Year |
Citation |
Score |
2021 |
Belato HB, D'Ordine AM, Nierzwicki L, Arantes PR, Jogl G, Palermo G, Lisi GP. Structural and dynamic insights into the HNH nuclease of divergent Cas9 species. Journal of Structural Biology. 214: 107814. PMID 34871741 DOI: 10.1016/j.jsb.2021.107814 |
0.3 |
|
2020 |
Killeavy EE, Jogl G, Gregory ST. Tiamulin-Resistant Mutants of the Thermophilic Bacterium . Antibiotics (Basel, Switzerland). 9. PMID 32526926 DOI: 10.3390/Antibiotics9060313 |
0.403 |
|
2019 |
East KW, Newton JC, Morzan UN, Narkhede Y, Acharya A, Skeens E, Jogl G, Batista VS, Palermo G, Lisi GP. Allosteric Motions of the CRISPR-Cas9 HNH Nuclease Probed by NMR and Molecular Dynamics. Journal of the American Chemical Society. PMID 31885264 DOI: 10.2210/Pdb6O56/Pdb |
0.304 |
|
2018 |
Jogl G, Khayat R, Murphy E, Kleffmann T, Singh K, Murray B, Krause K. 164. Reporting the High-resolution Structure of the Enterococcal Ribosome: A New Template for Antibiotic Discovery Open Forum Infectious Diseases. 5: S15-S16. DOI: 10.1093/Ofid/Ofy209.034 |
0.33 |
|
2016 |
Duan L, Jogl G, Cane DE. The Cytochrome P450-Catalyzed Oxidative Rearrangement in the Final Step of Pentalenolactone Biosynthesis: Substrate Structure Determines Mechanism. Journal of the American Chemical Society. PMID 27588339 DOI: 10.1021/Jacs.6B08610 |
0.385 |
|
2015 |
Carr JF, Lee HJ, Jaspers JB, Dahlberg AE, Jogl G, Gregory ST. Phenotypic suppression of streptomycin-resistance by mutations in multiple components of the translation apparatus. Journal of Bacteriology. PMID 26148717 DOI: 10.1128/Jb.00219-15 |
0.309 |
|
2014 |
Gregory ST, Connetti JL, Carr JF, Jogl G, Dahlberg AE. Phenotypic interactions among mutations in a Thermus thermophilus 16S rRNA gene detected with genetic selections and experimental evolution. Journal of Bacteriology. 196: 3776-83. PMID 25157075 DOI: 10.1128/Jb.02104-14 |
0.336 |
|
2014 |
Demirci H, Murphy FV, Murphy EL, Connetti JL, Dahlberg AE, Jogl G, Gregory ST. Structural analysis of base substitutions in Thermus thermophilus 16S rRNA conferring streptomycin resistance. Antimicrobial Agents and Chemotherapy. 58: 4308-17. PMID 24820088 DOI: 10.1128/Aac.02857-14 |
0.433 |
|
2013 |
Demirci H, Wang L, Murphy FV, Murphy EL, Carr JF, Blanchard SC, Jogl G, Dahlberg AE, Gregory ST. The central role of protein S12 in organizing the structure of the decoding site of the ribosome. Rna (New York, N.Y.). 19: 1791-801. PMID 24152548 DOI: 10.1261/Rna.040030.113 |
0.379 |
|
2013 |
Demirci H, Sierra RG, Laksmono H, Shoeman RL, Botha S, Barends TR, Nass K, Schlichting I, Doak RB, Gati C, Williams GJ, Boutet S, Messerschmidt M, Jogl G, Dahlberg AE, et al. Serial femtosecond X-ray diffraction of 30S ribosomal subunit microcrystals in liquid suspension at ambient temperature using an X-ray free-electron laser. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 69: 1066-9. PMID 23989164 DOI: 10.1107/S174430911302099X |
0.326 |
|
2013 |
Demirci H, Murphy F, Murphy E, Gregory ST, Dahlberg AE, Jogl G. A structural basis for streptomycin-induced misreading of the genetic code. Nature Communications. 4: 1355. PMID 23322043 DOI: 10.1038/Ncomms2346 |
0.359 |
|
2013 |
Li H, Jogl G. Crystal structure of decaprenylphosphoryl-β- D-ribose 2'-epimerase from Mycobacterium smegmatis. Proteins. 81: 538-43. PMID 23184707 DOI: 10.1002/Prot.24220 |
0.443 |
|
2012 |
Larsen LH, Rasmussen A, Giessing AM, Jogl G, Kirpekar F. Identification and characterization of the Thermus thermophilus 5-methylcytidine (m5C) methyltransferase modifying 23 S ribosomal RNA (rRNA) base C1942. The Journal of Biological Chemistry. 287: 27593-600. PMID 22711535 DOI: 10.1074/Jbc.M112.376160 |
0.383 |
|
2011 |
Jogl G, Wang X, Mason SA, Kovalevsky A, Mustyakimov M, Fisher Z, Hoffman C, Kratky C, Langan P. High-resolution neutron crystallographic studies of the hydration of the coenzyme cob(II)alamin. Acta Crystallographica. Section D, Biological Crystallography. 67: 584-91. PMID 21636899 DOI: 10.1107/S090744491101496X |
0.325 |
|
2010 |
Demirci H, Murphy F, Belardinelli R, Kelley AC, Ramakrishnan V, Gregory ST, Dahlberg AE, Jogl G. Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function. Rna (New York, N.Y.). 16: 2319-24. PMID 20962038 DOI: 10.1261/Rna.2357210 |
0.369 |
|
2010 |
Demirci H, Larsen LH, Hansen T, Rasmussen A, Cadambi A, Gregory ST, Kirpekar F, Jogl G. Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus. Rna (New York, N.Y.). 16: 1584-96. PMID 20558545 DOI: 10.1261/Rna.2088310 |
0.369 |
|
2009 |
Gregory ST, Demirci H, Belardinelli R, Monshupanee T, Gualerzi C, Dahlberg AE, Jogl G. Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG. Rna (New York, N.Y.). 15: 1693-704. PMID 19622680 DOI: 10.1261/Rna.1652709 |
0.441 |
|
2009 |
Demirci H, Belardinelli R, Seri E, Gregory ST, Gualerzi C, Dahlberg AE, Jogl G. Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine. Journal of Molecular Biology. 388: 271-82. PMID 19285505 DOI: 10.1016/J.Jmb.2009.02.066 |
0.477 |
|
2009 |
Li H, Jogl G. Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator). The Journal of Biological Chemistry. 284: 1748-54. PMID 19015259 DOI: 10.1074/Jbc.M807821200 |
0.486 |
|
2008 |
Demirci H, Gregory ST, Dahlberg AE, Jogl G. Crystal structure of the Thermus thermophilus 16 S rRNA methyltransferase RsmC in complex with cofactor and substrate guanosine. The Journal of Biological Chemistry. 283: 26548-56. PMID 18667428 DOI: 10.1074/Jbc.M804005200 |
0.478 |
|
2008 |
Demirci H, Gregory ST, Dahlberg AE, Jogl G. Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase. Structure (London, England : 1993). 16: 1059-66. PMID 18611379 DOI: 10.1016/J.Str.2008.03.016 |
0.401 |
|
2007 |
You Z, Omura S, Ikeda H, Cane DE, Jogl G. Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis. The Journal of Biological Chemistry. 282: 36552-60. PMID 17942405 DOI: 10.1074/Jbc.M706358200 |
0.451 |
|
2007 |
Li H, Jogl G. Crystal structure of the zinc-binding transport protein ZnuA from Escherichia coli reveals an unexpected variation in metal coordination. Journal of Molecular Biology. 368: 1358-66. PMID 17399739 DOI: 10.1016/J.Jmb.2007.02.107 |
0.452 |
|
2007 |
Demirci H, Gregory ST, Dahlberg AE, Jogl G. Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA. The Embo Journal. 26: 567-77. PMID 17215866 DOI: 10.1038/Sj.Emboj.7601508 |
0.403 |
|
2006 |
Holmes W, Jogl G. Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity. The Journal of Biological Chemistry. 281: 38109-16. PMID 17050532 DOI: 10.1074/Jbc.M606883200 |
0.444 |
|
2006 |
Hsiao YS, Jogl G, Tong L. Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates. The Journal of Biological Chemistry. 281: 28480-7. PMID 16870616 DOI: 10.1074/Jbc.M602622200 |
0.436 |
|
2006 |
Hsiao YS, Jogl G, Esser V, Tong L. Crystal structure of rat carnitine palmitoyltransferase II (CPT-II). Biochemical and Biophysical Research Communications. 346: 974-80. PMID 16781677 DOI: 10.1016/J.Bbrc.2006.06.006 |
0.387 |
|
2005 |
Jogl G, Hsiao YS, Tong L. Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity. The Journal of Biological Chemistry. 280: 738-44. PMID 15492013 DOI: 10.1074/Jbc.M409894200 |
0.462 |
|
2004 |
Jogl G, Hsiao YS, Tong L. Structure and function of carnitine acyltransferases. Annals of the New York Academy of Sciences. 1033: 17-29. PMID 15591000 DOI: 10.1196/Annals.1320.002 |
0.456 |
|
2004 |
Gebauer D, Li J, Jogl G, Shen Y, Myszka DG, Tong L. Crystal structure of the PH-BEACH domains of human LRBA/BGL. Biochemistry. 43: 14873-80. PMID 15554694 DOI: 10.1021/Bi049498Y |
0.328 |
|
2004 |
Hsiao YS, Jogl G, Tong L. Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase. The Journal of Biological Chemistry. 279: 31584-9. PMID 15155726 DOI: 10.1074/Jbc.M403484200 |
0.462 |
|
2004 |
Jogl G, Tong L. Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP. Biochemistry. 43: 1425-31. PMID 14769018 DOI: 10.1021/Bi035911A |
0.462 |
|
2003 |
Gobin S, Thuillier L, Jogl G, Faye A, Tong L, Chi M, Bonnefont JP, Girard J, Prip-Buus C. Functional and structural basis of carnitine palmitoyltransferase 1A deficiency. The Journal of Biological Chemistry. 278: 50428-34. PMID 14517221 DOI: 10.1074/Jbc.M310130200 |
0.429 |
|
2003 |
Jogl G, Tong L. Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. Cell. 112: 113-22. PMID 12526798 DOI: 10.1016/S0092-8674(02)01228-X |
0.464 |
|
2003 |
Jogl G, Rozovsky S, McDermott AE, Tong L. Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution Proceedings of the National Academy of Sciences of the United States of America. 100: 50-55. PMID 12509510 DOI: 10.1073/Pnas.0233793100 |
0.385 |
|
2002 |
Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Krönke M, Tong L. Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain. The Embo Journal. 21: 4785-95. PMID 12234919 DOI: 10.1093/Emboj/Cdf502 |
0.369 |
|
2001 |
Rozovsky S, Jogl G, Tong L, McDermott AE. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics Journal of Molecular Biology. 310: 271-280. PMID 11419952 DOI: 10.1006/Jmbi.2001.4673 |
0.352 |
|
2000 |
Champloy F, Gruber K, Jogl G, Kratky C. XAS spectroscopy reveals X-ray-induced photoreduction of free and protein-bound B12 cofactors. Journal of Synchrotron Radiation. 7: 267-73. PMID 16609206 DOI: 10.1107/S0909049500006336 |
0.334 |
|
1999 |
Reitzer R, Gruber K, Jogl G, Wagner UG, Bothe H, Buckel W, Kratky C. Glutamate mutase from Clostridium cochlearium: The structure of a coenzyme B12-dependent enzyme provides new mechanistic insights Structure. 7: 891-902. PMID 10467146 DOI: 10.1016/S0969-2126(99)80116-6 |
0.344 |
|
1999 |
Langan P, Lehmann M, Wilkinson C, Jogl G, Kratky C. Neutron Laue diffraction studies of coenzyme cob(II)alamin. Acta Crystallographica. Section D, Biological Crystallography. 55: 51-9. PMID 10089394 DOI: 10.1107/S090744499800660X |
0.327 |
|
1999 |
Champloy F, Jogl G, Reitzer R, Buckel W, Bothe H, Beatrix B, Broeker G, Michalowicz A, Meyer-Klaucke W, Kratky C. EXAFS data indicate a 'normal' axial cobalt-nitrogen bond of the organo- B12 cofactor in the two coenzyme B12-dependent enzymes glutamate mutase and 2-methyleneglutarate mutase Journal of the American Chemical Society. 121: 11780-11789. DOI: 10.1021/Ja990349Q |
0.358 |
|
1998 |
Reitzer R, Krasser M, Jogl G, Buckel W, Bothe H, Kratky C. Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium. Acta Crystallographica. Section D, Biological Crystallography. 54: 1039-42. PMID 9757132 DOI: 10.1107/S0907444997020210 |
0.331 |
|
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