Anne Gangloff, Ph.D. - Related publications

2002 Universite Laval (Canada) 
Biochemistry, Animal Physiology Biology
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50 most relevant papers in past 60 days:
Year Citation  Score
2020 Chenprakhon P, Pimviriyakul P, Tongsook C, Chaiyen P. Phenolic hydroxylases. The Enzymes. 47: 283-326. PMID 32951826 DOI: 10.1016/bs.enz.2020.05.008   
2020 Seok J, Kim YJ, Kim IK, Kim KJ. Structural basis for stereospecificity to d-amino acid of glycine oxidase from Bacillus cereus ATCC 14579. Biochemical and Biophysical Research Communications. PMID 32993959 DOI: 10.1016/j.bbrc.2020.09.093   
2020 Sultana KN, Kuldeep J, Siddiqi MI, Srivastava SK. Crystallographic and molecular dynamics simulation analysis of NAD synthetase from methicillin resistant Staphylococcus aureus (MRSA). International Journal of Biological Macromolecules. 165: 2349-2362. PMID 33098904 DOI: 10.1016/j.ijbiomac.2020.10.096   
2020 Yilmazer B, Isupov MN, De Rose SA, Bulut H, Benninghoff JC, Binay B, Littlechild JA. Structural insights into the NAD-dependent formate dehydrogenase mechanism revealed from the NADH complex and the formate NAD ternary complex of the Chaetomium thermophilum enzyme. Journal of Structural Biology. 212: 107657. PMID 33148525 DOI: 10.1016/j.jsb.2020.107657   
2020 Gao LW, Zhu HT, Liu CY, Lv ZX, Fan XM, Zhang YW. A highly active heparinase I from Bacteroides cellulosilyticus: Cloning, high level expression, and molecular characterization. Plos One. 15: e0240920. PMID 33079966 DOI: 10.1371/journal.pone.0240920   
2020 Mhashal AR, Romero-Rivera A, Mydy LS, Cristobal JR, Gulick AM, Richard JP, Kamerlin SCL. Modeling the Role of a Flexible Loop and Active Site Side Chains in Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase. Acs Catalysis. 10: 11253-11267. PMID 33042609 DOI: 10.1021/acscatal.0c02757   
2020 Chappell BM, Fenton AW. The phosphate moiety of phosphoenolpyruvate does NOT contribute to allosteric regulation of liver pyruvate kinase by fructose-1,6-bisphosphate. Archives of Biochemistry and Biophysics. 695: 108633. PMID 33075302 DOI: 10.1016/   
2020 Raj P, Karthik S, Arif SM, Varshney U, Vijayan M. Plasticity, ligand conformation and enzyme action of Mycobacterium smegmatis MutT1. Acta Crystallographica. Section D, Structural Biology. 76: 982-992. PMID 33021500 DOI: 10.1107/S2059798320010992   
2020 Zhao S, Ni F, Qiu T, Wolff JT, Tsai SC, Luo R. Molecular Basis for Polyketide Ketoreductase-Substrate Interactions. International Journal of Molecular Sciences. 21. PMID 33066287 DOI: 10.3390/ijms21207562   
2020 Yang S, DeMars MD, Grandner JM, Olson NM, Anzai Y, Sherman DH, Houk KN. Computational-Based Mechanistic Study and Engineering of Cytochrome P450 MycG for Selective Oxidation of 16-Membered Macrolide Antibiotics. Journal of the American Chemical Society. PMID 33030347 DOI: 10.1021/jacs.0c04388   
2020 El-Shora HM, El-Sharkawy RM. Tyrosinase from Penicillium chrysogenum: Characterization and application in phenol removal from aqueous solution. The Journal of General and Applied Microbiology. PMID 33041267 DOI: 10.2323/jgam.2020.01.002   
2020 El-Shora HM, El-Sharkawy RM. Tyrosinase from Penicillium chrysogenum: Characterization and application in phenol removal from aqueous solution. The Journal of General and Applied Microbiology. PMID 33041267 DOI: 10.2323/jgam.2020.01.002   
2020 Wang P, Dhananjayan N, Hagras MA, Stuchebrukhov AA. Respiratory complex I: Bottleneck at the entrance of quinone site requires conformational change for its opening. Biochimica Et Biophysica Acta. Bioenergetics. 148326. PMID 33045211 DOI: 10.1016/j.bbabio.2020.148326   
2020 Yang M, Ma Y, Song M, Wu H, Jiang Q, Liu J, Qu L. Identification and biochemical characterisation of a novel methionine aminopeptidase from the taiga tick Ixodes persulcatus. Ticks and Tick-Borne Diseases. 12: 101554. PMID 33002807 DOI: 10.1016/j.ttbdis.2020.101554   
2020 Liu S, Li S, Shen G, Sukumar N, Krezel AM, Li W. Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation. Science (New York, N.Y.). PMID 33154105 DOI: 10.1126/science.abc5667   
2020 Stirling AJ, Gilbert SE, Conner M, Mallette E, Kimber MS, Seah SYK. A Key Glycine in Bacterial Steroid-Degrading Acyl-CoA Dehydrogenases Allows Flavin-Ring Repositioning and Modulates Substrate Side Chain Specificity. Biochemistry. 59: 4081-4092. PMID 33040522 DOI: 10.1021/acs.biochem.0c00568   
2020 Kneller DW, Phillips G, Kovalevsky A, Coates L. Room-temperature neutron and X-ray data collection of 3CL M from SARS-CoV-2. Acta Crystallographica. Section F, Structural Biology Communications. 76: 483-487. PMID 33006576 DOI: 10.1107/S2053230X20011814   
2020 Lima RAT, Oliveira GM, Souza AA, Lopes FAC, Santana RH, Istvan P, Quirino BF, Barbosa JA, Freitas SM, Garay AV, Krüger RH. Functional and structural characterization of a novel GH3 β-glucosidase from the gut metagenome of the Brazilian Cerrado termite Syntermes wheeleri. International Journal of Biological Macromolecules. PMID 33011259 DOI: 10.1016/j.ijbiomac.2020.09.236   
2020 Lee CH, Jin ES, Lee JH, Hwang ET. Immobilization and Stabilization of Enzyme in Biomineralized Calcium Carbonate Microspheres. Frontiers in Bioengineering and Biotechnology. 8: 553591. PMID 33163476 DOI: 10.3389/fbioe.2020.553591   
2020 Frias J, Toubarro D, Fraga A, Botelho C, Teixeira J, Pedrosa J, Simões N. Purification and characterization of a thrombolytic enzyme produced by a new strain of . Journal of Microbiology and Biotechnology. PMID 33148943 DOI: 10.4014/jmb.2008.08010   
2020 Broom A, Rakotoharisoa RV, Thompson MC, Zarifi N, Nguyen E, Mukhametzhanov N, Liu L, Fraser JS, Chica RA. Ensemble-based enzyme design can recapitulate the effects of laboratory directed evolution in silico. Nature Communications. 11: 4808. PMID 32968058 DOI: 10.1038/s41467-020-18619-x   
2020 Zhang T, Rao J, Li W, Wang K, Qiu F. Mechanism-based inactivation of cytochrome P450 enzymes by natural products based on metabolic activation. Drug Metabolism Reviews. 1-30. PMID 33043714 DOI: 10.1080/03602532.2020.1828910   
2020 Yoo W, Kim B, Jeon S, Kim KK, Kim TD. Identification, characterization, and immobilization of a novel YbfF esterase from Halomonas elongata. International Journal of Biological Macromolecules. PMID 33031847 DOI: 10.1016/j.ijbiomac.2020.09.247   
2020 Shah AB, Yoon S, Kim JH, Zhumanova K, Ban YJ, Lee KW, Park KH. Effectiveness of cyclohexyl functionality in ugonins from Helminthostachys zeylanica to PTP1B and α-glucosidase inhibitions. International Journal of Biological Macromolecules. PMID 33075336 DOI: 10.1016/j.ijbiomac.2020.10.061   
2020 Curtis BN, Smolen KA, Barlow SJ, Caselli E, Prati F, Taracila MA, Bonomo RA, Wallar BJ, Powers RA. Structural insights into inhibition of the derived cephalosporinase ADC-7 by ceftazidime and its boronic acid transition state analog. Antimicrobial Agents and Chemotherapy. PMID 32988830 DOI: 10.1128/AAC.01183-20   
2020 McGuire BE, Hettle A, Vickers C, King DT, Vocadlo DJ, Boraston AB. The structure of a family 110 glycoside hydrolase provides insight into the hydrolysis of α-(1,3)-galactosidic linkages in λ-carrageenan and blood group antigens. The Journal of Biological Chemistry. PMID 33127644 DOI: 10.1074/jbc.RA120.015776   
2020 Vodovoz M, Gadda G. Kinetic solvent viscosity effects reveal a protein isomerization in the reductive half-reaction of Neurospora crassa class II nitronate monooxygenase. Archives of Biochemistry and Biophysics. 108625. PMID 33038312 DOI: 10.1016/   
2020 Ouyang Y, Li Q, Kuang X, Wang H, Wu J, Ayepa E, Chen H, Abrha GT, Zhang Z, Li X, Ma M. YMR152W from Saccharomyces cerevisiae encoding a novel aldehyde reductase for detoxification of aldehydes derived from lignocellulosic biomass. Journal of Bioscience and Bioengineering. PMID 32967812 DOI: 10.1016/j.jbiosc.2020.09.004   
2020 Baklouti Z, Delattre C, Pierre G, Gardarin C, Abdelkafi S, Michaud P, Dubessay P. Biochemical Characterization of a Bifunctional Enzyme Constructed by the Fusion of a Glucuronan Lyase and a Chitinase from sp. Life (Basel, Switzerland). 10. PMID 33049934 DOI: 10.3390/life10100234   
2020 Lin KP, Feng GJ, Pu FL, Hou XD, Cao SL. Enhancing the Thermostability of Papain by Immobilizing on Deep Eutectic Solvents-Treated Chitosan With Optimal Microporous Structure and Catalytic Microenvironment. Frontiers in Bioengineering and Biotechnology. 8: 576266. PMID 33134288 DOI: 10.3389/fbioe.2020.576266   
2020 Kaushik A, Rahisuddin R, Saini N, Singh RP, Kaur R, Kaul S, Kumaran S. Molecular Mechanism of Selective Substrate Engagement and Inhibitor Dis-engagement of Cysteine Synthase. The Journal of Biological Chemistry. PMID 33162395 DOI: 10.1074/jbc.RA120.014490   
2020 Tang X, Zhang F, Zeng T, Li W, Yin S, Wu R. Enzymatic Plasticity Inspired by the Diterpene Cyclase CotB2. Acs Chemical Biology. PMID 32986400 DOI: 10.1021/acschembio.0c00645   
2020 Chengyao X, Yan Q, Chaonan D, Xiaopei C, Yanxin W, Ding L, Xianfeng Y, Jian H, Yan H, Zhongli C, Zhoukun L. Enzymatic properties of an efficient glucan branching enzyme and its potential application in starch modification. Protein Expression and Purification. 178: 105779. PMID 33115653 DOI: 10.1016/j.pep.2020.105779   
2020 Fonseca MJMD, Armstrong Z, Withers SG, Briers Y. High-throughput generation of product profiles for arabinoxylan-active enzymes from metagenomes. Applied and Environmental Microbiology. PMID 32948521 DOI: 10.1128/AEM.01505-20   
2020 Holehouse J, Sukys A, Grima R. Stochastic time-dependent enzyme kinetics: Closed-form solution and transient bimodality. The Journal of Chemical Physics. 153: 164113. PMID 33138415 DOI: 10.1063/5.0017573   
2020 Maurya B, Pochet L, Wouters J, Colaço M, Misquith S. MetA (Rv3341) from Mycobacterium tuberculosis H37Rv strain exhibits substrate dependent dual role of transferase and hydrolase activity. Biochimie. 179: 113-126. PMID 32976971 DOI: 10.1016/j.biochi.2020.09.013   
2020 George JT, Srivatsan SG. Responsive fluorescent nucleotides serve as efficient substrates to probe terminal uridylyl transferase. Chemical Communications (Cambridge, England). PMID 32939524 DOI: 10.1039/d0cc05092j   
2020 Ma J, Li T, Tan H, Liu W, Yin H. The Important Roles Played in Substrate Binding of Aromatic Amino Acids in Exo-Inulinase From CBS 4857. Frontiers in Molecular Biosciences. 7: 569797. PMID 33102520 DOI: 10.3389/fmolb.2020.569797   
2020 Sun D, Cheng X, Tian Y, Ding S, Zhang D, Cai P, Hu QN. EnzyMine: a comprehensive database for enzyme function annotation with enzymatic reaction chemical feature. Database : the Journal of Biological Databases and Curation. PMID 33002112 DOI: 10.1093/database/baaa065   
2020 Strzelczyk P, Zhang D, Dyba M, Wlodawer A, Lubkowski J. Generalized enzymatic mechanism of catalysis by tetrameric L-asparaginases from mesophilic bacteria. Scientific Reports. 10: 17516. PMID 33060684 DOI: 10.1038/s41598-020-74480-4   
2020 Makraki E, Darby JF, Carneiro MG, Firth JD, Heyam A, Ab E, O'Brien P, Siegal G, Hubbard RE. Fragment-derived modulators of an industrial β-glucosidase. The Biochemical Journal. PMID 33111951 DOI: 10.1042/BCJ20200507   
2020 Salim N, Santhiagu A, Joji K. Purification, characterization and anticancer evaluation of l-methioninase from . 3 Biotech. 10: 501. PMID 33163320 DOI: 10.1007/s13205-020-02494-w   
2020 Wang J, Ma Y, Wang X, Zhang Y, Tan H, Li X, Chen G. Theoretical study on the catalytic mechanism of human deoxyhypusine hydroxylase. Physical Chemistry Chemical Physics : Pccp. PMID 33020771 DOI: 10.1039/d0cp03598j   
2020 Goltsov A, Swat M, Peskov K, Kosinsky Y. Cycle Network Model of Prostaglandin H Synthase-1. Pharmaceuticals (Basel, Switzerland). 13. PMID 32977592 DOI: 10.3390/ph13100265   
2020 Abdelmagid WM, Mahmoodi N, Tanner ME. A guanidinium-based inhibitor of a type I isopentenyl diphosphate isomerase. Bioorganic & Medicinal Chemistry Letters. 30: 127577. PMID 32979487 DOI: 10.1016/j.bmcl.2020.127577   
2020 Nair AV, Robson A, Ackrill TD, Till M, Byrne MJ, Back CR, Tiwari K, Davies JA, Willis CL, Race PR. Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in polyketide β-methyl branch incorporation. Scientific Reports. 10: 15323. PMID 32948786 DOI: 10.1038/s41598-020-71850-w   
2020 Li X, Dou Z, Sun Y, Wang L, Gong B, Wan L. A sequence embedding method for enzyme optimal condition analysis. Bmc Bioinformatics. 21: 512. PMID 33167861 DOI: 10.1186/s12859-020-03851-5   
2020 Kampatsikas I, Rompel A. Similar but still different - which amino acid residues are responsible for varying activities in type-III copper enzymes? Chembiochem : a European Journal of Chemical Biology. PMID 33108057 DOI: 10.1002/cbic.202000647   
2020 Cho IS, Kim JH, Lin Y, Su XD, Kang JS, Yang SY, Kim YH. Inhibitory Activity of Quercetin 3--Arabinofuranoside and 2-Oxopomolic Acid Derived from on Soluble Epoxide Hydrolase. Molecules (Basel, Switzerland). 25. PMID 32972033 DOI: 10.3390/molecules25184352   
2020 Cho IS, Kim JH, Lin Y, Su XD, Kang JS, Yang SY, Kim YH. Inhibitory Activity of Quercetin 3--Arabinofuranoside and 2-Oxopomolic Acid Derived from on Soluble Epoxide Hydrolase. Molecules (Basel, Switzerland). 25. PMID 32972033 DOI: 10.3390/molecules25184352