Pure and Applied Chemistry

CrossRef Cited-by Linking

• Mayes Heather B., Broadbelt Linda J., Beckham Gregg T.: How Sugars Pucker: Electronic Structure Calculations Map the Kinetic Landscape of Five Biologically Paramount Monosaccharides and Their Implications for Enzymatic Catalysis. J. Am. Chem. Soc. 2014, 136, 1008. <http://dx.doi.org/10.1021/ja410264d>
• Cobucci-Ponzano Beatrice, Strazzulli Andrea, Rossi Mosé, Moracci Marco: Glycosynthases in Biocatalysis. Synth Catal 2011, 353, 2284. <http://dx.doi.org/10.1002/adsc.201100461>
• Jordan Douglas B., Wagschal Kurt: Properties and applications of microbial β-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium . Appl Microbiol Biotechnol 2010, 86, 1647. <http://dx.doi.org/10.1007/s00253-010-2538-y>
• Ge Yue, Antoulinakis Evan G., Gee Kyle R., Johnson Iain: An ultrasensitive, continuous assay for xylanase using the fluorogenic substrate 6,8-difluoro-4-methylumbelliferyl β-d-xylobioside. Analytical Biochemistry 2007, 362, 63. <http://dx.doi.org/10.1016/j.ab.2006.11.034>
• KIM SANG MOO, PENNER MICHAEL H.: TRICHODERMA REESEI ?-GALACTOSIDASE ACTIVITY ON LOCUST BEAN AND GUAR GALACTOMANNANS. J Food Biochemistry 2004, 28, 293. <http://dx.doi.org/10.1111/j.1745-4514.2004.tb00073.x>
• Kurahashi Takuya, Mizutani Tadashi, Yoshida Jun-ichi: Functionalized DMAP catalysts for regioselective acetylation of carbohydrates. Tetrahedron 2002, 58, 8669. <http://dx.doi.org/10.1016/S0040-4020(02)01098-0>
• Bravman Tsafrir, Zolotnitsky Gennady, Shulami Smadar, Belakhov Valery, Solomon Dmitry, Baasov Timor, Shoham Gil, Shoham Yuval: Stereochemistry of family 52 glycosyl hydrolases: a β-xylosidase from Bacillus stearothermophilus T-6 is a retaining enzyme. FEBS Letters 2001, 495, 39. <http://dx.doi.org/10.1016/S0014-5793(01)02360-2>
• Bravman Tsafrir, Mechaly Adva, Shulami Smadar, Belakhov Valery, Baasov Timor, Shoham Gil, Shoham Yuval: Glutamic acid 160 is the acid-base catalyst of β-xylosidase from Bacillus stearothermophilus T-6: a family 39 glycoside hydrolase. FEBS Letters 2001, 495, 115. <http://dx.doi.org/10.1016/S0014-5793(01)02371-7>
• Spagna Giovanni, Barbagallo Riccardo N., Martino Angela, Pifferi Pier Giorgio: A simple method for purifying glycosidases: α-l-rhamnopyranosidase from Aspergillus niger to increase the aroma of Moscato wine. Enzyme Microbiology Technology 2000, 27, 522. <http://dx.doi.org/10.1016/S0141-0229(00)00236-2>
• Heightman Tom D., Vasella Andrea T.: Neue Erkenntnisse über Hemmung, Struktur und Mechanismus konfigurationserhaltender Glycosidasen. Angew Chem 1999, 111, 794. <http://dx.doi.org/10.1002/(SICI)1521-3757(19990315)111:6<794::AID-ANGE794>3.0.CO;2-K>
• Henrissat B, Teeri T.T, Warren R.A.J: A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants. FEBS Letters 1998, 425, 352. <http://dx.doi.org/10.1016/S0014-5793(98)00265-8>
• Spagna Giovanni, Andreani Franco, Salatelli Elisabetta, Romagnoli Denis, Pifferi Pier Giorgio: Immobilization of α-l-arabinofuranosidase on chitin and chitosan. Process Biochem 1998, 33, 57. <http://dx.doi.org/10.1016/S0032-9592(97)00067-8>
• Hoos Roland, Vasella Andrea, Rupitz Karen, Withers Stephen G.: d-Glyconhydroximolactams strongly inhibit α-glycosidases. Carbohydrates Research 1997, 298, 291. <http://dx.doi.org/10.1016/S0008-6215(96)00320-5>
• Qian Xinhua, Morís-Varas Francisco, Fitzgerald Michael C., Wong Chi-Huey: C2-Symmetrical tetrahydroxyazepanes as inhibitors of glycosidases and HIV/FIV proteases. biorg med chem 1996, 4, 2055. <http://dx.doi.org/10.1016/S0968-0896(96)00218-0>