| Year |
Citation |
Score |
| 2019 |
Magala P, Klevit RE, Thomas WE, Sokurenko EV, Stenkamp RE. RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain. Proteins. PMID 31622514 DOI: 10.1002/Prot.25840 |
0.431 |
|
| 2018 |
Stenkamp RE. Identifying G protein-coupled receptor dimers from crystal packings. Acta Crystallographica. Section D, Structural Biology. 74: 655-670. PMID 29968675 DOI: 10.1107/S2059798318008136 |
0.513 |
|
| 2016 |
Baugh L, Le Trong I, Stayton PS, Stenkamp RE, Lybrand TP. A Streptavidin Binding Site Mutation Yields an Unexpected Result: An Ionized Asp128 Residue is Not Essential for Strong Biotin Binding. Biochemistry. PMID 27603565 DOI: 10.1021/Acs.Biochem.6B00698 |
0.35 |
|
| 2015 |
Scian M, Le Trong I, Mazari AM, Mannervik B, Atkins WM, Stenkamp RE. Comparison of epsilon- and delta-class glutathione S-transferases: the crystal structures of the glutathione S-transferases DmGSTE6 and DmGSTE7 from Drosophila melanogaster. Acta Crystallographica. Section D, Biological Crystallography. 71: 2089-98. PMID 26457432 DOI: 10.1107/S1399004715013929 |
0.431 |
|
| 2015 |
Kaminsky W, Stenkamp RE, Skubatz H. Crystal and molecular structure of the analgesic tetrapeptide, L-Phe-L-Leu-L-Pro-L-Ser. Biopolymers. 104: 84-90. PMID 25581776 DOI: 10.1002/Bip.22606 |
0.344 |
|
| 2014 |
Teller DC, Behnke CA, Pappan K, Shen Z, Reese JC, Reeck GR, Stenkamp RE. The structure of rice weevil pectin methylesterase. Acta Crystallographica. Section F, Structural Biology Communications. 70: 1480-4. PMID 25372813 DOI: 10.1107/S2053230X14020433 |
0.772 |
|
| 2014 |
Pruneda JN, Smith FD, Daurie A, Swaney DL, Villén J, Scott JD, Stadnyk AW, Le Trong I, Stenkamp RE, Klevit RE, Rohde JR, Brzovic PS. E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis. The Embo Journal. 33: 437-49. PMID 24446487 DOI: 10.1002/Embj.201386386 |
0.326 |
|
| 2013 |
Le Trong I, Chu V, Xing Y, Lybrand TP, Stayton PS, Stenkamp RE. Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidin. Acta Crystallographica. Section D, Biological Crystallography. 69: 968-77. PMID 23695241 DOI: 10.1107/S0907444913003855 |
0.447 |
|
| 2012 |
Scian M, Lin JC, Le Trong I, Makhatadze GI, Stenkamp RE, Andersen NH. Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction. Proceedings of the National Academy of Sciences of the United States of America. 109: 12521-5. PMID 22802678 DOI: 10.1073/Pnas.1121421109 |
0.497 |
|
| 2012 |
Li M, Le Trong I, Carl MA, Larson ET, Chou S, De Leon JA, Dove SL, Stenkamp RE, Mougous JD. Structural basis for type VI secretion effector recognition by a cognate immunity protein. Plos Pathogens. 8: e1002613. PMID 22511866 DOI: 10.1371/Journal.Ppat.1002613 |
0.354 |
|
| 2012 |
Baugh L, Le Trong I, Cerutti DS, Mehta N, Gülich S, Stayton PS, Stenkamp RE, Lybrand TP. Second-contact shell mutation diminishes streptavidin-biotin binding affinity through transmitted effects on equilibrium dynamics. Biochemistry. 51: 597-607. PMID 22145986 DOI: 10.1021/Bi201221J |
0.364 |
|
| 2011 |
Le Trong I, Wang Z, Hyre DE, Lybrand TP, Stayton PS, Stenkamp RE. Streptavidin and its biotin complex at atomic resolution. Acta Crystallographica. Section D, Biological Crystallography. 67: 813-21. PMID 21904034 DOI: 10.1107/S0907444911027806 |
0.483 |
|
| 2011 |
Aprikian P, Interlandi G, Kidd BA, Le Trong I, Tchesnokova V, Yakovenko O, Whitfield MJ, Bullitt E, Stenkamp RE, Thomas WE, Sokurenko EV. The bacterial fimbrial tip acts as a mechanical force sensor. Plos Biology. 9: e1000617. PMID 21572990 DOI: 10.1371/Journal.Pbio.1000617 |
0.324 |
|
| 2010 |
Le Trong I, Aprikian P, Kidd BA, Thomas WE, Sokurenko EV, Stenkamp RE. Donor strand exchange and conformational changes during E. coli fimbrial formation. Journal of Structural Biology. 172: 380-8. PMID 20570733 DOI: 10.1016/J.Jsb.2010.06.002 |
0.455 |
|
| 2010 |
Le Trong I, Aprikian P, Kidd BA, Forero-Shelton M, Tchesnokova V, Rajagopal P, Rodriguez V, Interlandi G, Klevit R, Vogel V, Stenkamp RE, Sokurenko EV, Thomas WE. Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting. Cell. 141: 645-55. PMID 20478255 DOI: 10.1016/J.Cell.2010.03.038 |
0.365 |
|
| 2010 |
Baugh L, Le Trong I, Cerutti DS, Gülich S, Stayton PS, Stenkamp RE, Lybrand TP. A distal point mutation in the streptavidin-biotin complex preserves structure but diminishes binding affinity: experimental evidence of electronic polarization effects? Biochemistry. 49: 4568-70. PMID 20462252 DOI: 10.1021/Bi1005392 |
0.382 |
|
| 2010 |
Behnke CA, Le Trong I, Godden JW, Merritt EA, Teller DC, Bajorath J, Stenkamp RE. Atomic resolution studies of carbonic anhydrase II. Acta Crystallographica. Section D, Biological Crystallography. 66: 616-27. PMID 20445237 DOI: 10.1107/S0907444910006554 |
0.799 |
|
| 2010 |
Balogh LM, Le Trong I, Kripps KA, Shireman LM, Stenkamp RE, Zhang W, Mannervik B, Atkins WM. Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal. Biochemistry. 49: 1541-8. PMID 20085333 DOI: 10.1021/Bi902038U |
0.302 |
|
| 2010 |
Stenkamp RE, Teller DC, Palczewski K. ChemInform Abstract: Crystal Structure of Rhodopsin: A G-Protein-Coupled Receptor Cheminform. 33: no-no. DOI: 10.1002/chin.200249275 |
0.638 |
|
| 2009 |
Balogh LM, Le Trong I, Kripps KA, Tars K, Stenkamp RE, Mannervik B, Atkins WM. Structural analysis of a glutathione transferase A1-1 mutant tailored for high catalytic efficiency with toxic alkenals. Biochemistry. 48: 7698-704. PMID 19618965 DOI: 10.1021/Bi900895B |
0.436 |
|
| 2009 |
Saari JC, Nawrot M, Stenkamp RE, Teller DC, Garwin GG. Release of 11-cis-retinal from cellular retinaldehyde-binding protein by acidic lipids. Molecular Vision. 15: 844-54. PMID 19390642 |
0.536 |
|
| 2009 |
Cerutti DS, Le Trong I, Stenkamp RE, Lybrand TP. Dynamics of the streptavidin-biotin complex in solution and in its crystal lattice: distinct behavior revealed by molecular simulations. The Journal of Physical Chemistry. B. 113: 6971-85. PMID 19374419 DOI: 10.1021/Jp9010372 |
0.326 |
|
| 2009 |
Thomas WE, Le Trong I, Aprikian P, Forero M, Kidd B, Interlandi G, Tchesnekova V, Yakovenko O, Vogel V, Stenkamp R, Sokurenko E. Allosteric Regulation Across a β-Sandwich Protein: How a Bacterial Adhesive Protein is Activated by Mechanical Force Biophysical Journal. 96: 548a. DOI: 10.1016/J.Bpj.2008.12.2969 |
0.454 |
|
| 2008 |
Cerutti DS, Le Trong I, Stenkamp RE, Lybrand TP. Simulations of a protein crystal: explicit treatment of crystallization conditions links theory and experiment in the streptavidin-biotin complex. Biochemistry. 47: 12065-77. PMID 18950193 DOI: 10.1021/Bi800894U |
0.372 |
|
| 2008 |
Stenkamp RE. Alternative models for two crystal structures of bovine rhodopsin. Acta Crystallographica. Section D, Biological Crystallography. 902-4. PMID 18645239 DOI: 10.1107/S0907444908017162 |
0.407 |
|
| 2008 |
Rutherford K, Le Trong I, Stenkamp RE, Parson WW. Crystal Structures of Human 108V and 108M Catechol O-Methyltransferase Journal of Molecular Biology. 380: 120-130. PMID 18486144 DOI: 10.1016/J.Jmb.2008.04.040 |
0.428 |
|
| 2008 |
Fox D, Le Trong I, Rajagopal P, Brzovic PS, Stenkamp RE, Klevit RE. Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences Journal of Biological Chemistry. 283: 21179-21186. PMID 18480049 DOI: 10.1074/Jbc.M802333200 |
0.391 |
|
| 2008 |
Le Trong I, Stenkamp RE. Alternative models for two crystal structures of Candida albicans 3,4-dihydroxy-2-butanone 4-phosphate synthase. Acta Crystallographica. Section D, Biological Crystallography. 64: 219-20. PMID 18219123 DOI: 10.1107/S0907444907056132 |
0.444 |
|
| 2008 |
Creus M, Pordea A, Rossel T, Sardo A, Letondor C, Ivanova A, LeTrong I, Stenkamp RE, Ward TR. X-ray structure and designed evolution of an artificial transfer hydrogenase Angewandte Chemie - International Edition. 47: 1400-1404. PMID 18176932 DOI: 10.1002/Anie.200704865 |
0.351 |
|
| 2008 |
Korotkova N, Yang Y, Le Trong I, Cota E, Demeler B, Marchant J, Thomas WE, Stenkamp RE, Moseley SL, Matthews S. Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation. Molecular Microbiology. 67: 420-34. PMID 18086185 DOI: 10.1111/J.1365-2958.2007.06054.X |
0.417 |
|
| 2008 |
Creus M, Pordea A, Rossel T, Sardo A, Letondor C, Ivanova A, LeTrong I, Stenkamp R, Ward T. Inside Cover: X-Ray Structure and Designed Evolution of an Artificial Transfer Hydrogenase (Angew. Chem. Int. Ed. 8/2008) Angewandte Chemie International Edition. 47: 1342-1342. DOI: 10.1002/Anie.200890025 |
0.315 |
|
| 2008 |
Creus M, Pordea A, Rossel T, Sardo A, Letondor C, Ivanova A, LeTrong I, Stenkamp R, Ward T. Innentitelbild: X-Ray Structure and Designed Evolution of an Artificial Transfer Hydrogenase (Angew. Chem. 8/2008) Angewandte Chemie. 120: 1362-1362. DOI: 10.1002/Ange.200890025 |
0.316 |
|
| 2007 |
Lodowski DT, Salom D, Le Trong I, Teller DC, Ballesteros JA, Palczewski K, Stenkamp RE. Reprint of "Crystal packing analysis of Rhodopsin crystals" [J. Struct. Biol. 158 (2007) 455-462]. Journal of Structural Biology. 159: 253-60. PMID 17660064 DOI: 10.1016/S1047-8477(07)00166-9 |
0.666 |
|
| 2007 |
Lodowski DT, Salom D, Le Trong I, Teller DC, Ballesteros JA, Palczewski K, Stenkamp RE. Crystal packing analysis of Rhodopsin crystals. Journal of Structural Biology. 158: 455-62. PMID 17374491 DOI: 10.1016/J.Jsb.2007.01.017 |
0.666 |
|
| 2007 |
Le Trong I, Stenkamp RE. An alternate description of two crystal structures of phospholipase A2 from Bungarus caeruleus. Acta Crystallographica. Section D, Biological Crystallography. 63: 548-9. PMID 17372360 DOI: 10.1107/S0907444907007354 |
0.4 |
|
| 2006 |
Salom D, Lodowski DT, Stenkamp RE, Le Trong I, Golczak M, Jastrzebska B, Harris T, Ballesteros JA, Palczewski K. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 103: 16123-8. PMID 17060607 DOI: 10.1073/Pnas.0608022103 |
0.464 |
|
| 2006 |
Salom D, Le Trong I, Pohl E, Ballesteros JA, Stenkamp RE, Palczewski K, Lodowski DT. Improvements in G protein-coupled receptor purification yield light stable rhodopsin crystals. Journal of Structural Biology. 156: 497-504. PMID 16837211 DOI: 10.1016/J.Jsb.2006.05.003 |
0.486 |
|
| 2006 |
Korotkova N, Le Trong I, Samudrala R, Korotkov K, Van Loy CP, Bui AL, Moseley SL, Stenkamp RE. Crystal structure and mutational analysis of the DaaE adhesin of Escherichia coli Journal of Biological Chemistry. 281: 22367-22377. PMID 16751628 DOI: 10.1074/Jbc.M604646200 |
0.457 |
|
| 2006 |
Le Trong I, Aubert DG, Thomas NR, Stenkamp RE. The high-resolution structure of (+)-epi-biotin bound to streptavidin. Acta Crystallographica. Section D, Biological Crystallography. 62: 576-81. PMID 16699183 DOI: 10.1107/S0907444906011887 |
0.482 |
|
| 2006 |
Jastrzebska B, Fotiadis D, Jang GF, Stenkamp RE, Engel A, Palczewski K. Functional and structural characterization of rhodopsin oligomers Journal of Biological Chemistry. 281: 11917-11922. PMID 16495215 DOI: 10.1074/Jbc.M600422200 |
0.339 |
|
| 2006 |
Hyre DE, Le Trong I, Merritt EA, Eccleston JF, Green NM, Stenkamp RE, Stayton PS. Cooperative hydrogen bond interactions in the streptavidin-biotin system. Protein Science : a Publication of the Protein Society. 15: 459-67. PMID 16452627 DOI: 10.1110/Ps.051970306 |
0.363 |
|
| 2006 |
Le Trong I, Humbert N, Ward TR, Stenkamp RE. Crystallographic analysis of a full-length streptavidin with its C-terminal polypeptide bound in the biotin binding site Journal of Molecular Biology. 356: 738-745. PMID 16384581 DOI: 10.1016/J.Jmb.2005.11.086 |
0.389 |
|
| 2005 |
Stenkamp RE. Anatomy of a trans-cis peptide transition during least-squares refinement of rubrerythrin. Acta Crystallographica. Section D, Biological Crystallography. 61: 1599-602. PMID 16301793 DOI: 10.1107/S090744490503043X |
0.301 |
|
| 2005 |
Stenkamp RE, Teller DC, Palczewski K. Rhodopsin: a structural primer for G-protein coupled receptors. Archiv Der Pharmazie. 338: 209-16. PMID 15952240 DOI: 10.1002/Ardp.200400995 |
0.694 |
|
| 2004 |
Jastrzebska B, Maeda T, Zhu L, Fotiadis D, Filipek S, Engel A, Stenkamp RE, Palczewski K. Functional characterization of rhodopsin monomers and dimers in detergents. The Journal of Biological Chemistry. 279: 54663-75. PMID 15489507 DOI: 10.1074/Jbc.M408691200 |
0.384 |
|
| 2004 |
Zhu L, Jang GF, Jastrzebska B, Filipek S, Pearce-Kelling SE, Aguirre GD, Stenkamp RE, Acland GM, Palczewski K. A naturally occurring mutation of the opsin gene (T4R) in dogs affects glycosylation and stability of the G protein-coupled receptor. The Journal of Biological Chemistry. 279: 53828-39. PMID 15459196 DOI: 10.1074/Jbc.M408472200 |
0.312 |
|
| 2003 |
Teller DC, Stenkamp RE, Palczewski K. Evolutionary analysis of rhodopsin and cone pigments: connecting the three-dimensional structure with spectral tuning and signal transfer. Febs Letters. 555: 151-9. PMID 14630336 DOI: 10.1016/S0014-5793(03)01152-9 |
0.654 |
|
| 2003 |
Le Trong I, Freitag S, Klumb LA, Chu V, Stayton PS, Stenkamp RE. Structural studies of hydrogen bonds in the high-affinity streptavidin-biotin complex: mutations of amino acids interacting with the ureido oxygen of biotin. Acta Crystallographica. Section D, Biological Crystallography. 59: 1567-73. PMID 12925786 DOI: 10.1107/S0907444903014562 |
0.411 |
|
| 2003 |
Le Trong I, McDevitt TC, Nelson KE, Stayton PS, Stenkamp RE. Structural characterization and comparison of RGD cell-adhesion recognition sites engineered into streptavidin. Acta Crystallographica. Section D, Biological Crystallography. 59: 828-34. PMID 12777798 DOI: 10.1107/S0907444903004153 |
0.464 |
|
| 2003 |
Filipek S, Teller DC, Palczewski K, Stenkamp R. The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors. Annual Review of Biophysics and Biomolecular Structure. 32: 375-97. PMID 12574068 DOI: 10.1146/Annurev.Biophys.32.110601.142520 |
0.672 |
|
| 2003 |
Filipek S, Stenkamp RE, Teller DC, Palczewski K. G protein-coupled receptor rhodopsin: a prospectus. Annual Review of Physiology. 65: 851-79. PMID 12471166 DOI: 10.1146/Annurev.Physiol.65.092101.142611 |
0.659 |
|
| 2002 |
Nauli S, Kuhlman B, Le Trong I, Stenkamp RE, Teller D, Baker D. Crystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2. Protein Science : a Publication of the Protein Society. 11: 2924-31. PMID 12441390 DOI: 10.1110/Ps.0216902 |
0.668 |
|
| 2002 |
Stenkamp RE, Filipek S, Driessen CA, Teller DC, Palczewski K. Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors. Biochimica Et Biophysica Acta. 1565: 168-82. PMID 12409193 DOI: 10.1016/S0005-2736(02)00567-9 |
0.672 |
|
| 2002 |
Stenkamp RE, Teller DC, Palczewski K. Crystal structure of rhodopsin: a G-protein-coupled receptor. Chembiochem : a European Journal of Chemical Biology. 3: 963-7. PMID 12362360 DOI: 10.1002/1439-7633(20021004)3:10<963::Aid-Cbic963>3.0.Co;2-9 |
0.67 |
|
| 2002 |
Le Trong I, Stenkamp RE, Ibarra C, Atkins WM, Adman ET. 1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site. Proteins. 48: 618-27. PMID 12211029 DOI: 10.1002/Prot.10162 |
0.42 |
|
| 2002 |
Hyre DE, Amon LM, Penzotti JE, Le Trong I, Stenkamp RE, Lybrand TP, Stayton PS. Early mechanistic events in biotin dissociation from streptavidin. Nature Structural Biology. 9: 582-5. PMID 12134141 DOI: 10.1038/Nsb825 |
0.305 |
|
| 2002 |
Dixon RW, Radmer RJ, Kuhn B, Kollman PA, Yang J, Raposo C, Wilcox CS, Klumb LA, Stayton PS, Behnke C, Le Trong I, Stenkamp R. Theoretical and experimental studies of biotin analogues that bind almost as tightly to streptavidin as biotin. The Journal of Organic Chemistry. 67: 1827-37. PMID 11895399 DOI: 10.1021/Jo991846S |
0.73 |
|
| 2001 |
Teller DC, Okada T, Behnke CA, Palczewski K, Stenkamp RE. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry. 40: 7761-72. PMID 11425302 DOI: 10.1021/Bi0155091 |
0.799 |
|
| 2001 |
Adman ET, Le Trong I, Stenkamp RE, Nieslanik BS, Dietze EC, Tai G, Ibarra C, Atkins WM. Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y. Proteins. 42: 192-200. PMID 11119643 DOI: 10.1002/1097-0134(20010201)42:2<192::Aid-Prot60>3.0.Co;2-# |
0.435 |
|
| 2000 |
Sieker LC, Holmes M, Trong IL, Turley S, Liu M-, LeGall J, Stenkamp RE. The 1.9 A crystal structure of the "as isolated" rubrerythrin from Desulfovibrio vulgaris: some surprising results. Journal of Biological Inorganic Chemistry. 5: 505-513. PMID 10968622 DOI: 10.1007/Pl00021450 |
0.431 |
|
| 2000 |
Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M. Crystal structure of rhodopsin: A G protein-coupled receptor. Science (New York, N.Y.). 289: 739-45. PMID 10926528 DOI: 10.1126/Science.289.5480.739 |
0.807 |
|
| 2000 |
Hyre DE, Le Trong I, Freitag S, Stenkamp RE, Stayton PS. Ser45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system Protein Science. 9: 878-885. PMID 10850797 DOI: 10.1110/Ps.9.5.878 |
0.305 |
|
| 2000 |
Okada T, Le Trong I, Fox BA, Behnke CA, Stenkamp RE, Palczewski K. X-Ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles. Journal of Structural Biology. 130: 73-80. PMID 10806093 DOI: 10.1006/Jsbi.1999.4209 |
0.763 |
|
| 1999 |
Stayton PS, Freitag S, Klumb LA, Chilkoti A, Chu V, Penzotti JE, To R, Hyre D, Le Trong I, Lybrand TP, Stenkamp RE. Streptavidin-biotin binding energetics. Biomolecular Engineering. 16: 39-44. PMID 10796983 DOI: 10.1016/S1050-3862(99)00042-X |
0.356 |
|
| 1999 |
Freitag S, Le Trong I, Klumb LA, Chu V, Chilkoti A, Stayton PS, Stenkamp RE. X-ray crystallographic studies of streptavidin mutants binding to biotin Biomolecular Engineering. 16: 13-19. PMID 10796980 DOI: 10.1016/S1050-3862(99)00048-0 |
0.421 |
|
| 1999 |
Freitag S, Chu V, Penzotti JE, Klumb LA, To R, Hyre D, Le Trong I, Lybrand TP, Stenkamp RE, Stayton PS. A structural snapshot of an intermediate on the streptavidin-biotin dissociation pathway. Proceedings of the National Academy of Sciences of the United States of America. 96: 8384-9. PMID 10411884 DOI: 10.1073/Pnas.96.15.8384 |
0.363 |
|
| 1999 |
Freitag S, Le Trong I, Klumb LA, Stayton PS, Stenkamp RE. Atomic resolution structure of biotin-free Tyr43Phe streptavidin: What is in the binding site? Acta Crystallographica Section D: Biological Crystallography. 55: 1118-1126. PMID 10329773 DOI: 10.1107/S0907444999002322 |
0.499 |
|
| 1999 |
Fox BA, Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC. Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by x-ray crystallography. The Journal of Biological Chemistry. 274: 4917-23. PMID 9988734 DOI: 10.1074/Jbc.274.8.4917 |
0.656 |
|
| 1998 |
Behnke CA, Yee VC, Trong IL, Pedersen LC, Stenkamp RE, Kim SS, Reeck GR, Teller DC. Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution. Biochemistry. 37: 15277-88. PMID 9799488 DOI: 10.1021/Bi9812266 |
0.767 |
|
| 1998 |
Freitag S, Le Trong I, Chilkoti A, Klumb LA, Stayton PS, Stenkamp RE. Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex Journal of Molecular Biology. 279: 211-221. PMID 9636711 DOI: 10.1006/Jmbi.1998.1735 |
0.435 |
|
| 1998 |
Chu V, Freitag S, Trong ILE, Stenkamp RE, Stayton PS. Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system Protein Science. 7: 848-859. PMID 9568892 DOI: 10.1002/Pro.5560070403 |
0.4 |
|
| 1998 |
Edwards TC, Koppenol S, Frey W, Schief WR, Vogel V, Stenkamp RE, Stayton PS. Molecular basis for ionic strength dependence and crystal morphology in two-dimensional streptavidin crystallization Langmuir. 14: 4683-4687. DOI: 10.1021/La9801918 |
0.424 |
|
| 1997 |
Pratt KP, Côté HC, Chung DW, Stenkamp RE, Davie EW. The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proceedings of the National Academy of Sciences of the United States of America. 94: 7176-81. PMID 9207064 DOI: 10.1073/Pnas.94.14.7176 |
0.354 |
|
| 1997 |
Freitag S, Trong ILE, Klumb L, Stayton PS, Stenkamp RE. Structural studies of the streptavidin binding loop Protein Science. 6: 1157-1166. PMID 9194176 DOI: 10.1002/Pro.5560060604 |
0.488 |
|
| 1997 |
Yee VC, Pratt KP, Côté HC, Trong IL, Chung DW, Davie EW, Stenkamp RE, Teller DC. Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen. Structure (London, England : 1993). 5: 125-38. PMID 9016719 DOI: 10.1016/S0969-2126(97)00171-8 |
0.632 |
|
| 1996 |
Yee VC, Le Trong I, Bishop PD, Pedersen LC, Stenkamp RE, Teller DC. Structure and function studies of factor XIIIa by x-ray crystallography. Seminars in Thrombosis and Hemostasis. 22: 377-84. PMID 8989820 DOI: 10.1055/S-2007-999035 |
0.684 |
|
| 1996 |
Fox BA, Bishop PD, Stenkamp RE, Teller DC, Yee VC. Crystal structure of human factor XIII bound to ytterbium: probing calcium binding Acta Crystallographica Section a Foundations of Crystallography. 52: C104-C104. DOI: 10.1107/S0108767396094986 |
0.634 |
|
| 1996 |
Yee VC, Pratt KP, Cote HC, Le Trong I, Chung DW, Stenkamp RE, Teller DC. Gamma-fibrinogen: crystal structure of a 30 kDa C-terminus fragment at 2.1 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 52: C174-C174. DOI: 10.1107/S010876739609232X |
0.652 |
|
| 1996 |
Freitag S, Le Trong I, Stenkamp RE, Chilkoti A, Stayton PS. Comparison of streptavidin WxF and WxA mutants with the native protein Acta Crystallographica Section a Foundations of Crystallography. 52: C233-C233. DOI: 10.1107/S0108767396090071 |
0.315 |
|
| 1996 |
Stenkamp RE, Freitag S, Le Trong I, Chilkoti A, Stayton PS. Crystal packing interactions in streptavidin crystals Acta Crystallographica Section a Foundations of Crystallography. 52: C240-C240. DOI: 10.1107/S0108767396089799 |
0.364 |
|
| 1995 |
Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC. Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thrombosis Research. 78: 389-97. PMID 7660355 DOI: 10.1016/0049-3848(95)00072-Y |
0.652 |
|
| 1995 |
Bajorath J, Stenkamp R, Aruffo A. Comparison of a protein model with its X-ray structure: the ligand binding domain of E-selectin. Bioconjugate Chemistry. 6: 3-6. PMID 7536042 DOI: 10.1021/Bc00031A001 |
0.405 |
|
| 1994 |
Pedersen LC, Yee VC, von Dassow G, Hazeghazam M, Reeck GR, Stenkamp RE, Teller DC. The corn inhibitor of blood coagulation factor XIIa. Crystallization and preliminary crystallographic analysis. Journal of Molecular Biology. 236: 385-7. PMID 8107123 DOI: 10.1006/Jmbi.1994.1147 |
0.731 |
|
| 1994 |
Pedersen LC, Yee VC, Bishop PD, Le Trong I, Teller DC, Stenkamp RE. Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Protein Science : a Publication of the Protein Society. 3: 1131-5. PMID 7920263 DOI: 10.1002/Pro.5560030720 |
0.656 |
|
| 1994 |
Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC. Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proceedings of the National Academy of Sciences of the United States of America. 91: 7296-300. PMID 7913750 DOI: 10.1073/Pnas.91.15.7296 |
0.671 |
|
| 1994 |
Sieker LC, Stenkamp RE, Legall J. Rubredoxin in crystalline state. Methods in Enzymology. 243: 203-216. PMID 7830611 DOI: 10.1016/0076-6879(94)43016-0 |
0.37 |
|
| 1993 |
Hollenbaugh D, Bajorath J, Stenkamp R, Aruffo A. Interaction of P-selectin (CD62) and its cellular ligand: analysis of critical residues. Biochemistry. 32: 2960-2966. PMID 7681324 DOI: 10.1021/Bi00063A006 |
0.36 |
|
| 1993 |
Bajorath J, Stenkamp R, Aruffo A. Knowledge-based model building of proteins: concepts and examples. Protein Science. 2: 1798-1810. PMID 7505680 DOI: 10.1002/Pro.5560021103 |
0.394 |
|
| 1991 |
Holmes MA, Trong IL, Turley S, Sieker LC, Stenkamp RE. Structures of deoxy and oxy hemerythrin at 2.0 A resolution. Journal of Molecular Biology. 218: 583-593. PMID 2016748 DOI: 10.1016/0022-2836(91)90703-9 |
0.393 |
|
| 1991 |
Holmes MA, Stenkamp RE. Structures of met and azidomet hemerythrin at 1.66 A resolution. Journal of Molecular Biology. 220: 723-737. PMID 1870128 DOI: 10.1016/0022-2836(91)90113-K |
0.364 |
|
| 1991 |
Vasilevesky I, Rose NR, Stenkamp R, Willett RD. Crystal structure and magnetic behavior of (tetramethylcyclotetraazatetradecatetraene) copper tetrachlorocuprate: an alternating-metal-site, alternating-exchange, spin 1/2 linear-chain system Inorganic Chemistry. 30: 4082-4084. DOI: 10.1021/Ic00021A021 |
0.318 |
|
| 1990 |
Stenkamp RE, Sieker LC, Jensen LH. The structure of rubredoxin from Desulfovibrio desulfuricans strain 27774 at 1.5 Å resolution Proteins: Structure, Function and Genetics. 8: 352-364. PMID 2091025 DOI: 10.1002/Prot.340080409 |
0.408 |
|
| 1990 |
Perkins CM, Rose NJ, Stenkamp RE. The structure of cobalt methylmalonate complexes, CoClN4O7C10H28 and CoCl2N4O5.5C11H28, models for metal complexes of γ-carboxyglutamic acid Inorganica Chimica Acta. 172: 119-125. DOI: 10.1016/S0020-1693(00)80460-0 |
0.356 |
|
| 1988 |
Sieker LC, Turley S, Trong IL, Stenkamp RE, Weller PF, Ackerman SJ. Crystallographic characterization of human eosinophil Charcot-Leyden crystals. Journal of Molecular Biology. 204: 489-491. PMID 3221396 DOI: 10.1016/0022-2836(88)90590-6 |
0.405 |
|
| 1987 |
Norman RE, Rose NJ, Stenkamp RE. Crystal structure of a copper complex of 2-carboxypentonic acid; a decomposition product of dehydroascorbic acid Journal of the Chemical Society-Dalton Transactions. 2905-2910. DOI: 10.1039/Dt9870002905 |
0.311 |
|
| 1986 |
Sieker LC, Stenkamp RE, Jensen LH, Prickril B, LeGall J. Structure of rubredoxin from the bacterium Desulfovibrio desulfuricans Febs Letters. 208: 73-76. PMID 3770211 DOI: 10.1016/0014-5793(86)81535-6 |
0.394 |
|
| 1986 |
Maroney MJ, Fey EO, Baldwin DA, Stenkamp RE, Jensen LH, Rose NJ. Bonding Mode of Axial NCS- Ligands of Iron Macrocyclic Complexes. Crystal Structure of [Fe(TIM)(SCN)2]PF6. Inorganic Chemistry. 25: 1409-1414. DOI: 10.1021/Ic00229A023 |
0.353 |
|
| 1985 |
Sheriff S, Hendrickson WA, Stenkamp RE, Sieker LC, Jensen LH. Influence of solvent accessibility and intermolecular contacts on atomic mobilities in hemerythrins Proceedings of the National Academy of Sciences of the United States of America. 82: 1104-1107. PMID 3856249 DOI: 10.1073/Pnas.82.4.1104 |
0.364 |
|
| 1985 |
Stenkamp RE, Sieker LC, Jensen LH, McCallum JD, Sanders-Loehr J. Active site structures of deoxyhemerythrin and oxyhemerythrin. Proceedings of the National Academy of Sciences of the United States of America. 82: 713-6. PMID 3856224 DOI: 10.1073/Pnas.82.3.713 |
0.331 |
|
| 1985 |
Kissinger CR, Adman ET, Clark JI, Stenkamp RE. Crystal structure of sorbinil, C11H9FN2O3 Acta Crystallographica Section C Crystal Structure Communications. 41: 988-990. DOI: 10.1107/S0108270185006291 |
0.348 |
|
| 1984 |
Stenkamp RE, Sieker LC, Jensen LH. Structural studies of hemerythrin Acta Crystallographica Section A. 40. DOI: 10.1107/S010876738409869X |
0.42 |
|
| 1984 |
Perkins CM, Rose NJ, Weinstein B, Stenkamp RE, Jensen LH, Pickart L. The structure of a copper complex of the growth factor glycyl-L-histidyl-L-lysine at 1.1 Å resolution Inorganica Chimica Acta. 82: 93-99. DOI: 10.1016/S0020-1693(00)82544-X |
0.333 |
|
| 1984 |
Essig MG, Shafizadeh F, Cochran TG, Stenkamp RE. The crystal structure of a septanose derived from levoglucosenone Carbohydrate Research. 129: 55-61. DOI: 10.1016/0008-6215(84)85298-2 |
0.405 |
|
| 1983 |
Sanders-Loehr J, McCallum JD, Elam W, Stern EA, Stenkamp RE, Sieker LC, Jensen LH. EXAFS and X-ray crystallographic studies of hemerythrin Inorganica Chimica Acta. 79: 133. DOI: 10.1016/S0020-1693(00)95166-1 |
0.35 |
|
| 1983 |
Stenkamp RE, Sieker LC, Jensen LH. The structure of the iron complex in metaquohemerythrin Journal of Inorganic Biochemistry. 19: 247-253. DOI: 10.1016/0162-0134(83)85029-6 |
0.332 |
|
| 1983 |
Stevenson TT, Furneaux RH, Pang D, Shafizadeh F, Jensen LH, Stenkamp RE. The crystal structure of a nonalkenic, cyclic trimer of levoglucosenone Carbohydrate Research. 112: 179-187. DOI: 10.1016/0008-6215(83)88283-4 |
0.456 |
|
| 1983 |
Stevenson TT, Essig MG, Shafizadeh F, Jensen LH, Stenkamp RE. The crystal structure of an epoxide of a levoglucosenone-cyclopentadiene adduct Carbohydrate Research. 118: 261-268. DOI: 10.1016/0008-6215(83)88054-9 |
0.454 |
|
| 1982 |
Stenkamp RE, Jensen LH, Murphy TB, Rose NJ. Structure of a benzene solvate of α‐furildioxime Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 38: 1169-1172. DOI: 10.1107/S0567740882005226 |
0.42 |
|
| 1982 |
Stenkamp RE, Sieker LC, Jensen LH. Restrained least-squares refinement of Themiste dyscritum methydroxohemerythrin at 2.0 Å resolution Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 38: 784-792. DOI: 10.1107/S0567740882004087 |
0.329 |
|
| 1982 |
Engstrom GW, Stenkamp RE, McDorman DJ, Jensen LH. Spectral identification, x-ray structure determination and iron-chelating capability of erythroglaucin, a red pigment from Aspergillus ruber Journal of Agricultural and Food Chemistry. 30: 304-307. DOI: 10.1021/Jf00110A022 |
0.322 |
|
| 1982 |
Stevenson TT, Stenkamp RE, Jensen LH, Shafizadeh F, Furneaux RH. The crystal structure of an olefinic cyclic trimer of levoglucosenone Carbohydrate Research. 104: 11-19. DOI: 10.1016/S0008-6215(00)82216-8 |
0.464 |
|
| 1981 |
Sieker LC, Bolles L, Stenkamp RE, Jensen LH, Appleby CA. Preliminary X-ray study of a dimeric form of hemerythrin from Phascolosoma arcuatum Journal of Molecular Biology. 148: 493-494. PMID 7310875 DOI: 10.1016/0022-2836(81)90189-3 |
0.334 |
|
| 1981 |
Stenkamp RE, Sieker LC, Jensen LH. Structure of the iron complex in hemerythrin Acta Crystallographica Section A. 37. DOI: 10.1107/S0108767381098814 |
0.308 |
|
| 1981 |
Stenkamp RE, Siecker LC, Jensen LH, Sanders-loehr J. Structure of the binuclear iron complex in metazidohaemerythrin from Themiste dyscritum at 2.2. å resolution Nature. 291: 263-264. DOI: 10.1038/291263A0 |
0.356 |
|
| 1981 |
Stevenson TT, Stenkamp RE, Jensen LH, Cochran TG, Shafizadeh F, Furneaux RH. The crystal structure of 1,5-anhydro-4-deoxy-d-glycero-hex-1-en-3-ulose Carbohydrate Research. 90: 319-325. DOI: 10.1016/S0008-6215(00)85930-3 |
0.399 |
|
| 1978 |
Stenkamp RE, Sieker LC, Jensen LH, McQueen JE. Structure of methemerythrin at 2.8-Å resolution: Computer graphics fit of an averaged electron density map Biochemistry. 17: 2499-2504. PMID 678527 DOI: 10.1021/Bi00606A007 |
0.403 |
|
| 1978 |
Anderson CM, Stenkamp RE, McDonald RC, Steitz TA. A refined model of the sugar binding site of yeast hexokinase B Journal of Molecular Biology. 123: 207-219. PMID 355645 DOI: 10.1016/0022-2836(78)90321-2 |
0.341 |
|
| 1978 |
Anderson CM, Stenkamp RE, Steitz TA. Sequencing a protein by x-ray crystallography. II. Refinement of yeast hexokinase B co-ordinates and sequence at 2.1 A resolution. Journal of Molecular Biology. 123: 15-33. PMID 355643 DOI: 10.1016/0022-2836(78)90374-1 |
0.315 |
|
| 1978 |
Stenkamp RE, Sieker LC, Jensen LH. Crystallographic studies of azide, thiocyanate and perchlorate complexes of methemerythrin Journal of Molecular Biology. 126: 457-466. PMID 218017 DOI: 10.1016/0022-2836(78)90052-9 |
0.379 |
|
| 1978 |
Adman ET, Stenkamp RE, Sieker LC, Jensen LH. A crystallographic model for azurin at 3 Å resolution Journal of Molecular Biology. 123: 35-47. PMID 98639 DOI: 10.1016/0022-2836(78)90375-3 |
0.374 |
|
| 1977 |
Steitz TA, Anderson C, Bennett W, McDonald R, Stenkamp R. Protomer structure of oligomeric enzymes: symmetry and allosteric interactions in yeast hexokinase. Biochemical Society Transactions. 5: 620-3. PMID 332556 DOI: 10.1042/Bst0050620 |
0.369 |
|
| 1977 |
Fitzgerald A, Stenkamp RE, Watenpaugh KD, Jensen LH. The crystal and molecular structure of dihydroxo(1,2,3,4,5,6,7,8-octaethylporphinato)antimony(V) perchlorate monoethanol solvate: a crystal structure that exhibits a subcell Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 33: 1688-1696. DOI: 10.1107/S0567740877006864 |
0.348 |
|
| 1976 |
Stenkamp RE, Sieker LC, Jensen LH, Loehr JS. Structure of methemerythrin at 5 Å resolution Journal of Molecular Biology. 100: 23-34. PMID 1249839 DOI: 10.1016/S0022-2836(76)80031-9 |
0.371 |
|
| 1976 |
Stenkamp RE, Sieker LC, Jensen LH. Structure of the iron complex in methemerythrin Proceedings of the National Academy of Sciences of the United States of America. 73: 349-351. PMID 1061139 DOI: 10.1073/Pnas.73.2.349 |
0.313 |
|
| 1976 |
Stenkamp RE, Jensen LH. Test refinements with simulated protein data sets Acta Crystallographica Section A. 32: 255-258. DOI: 10.1107/S0567739476000569 |
0.302 |
|
| 1975 |
Stenkamp RE, Jensen LH. The crystal structure of L-methionyl-L-methionine Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 31: 857-861. DOI: 10.1107/S0567740875003937 |
0.327 |
|
| 1973 |
Matthews BW, Stenkamp RE, Colman PM. The crystal and molecular structure of the polymethine dye 1,3-bis(dimethylamino)trimethinium perchlorate: a comparison of optical and X-ray crystal structure determination Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 29: 449-454. DOI: 10.1107/S0567740873002736 |
0.33 |
|
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