| Year |
Citation |
Score |
| 2011 |
Kruse AC, Huseby MJ, Shi K, Digre J, Ohlendorf DH, Earhart CA. Structure of a mutant β toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 438-41. PMID 21505235 DOI: 10.1107/S1744309111005239 |
0.739 |
|
| 2010 |
Huseby MJ, Kruse AC, Digre J, Kohler PL, Vocke JA, Mann EE, Bayles KW, Bohach GA, Schlievert PM, Ohlendorf DH, Earhart CA. Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms. Proceedings of the National Academy of Sciences of the United States of America. 107: 14407-12. PMID 20660751 DOI: 10.1073/Pnas.0911032107 |
0.734 |
|
| 2010 |
Hellberg K, Grimsrud PA, Kruse AC, Banaszak LJ, Ohlendorf DH, Bernlohr DA. X-ray crystallographic analysis of adipocyte fatty acid binding protein (aP2) modified with 4-hydroxy-2-nonenal. Protein Science : a Publication of the Protein Society. 19: 1480-9. PMID 20509169 DOI: 10.1002/Pro.427 |
0.375 |
|
| 2009 |
Hertzel AV, Hellberg K, Reynolds JM, Kruse AC, Juhlmann BE, Smith AJ, Sanders MA, Ohlendorf DH, Suttles J, Bernlohr DA. Identification and characterization of a small molecule inhibitor of Fatty Acid binding proteins. Journal of Medicinal Chemistry. 52: 6024-31. PMID 19754198 DOI: 10.1021/Jm900720M |
0.315 |
|
| 2008 |
Yoder AR, Kruse AC, Earhart CA, Ohlendorf DH, Potter LR. Reduced ability of C-type natriuretic peptide (CNP) to activate natriuretic peptide receptor B (NPR-B) causes dwarfism in lbab -/- mice. Peptides. 29: 1575-81. PMID 18554750 DOI: 10.1016/J.Peptides.2008.04.020 |
0.301 |
|
| 2008 |
Getun IV, Brown CK, Tulla-Puche J, Ohlendorf D, Woodward C, Barany G. Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin. Journal of Molecular Biology. 375: 812-23. PMID 18054043 DOI: 10.1016/J.Jmb.2007.10.084 |
0.454 |
|
| 2008 |
Huseby M, Shi K, Kruse A, Schlievert P, Ohlendorf D, Earhart C. Activities and structure of beta toxin Acta Crystallographica Section a Foundations of Crystallography. 64: C355-C355. DOI: 10.1107/S0108767308088648 |
0.748 |
|
| 2007 |
Huseby M, Shi K, Brown CK, Digre J, Mengistu F, Seo KS, Bohach GA, Schlievert PM, Ohlendorf DH, Earhart CA. Structure and biological activities of beta toxin from Staphylococcus aureus. Journal of Bacteriology. 189: 8719-26. PMID 17873030 DOI: 10.1128/Jb.00741-07 |
0.763 |
|
| 2005 |
Brown CK, Gu ZY, Matsuka YV, Purushothaman SS, Winter LA, Cleary PP, Olmsted SB, Ohlendorf DH, Earhart CA. Structure of the streptococcal cell wall C5a peptidase. Proceedings of the National Academy of Sciences of the United States of America. 102: 18391-6. PMID 16344483 DOI: 10.1073/Pnas.0504954102 |
0.407 |
|
| 2005 |
Shi K, Brown CK, Gu ZY, Kozlowicz BK, Dunny GM, Ohlendorf DH, Earhart CA. Structure of peptide sex pheromone receptor PrgX and PrgX/pheromone complexes and regulation of conjugation in Enterococcus faecalis. Proceedings of the National Academy of Sciences of the United States of America. 102: 18596-601. PMID 16339309 DOI: 10.1073/Pnas.0506163102 |
0.326 |
|
| 2005 |
Earhart CA, Vetting MW, Gosu R, Michaud-Soret I, Que L, Ohlendorf DH. Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla. Biochemical and Biophysical Research Communications. 338: 198-205. PMID 16171781 DOI: 10.1016/J.Bbrc.2005.08.221 |
0.71 |
|
| 2005 |
Valley MP, Brown CK, Burk DL, Vetting MW, Ohlendorf DH, Lipscomb JD. Roles of the equatorial tyrosyl iron ligand of protocatechuate 3,4-dioxygenase in catalysis. Biochemistry. 44: 11024-39. PMID 16101286 DOI: 10.1021/Bi050902I |
0.658 |
|
| 2005 |
Ohlendorf DH. Acuracy of refined protein structures. II. Comparison of four independently refined models of human interleukin 1beta. Acta Crystallographica. Section D, Biological Crystallography. 50: 808-12. PMID 15299347 DOI: 10.1107/S0907444994002659 |
0.411 |
|
| 2004 |
Brown CK, Vetting MW, Earhart CA, Ohlendorf DH. Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1. Annual Review of Microbiology. 58: 555-85. PMID 15487948 DOI: 10.1146/Annurev.Micro.57.030502.090927 |
0.634 |
|
| 2004 |
Vetting MW, Wackett LP, Que L, Lipscomb JD, Ohlendorf DH. Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. Journal of Bacteriology. 186: 1945-58. PMID 15028678 DOI: 10.1128/Jb.186.7.1945-1958.2004 |
0.666 |
|
| 2003 |
Ohlendorf DH. Special issue on structural biology. Journal of Bacteriology. 185: 3989. PMID 16559378 DOI: 10.1128/Jb.185.14.3989.2003 |
0.362 |
|
| 2002 |
Orwin PM, Leung DY, Tripp TJ, Bohach GA, Earhart CA, Ohlendorf DH, Schlievert PM. Characterization of a novel staphylococcal enterotoxin-like superantigen, a member of the group V subfamily of pyrogenic toxins. Biochemistry. 41: 14033-40. PMID 12437361 DOI: 10.1021/Bi025977Q |
0.314 |
|
| 2000 |
Mitchell DT, Levitt DG, Schlievert PM, Ohlendorf DH. Structural evidence for the evolution of pyrogenic toxin superantigens. Journal of Molecular Evolution. 51: 520-31. PMID 11116326 DOI: 10.1007/S002390010116 |
0.404 |
|
| 2000 |
Earhart CA, Vath GM, Roggiani M, Schlievert PM, Ohlendorf DH. Structure of streptococcal pyrogenic exotoxin A reveals a novel metal cluster Protein Science. 9: 1847-1851. PMID 11045630 DOI: 10.1110/Ps.9.9.1847 |
0.427 |
|
| 2000 |
Badasso MO, Leiman PG, Tao Y, He Y, Ohlendorf DH, Rossmann MG, Anderson D. Purification, crystallization and initial X-ray analysis of the head-tail connector of bacteriophage phi29. Acta Crystallographica. Section D, Biological Crystallography. 56: 1187-90. PMID 10957642 DOI: 10.1107/S0907444900009239 |
0.405 |
|
| 2000 |
Roggiani M, Stoehr JA, Olmsted SB, Matsuka YV, Pillai S, Ohlendorf DH, Schlievert PM. Toxoids of streptococcal pyrogenic exotoxin A are protective in rabbit models of streptococcal toxic shock syndrome Infection and Immunity. 68: 5011-5017. PMID 10948118 DOI: 10.1128/Iai.68.9.5011-5017.2000 |
0.322 |
|
| 2000 |
McCormick JK, Tripp TJ, Olmsted SB, Matsuka YV, Gahr PJ, Ohlendorf DH, Schlievert PM. Development of streptococcal pyrogenic exotoxin C vaccine toxoids that are protective in the rabbit model of toxic shock syndrome. Journal of Immunology (Baltimore, Md. : 1950). 165: 2306-12. PMID 10925320 DOI: 10.4049/Jimmunol.165.4.2306 |
0.309 |
|
| 2000 |
Vetting MW, D'Argenio DA, Ornston LN, Ohlendorf DH. Structure of Acinetobacter strain ADP1 protocatechuate 3, 4-dioxygenase at 2.2 A resolution: implications for the mechanism of an intradiol dioxygenase. Biochemistry. 39: 7943-55. PMID 10891075 DOI: 10.1021/Bi000151E |
0.698 |
|
| 2000 |
Vetting MW, Ohlendorf DH. The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure (London, England : 1993). 8: 429-40. PMID 10801478 DOI: 10.1016/S0969-2126(00)00122-2 |
0.686 |
|
| 2000 |
Rago JV, Vath GM, Tripp TJ, Bohach GA, Ohlendorf DH, Schlievert PM. Staphylococcal exfoliative toxins cleave α- and β-melanocyte- stimulating hormones Infection and Immunity. 68: 2366-2368. PMID 10722646 DOI: 10.1128/Iai.68.4.2366-2368.2000 |
0.326 |
|
| 2000 |
Rago JV, Vath GM, Bohach GA, Ohlendorf DH, Schlievert PM. Mutational analysis of the superantigen staphylococcal exfoliative toxin A (ETA) Journal of Immunology. 164: 2207-2213. PMID 10657676 DOI: 10.4049/Jimmunol.164.4.2207 |
0.324 |
|
| 1999 |
D'Argenio DA, Vetting MW, Ohlendorf DH, Ornston LN. Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases. Journal of Bacteriology. 181: 6478-87. PMID 10515940 DOI: 10.1128/Jb.181.20.6478-6487.1999 |
0.662 |
|
| 1999 |
Vath GM, Earhart CA, Monie DD, Iandolo JJ, Schlievert PM, Ohlendorf DH. The crystal structure of exfoliative toxin B: a superantigen with enzymatic activity. Biochemistry. 38: 10239-46. PMID 10441117 DOI: 10.1021/Bi990721E |
0.437 |
|
| 1998 |
Ohlendorf DH, Tronrud DE, Matthews BW. Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity. Journal of Molecular Biology. 280: 129-36. PMID 9653036 DOI: 10.1006/jmbi.1998.1849 |
0.328 |
|
| 1998 |
Earhart CA, Mitchell DT, Murray DL, Pinheiro DM, Matsumura M, Schlievert PM, Ohlendorf DH. Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity. Biochemistry. 37: 7194-202. PMID 9585531 DOI: 10.1021/Bi9721896 |
0.404 |
|
| 1998 |
Frazee RW, Orville AM, Dolbeare KB, Yu H, Ohlendorf DH, Lipscomb JD. The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates. Biochemistry. 37: 2131-44. PMID 9485360 DOI: 10.1021/Bi972047B |
0.425 |
|
| 1998 |
Orville AM, Lipscomb JD, Ohlendorf DH. Probing the Reaction Mechanism of Protocatechuate 3,4-Dioxygenase with X-Ray Crystallography The Keio Journal of Medicine. 45: 282-288. DOI: 10.1007/978-4-431-68476-3_35 |
0.333 |
|
| 1998 |
Lipscomb JD, Orville AM, Frazee RW, Miller MA, Ohlendorf DH. Fundamentally Divergent Strategies for Oxygen Activation by Fe 2+ and Fe 3+ Catecholic Dioxygenases The Keio Journal of Medicine. 45: 263-275. DOI: 10.1007/978-4-431-68476-3_33 |
0.304 |
|
| 1997 |
Elgren TE, Orville AM, Kelly KA, Lipscomb JD, Ohlendorf DH, Que L. Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate. Biochemistry. 36: 11504-13. PMID 9298971 DOI: 10.1021/Bi970691K |
0.41 |
|
| 1997 |
Orville AM, Lipscomb JD, Ohlendorf DH. Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding. Biochemistry. 36: 10052-66. PMID 9254600 DOI: 10.1021/Bi970469F |
0.41 |
|
| 1997 |
Orville AM, Elango N, Lipscomb JD, Ohlendorf DH. Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site. Biochemistry. 36: 10039-51. PMID 9254599 DOI: 10.1021/Bi970468N |
0.378 |
|
| 1997 |
Prasad GS, Radhakrishnan R, Mitchell DT, Earhart CA, Dinges MM, Cook WJ, Schlievert PM, Ohlendorf DH. Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activity. Protein Science : a Publication of the Protein Society. 6: 1220-7. PMID 9194182 DOI: 10.1002/Pro.5560060610 |
0.397 |
|
| 1997 |
Elango N, Radhakrishnan R, Froland WA, Wallar BJ, Earhart CA, Lipscomb JD, Ohlendorf DH. Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b. Protein Science : a Publication of the Protein Society. 6: 556-68. PMID 9070438 DOI: 10.1002/Pro.5560060305 |
0.45 |
|
| 1997 |
Vath GM, Earhart CA, Rago JV, Kim MH, Bohach GA, Schlievert PM, Ohlendorf DH. The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease Biochemistry. 36: 1559-1566. PMID 9048539 DOI: 10.1021/Bi962614F |
0.422 |
|
| 1996 |
Murray DL, Earhart CA, Mitchell DT, Ohlendorf DH, Novick RP, Schlievert PM. Localization of biologically important regions on toxic shock syndrome toxin 1. Infection and Immunity. 64: 371-4. PMID 8557369 DOI: 10.1128/Iai.64.1.371-374.1996 |
0.357 |
|
| 1995 |
Schlievert PM, Bohach GA, Ohlendorf DH, Stauffacher CV, Leung DY, Murray DL, Prasad GS, Earhart CA, Jablonski LM, Hoffmann ML, Chi YI. Molecular structure of staphylococcus and streptococcus superantigens. Journal of Clinical Immunology. 15: 4S-10S. PMID 8613491 DOI: 10.1007/Bf01540887 |
0.347 |
|
| 1995 |
Malchiodi EL, Eisenstein E, Fields BA, Ohlendorf DH, Schlievert PM, Karjalainen K, Mariuzza RA. Superantigen binding to a T cell receptor γ chain of known three-dimensional structure Journal of Experimental Medicine. 182: 1833-1845. PMID 7500029 DOI: 10.1084/Jem.182.6.1833 |
0.338 |
|
| 1995 |
Orville AM, Elango N, Ohlendorf DH, Lipscomb JD. Crystal structures of substrate & substrate analog complexes of protocatechuate 3,4-dioxygenase yield mechanistic insights Journal of Inorganic Biochemistry. 59: 367. DOI: 10.1016/0162-0134(95)97465-3 |
0.374 |
|
| 1995 |
Schad EM, Zaitseva I, Zaitsev VN, Dohlsten M, Kalland T, Schlievert PM, Ohlendorf DH, Svensson LA. Crystal structure of the superantigen staphylococcal enterotoxin type A. The Embo Journal. 14: 3292-3301. DOI: 10.1002/J.1460-2075.1995.Tb07336.X |
0.459 |
|
| 1994 |
Froland WA, Dyer DH, Radhakrishnan R, Earhart CA, Lipscomb JD, Ohlendorf DH. Preliminary crystallographic analysis of methane mono-oxygenase hydroxylase from Methylosinus trichosporium OB3b. Journal of Molecular Biology. 236: 379-81. PMID 8107121 DOI: 10.1006/Jmbi.1994.1145 |
0.348 |
|
| 1994 |
Earhart CA, Hall MD, Michaud-Soret I, Que L, Ohlendorf DH. Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1. Journal of Molecular Biology. 236: 377-8. PMID 8107120 DOI: 10.1006/Jmbi.1994.1144 |
0.41 |
|
| 1994 |
Earhart CA, Radhakrishnan R, Orville AM, Lipscomb JD, Ohlendorf DH. Preliminary crystallographic study of protocatechuate 3,4-dioxygenase from Brevibacterium fuscum. Journal of Molecular Biology. 236: 374-6. PMID 8107119 DOI: 10.1006/Jmbi.1994.1143 |
0.409 |
|
| 1994 |
Vetting MW, Earhart CA, Ohlendorf DH. Crystallization and preliminary X-ray analysis of protocatechuate 3,4-dioxygenase from Acinetobacter calcoaceticus. Journal of Molecular Biology. 236: 372-3. PMID 8107118 DOI: 10.1006/Jmbi.1994.1142 |
0.666 |
|
| 1994 |
Ohlendorf DH, Orville AM, Lipscomb JD. Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution. Journal of Molecular Biology. 244: 586-608. PMID 7990141 DOI: 10.1006/Jmbi.1994.1754 |
0.462 |
|
| 1993 |
Earhart CA, Prasad GS, Murray DL, Novick RP, Schlievert PM, Ohlendorf DH. Growth and analysis of crystal forms of toxic shock syndrome toxin 1. Proteins. 17: 329-34. PMID 8272430 DOI: 10.1002/Prot.340170310 |
0.382 |
|
| 1993 |
Prasad GS, Earhart CA, Murray DL, Novick RP, Schlievert PM, Ohlendorf DH. Structure of toxic shock syndrome toxin 1. Biochemistry. 32: 13761-6. PMID 8268150 DOI: 10.1021/Bi00213A001 |
0.346 |
|
| 1992 |
Siu DC, Orville AM, Lipscomb JD, Ohlendorf DH, Que L. Resonance Raman studies of the protocatechuate 3,4-dioxygenase from Brevibacterium fuscum. Biochemistry. 31: 10443-8. PMID 1420163 DOI: 10.1021/Bi00158A005 |
0.331 |
|
| 1991 |
DeLucas LJ, Smith CD, Smith W, Vijay-Kumar S, Senadhi SE, Ealick SE, Carter DC, Snyder RS, Weber PC, Salemme FR, Ohlendorf DH, Einspahr HM, Clancy LL, Navia MA, McKeever BM, et al. Protein crystal growth results for shuttle flights STS-26 and STS-29 Journal of Crystal Growth. 110: 302-311. DOI: 10.1016/0022-0248(91)90899-G |
0.331 |
|
| 1990 |
Ohlendorf DH, Anderson WF, Takeda Y, Matthews BW. High resolution structural studies of Cro repressor protein and implications for DNA recognition. Journal of Biomolecular Structure & Dynamics. 1: 553-63. PMID 6400887 DOI: 10.1080/07391102.1983.10507461 |
0.357 |
|
| 1989 |
Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR. Structural origins of high-affinity biotin binding to streptavidin. Science. 243: 85-88. DOI: 10.2210/Pdb1Stp/Pdb |
0.439 |
|
| 1988 |
Ohlendorf DH, Lipscomb JD, Weber PC. Structure and assembly of protocatechuate 3,4-dioxygenase. Nature. 336: 403-5. PMID 3194022 DOI: 10.1038/336403A0 |
0.418 |
|
| 1988 |
Takeda Y, Kim JG, Caday CG, Steers E, Ohlendorf DH, Anderson WF, Matthews BW. Different interactions used by Cro repressor in specific and nonspecific DNA binding. Journal of Biological Chemistry. 261: 8608-8616. DOI: 10.2210/Pdb1Cro/Pdb |
0.305 |
|
| 1987 |
Ohlendorf DH, Weber PC, Lipscomb JD. Determination of the quaternary structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. Journal of Molecular Biology. 195: 225-7. PMID 3116260 DOI: 10.1016/0022-2836(87)90340-8 |
0.411 |
|
| 1986 |
Ohlendorf DH, Anderson WF, Matthews BW. Many gene-regulatory proteins appear to have a similar alpha-helical fold that binds DNA and evolved from a common precursor. Journal of Molecular Evolution. 19: 109-14. PMID 6571216 DOI: 10.1007/Bf02300748 |
0.319 |
|
| 1985 |
Weber PC, Sheriff S, Ohlendorf DH, Finzel BC, Salemme FR. The 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41. Proceedings of the National Academy of Sciences of the United States of America. 82: 8473-7. PMID 3936036 DOI: 10.1073/Pnas.82.24.8473 |
0.393 |
|
| 1985 |
Ohlendorf DH, Matthew JB. Electrostatics and flexibility in protein-DNA interactions Advances in Biophysics. 20: 137-151. PMID 3914833 DOI: 10.1016/0065-227X(85)90034-6 |
0.304 |
|
| 1983 |
Anderson WF, Cygler M, Vandonselaar M, Ohlendorf DH, Matthews BW, Kim J, Takeda Y. Crystallographic data for complexes of the Cro repressor with DNA. Journal of Molecular Biology. 168: 903-6. PMID 6887256 DOI: 10.1016/S0022-2836(83)80082-5 |
0.364 |
|
| 1983 |
Takeda Y, Ohlendorf DH, Anderson WF, Matthews BW. DNA-binding proteins. Science (New York, N.Y.). 221: 1020-6. PMID 6308768 DOI: 10.1126/Science.6308768 |
0.327 |
|
| 1983 |
Ohlendorf DH, Anderson WF, Lewis M, Pabo CO, Matthews BW. Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda. Journal of Molecular Biology. 169: 757-69. PMID 6226802 DOI: 10.1016/S0022-2836(83)80169-7 |
0.338 |
|
| 1983 |
Matthews B, Ohlendorf D, Anderson W, Fisher R, Takeda Y. How does cro repressor recognize its DNA target sites? Trends in Biochemical Sciences. 8: 25-29. DOI: 10.1016/0968-0004(83)90065-8 |
0.309 |
|
| 1982 |
Matthews BW, Ohlendorf DH, Anderson WF, Takeda Y. Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor. Proceedings of the National Academy of Sciences of the United States of America. 79: 1428-32. PMID 6951187 DOI: 10.1073/Pnas.79.5.1428 |
0.341 |
|
| 1982 |
Ohlendorf DH, Anderson WF, Fisher RG, Takeda Y, Matthews BW. The molecular basis of DNA-protein recognition inferred from the structure of cro repressor. Nature. 298: 718-23. PMID 6213863 DOI: 10.1038/298718A0 |
0.328 |
|
| 1982 |
Steitz TA, Ohlendorf DH, McKay DB, Anderson WF, Matthews BW. Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins. Proceedings of the National Academy of Sciences of the United States of America. 79: 3097-100. PMID 6212926 DOI: 10.1073/Pnas.79.10.3097 |
0.368 |
|
| 1981 |
Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. Structure of the cro repressor from bacteriophage lambda and its interaction with DNA. Nature. 290: 754-8. PMID 6452580 DOI: 10.1038/290754A0 |
0.346 |
|
| 1981 |
Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW. Structure of the bacteriophage lambda Cro repressor: model for protein–DNA interactions Acta Crystallographica Section a Foundations of Crystallography. 37: C46-C46. DOI: 10.1107/S010876738109819X |
0.325 |
|
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