Caprini G - Search Results

1

L-lactate dehydrogenation in flavocytochrome b2: a first principles molecular dynamics study.

Tabacchi G, Zucchini D, Caprini G, Gamba A, Lederer F, Vanoni MA, Fois E. Tabacchi G, et al. Among authors: caprini g. FEBS J. 2009 Apr;276(8):2368-80. doi: 10.1111/j.1742-4658.2009.06969.x. FEBS J. 2009. PMID: 19348008 Free article.

2

Epigenetic-based cancer therapeutics: new potential HDAC8 inhibitors.

Hassanzadeh M, Mahernia S, Caprini G, Fossati G, Adib M, Moakedi F, Amanlou M. Hassanzadeh M, et al. Among authors: caprini g. J Biomol Struct Dyn. 2022 Jan;40(1):297-311. doi: 10.1080/07391102.2020.1813203. Epub 2020 Sep 4. J Biomol Struct Dyn. 2022. PMID: 32886033

3

Novel HDAC inhibitors exhibit pre-clinical efficacy in lymphoma models and point to the importance of CDKN1A expression levels in mediating their anti-tumor response.

Mensah AA, Kwee I, Gaudio E, Rinaldi A, Ponzoni M, Cascione L, Fossati G, Stathis A, Zucca E, Caprini G, Bertoni F. Mensah AA, et al. Among authors: caprini g. Oncotarget. 2015 Mar 10;6(7):5059-71. doi: 10.18632/oncotarget.3239. Oncotarget. 2015. PMID: 25671298 Free PMC article.

4

The subnanometer resolution structure of the glutamate synthase 1.2-MDa hexamer by cryoelectron microscopy and its oligomerization behavior in solution: functional implications.

Cottevieille M, Larquet E, Jonic S, Petoukhov MV, Caprini G, Paravisi S, Svergun DI, Vanoni MA, Boisset N. Cottevieille M, et al. Among authors: caprini g. J Biol Chem. 2008 Mar 28;283(13):8237-49. doi: 10.1074/jbc.M708529200. Epub 2008 Jan 16. J Biol Chem. 2008. PMID: 18199747 Free article.

5

Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1.

Zucchini D, Caprini G, Pasterkamp RJ, Tedeschi G, Vanoni MA. Zucchini D, et al. Among authors: caprini g. Arch Biochem Biophys. 2011 Nov;515(1-2):1-13. doi: 10.1016/j.abb.2011.08.004. Epub 2011 Aug 16. Arch Biochem Biophys. 2011. PMID: 21864500

6

Difluoromethyl-1,3,4-oxadiazoles are slow-binding substrate analog inhibitors of histone deacetylase 6 with unprecedented isotype selectivity.

Cellupica E, Caprini G, Cordella P, Cukier C, Fossati G, Marchini M, Rocchio I, Sandrone G, Vanoni MA, Vergani B, Źrubek K, Stevenazzi A, Steinkühler C. Cellupica E, et al. Among authors: caprini g. J Biol Chem. 2023 Jan;299(1):102800. doi: 10.1016/j.jbc.2022.102800. Epub 2022 Dec 15. J Biol Chem. 2023. PMID: 36528061 Free PMC article.

7

The Importance of the "Time Factor" for the Evaluation of Inhibition Mechanisms: The Case of Selected HDAC6 Inhibitors.

Cellupica E, Caprini G, Fossati G, Mirdita D, Cordella P, Marchini M, Rocchio I, Sandrone G, Stevenazzi A, Vergani B, Steinkühler C, Vanoni MA. Cellupica E, et al. Among authors: caprini g. Biology (Basel). 2023 Jul 26;12(8):1049. doi: 10.3390/biology12081049. Biology (Basel). 2023. PMID: 37626935 Free PMC article.

8

Ferredoxin-NADP+ reductase and ferredoxin of the protozoan parasite Toxoplasma gondii interact productively in Vitro and in Vivo.

Pandini V, Caprini G, Thomsen N, Aliverti A, Seeber F, Zanetti G. Pandini V, et al. Among authors: caprini g. J Biol Chem. 2002 Dec 13;277(50):48463-71. doi: 10.1074/jbc.M209388200. Epub 2002 Oct 4. J Biol Chem. 2002. PMID: 12370173 Free article.

9

Roles of the species-specific subdomain and the N-terminal peptide of Toxoplasma gondii ferredoxin-NADP+ reductase in ferredoxin binding.

Pandini V, Caprini G, Tedeschi G, Seeber F, Zanetti G, Aliverti A. Pandini V, et al. Among authors: caprini g. Biochemistry. 2006 Mar 21;45(11):3563-71. doi: 10.1021/bi052326w. Biochemistry. 2006. PMID: 16533038

10

A single in vivo-selected point mutation in the active center of Toxoplasma gondii ferredoxin-NADP+ reductase leads to an inactive enzyme with greatly enhanced affinity for ferredoxin.

Thomsen-Zieger N, Pandini V, Caprini G, Aliverti A, Cramer J, Selzer PM, Zanetti G, Seeber F. Thomsen-Zieger N, et al. Among authors: caprini g. FEBS Lett. 2004 Oct 22;576(3):375-80. doi: 10.1016/j.febslet.2004.09.042. FEBS Lett. 2004. PMID: 15498566 Free article.

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