Year |
Citation |
Score |
2018 |
Lee CC, Jordan DB, Stoller JR, Kibblewhite RE, Wagschal K. Biochemical characterization of Caulobacter crescentus xylose dehydrogenase. International Journal of Biological Macromolecules. PMID 29959017 DOI: 10.1016/j.ijbiomac.2018.06.124 |
0.396 |
|
2017 |
Wagschal KC, Rose Stoller J, Chan VJ, Jordan DB. Expression and Characterization of Hyperthermostable Exopolygalacturonase RmGH28 from Rhodothermus marinus. Applied Biochemistry and Biotechnology. PMID 28555295 DOI: 10.1007/s12010-017-2518-0 |
0.352 |
|
2016 |
Jordan DB, Braker JD, Wagschal K, Stoller JR, Lee CC. Isolation and divalent-metal activation of a β-xylosidase, RUM630-BX. Enzyme and Microbial Technology. 82: 158-63. PMID 26672463 DOI: 10.1016/j.enzmictec.2015.10.001 |
0.345 |
|
2015 |
Wagschal K, Jordan DB, Lee CC, Younger A, Braker JD, Chan VJ. Biochemical characterization of uronate dehydrogenases from three Pseudomonads, Chromohalobacter salixigens, and Polaromonas naphthalenivorans. Enzyme and Microbial Technology. 69: 62-8. PMID 25640726 DOI: 10.1016/j.enzmictec.2014.12.008 |
0.372 |
|
2013 |
Lee CC, Braker JD, Grigorescu AA, Wagschal K, Jordan DB. Divalent metal activation of a GH43 β-xylosidase. Enzyme and Microbial Technology. 52: 84-90. PMID 23273276 DOI: 10.1016/j.enzmictec.2012.10.010 |
0.326 |
|
2013 |
Jordan DB, Wagschal K, Grigorescu AA, Braker JD. Highly active β-xylosidases of glycoside hydrolase family 43 operating on natural and artificial substrates. Applied Microbiology and Biotechnology. 97: 4415-28. PMID 23053115 DOI: 10.1007/s00253-012-4475-4 |
0.343 |
|
2010 |
Mertens JA, Braker JD, Jordan DB. Catalytic properties of two Rhizopus oryzae 99-880 glucoamylase enzymes without starch binding domains expressed in Pichia pastoris. Applied Biochemistry and Biotechnology. 162: 2197-213. PMID 20549574 DOI: 10.1007/s12010-010-8994-0 |
0.408 |
|
2010 |
Jordan DB, Braker JD. beta-D-Xylosidase from Selenomonas ruminantium: role of glutamate 186 in catalysis revealed by site-directed mutagenesis, alternate substrates, and active-site inhibitor. Applied Biochemistry and Biotechnology. 161: 395-410. PMID 20127424 DOI: 10.1007/s12010-009-8874-7 |
0.361 |
|
2010 |
Fan Z, Yuan L, Jordan DB, Wagschal K, Heng C, Braker JD. Engineering lower inhibitor affinities in beta-D-xylosidase. Applied Microbiology and Biotechnology. 86: 1099-113. PMID 19921178 DOI: 10.1007/S00253-009-2335-7 |
0.302 |
|
2009 |
Bischoff KM, Wicklow DT, Jordan DB, de Rezende ST, Liu S, Hughes SR, Rich JO. Extracellular hemicellulolytic enzymes from the maize endophyte Acremonium zeae. Current Microbiology. 58: 499-503. PMID 19184610 DOI: 10.1007/s00284-008-9353-z |
0.361 |
|
2004 |
Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T. Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry. 43: 11403-16. PMID 15350127 DOI: 10.1021/bi049053+ |
0.32 |
|
2002 |
Liao DI, Zheng YJ, Viitanen PV, Jordan DB. Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase. Biochemistry. 41: 1795-806. PMID 11827524 DOI: 10.1021/bi015652u |
0.353 |
|
2002 |
Zheng YJ, Basarab GS, Jordan DB. Roles of substrate distortion and intramolecular hydrogen bonding in enzymatic catalysis by scytalone dehydratase. Biochemistry. 41: 820-6. PMID 11790103 DOI: 10.1021/bi015848u |
0.36 |
|
2001 |
Björnberg O, Jordan DB, Palfey BA, Jensen KF. Dihydrooxonate is a substrate of dihydroorotate dehydrogenase (DHOD) providing evidence for involvement of cysteine and serine residues in base catalysis. Archives of Biochemistry and Biophysics. 391: 286-94. PMID 11437361 DOI: 10.1006/Abbi.2001.2409 |
0.429 |
|
2001 |
Liao D, Basarab GS, Gatenby AA, Valent B, Jordan DB. Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis. Structure (London, England : 1993). 9: 19-27. PMID 11342131 DOI: 10.1016/S0969-2126(00)00548-7 |
0.371 |
|
2001 |
Liao DI, Calabrese JC, Wawrzak Z, Viitanen PV, Jordan DB. Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis. Structure (London, England : 1993). 9: 11-8. PMID 11342130 DOI: 10.1016/S0969-2126(00)00550-5 |
0.383 |
|
2001 |
Picollelli MA, Viitanen PV, Jordan DB. Spectrophotometric determination of 3, 4-dihydroxy-2-butanone-4-phosphate synthase activity. Analytical Biochemistry. 287: 347-9. PMID 11112287 DOI: 10.1006/ABIO.2000.4867 |
0.331 |
|
2001 |
Thompson JE, Fahnestock S, Farrall L, Liao DI, Valent B, Jordan DB. The second naphthol reductase of fungal melanin biosynthesis in Magnaporthe grisea: tetrahydroxynaphthalene reductase. The Journal of Biological Chemistry. 275: 34867-72. PMID 10956664 DOI: 10.1074/Jbc.M006659200 |
0.356 |
|
2000 |
Liao DI, Qian J, Chisholm DA, Jordan DB, Diner BA. Crystal structures of the photosystem II D1 C-terminal processing protease. Nature Structural Biology. 7: 749-53. PMID 10966643 DOI: 10.1038/78973 |
0.361 |
|
2000 |
Jennings LD, Rayner DR, Jordan DB, Okonya JF, Basarab GS, Amorose DK, Anaclerio BM, Lee JK, Schwartz RS, Whitmore KA. Cyclobutane carboxamide inhibitors of fungal melanin: Biosynthesis and their evaluation as fungicides Bioorganic and Medicinal Chemistry. 8: 897-907. PMID 10882002 DOI: 10.1016/S0968-0896(00)00034-1 |
0.318 |
|
2000 |
Jordan DB, Bisaha JJ, Picollelli MA. Catalytic properties of dihydroorotate dehydrogenase from Saccharomyces cerevisiae: studies on pH, alternate substrates, and inhibitors. Archives of Biochemistry and Biophysics. 378: 84-92. PMID 10871048 DOI: 10.1006/abbi.2000.1823 |
0.403 |
|
2000 |
Jordan DB, Zheng YJ, Lockett BA, Basarab GS. Stereochemistry of the enolization of scytalone by scytalone dehydratase. Biochemistry. 39: 2276-82. PMID 10694394 DOI: 10.1021/BI991839Y |
0.392 |
|
2000 |
Persson K, Schneider G, Jordan DB, Viitanen PV, Sandalova T. Crystal structure analysis of a pentameric fungal and an icosahedral plant lumazine synthase reveals the structural basis for differences in assembly. Protein Science : a Publication of the Protein Society. 8: 2355-65. PMID 10595538 DOI: 10.1110/PS.8.11.2355 |
0.303 |
|
1999 |
Basarab GS, Jordan DB. Wild-type enzyme as a reporter of inhibitor binding by catalytically impaired mutant enzymes. Biochemical and Biophysical Research Communications. 263: 617-20. PMID 10512727 DOI: 10.1006/BBRC.1999.1423 |
0.39 |
|
1999 |
Basarab GS, Steffens JJ, Wawrzak Z, Schwartz RS, Lundqvist T, Jordan DB. Catalytic mechanism of scytalone dehydratase: site-directed mutagenisis, kinetic isotope effects, and alternate substrates. Biochemistry. 38: 6012-24. PMID 10320327 DOI: 10.1021/BI982952B |
0.438 |
|
1998 |
Thompson JE, Jordan DB. Partition analysis of an enzyme acting concurrently upon two substrates in a continuous multiwavelength assay. Analytical Biochemistry. 256: 7-13. PMID 9466792 DOI: 10.1006/ABIO.1997.2490 |
0.39 |
|
1998 |
Thompson JE, Basarab GS, Pierce J, Hodge CN, Jordan DB. 2,3-Dihydro-2,5-dihydroxy-4H-benzopyran-4-one: a nonphysiological substrate for fungal melanin biosynthetic enzymes. Analytical Biochemistry. 256: 1-6. PMID 9466791 DOI: 10.1006/ABIO.1997.2489 |
0.304 |
|
1997 |
Trost JT, Chisholm DA, Jordan DB, Diner BA. The D1 C-terminal processing protease of photosystem II from Scenedesmus obliquus. Protein purification and gene characterization in wild type and processing mutants. The Journal of Biological Chemistry. 272: 20348-56. PMID 9252339 DOI: 10.1074/JBC.272.33.20348 |
0.315 |
|
1997 |
Thompson JE, Basarab GS, Andersson A, Lindqvist Y, Jordan DB. Trihydroxynaphthalene reductase from Magnaporthe grisea: Realization of an active center inhibitor and elucidation of the kinetic mechanism Biochemistry. 36: 1852-1860. PMID 9048570 DOI: 10.1021/bi962355u |
0.304 |
|
1997 |
Andersson A, Jordan D, Schneider G, Lindqvist Y. A flexible lid controls access to the active site in 1,3,8-trihydroxynaphthalene reductase Febs Letters. 400: 173-176. PMID 9001392 DOI: 10.1016/S0014-5793(96)01382-8 |
0.403 |
|
1996 |
Andersson A, Jordan D, Schneider G, Lindqvist Y. Crystal structure of the ternary complex of 1,3,8-trihydroxy-naphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor Structure. 4: 1161-1170. PMID 8939741 DOI: 10.1016/S0969-2126(96)00124-4 |
0.481 |
|
1985 |
Holbrook GP, Jordan DB, Chollet R. Reduced Apparent Photorespiration by the C(3)-C(4) Intermediate Species, Moricandia arvensis and Panicum milioides. Plant Physiology. 77: 578-83. PMID 16664101 DOI: 10.1104/Pp.77.3.578 |
0.58 |
|
1985 |
Jordan DB, Chollet R. Subunit dissociation and reconstitution of ribulose-1,5-bisphosphate carboxylase from Chromatium vinosum. Archives of Biochemistry and Biophysics. 236: 487-96. PMID 3918498 DOI: 10.1016/0003-9861(85)90651-4 |
0.636 |
|
1984 |
Jordan DB, Ogren WL. The CO2/O2 specificity of ribulose 1,5-bisphosphate carboxylase/oxygenase - Dependence on ribulosebisphosphate concentration, pH and temperature Planta. 161: 308-313. DOI: 10.1007/BF00398720 |
0.526 |
|
1983 |
Meyers SP, Brinegar AC, Schrader LE, Jordan DB, Ogren WL. Ploidy Effects in Isogenic Populations of Alfalfa (Medicago sativa L.) : IV. Similarity in Physical and Kinetic Properties of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase. Plant Physiology. 71: 966-8. PMID 16662937 DOI: 10.1104/Pp.71.4.966 |
0.547 |
|
1983 |
Jordan DB, Ogren WL. Species variation in kinetic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase Archives of Biochemistry and Biophysics. 227: 425-433. PMID 6582802 DOI: 10.1016/0003-9861(83)90472-1 |
0.672 |
|
1983 |
Jordan DB, Chollet R, Ogren WL. Binding of phosphorylated effectors by active and inactive forms of ribulose-1,5-bisphosphate carboxylase Biochemistry. 22: 3410-3418. DOI: 10.1021/Bi00283A017 |
0.66 |
|
1982 |
Spreitzer RJ, Jordan DB, Ogren WL. Biochemical and genetic analysis of an RuBP carboxylase/oxygenase-deficient mutant and revertants of Chlamydomonas reinhardii Febs Letters. 148: 117-121. DOI: 10.1016/0014-5793(82)81255-6 |
0.64 |
|
1981 |
Jordan DB, Ogren WL. A Sensitive Assay Procedure for Simultaneous Determination of Ribulose-1,5-bisphosphate Carboxylase and Oxygenase Activities. Plant Physiology. 67: 237-45. PMID 16661654 DOI: 10.1104/Pp.67.2.237 |
0.595 |
|
1981 |
Jordan DB, Ogren WL. Species variation in the specificity of ribulose biphosphate carboxylase/oxygenase Nature. 291: 513-515. DOI: 10.1038/291513A0 |
0.629 |
|
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