| Year |
Citation |
Score |
| 2023 |
Wang Y, Shi Y, Hellinga HW, Beese LS. Thermally controlled intein splicing of engineered DNA polymerases provides a robust and generalizable solution for accurate and sensitive molecular diagnostics. Nucleic Acids Research. PMID 37166959 DOI: 10.1093/nar/gkad368 |
0.317 |
|
| 2019 |
Beese LS, Shi Y, Wang Y. Using time-resolved crystallography and cryo-EM to investigate human DNA repair nucleases Acta Crystallographica Section a Foundations and Advances. 75: a153-a153. DOI: 10.1107/s0108767319098465 |
0.317 |
|
| 2017 |
Kato N, Kawasoe Y, Williams H, Coates E, Roy U, Shi Y, Beese LS, Schärer OD, Yan H, Gottesman ME, Takahashi TS, Gautier J. Sensing and Processing of DNA Interstrand Crosslinks by the Mismatch Repair Pathway. Cell Reports. 21: 1375-1385. PMID 29091773 DOI: 10.1016/J.Celrep.2017.10.032 |
0.467 |
|
| 2017 |
Shi Y, Hellinga HW, Beese LS. Interplay of catalysis, fidelity, threading, and processivity in the exo- and endonucleolytic reactions of human exonuclease I. Proceedings of the National Academy of Sciences of the United States of America. PMID 28533382 DOI: 10.1073/Pnas.1704845114 |
0.459 |
|
| 2015 |
Miller BR, Beese LS, Parish CA, Wu EY. The Closing Mechanism of DNA Polymerase I at Atomic Resolution. Structure (London, England : 1993). 23: 1609-20. PMID 26211612 DOI: 10.1016/J.Str.2015.06.016 |
0.51 |
|
| 2014 |
Wang YC, Dozier JK, Beese LS, Distefano MD. Rapid analysis of protein farnesyltransferase substrate specificity using peptide libraries and isoprenoid diphosphate analogues. Acs Chemical Biology. 9: 1726-35. PMID 24841702 DOI: 10.1021/Cb5002312 |
0.315 |
|
| 2014 |
Mabanglo MF, Hast MA, Lubock NB, Hellinga HW, Beese LS. Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design. Protein Science : a Publication of the Protein Society. 23: 289-301. PMID 24347326 DOI: 10.1002/Pro.2411 |
0.429 |
|
| 2013 |
Grimley JS, Li L, Wang W, Wen L, Beese LS, Hellinga HW, Augustine GJ. Visualization of synaptic inhibition with an optogenetic sensor developed by cell-free protein engineering automation. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 33: 16297-309. PMID 24107961 DOI: 10.1523/Jneurosci.4616-11.2013 |
0.512 |
|
| 2012 |
Khatwani SL, Kang JS, Mullen DG, Hast MA, Beese LS, Distefano MD, Taton TA. Covalent protein-oligonucleotide conjugates by copper-free click reaction. Bioorganic & Medicinal Chemistry. 20: 4532-9. PMID 22682299 DOI: 10.1016/J.Bmc.2012.05.017 |
0.316 |
|
| 2012 |
Wang W, Wu EY, Hellinga HW, Beese LS. Structural factors that determine selectivity of a high fidelity DNA polymerase for deoxy-, dideoxy-, and ribonucleotides. The Journal of Biological Chemistry. 287: 28215-26. PMID 22648417 DOI: 10.1074/Jbc.M112.366609 |
0.655 |
|
| 2011 |
Wang W, Hellinga HW, Beese LS. Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis. Proceedings of the National Academy of Sciences of the United States of America. 108: 17644-8. PMID 22006298 DOI: 10.1073/Pnas.1114496108 |
0.638 |
|
| 2011 |
Tseng Q, Orans J, Hast MA, Iyer RR, Changela A, Modrich PL, Beese LS. Purification, crystallization and preliminary X-ray diffraction analysis of the human mismatch repair protein MutSβ. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 947-52. PMID 21821902 DOI: 10.1107/S1744309111019300 |
0.479 |
|
| 2011 |
Hast MA, Nichols CB, Armstrong SM, Kelly SM, Hellinga HW, Alspaugh JA, Beese LS. Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens. The Journal of Biological Chemistry. 286: 35149-62. PMID 21816822 DOI: 10.1074/Jbc.M111.250506 |
0.376 |
|
| 2011 |
Orans J, McSweeney EA, Iyer RR, Hast MA, Hellinga HW, Modrich P, Beese LS. Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family. Cell. 145: 212-23. PMID 21496642 DOI: 10.1016/J.Cell.2011.03.005 |
0.519 |
|
| 2011 |
Wu EY, Beese LS. The structure of a high fidelity DNA polymerase bound to a mismatched nucleotide reveals an "ajar" intermediate conformation in the nucleotide selection mechanism. The Journal of Biological Chemistry. 286: 19758-67. PMID 21454515 DOI: 10.1074/Jbc.M110.191130 |
0.508 |
|
| 2011 |
Orans J, McSweeney E, Modrich P, Beese LS. Crystal Structures of Human Exonuclease I with DNA Provides Insight into Substrate Selectivity and Mechanism Biophysical Journal. 100: 241a. DOI: 10.1016/J.Bpj.2010.12.1533 |
0.557 |
|
| 2011 |
Hast MA, Beese LS. Structural Biochemistry of CaaX Protein Prenyltransferases Enzymes. 29: 235-257. DOI: 10.1016/B978-0-12-381339-8.00013-5 |
0.394 |
|
| 2010 |
Fletcher S, Keaney EP, Cummings CG, Blaskovich MA, Hast MA, Glenn MP, Chang SY, Bucher CJ, Floyd RJ, Katt WP, Gelb MH, Van Voorhis WC, Beese LS, Sebti SM, Hamilton AD. Structure-based design and synthesis of potent, ethylenediamine-based, mammalian farnesyltransferase inhibitors as anticancer agents. Journal of Medicinal Chemistry. 53: 6867-88. PMID 20822181 DOI: 10.1021/Jm1001748 |
0.326 |
|
| 2010 |
Iyer RR, Pluciennik A, Genschel J, Tsai MS, Beese LS, Modrich P. MutLalpha and proliferating cell nuclear antigen share binding sites on MutSbeta. The Journal of Biological Chemistry. 285: 11730-9. PMID 20154325 DOI: 10.1074/Jbc.M110.104125 |
0.447 |
|
| 2010 |
Golosov AA, Warren JJ, Beese LS, Karplus M. The mechanism of the translocation step in DNA replication by DNA polymerase I: a computer simulation analysis. Structure (London, England : 1993). 18: 83-93. PMID 20152155 DOI: 10.1016/J.Str.2009.10.014 |
0.47 |
|
| 2009 |
Cuneo MJ, Beese LS, Hellinga HW. Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold. The Journal of Biological Chemistry. 284: 33217-23. PMID 19801540 DOI: 10.1074/Jbc.M109.041624 |
0.391 |
|
| 2009 |
Cuneo MJ, Changela A, Beese LS, Hellinga HW. Structural adaptations that modulate monosaccharide, disaccharide, and trisaccharide specificities in periplasmic maltose-binding proteins. Journal of Molecular Biology. 389: 157-66. PMID 19361522 DOI: 10.1016/J.Jmb.2009.04.008 |
0.378 |
|
| 2009 |
Hast MA, Fletcher S, Cummings CG, Pusateri EE, Blaskovich MA, Rivas K, Gelb MH, Van Voorhis WC, Sebti SM, Hamilton AD, Beese LS. Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase. Chemistry & Biology. 16: 181-92. PMID 19246009 DOI: 10.1016/J.Chembiol.2009.01.014 |
0.361 |
|
| 2008 |
Cuneo MJ, Beese LS, Hellinga HW. Ligand-induced conformational changes in a thermophilic ribose-binding protein. Bmc Structural Biology. 8: 50. PMID 19019243 DOI: 10.1186/1472-6807-8-50 |
0.377 |
|
| 2008 |
DeGraw AJ, Hast MA, Xu J, Mullen D, Beese LS, Barany G, Distefano MD. Caged protein prenyltransferase substrates: tools for understanding protein prenylation. Chemical Biology & Drug Design. 72: 171-81. PMID 18844669 DOI: 10.1111/J.1747-0285.2008.00698.X |
0.386 |
|
| 2008 |
Cuneo MJ, Changela A, Miklos AE, Beese LS, Krueger JK, Hellinga HW. Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport. The Journal of Biological Chemistry. 283: 32812-20. PMID 18723845 DOI: 10.1074/Jbc.M803595200 |
0.353 |
|
| 2008 |
Hast MA, Beese LS. Structure of protein geranylgeranyltransferase-I from the human pathogen Candida albicans complexed with a lipid substrate. The Journal of Biological Chemistry. 283: 31933-40. PMID 18713740 DOI: 10.1074/Jbc.M805330200 |
0.399 |
|
| 2008 |
Iyer RR, Pohlhaus TJ, Chen S, Hura GL, Dzantiev L, Beese LS, Modrich P. The MutSalpha-proliferating cell nuclear antigen interaction in human DNA mismatch repair. The Journal of Biological Chemistry. 283: 13310-9. PMID 18326858 DOI: 10.1074/Jbc.M800606200 |
0.72 |
|
| 2008 |
Büsch F, Pieck JC, Ober M, Gierlich J, Hsu GW, Beese LS, Carell T. Dissecting the differences between the alpha and beta anomers of the oxidative DNA lesion FaPydG. Chemistry (Weinheim An Der Bergstrasse, Germany). 14: 2125-32. PMID 18196510 DOI: 10.1002/Chem.200701373 |
0.723 |
|
| 2007 |
Tian Y, Cuneo MJ, Changela A, Höcker B, Beese LS, Hellinga HW. Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein. Protein Science : a Publication of the Protein Society. 16: 2240-50. PMID 17766373 DOI: 10.1110/Ps.072969407 |
0.318 |
|
| 2007 |
Xu P, Oum L, Beese LS, Geacintov NE, Broyde S. Following an environmental carcinogen N2-dG adduct through replication: elucidating blockage and bypass in a high-fidelity DNA polymerase. Nucleic Acids Research. 35: 4275-88. PMID 17576677 DOI: 10.1093/Nar/Gkm416 |
0.446 |
|
| 2007 |
Warren JJ, Pohlhaus TJ, Changela A, Iyer RR, Modrich PL, Beese LS. Structure of the human MutSalpha DNA lesion recognition complex. Molecular Cell. 26: 579-92. PMID 17531815 DOI: 10.1016/J.Molcel.2007.04.018 |
0.726 |
|
| 2007 |
Eastman RT, White J, Hucke O, Yokoyama K, Verlinde CL, Hast MA, Beese LS, Gelb MH, Rathod PK, Van Voorhis WC. Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase. Molecular and Biochemical Parasitology. 152: 66-71. PMID 17208314 DOI: 10.1016/J.Molbiopara.2006.11.012 |
0.361 |
|
| 2006 |
Warren JJ, Forsberg LJ, Beese LS. The structural basis for the mutagenicity of O(6)-methyl-guanine lesions. Proceedings of the National Academy of Sciences of the United States of America. 103: 19701-6. PMID 17179038 DOI: 10.1073/Pnas.0609580103 |
0.476 |
|
| 2006 |
Cuneo MJ, Changela A, Warren JJ, Beese LS, Hellinga HW. The crystal structure of a thermophilic glucose binding protein reveals adaptations that interconvert mono and di-saccharide binding sites. Journal of Molecular Biology. 362: 259-70. PMID 16904687 DOI: 10.1016/J.Jmb.2006.06.084 |
0.391 |
|
| 2006 |
Terry KL, Casey PJ, Beese LS. Conversion of protein farnesyltransferase to a geranylgeranyltransferase. Biochemistry. 45: 9746-55. PMID 16893176 DOI: 10.1021/Bi060295E |
0.626 |
|
| 2006 |
Lane KT, Beese LS. Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. Journal of Lipid Research. 47: 681-99. PMID 16477080 DOI: 10.1194/Jlr.R600002-Jlr200 |
0.401 |
|
| 2005 |
Hsu GW, Huang X, Luneva NP, Geacintov NE, Beese LS. Structure of a high fidelity DNA polymerase bound to a benzo[a]pyrene adduct that blocks replication. The Journal of Biological Chemistry. 280: 3764-70. PMID 15548515 DOI: 10.1074/Jbc.M411276200 |
0.768 |
|
| 2004 |
Reid TS, Terry KL, Casey PJ, Beese LS. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. Journal of Molecular Biology. 343: 417-33. PMID 15451670 DOI: 10.1016/J.Jmb.2004.08.056 |
0.653 |
|
| 2004 |
Hsu GW, Kiefer JR, Burnouf D, Becherel OJ, Fuchs RP, Beese LS. Observing translesion synthesis of an aromatic amine DNA adduct by a high-fidelity DNA polymerase. The Journal of Biological Chemistry. 279: 50280-5. PMID 15385534 DOI: 10.1074/Jbc.M409224200 |
0.728 |
|
| 2004 |
Hsu GW, Ober M, Carell T, Beese LS. Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature. 431: 217-21. PMID 15322558 DOI: 10.1038/Nature02908 |
0.759 |
|
| 2004 |
Reid TS, Long SB, Beese LS. Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes. Biochemistry. 43: 9000-8. PMID 15248757 DOI: 10.1021/Bi049280B |
0.644 |
|
| 2004 |
Reid TS, Beese LS. Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity. Biochemistry. 43: 6877-84. PMID 15170324 DOI: 10.1021/Bi049723B |
0.349 |
|
| 2004 |
Johnson SJ, Beese LS. Structures of mismatch replication errors observed in a DNA polymerase. Cell. 116: 803-16. PMID 15035983 DOI: 10.1016/S0092-8674(04)00252-1 |
0.465 |
|
| 2003 |
Taylor JS, Reid TS, Terry KL, Casey PJ, Beese LS. Structure of mammalian protein geranylgeranyltransferase type-I. The Embo Journal. 22: 5963-74. PMID 14609943 DOI: 10.1093/Emboj/Cdg571 |
0.636 |
|
| 2003 |
deSolms SJ, Ciccarone TM, MacTough SC, Shaw AW, Buser CA, Ellis-Hutchings M, Fernandes C, Hamilton KA, Huber HE, Kohl NE, Lobell RB, Robinson RG, Tsou NN, Walsh ES, Graham SL, ... Beese LS, et al. Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents. Journal of Medicinal Chemistry. 46: 2973-84. PMID 12825937 DOI: 10.1021/Jm020587N |
0.357 |
|
| 2003 |
Johnson SJ, Taylor JS, Beese LS. Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proceedings of the National Academy of Sciences of the United States of America. 100: 3895-900. PMID 12649320 DOI: 10.1073/Pnas.0630532100 |
0.502 |
|
| 2002 |
Long SB, Casey PJ, Beese LS. Reaction path of protein farnesyltransferase at atomic resolution. Nature. 419: 645-50. PMID 12374986 DOI: 10.1038/Nature00986 |
0.644 |
|
| 2001 |
Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. Proceedings of the National Academy of Sciences of the United States of America. 98: 12948-53. PMID 11687658 DOI: 10.1073/Pnas.241407898 |
0.663 |
|
| 2001 |
Terry KL, Long SB, Beese LS. 2 Structure of protein farnesyltransferase Enzymes. 21: 19-46. DOI: 10.1016/S1874-6047(01)80015-9 |
0.692 |
|
| 2001 |
Long SB, Beese LS. Structures of Protein Farnesyltransferase The Enzymes. 21: 37-48. DOI: 10.1007/978-1-59259-013-1_3 |
0.646 |
|
| 2000 |
Spence RA, Hightower KE, Terry KL, Beese LS, Fierke CA, Casey PJ. Conversion of Tyr361 beta to Leu in mammalian protein farnesyltransferase impairs product release but not substrate recognition. Biochemistry. 39: 13651-9. PMID 11076503 DOI: 10.1021/Bi001084R |
0.636 |
|
| 2000 |
Rodriguez AC, Park HW, Mao C, Beese LS. Crystal structure of a pol alpha family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7. Journal of Molecular Biology. 299: 447-62. PMID 10860752 DOI: 10.1006/Jmbi.2000.3728 |
0.429 |
|
| 2000 |
Long SB, Casey PJ, Beese LS. The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures. Structure (London, England : 1993). 8: 209-22. PMID 10673434 DOI: 10.1016/S0969-2126(00)00096-4 |
0.646 |
|
| 1998 |
Strickland CL, Windsor WT, Syto R, Wang L, Bond R, Wu Z, Schwartz J, Le HV, Beese LS, Weber PC. Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue. Biochemistry. 37: 16601-11. PMID 9843427 DOI: 10.1021/Bi981197Z |
0.389 |
|
| 1998 |
Zhou M, Mao C, Rodriguez AC, Kiefer JR, Kucera RB, Beese LS. Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon. Acta Crystallographica. Section D, Biological Crystallography. 54: 994-5. PMID 9757117 DOI: 10.1107/S0907444998001553 |
0.45 |
|
| 1998 |
Long SB, Casey PJ, Beese LS. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry. 37: 9612-8. PMID 9657673 DOI: 10.1021/Bi980708E |
0.665 |
|
| 1998 |
Fu HW, Beese LS, Casey PJ. Kinetic analysis of zinc ligand mutants of mammalian protein farnesyltransferase. Biochemistry. 37: 4465-72. PMID 9521766 DOI: 10.1021/Bi972511C |
0.378 |
|
| 1998 |
Kiefer JR, Mao C, Braman JC, Beese LS. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature. 391: 304-7. PMID 9440698 DOI: 10.1038/34693 |
0.515 |
|
| 1997 |
Park HW, Boduluri SR, Moomaw JF, Casey PJ, Beese LS. Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Science (New York, N.Y.). 275: 1800-4. PMID 9065406 DOI: 10.1126/Science.275.5307.1800 |
0.418 |
|
| 1997 |
Kiefer JR, Mao C, Hansen CJ, Basehore SL, Hogrefe HH, Braman JC, Beese LS. Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. Structure (London, England : 1993). 5: 95-108. PMID 9016716 DOI: 10.1016/S0969-2126(97)00169-X |
0.532 |
|
| 1996 |
Beese LS, Mao C, Kiefer JR, Long SB, Braman J. Structures of nascent duplex DNA bound to a thermostable DNA polymerase at 1.9 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 52: C153-C153. DOI: 10.1107/S0108767396093129 |
0.663 |
|
| 1996 |
Mao C, Zhou M, Kiefer JR, Kucera R, Southworth M, Perler F, Beese LS. Crystallization and preliminary characterization of a hyperthermostable archeal DNA polymerase Acta Crystallographica Section a Foundations of Crystallography. 52: C157-C157. DOI: 10.1107/S0108767396092963 |
0.316 |
|
| 1993 |
Beese LS, Derbyshire V, Steitz TA. Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science (New York, N.Y.). 260: 352-5. PMID 8469987 DOI: 10.1126/Science.8469987 |
0.644 |
|
| 1993 |
Beese LS, Friedman JM, Steitz TA. Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Biochemistry. 32: 14095-101. PMID 8260491 DOI: 10.1021/Bi00214A004 |
0.612 |
|
| 1993 |
Steitz TA, Smerdon S, Jäger J, Wang J, Kohlstaedt LA, Friedman JM, Beese LS, Rice PA. Two DNA polymerases: HIV reverse transcriptase and the Klenow fragment of Escherichia coli DNA polymerase I. Cold Spring Harbor Symposia On Quantitative Biology. 58: 495-504. PMID 7525146 DOI: 10.1101/Sqb.1993.058.01.056 |
0.688 |
|
| 1991 |
Beese LS, Steitz TA. Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. The Embo Journal. 10: 25-33. PMID 1989886 DOI: 10.1002/J.1460-2075.1991.Tb07917.X |
0.619 |
|
| 1988 |
Freemont PS, Friedman JM, Beese LS, Sanderson MR, Steitz TA. Cocrystal structure of an editing complex of Klenow fragment with DNA. Proceedings of the National Academy of Sciences of the United States of America. 85: 8924-8. PMID 3194400 DOI: 10.1073/Pnas.85.23.8924 |
0.67 |
|
| 1988 |
Derbyshire V, Freemont PS, Sanderson MR, Beese L, Friedman JM, Joyce CM, Steitz TA. Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Science (New York, N.Y.). 240: 199-201. PMID 2832946 DOI: 10.1126/Science.2832946 |
0.604 |
|
| 1987 |
Beese L, Stubbs G, Thomas J, Cohen C. Structure of microtubules with reduced hydration. Comparison of results from X-ray diffraction and electron microscopy Journal of Molecular Biology. 196: 575-580. PMID 3681968 DOI: 10.1016/0022-2836(87)90033-7 |
0.49 |
|
| 1987 |
Beese L, Stubbs G, Cohen C. Microtubule structure at 18 Å resolution Journal of Molecular Biology. 194: 257-264. PMID 3612805 DOI: 10.1016/0022-2836(87)90373-1 |
0.498 |
|
| 1987 |
Steitz TA, Beese L, Freemont PS, Friedman JM, Sanderson MR. Structural studies of Klenow fragment: an enzyme with two active sites. Cold Spring Harbor Symposia On Quantitative Biology. 52: 465-71. PMID 3331343 DOI: 10.1101/Sqb.1987.052.01.053 |
0.538 |
|
| 1980 |
Craig R, Szent-Györgyi AG, Beese L, Flicker P, Vibert P, Cohen C. Electron microscopy of thin filaments decorated with a Ca2+-regulated myosin. Journal of Molecular Biology. 140: 35-55. PMID 6997502 DOI: 10.1016/0022-2836(80)90355-1 |
0.486 |
|
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