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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1998 1
1999 1
2001 1
2003 3
2005 1
2007 2
2008 1
2009 2
2010 3
2011 2
2012 3
2013 5
2014 4
2015 9
2016 8
2017 5
2018 4
2019 1
2020 3
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53 results
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Chemical constituents and synergistic anti-gout studies on Eurycoma longifolia and potential mechanisms evaluation based on systemic analysis approach.
Liu Y, Lai L, Ju Y, Liu C, Meng D. Liu Y, et al. Bioorg Chem. 2019 Nov;92:103302. doi: 10.1016/j.bioorg.2019.103302. Epub 2019 Sep 17. Bioorg Chem. 2019. PMID: 31634989
Aiming to search potential compounds and probable mechanisms, network pharmacology, molecular docking and Kyoto encyclopedia of genes and genomes (KEGG) pathway enrichment analysis were adopted, leading to the hypothesis of 17 targets related to different pathogenesis of g …
Aiming to search potential compounds and probable mechanisms, network pharmacology, molecular docking and Kyoto encyclopedia of genes …
Docking and small angle X-ray scattering studies of purine nucleoside phosphorylase.
Filgueira de Azevedo W Jr, dos Santos GC, dos Santos DM, Olivieri JR, Canduri F, Silva RG, Basso LA, Renard G, da Fonseca IO, Mendes MA, Palma MS, Santos DS. Filgueira de Azevedo W Jr, et al. Biochem Biophys Res Commun. 2003 Oct 3;309(4):923-8. Biochem Biophys Res Commun. 2003. PMID: 13679062
Docking simulations have been used to assess protein complexes with some success. Small angle X-ray scattering (SAXS) is a well-established technique to investigate protein spatial configuration. This work describes the integration of geometric docking with SAXS to
Docking simulations have been used to assess protein complexes with some success. Small angle X-ray scattering (SAXS) is a well-estab
Oxidation and nitration of mononitrophenols by a DyP-type peroxidase.
Büttner E, Ullrich R, Strittmatter E, Piontek K, Plattner DA, Hofrichter M, Liers C. Büttner E, et al. Arch Biochem Biophys. 2015 May 15;574:86-92. doi: 10.1016/j.abb.2015.03.003. Epub 2015 Mar 18. Arch Biochem Biophys. 2015. PMID: 25796533
In the case of oNP and pNP conversion, dinitrophenols (2,4-DNP and 2,6-DNP) were identified as products and for pNP additionally p-benzoquinone. ...The additional nitrogen in DNPs formed during enzymatic conversion was found to originate both from (15)N-pNP a …
In the case of oNP and pNP conversion, dinitrophenols (2,4-DNP and 2,6-DNP) were identified as products and for pNP additional …
Hydroxyl-related differences for three dietary flavonoids as inhibitors of human purine nucleoside phosphorylase.
Wen QH, Wang LH, Zeng XA, Niu DB, Wang MS. Wen QH, et al. Int J Biol Macromol. 2018 Oct 15;118(Pt A):588-598. doi: 10.1016/j.ijbiomac.2018.06.045. Epub 2018 Jun 15. Int J Biol Macromol. 2018. PMID: 29894785
In this work, the hydroxyl-related differences of binding properties and inhibitory activities of dietary flavonoids, namely chrysin, baicalein and apigenin against purine nucleoside phosphorylase (PNP) were investigated. ...Results from molecular modeling revealed that th …
In this work, the hydroxyl-related differences of binding properties and inhibitory activities of dietary flavonoids, namely chrysin, baical …
Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.
Korkhov VM, Mireku SA, Veprintsev DB, Locher KP. Korkhov VM, et al. Nat Struct Mol Biol. 2014 Dec;21(12):1097-9. doi: 10.1038/nsmb.2918. Epub 2014 Nov 17. Nat Struct Mol Biol. 2014. PMID: 25402482
Here we present the structure of the last missing state in the form of AMP-PNP-bound BtuCD, trapped by a disulfide cross-link. ...
Here we present the structure of the last missing state in the form of AMP-PNP-bound BtuCD, trapped by a disulfide cross-link. ...
In silico approach to support that p-nitrophenol monooxygenase from Arthrobacter sp. strain JS443 catalyzes the initial two sequential monooxygenations.
Kallubai M, Amineni U, Mallavarapu M, Kadiyala V. Kallubai M, et al. Interdiscip Sci. 2015 Feb 6. doi: 10.1007/s12539-013-0216-3. Online ahead of print. Interdiscip Sci. 2015. PMID: 25663108
Molecular docking of the physiological substrates, PNP and 4-nitrocatechol (4-NC), was carried out using Glide v5.7 implemented in Maestro v9.2, and the binding energies were calculated to substantiate the prediction. Docking complexes formed by molecular lev …
Molecular docking of the physiological substrates, PNP and 4-nitrocatechol (4-NC), was carried out using Glide v5.7 implemente …
In Silico Approach to Support that p-Nitrophenol Monooxygenase from Arthrobacter sp. Strain JS443 Catalyzes the Initial Two Sequential Monooxygenations.
Kallubai M, Amineni U, Mallavarapu M, Kadiyala V. Kallubai M, et al. Interdiscip Sci. 2015 Jun;7(2):157-67. doi: 10.1007/s12539-015-0018-x. Epub 2015 Aug 14. Interdiscip Sci. 2015. PMID: 26272475
Molecular docking of the physiological substrates, PNP and 4-nitrocatechol (4-NC), was carried out using Glide v5.7 implemented in Maestro v9.2, and the binding energies were calculated to substantiate the prediction. Docking complexes formed by molecular lev …
Molecular docking of the physiological substrates, PNP and 4-nitrocatechol (4-NC), was carried out using Glide v5.7 implemente …
Molecular modeling, dynamics and docking studies of purine nucleoside phosphorylase from Streptococcus pyogenes.
Timmers LF, Caceres RA, Dias R, Basso LA, Santos DS, de Azevedo WF Jr. Timmers LF, et al. Biophys Chem. 2009 Jun;142(1-3):7-16. doi: 10.1016/j.bpc.2009.02.006. Epub 2009 Feb 26. Biophys Chem. 2009. PMID: 19282092
Purine Nucleoside Phosphorylase (PNP) catalyzes the reversible phosphorolysis of N-glycosidic bonds of purine nucleosides and deoxynucleosides, except for adenosine, to generate ribose 1-phosphate and the purine base. PNP has been submitted to intensive structural s …
Purine Nucleoside Phosphorylase (PNP) catalyzes the reversible phosphorolysis of N-glycosidic bonds of purine nucleosides and deoxynu …
A Novel β-Glucuronidase from Talaromyces pinophilus Li-93 Precisely Hydrolyzes Glycyrrhizin into Glycyrrhetinic Acid 3-O-Mono-β-d-Glucuronide.
Xu Y, Feng X, Jia J, Chen X, Jiang T, Rasool A, Lv B, Qu L, Li C. Xu Y, et al. Appl Environ Microbiol. 2018 Sep 17;84(19):e00755-18. doi: 10.1128/AEM.00755-18. Print 2018 Oct 1. Appl Environ Microbiol. 2018. PMID: 30054355 Free PMC article.
TpGUS79A showed a much higher catalytic efficiency on GL (k(cat)/K(m) of 11.14 mM(-1) s(-1)) than on the artificial substrate pNP β-glucopyranosiduronic acid (k(cat)/K(m) of 0.01 mM(-1) s(-1)), which is different from the case for most GUSs. Homology modeling, substrate …
TpGUS79A showed a much higher catalytic efficiency on GL (k(cat)/K(m) of 11.14 mM(-1) s(-1)) than on the artificial substrate pNP β-g …
Efficient Fludarabine-Activating PNP From Archaea as a Guidance for Redesign the Active Site of E. Coli PNP.
Cacciapuoti G, Bagarolo ML, Martino E, Scafuri B, Marabotti A, Porcelli M. Cacciapuoti G, et al. J Cell Biochem. 2016 May;117(5):1126-35. doi: 10.1002/jcb.25396. Epub 2015 Oct 18. J Cell Biochem. 2016. PMID: 26477689
Substrate specificity and catalytic efficiency of SsMTAP and SsMTAPII for fludarabine were analyzed by kinetic studies and compared with E. coli PNP. ...A computational analysis of the interactions of fludarabine in the active sites of E. coli PNP, SsMTAP, and SsMTA …
Substrate specificity and catalytic efficiency of SsMTAP and SsMTAPII for fludarabine were analyzed by kinetic studies and compared with E. …
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