Výsledky vyhledávání - "Carlotta Zamparelli"

Akademický článek

Monomeric and dimeric states of human ZO1-PDZ2 are functional partners of the SARS-CoV-2 E protein

Autor: Noah Giacon, Ettore Lo Cascio, Darcy S. Davidson, Marcelo D. Polêto, Justin A. Lemkul, Valeria Pennacchietti, Livia Pagano, Carlotta Zamparelli, Angelo Toto, Alessandro Arcovito

Publikováno v: Computational and Structural Biotechnology Journal, Vol 21, Iss , Pp 3259-3271 (2023)

The Envelope (E) protein of SARS-CoV-2 plays a key role in virus maturation, assembly, and virulence mechanisms. The E protein is characterized by the presence of a PDZ-binding motif (PBM) at its C-terminus that allows it to interact with several PDZ

Externí odkaz: https://doaj.org/article/5f87ea47f88e4bfda42747021ccdc226

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Probing the Role of Murine Neuroglobin CDloop–D-Helix Unit in CO Ligand Binding and Structural Dynamics

Autor: Cécile Exertier, Federico Sebastiani, Ida Freda, Elena Gugole, Gabriele Cerutti, Giacomo Parisi, Linda Celeste Montemiglio, Maurizio Becucci, Cristiano Viappiani, Stefano Bruno, Carmelinda Savino, Carlotta Zamparelli, Massimiliano Anselmi, Stefania Abbruzzetti, Giulietta Smulevich, Beatrice Vallone

Publikováno v: ACS Chemical Biology. 17:2099-2108

We produced a neuroglobin variant, namely, Ngb CDless, with the excised CDloop- and D-helix, directly joining the C- and E-helices. The CDless variant retained bis-His hexacoordination, and we investigated the role of the CDloop-D-helix unit in contr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9e9bb9ed4f95b01d43f4acb3e034be2
https://doi.org/10.1021/acschembio.2c00172

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Effects of Y361-auto-phosphorylation on structural plasticity of the HIPK2 kinase domain

Autor: Francesca Siepi, Daniela Verzili, Cinzia Rinaldo, Antonella Scaglione, Silvia Soddu, Cristina Cecchetti, Carlotta Zamparelli, Giacomo Parisi, C. Savino, Linda Celeste Montemiglio, Alessandra Giorgi, Beatrice Vallone, Laura Monteonofrio

Publikováno v: Protein Science. 27:725-737

The dual-specificity activity of the homeodomain interacting protein kinase 2 (HIPK2) is regulated by cis-auto-phosphorylation of tyrosine 361 (Y361) on the activation loop. Inhibition of this process or substitution of Y361 with nonphosphorylatable

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::01f625935753568eac3a33fb974f8dd6
https://doi.org/10.1002/pro.3367

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Oligomeric State and Thermal Stability of Apo- and Holo- Human Ornithine δ-Aminotransferase

Autor: Barbara Cellini, Carlotta Zamparelli, Riccardo Montioli, Carla Borri Voltattorni

Publikováno v: The Protein Journal

Human ornithine δ-aminotransferase (hOAT) (EC 2.6.1.13) is a mitochondrial pyridoxal 5′-phosphate (PLP)-dependent aminotransferase whose deficit is associated with gyrate atrophy, a rare autosomal recessive disorder causing progressive blindness a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66168d2c2dd9723613e3e15a06436e15
https://doi.org/10.1007/s10930-017-9710-5

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The oligomeric assembly of the phosphodiesterase-5 is a mixture of dimers and tetramers: A putative role in the regulation of function

Autor: Francesco Malatesta, Stefano Biagioni, Silvia Cardarelli, Michele Saliola, Adriana E. Miele, Fabio Naro, Carlotta Zamparelli, Mauro Giorgi

Publikováno v: Biochimica et Biophysica Acta (BBA)-General Subjects
Biochimica et Biophysica Acta (BBA)-General Subjects, Elsevier, 2018, 1862 (10), pp.2183-2190. ⟨10.1016/j.bbagen.2018.07.010⟩

Background Phosphodiesterases (PDEs) are a superfamily of evolutionary conserved cyclic nucleotides (cAMP/cGMP) hydrolysing enzymes, components of transduction pathways regulating crucial aspects of cell life. PDE5, one of these families, is the mole

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aec8cafcd98648ddeb3766706783df94
https://pubmed.ncbi.nlm.nih.gov/30025857

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The catalytic activity of serine hydroxymethyltransferase is essential for denovo nuclear dTMP synthesis in lung cancer cells

Autor: Francesca Cutruzzolà, Alessandro Paiardini, Maria Chiara Magnifico, Serena Rinaldo, Angela Tramonti, Giorgio Giardina, Marina Marani, Amani Bouzidi, Alessio Paone, Giulia Guiducci, Valentino Pontecorvi, Roberta Lucchi, Roberto Contestabile, Carlotta Zamparelli

Publikováno v: The FEBS journal
285 (2018): 3238–3253. doi:10.1111/febs.14610
info:cnr-pdr/source/autori:Giardina, Giorgio; Paone, Alessio; Tramonti, Angela; Lucchi, Roberta; Marani, Marina; Magnifico, Maria Chiara; Bouzidi, Amani; Pontecorvi, Valentino; Guiducci, Giulia; Zamparelli, Carlotta; Rinaldo, Serena; Paiardini, Alessandro; Contestabile, Roberto; Cutruzzola, Francesca/titolo:The catalytic activity of serine hydroxymethyltransferase is essential for denovo nuclear dTMP synthesis in lung cancer cells/doi:10.1111%2Ffebs.14610/rivista:The FEBS journal (Print)/anno:2018/pagina_da:3238/pagina_a:3253/intervallo_pagine:3238–3253/volume:285

Cancer cells reprogramme one-carbon metabolism (OCM) to sustain growth and proliferation. Depending on cell demands, serine hydroxymethyltransferase (SHMT) dynamically changes the fluxes of OCM by reversibly converting serine and tetrahydrofolate (TH

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08aa05f44ca0f20c2fe6d048fed7766e

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The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase

Autor: Christopher J. Danpure, Jackie Lewin, Carla Borri Voltattorni, Barbara Cellini, Sonia Fargue, Carlotta Zamparelli, Riccardo Montioli

Publikováno v: The International Journal of Biochemistry & Cell Biology. 44:536-546

Alanine:glyoxylate aminotransferase (AGT) is a pyridoxal-phosphate (PLP)-dependent enzyme. Its deficiency causes the hereditary kidney stone disease primary hyperoxaluria type 1. AGT is a highly stable compact dimer and the first 21 residues of each

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc801ecf242cff2fbdc15b65850c3ecc
https://doi.org/10.1016/j.biocel.2011.12.007

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Effect of the charge distribution along the 'ferritin-like' pores of the proteins from the Dps family on the iron incorporation process

Autor: Francesco Oteri, Gisa Di Cecca, Mattia Falconi, Pierpaolo Ceci, Emilia Chiancone, Carlotta Zamparelli

Publikováno v: JBIC Journal of Biological Inorganic Chemistry. 16:869-880

DNA-binding proteins from starved cells (Dps) differ in the number and position of charged residues along the "ferritin-like" pores that are used by iron to reach the ferroxidase center and the protein cavity. These differences are shown to affect si

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7543dd24135e4aadb0a17b788c092d80
https://doi.org/10.1007/s00775-011-0784-9

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Iron Translocation into and out of Listeria innocua Dps and Size Distribution of the Protein-enclosed Nanomineral Are Modulated by the Electrostatic Gradient at the 3-fold 'Ferritin-like' Pores

Autor: Emilia Chiancone, Simonetta Stefanini, Giuliano Bellapadrona, Elizabeth C. Theil, Carlotta Zamparelli

Publikováno v: Journal of Biological Chemistry. 284:19101-19109

Elucidating pore function at the 3-fold channels of 12-subunit, microbial Dps proteins is important in understanding their role in the management of iron/hydrogen peroxide. The Dps pores are called “ferritin-like” because of the structural resemb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f344e8a55f36f608bb84c20482da54d8
https://doi.org/10.1074/jbc.m109.014670

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The W105G and W99G Sorcin Mutants Demonstrate the Role of the D Helix in the Ca2+-Dependent Interaction with Annexin VII and the Cardiac Ryanodine Receptor

Autor: Christopher M. Loughrey, Emilia Chiancone, Gianni Colotti, Daniela Verzili, Godfrey L. Smith, Carlotta Zamparelli, Manuela Mella

Publikováno v: Biochemistry (Easton) 45 (2006): 12519–12529. doi:10.1021/bi060416a
info:cnr-pdr/source/autori:Colotti, G.; Zamparelli, C.; Verzili D.; Mella M.; Loughrey C. M.; Smith G. L.; Chiancone. E./titolo:The W105G and W99G sorcin mutants demonstrate the role of the D helix in the Ca2+-dependent interaction with annexin VII and the cardiac ryanodine receptor./doi:10.1021%2Fbi060416a/rivista:Biochemistry (Easton)/anno:2006/pagina_da:12519/pagina_a:12529/intervallo_pagine:12519–12529/volume:45

Sorcin, a 21.6 kDa two-domain penta-EF-hand (PEF) protein, when activated by Ca(2+) binding, interacts with target proteins in a largely uncharacterized process. The two physiological EF-hands EF3 and EF2 do not belong to a structural pair but are co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b56f34222781a7ce1d30b15e73f3b054
https://doi.org/10.1021/bi060416a

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