483 |
|
| 1998 |
Brucker EA, Olson JS, Ikeda-Saito M, Phillips GN. Nitric oxide myoglobin: crystal structure and analysis of ligand geometry. Proteins. 30: 352-6. PMID 9533619 DOI: 10.1002/(Sici)1097-0134(19980301)30:4<352::Aid-Prot2>3.0.Co;2-L |
0.77 |
|
| 1998 |
Migita CT, Matera KM, Ikeda-Saito M, Olson JS, Fujii H, Yoshimura T, Zhou H, Yoshida T. The oxygen and carbon monoxide reactions of heme oxygenase. The Journal of Biological Chemistry. 273: 945-9. PMID 9422754 DOI: 10.1074/Jbc.273.2.945 |
0.468 |
|
| 1998 |
Mukai M, Nakashima S, Olson JS, Kitagawa T. Time-resolved UV resonance raman detection of a transient open form of the ligand pathway in tyr64(E7) myoglobin Journal of Physical Chemistry B. 102: 3624-3630. DOI: 10.1021/Jp980070G |
0.345 |
|
| 1998 |
Unno M, Christian JF, Olson JS, Sage JT, Champion PM. Evidence for hydrogen bonding effects in the iron ligand vibrations of carbonmonoxy myoglobin [11] Journal of the American Chemical Society. 120: 2670-2671. DOI: 10.1021/Ja973293D |
0.313 |
|
| 1997 |
Arredondo-Peter R, Hargrove MS, Sarath G, Moran JF, Lohrman J, Olson JS, Klucas RV. Rice hemoglobins. Gene cloning, analysis, and O2-binding kinetics of a recombinant protein synthesized in Escherichia coli. Plant Physiology. 115: 1259-66. PMID 9390447 DOI: 10.1104/Pp.115.3.1259 |
0.409 |
|
| 1997 |
Hargrove MS, Whitaker T, Olson JS, Vali RJ, Mathews AJ. Quaternary structure regulates hemin dissociation from human hemoglobin. The Journal of Biological Chemistry. 272: 17385-9. PMID 9211878 DOI: 10.1074/Jbc.272.28.17385 |
0.385 |
|
| 1997 |
Hargrove MS, Barry JK, Brucker EA, Berry MB, Phillips GN, Olson JS, Arredondo-Peter R, Dean JM, Klucas RV, Sarath G. Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants. Journal of Molecular Biology. 266: 1032-42. PMID 9086279 DOI: 10.1006/Jmbi.1996.0833 |
0.602 |
|
| 1997 |
Olson JS, Eich RF, Smith LP, Warren JJ, Knowles BC. Protein engineering strategies for designing more stable hemoglobin-based blood substitutes. Artificial Cells, Blood Substitutes, and Immobilization Biotechnology. 25: 227-41. PMID 9083641 DOI: 10.3109/10731199709118912 |
0.492 |
|
| 1997 |
Olson JS, Phillips GN. Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand Journal of Biological Inorganic Chemistry. 2: 544-552. DOI: 10.1007/S007750050169 |
0.479 |
|
| 1996 |
Zhu H, Hargrove M, Xie Q, Nozaki Y, Linse K, Smith SS, Olson JS, Riggs AF. Stoichiometry of subunits and heme content of hemoglobin from the earthworm Lumbricus terrestris. The Journal of Biological Chemistry. 271: 29999-30006. PMID 8939946 DOI: 10.1074/Jbc.271.47.29999 |
0.398 |
|
| 1996 |
Brucker EA, Olson JS, Phillips GN, Dou Y, Ikeda-Saito M. High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin. The Journal of Biological Chemistry. 271: 25419-22. PMID 8810310 DOI: 10.1074/Jbc.271.41.25419 |
0.387 |
|
| 1996 |
Hargrove MS, Olson JS. The stability of holomyoglobin is determined by heme affinity. Biochemistry. 35: 11310-8. PMID 8784185 DOI: 10.1021/Bi9603736 |
0.49 |
|
| 1996 |
Hargrove MS, Wilkinson AJ, Olson JS. Structural factors governing hemin dissociation from metmyoglobin. Biochemistry. 35: 11300-9. PMID 8784184 DOI: 10.1021/Bi960372D |
0.411 |
|
| 1996 |
Hargrove MS, Barrick D, Olson JS. The association rate constant for heme binding to globin is independent of protein structure. Biochemistry. 35: 11293-9. PMID 8784183 DOI: 10.1021/Bi960371L |
0.455 |
|
| 1996 |
Olson JS, Phillips GN. Kinetic pathways and barriers for ligand binding to myoglobin. The Journal of Biological Chemistry. 271: 17593-6. PMID 8698688 DOI: 10.1074/Jbc.271.30.17593 |
0.406 |
|
| 1996 |
Dou Y, Olson JS, Wilkinson AJ, Ikeda-Saito M. Mechanism of hydrogen cyanide binding to myoglobin. Biochemistry. 35: 7107-13. PMID 8679537 DOI: 10.1021/Bi9600299 |
0.483 |
|
| 1996 |
Eich RF, Li T, Lemon DD, Doherty DH, Curry SR, Aitken JF, Mathews AJ, Johnson KA, Smith RD, Phillips GN, Olson JS. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry. 35: 6976-83. PMID 8679521 DOI: 10.1021/Bi960442G |
0.595 |
|
| 1995 |
Quillin ML, Li T, Olson JS, Phillips GN, Dou Y, Ikeda-Saito M, Regan R, Carlson M, Gibson QH, Li H. Structural and functional effects of apolar mutations of the distal valine in myoglobin. Journal of Molecular Biology. 245: 416-36. PMID 7837273 DOI: 10.1006/Jmbi.1994.0034 |
0.688 |
|
| 1995 |
Zhao X, Vyas K, Nguyen BD, Rajarathnam K, La Mar GN, Li T, Phillips GN, Eich RF, Olson JS, Ling J. A double mutant of sperm whale myoglobin mimics the structure and function of elephant myoglobin. The Journal of Biological Chemistry. 270: 20763-74. PMID 7657659 DOI: 10.1074/Jbc.270.35.20763 |
0.553 |
|
| 1995 |
Smerdon SJ, Krzywda S, Brzozowski AM, Davies GJ, Wilkinson AJ, Brancaccio A, Cutruzzola F, Allocatelli CT, Brunori M, Brantley RE, Carver TE, Eich RF, Singleton E, Olson JS. Interactions among residues CD3, E7, E10, and E11 in myoglobins: Attempts to simulate the ligand-binding properties of aplysia myoglobin Biochemistry®. 34: 8715-8725. PMID 7612611 DOI: 10.1021/Bi00027A022 |
0.488 |
|
| 1995 |
Dou Y, Admiraal SJ, Ikeda-Saito M, Krzywda S, Wilkinson AJ, Li T, Olson JS, Prince RC, Pickering IJ, George GN. Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant. The Journal of Biological Chemistry. 270: 15993-6001. PMID 7608158 DOI: 10.1074/Jbc.270.27.15993 |
0.352 |
|
| 1995 |
Whitaker TL, Berry MB, Ho EL, Hargrove MS, Phillips GN, Komiyama NH, Nagai K, Olson JS. The D-helix in myoglobin and in the beta subunit of hemoglobin is required for the retention of heme. Biochemistry. 34: 8221-6. PMID 7599114 DOI: 10.1021/Bi00026A002 |
0.513 |
|
| 1995 |
Lai HH, Li T, Lyons DS, Phillips GN, Olson JS, Gibson QH. Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin. Proteins. 22: 322-39. PMID 7479707 DOI: 10.1002/Prot.340220404 |
0.687 |
|
| 1995 |
Nakashima S, Kitagawa T, Olson JS. Time-resolved resonance raman study of the recombination dynamics photodissociated carbon monoxide to sperm whale myoglobin and its mutants Journal of Molecular Liquids. 83: 317-320. DOI: 10.1016/0167-7322(95)00822-1 |
0.386 |
|
| 1994 |
Li T, Quillin ML, Phillips GN, Olson JS. Structural determinants of the stretching frequency of CO bound to myoglobin. Biochemistry. 33: 1433-46. PMID 8312263 DOI: 10.1021/Bi00172A021 |
0.521 |
|
| 1994 |
Hargrove MS, Singleton EW, Quillin ML, Ortiz LA, Phillips GN, Olson JS, Mathews AJ. His64(E7)-->Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation. The Journal of Biological Chemistry. 269: 4207-14. PMID 8307983 DOI: 10.2210/Pdb1Mgn/Pdb |
0.634 |
|
| 1994 |
Carlson ML, Regan R, Elber R, Li H, Phillips GN, Olson JS, Gibson QH. Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket. Biochemistry. 33: 10597-606. PMID 8075059 DOI: 10.2210/Pdb1Mlu/Pdb |
0.716 |
|
| 1994 |
Mathews AJ, Olson JS. Assignment of rate constants for O2 and CO binding to alpha and beta subunits within R- and T-state human hemoglobin. Methods in Enzymology. 232: 363-86. PMID 8057869 DOI: 10.1016/0076-6879(94)32055-1 |
0.384 |
|
| 1994 |
Olson JS. Genetic engineering of myoglobin as a simple prototype for hemoglobin-based blood substitutes. Artificial Cells, Blood Substitutes, and Immobilization Biotechnology. 22: 429-41. PMID 7994366 DOI: 10.3109/10731199409117872 |
0.519 |
|
| 1994 |
Hargrove MS, Krzywda S, Wilkinson AJ, Dou Y, Ikeda-Saito M, Olson JS. Stability of myoglobin: a model for the folding of heme proteins. Biochemistry. 33: 11767-75. PMID 7918393 DOI: 10.1021/Bi00205A012 |
0.451 |
|
| 1994 |
Ling J, Li T, Olson JS, Bocian DF. Identification of the iron-carbonyl stretch in distal histidine mutants of carbonmonoxymyoglobin. Biochimica Et Biophysica Acta. 1188: 417-21. PMID 7803455 DOI: 10.1016/0005-2728(94)90063-9 |
0.302 |
|
| 1994 |
Carver TE, Brantley RE, Singleton EW, Arduini RM, Quillin ML, Phillips GN, Olson JS. A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate. Journal of Biological Chemistry. 267: 14443-14450. DOI: 10.2210/Pdb1Moa/Pdb |
0.592 |
|
| 1994 |
Springer BA, Sligar SG, Olson JS, Phillips GNJ. Mechanisms of Ligand Recognition in Myoglobin Chemical Reviews. 94: 699-714. DOI: 10.1021/Cr00027A007 |
0.336 |
|
| 1994 |
Carlson ML, Regan R, Elber R, Li H, Phillips GN, Olson JS, Gibson QH. Nitric Oxide Recombination to Double Mutants of Myoglobin: Role of Ligand Diffusion in a Fluctuating Heme Pocket Biochemistry. 33: 10597-10606. DOI: 10.1021/bi00201a005 |
0.581 |
|
| 1993 |
Smerdon SJ, Krzywda S, Wilkinson AJ, Brantley RE, Carver TE, Hargrove MS, Olson JS. Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin. Biochemistry. 32: 5132-8. PMID 8494890 DOI: 10.1021/Bi00070A023 |
0.485 |
|
| 1993 |
Brantley RE, Smerdon SJ, Wilkinson AJ, Singleton EW, Olson JS. The mechanism of autooxidation of myoglobin. The Journal of Biological Chemistry. 268: 6995-7010. PMID 8463233 |
0.383 |
|
| 1993 |
Ikeda-Saito M, Dou Y, Yonetani T, Olson JS, Li T, Regan R, Gibson QH. Ligand diffusion in the distal heme pocket of myoglobin. A primary determinant of geminate rebinding. The Journal of Biological Chemistry. 268: 6855-7. PMID 8463211 |
0.559 |
|
| 1993 |
Chang WI, Olson JS, Matthews KS. Lysine 84 is at the subunit interface of lac repressor protein. The Journal of Biological Chemistry. 268: 17613-22. PMID 8349640 |
0.325 |
|
| 1993 |
Gibson QH, Regan R, Olson JS, Carver TE, Dixon B, Pohajdak B, Sharma PK, Vinogradov SN. Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29-->Tyr sperm whale myoglobin mutant. The Journal of Biological Chemistry. 268: 16993-8. PMID 8349589 |
0.577 |
|
| 1993 |
Cameron AD, Smerdon SJ, Wilkinson AJ, Habash J, Helliwell JR, Li T, Olson JS. Distal pocket polarity in ligand binding to myoglobin: deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by X-ray crystallography and infrared spectroscopy. Biochemistry. 32: 13061-70. PMID 8241160 DOI: 10.1021/Bi00211A016 |
0.519 |
|
| 1993 |
Quillin ML, Arduini RM, Olson JS, Phillips GN. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. Journal of Molecular Biology. 234: 140-55. PMID 8230194 DOI: 10.1006/Jmbi.1993.1569 |
0.594 |
|
| 1992 |
Carver TE, Brantley RE, Singleton EW, Arduini RM, Quillin ML, Phillips GN, Olson JS. A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate. The Journal of Biological Chemistry. 267: 14443-50. PMID 1629229 |
0.41 |
|
| 1992 |
Gibson QH, Regan R, Elber R, Olson JS, Carver TE. Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants. The Journal of Biological Chemistry. 267: 22022-34. PMID 1429552 |
0.6 |
|
| 1991 |
Carver TE, Olson JS, Smerdon SJ, Krzywda S, Wilkinson AJ, Gibson QH, Blackmore RS, Ropp JD, Sligar SG. Contributions of residue 45(CD3) and heme-6-propionate to the biomolecular and geminate recombination reactions of myoglobin. Biochemistry. 30: 4697-705. PMID 2029516 DOI: 10.1021/Bi00233A009 |
0.636 |
|
| 1991 |
Mathews AJ, Olson JS, Renaud JP, Tame J, Nagai K. The assignment of carbon monoxide association rate constants to the alpha and beta subunits in native and mutant human deoxyhemoglobin tetramers. The Journal of Biological Chemistry. 266: 21631-9. PMID 1939192 |
0.301 |
|
| 1991 |
Vandegriff KD, Le Tellier YC, Winslow RM, Rohlfs RJ, Olson JS. Determination of the rate and equilibrium constants for oxygen and carbon monoxide binding to R-state human hemoglobin cross-linked between the alpha subunits at lysine 99. The Journal of Biological Chemistry. 266: 17049-59. PMID 1910038 |
0.326 |
|
| 1990 |
Carver TE, Rohlfs RJ, Olson JS, Gibson QH, Blackmore RS, Springer BA, Sligar SG. Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques. The Journal of Biological Chemistry. 265: 20007-20. PMID 2246277 |
0.638 |
|
| 1989 |
Johnson KA, Olson JS, Phillips GN. Structure of myoglobin-ethyl isocyanide histidine as a swinging door for ligand entry Journal of Molecular Biology. 207: 459-463. PMID 2754735 DOI: 10.1016/0022-2836(89)90269-6 |
0.509 |
|
| 1988 |
Rohlfs RJ, Olson JS, Gibson QH. A comparison of the geminate recombination kinetics of several monomeric heme proteins. The Journal of Biological Chemistry. 263: 1803-13. PMID 3338995 |
0.627 |
|
| 1988 |
Olson JS, Mathews AJ, Rohlfs RJ, Springer BA, Egeberg KD, Sligar SG, Tame J, Renaud JP, Nagai K. The role of the distal histidine in myoglobin and haemoglobin. Nature. 336: 265-6. PMID 3057383 DOI: 10.1038/336265A0 |
0.51 |
|
| 1987 |
Olson JS, Rohlfs RJ, Gibson QH. Ligand recombination to the alpha and beta subunits of human hemoglobin. The Journal of Biological Chemistry. 262: 12930-8. PMID 3654596 |
0.592 |
|
| 1987 |
Lemon DD, Nair PK, Boland EJ, Olson JS, Hellums JD. Physiological factors affecting O2 transport by hemoglobin in an in vitro capillary system Journal of Applied Physiology. 62: 798-806. PMID 3558239 DOI: 10.1152/Jappl.1987.62.2.798 |
0.349 |
|
| 1987 |
Boland EJ, Nair PK, Lemon DD, Olson JS, Hellums JD. An in vitro capillary system for studies on microcirculatory O2 transport Journal of Applied Physiology. 62: 791-797. PMID 3558238 DOI: 10.1152/Jappl.1987.62.2.791 |
0.325 |
|
| 1987 |
Chakerian AE, Olson JS, Matthews KS. Thermodynamic analysis of inducer binding to the lactose repressor protein: contributions of galactosyl hydroxyl groups and beta substituents. Biochemistry. 26: 7250-5. PMID 3427073 DOI: 10.1021/Bi00397A009 |
0.379 |
|
| 1986 |
Gibson QH, Olson JS, McKinnie RE, Rohlfs RJ. A kinetic description of ligand binding to sperm whale myoglobin. The Journal of Biological Chemistry. 261: 10228-39. PMID 3733708 |
0.587 |
|
| 1986 |
Daly TJ, Olson JS, Matthews KS. Formation of mixed disulfide adducts at cysteine-281 of the lactose repressor protein affects operator and inducer binding parameters. Biochemistry. 25: 5468-74. PMID 3535878 DOI: 10.1021/Bi00367A018 |
0.411 |
|
| 1986 |
Whitson PA, Olson JS, Matthews KS. Thermodynamic analysis of the lactose repressor-operator DNA interaction. Biochemistry. 25: 3852-8. PMID 3527258 DOI: 10.1021/Bi00361A017 |
0.325 |
|
| 1985 |
Chakerian AE, Pfahl M, Olson JS, Matthews KS. A mutant lactose represser with altered inducer and operator binding parameters Journal of Molecular Biology. 183: 43-51. PMID 3892017 DOI: 10.1016/0022-2836(85)90279-7 |
0.437 |
|
| 1983 |
Olson JS, McKinnie RE, Mims MP, White DK. Mechanisms of ligand binding to pentacoordinate protoheme Journal of the American Chemical Society. 105: 1522-1527. DOI: 10.1021/Ja00344A019 |
0.391 |
|
| 1979 |
Hille R, Olson JS, Palmer G. Spectral transitions of nitrosyl hemes during ligand binding to hemoglobin. The Journal of Biological Chemistry. 254: 12110-20. PMID 40990 |
0.677 |
|
| 1977 |
Hille R, Palmer G, Olson JS. Chain equivalence in reaction of nitric oxide with hemoglobin. The Journal of Biological Chemistry. 252: 403-5. PMID 188812 |
0.683 |
|
| 1977 |
Ellen Friedman B, Olson JS, Matthews KS. Interaction of lac repressor with inducer. Kinetic and equilibrium measurements Journal of Molecular Biology. 111: 27-39. PMID 16140 DOI: 10.1016/S0022-2836(77)80129-0 |
0.385 |
|
| 1976 |
Olson JS. Spectral differences between the α and β heme groups within human deoxyhemoglobin Proceedings of the National Academy of Sciences of the United States of America. 73: 1140-1144. PMID 1063394 DOI: 10.1073/Pnas.73.4.1140 |
0.36 |
|
| 1976 |
Olson JS, Binger C. The effect of ligand size and stereochemistry on the reactivity of the α and β chains within hemoglobin Bba - Protein Structure. 434: 428-439. PMID 952895 DOI: 10.1016/0005-2795(76)90233-6 |
0.358 |
|
| 1974 |
Olson JS, Ballou DP, Palmer G, Massey V. The mechanism of action of xanthine oxidase. The Journal of Biological Chemistry. 249: 4363-82. PMID 4367215 |
0.634 |
|
| 1974 |
Olson JS, Ballow DP, Palmer G, Massey V. The reaction of xanthine oxidase with molecular oxygen. The Journal of Biological Chemistry. 249: 4350-62. PMID 4367214 |
0.66 |
|
| 1973 |
Moffat K, Olson JS, Gibson QH, Kilmartin JV. The ligand-binding properties of desHis (146beta) hemoglobin. The Journal of Biological Chemistry. 248: 6387-93. PMID 4730324 |
0.646 |
|
| 1973 |
Olson JS, Gibson QH. The release of protons and anions during ligand binding to human deoxyhemoglobin. The Journal of Biological Chemistry. 248: 1623-30. PMID 4694728 |
0.534 |
|
| 1973 |
Olson JS, Gibson QH. The effects of pH and anions on the properties of the alpha and beta chains within human deoxyhemoglobin. The Journal of Biological Chemistry. 248: 1616-22. PMID 4694727 |
0.472 |
|
| 1973 |
Andersen ME, Olson JS, Gibson QH, Carey FG. Studies on ligand binding to hemoglobins from teleosts and elasmobranchs. The Journal of Biological Chemistry. 248: 331-41. PMID 4692838 |
0.555 |
|
| 1972 |
Olson JS, Gibson QH. The functional properties of hemoglobin Bethesda ( 2 2 145His ). The Journal of Biological Chemistry. 247: 3662-70. PMID 5030636 |
0.431 |
|
| 1972 |
Olson JS, Gibson QH. The reaction of n-butyl isocyanide with human hemoglobin. II. The ligand-binding properties of the and chains within deoxyhemoglobin. The Journal of Biological Chemistry. 247: 1713-26. PMID 5012756 |
0.538 |
|
| 1972 |
Olson JS, Gibson QH, Nagel RL, Hamilton HB. The ligand-binding properties of hemoglobin Hiroshima ( 2 2 146asp ). The Journal of Biological Chemistry. 247: 7485-93. PMID 4636319 |
0.554 |
|
| 1971 |
Linstrom TR, Olson JS, Mock NH, Gibson QH, Ho C. Nuclear magnetic resonance studies of hemoglobins. 8. Evidence for preferential ligand binding to chains within deoxyhemoglobins. Biochemical and Biophysical Research Communications. 45: 22-6. PMID 5139924 DOI: 10.1016/0006-291X(71)90044-1 |
0.498 |
|
| 1971 |
Olson JS, Andersen ME, Gibson QH. The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins. The Journal of Biological Chemistry. 246: 5919-23. PMID 5116659 |
0.46 |
|
| 1971 |
Olson JS, Gibson QH. The reaction of n-butyl isocyanide with human hemoglobin. I. Determination of the kinetic parameters involved in the last step in ligand binding. The Journal of Biological Chemistry. 246: 5241-53. PMID 5106729 |
0.537 |
|
| 1970 |
Olson JS, Gibson QH. Organic phosphates and the reaction of N-butyl isocyanide with human hemoglobin. Biochemical and Biophysical Research Communications. 41: 421-6. PMID 5518171 DOI: 10.1016/0006-291X(70)90521-8 |
0.504 |
|
| 1970 |
Edelstein SJ, Rehmar MJ, Olson JS, Gibson QH. Functional aspects of the subunit association-dissociation equilibria of hemoglobin. The Journal of Biological Chemistry. 245: 4372-81. PMID 5498425 |
0.451 |
|
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