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158 results on '"Nuti, E"'

1. Identification of N-Acyl Hydrazones as New Non-Zinc-Binding MMP-13 Inhibitors by Structure-Based Virtual Screening Studies and Chemical Optimization

Author

Universitat Rovira i Virgili, Cuffaro, D; Gimeno, A; Bernardoni, BL; Di Leo, R; Pujadas, G; Garcia-Vallve, S; Nencetti, S; Rossello, A; Nuti, E, Universitat Rovira i Virgili, and Cuffaro, D; Gimeno, A; Bernardoni, BL; Di Leo, R; Pujadas, G; Garcia-Vallve, S; Nencetti, S; Rossello, A; Nuti, E

Abstract

Matrix metalloproteinase 13 plays a central role in osteoarthritis (OA), as its overexpression induces an excessive breakdown of collagen that results in an imbalance between collagen synthesis and degradation in the joint, leading to progressive articular cartilage degradation. Therefore, MMP-13 has been proposed as a key therapeutic target for OA. Here we have developed a virtual screening workflow aimed at identifying selective non-zinc-binding MMP-13 inhibitors by targeting the deep S1′ pocket of MMP-13. Three ligands were found to inhibit MMP-13 in the µM range, and one of these showed selectivity over other MMPs. A structure-based analysis guided the chemical optimization of the hit compound, leading to the obtaining of a new N-acyl hydrazone-based derivative with improved inhibitory activity and selectivity for the target enzyme.

Published
2023

4. Exosite inhibition of A Disintegrin And Metalloproteinase with Thrombospondin motif (ADAMTS)-5 by a glycoconjugated arylsulfonamide

Author

Salvatore, S, Cuffaro, D, Nuti, E, Ciccone, L, Tuccinardi, T, Liva, F, D’Andrea, F, De Groot, R, Rossello, A, Ahnström, J, and British Heart Foundation

Abstract

ADAMTS-5 is a major protease involved in the turnover of proteoglycans such as aggrecan and versican. Its aggrecanase activity has been directly linked to the etiology of osteoarthritis (OA), identifying ADAMTS-5 as a pharmaceutical target for OA treatment. However, most existing ADAMTS-5 inhibitors target its active site and therefore suffer from poor selectivity. Here, using a novel approach, we have designed a new class of sugar-based arylsulfonamide inhibitors, which are selective for ADAMTS-5 through binding to a previously unknown substrate-binding site (exosite). Docking calculations combined with molecular dynamics simulations demonstrated that our lead compound is a cross-domain inhibitor that targets the interface of the metalloproteinase and disintegrin-like domains. Targeted mutagenesis identified disintegrin-like domain residues K532 and K533 as an exosite which is critical for substrate recognition. Furthermore, we show that this exosite acts as major determinant for inhibitor binding and, therefore, can be targeted for development of selective ADAMTS-5 inhibitors.

Published
2020

7. Synthesis and antiangiogenic activity study of new hop chalcone Xanthohumol analogues

Author

Nuti, E, Bassani, B, Camodeca, C, Rosalia, L, Cantelmo, A, Gallo, C, Baci, D, Bruno, A, Orlandini, E, Nencetti, S, Noonan, D, Albini, A, Rossello, A, Nuti E, Bassani B, Camodeca C, Rosalia L, Cantelmo A, Gallo C, Baci D, Bruno A, Orlandini E, Nencetti S, Noonan DM, Albini A, Rossello A, Nuti, E, Bassani, B, Camodeca, C, Rosalia, L, Cantelmo, A, Gallo, C, Baci, D, Bruno, A, Orlandini, E, Nencetti, S, Noonan, D, Albini, A, Rossello, A, Nuti E, Bassani B, Camodeca C, Rosalia L, Cantelmo A, Gallo C, Baci D, Bruno A, Orlandini E, Nencetti S, Noonan DM, Albini A, and Rossello A

Abstract

Angiogenesis induction is a hallmark of cancer. Antiangiogenic properties of Xanthohumol (XN), a naturally occurring prenylated chalcone from hops, have been widely reported. Here we describe the synthesis and study the antiangiogenic activity in vitro of a series of XN derivatives, where different substituents on the B-ring of the chalcone scaffold were inserted. The new XN derivatives inhibited human umbilical-vein endothelial cell (HUVEC) proliferation, adhesion, migration, invasion and their ability to form capillary-like structures in vitro at 10 mu M concentration. The preliminary results indicate that the phenolic OH group in R, present in natural XN, is not necessary for having antiangiogenic activity. In fact, the most effective compound from this series, 13, was characterized by a para-methoxy group in R and a fluorine atom in R-2 on B-ring. This study paves the way for future development of synthetic analogues of XN to be used as cancer angiopreventive and chemopreventive agents

Published
2017

8. Probing the Quantum Interference between Singly and Doubly Resonant Top-Quark Production in pp Collisions at root s=13 TeV with the ATLAS Detector

Author

Aaboud, M, Aad, G, Abbott, B, Abdinov, O, Abeloos, B, Abhayasinghe, DK, Abidi, SH, AbouZeid, OS, Abraham, NL, Abramowicz, H, Abreu, H, Ahulaiti, Y, Acharya, BS, Adachi, S, Adamczyk, L, Adelman, J, Adersberger, M, Adiguzel, A, Adye, T, Affolder, AA, Afik, Y, Agheorghiesei, C, Aguilar-Saavedra, JA, Ahmadov, F, Aielli, G, Akatsuka, S, Akesson, TPA, Akilli, E, Akimov, AV, Alberghi, GL, Albert, J, Albicocco, P, Verzini, MJ Alconada, Alderweireldt, S, Aleksa, M, Aleksandrov, IN, Alexa, C, Alexopoulos, T, Alhroob, M, Ali, B, Alimonti, G, Alison, J, Alkire, SP, Allaire, C, Allbrooke, BMM, Allen, BW, Allport, PP, Aloisio, A, Alonso, A, Alonso, F, Alpigiani, C, Alshehri, AA, Alstaty, MI, Gonzalez, B Alvarez, Piqueras, D Alvarez, Alviggi, MG, Arnadio, BT, Coutinho, Y Amaral, Ambroz, L, Amelung, C, Amidei, D, Dos Santos, SP Amor, Amoroso, S, Amrouche, CS, Anastopoulos, C, Ancu, LS, Andari, N, Andeen, T, Anders, CF, Anders, JK, Anderson, KJ, Andreazza, A, Andrei, V, Anelli, CR, Angelidakis, S, Angelozzi, I, Angerami, A, Anisenkov, AV, Annovi, A, Antel, C, Anthony, MT, Antonelli, M, Antrim, DJA, Anulli, F, Aoki, M, Bella, L Aperio, Arabidze, G, Araque, JP, Ferraz, V Araujo, Pereira, R Araujo, Arce, ATH, Ardell, RE, Arduh, FA, Arguin, J-F, Argyropoulos, S, Armbruster, AJ, Armitage, LJ, Armstrong, A, Amaez, O, Arnold, H, Arratia, M, Arslan, O, Artamonov, A, Artoni, G, Artz, S, Asai, S, Asbah, N, Ashkenazi, A, Asimakopoulou, EM, Asquith, L, Assamagan, K, Astalos, R, Atkin, RJ, Atkinson, M, Atlay, NB, Augsten, K, Avolio, G, Avramidou, R, Ayoub, MK, Azuelos, G, Baas, AE, Baca, MJ, Bachacou, H, Bachas, K, Backes, M, Bagnaia, P, Bahmani, M, Bahrasemani, H, Bailey, AJ, Baines, JT, Bajic, M, Bakalis, C, Baker, OK, Bakker, PJ, Gupta, D Bakshi, Baldin, EM, Balek, P, Balli, F, Balunas, WK, Balz, J, Banas, E, Bandyopadhyay, A, Banerjee, S, Bannoura, AAE, Barak, L, Barbe, WM, Barberio, EL, Barberis, D, Barbero, M, Barillari, T, Barisits, M-S, Barkeloo, J, Barklow, T, Barlow, N, Barnea, R, Barnes, SL, Barnett, BM, Barnett, RM, Barnovska-Blenessy, Z, Baroncelli, G, Barone, G, Barr, AJ, Navarro, L Barranco, Barreiro, F, Da Costa, J Barreiro Guimaraes, Bartoldus, R, Barton, AE, Bartos, P, Basalaev, A, Bassalat, A, Bates, RL, Batista, SJ, Batlamous, S, Batley, JR, Battaglia, M, Bauce, M, Bauer, F, Bauer, KT, Bawa, HS, Beacham, JB, Beattie, MD, Beau, T, Beauchemin, PH, Bechtle, P, Beck, HC, Beck, HP, Becker, K, Becker, M, Becot, C, Beddall, A, Beddall, AJ, Bednyakov, VA, Bedognetti, M, Bee, CP, Beermann, TA, Begalli, M, Begel, M, Behera, A, Behr, JK, Bell, AS, Bella, G, Bellagamba, L, Bellerive, A, Bellomo, M, Bellos, P, Belotskiy, K, Belyaev, NL, Benarya, O, Benchelcroun, D, Bender, M, Benekos, N, Benhammou, Y, Noccioli, E Benhar, Benitez, J, Benjamin, DP, Benoit, M, Bensinger, JR, Bentvelsen, S, Beresford, L, Beretta, M, Berge, D, Kuutmann, E Bergeaas, Berger, N, Bergsten, LJ, Beringer, J, Berlendis, S, Bernard, NR, Bernardi, G, Bernius, C, Bernlochner, FU, Berry, T, Berta, P, Bertella, C, Bertoli, G, Bertram, IA, Besjes, GJ, Bylund, O Bessidskaia, Bessner, M, Besson, N, Bethani, A, Bethke, S, Betti, A, Bevan, AJ, Beyer, J, Bianchi, RM, Biebel, O, Biedermann, D, Bielski, R, Bierwagen, K, Biesuz, NV, Biglietti, M, Billoud, TRV, Bindi, M, Bingul, A, Bini, C, Biondi, S, Birman, M, Bisanz, T, Biswal, JP, Bittrich, C, Bjergaard, DM, Black, JE, Black, KM, Blazek, T, Bloch, I, Blocker, C, Blue, A, Blumenschein, U, Blunier, Dr, Bobbink, GJ, Bobrovnikov, VS, Bocchetta, SS, Bocci, A, Boerner, D, Bogavac, D, Bogdanchikov, AC, Bohm, C, Boisvert, V, Bokan, P, Bold, T, Boldyrev, AS, Bolz, AE, Borriben, M, Bona, M, Bonilla, JS, Boonekamp, M, Borisov, A, Borissov, G, Bortfeldt, J, Bortoletto, D, Bortolotto, V, Boscherini, D, Bosman, M, Sola, JD Bossio, Bouaouda, K, Boudreau, J, Bouhova-Thacker, EV, Boumediene, D, Bourdarios, C, Boutle, SK, Boveia, A, Boyd, J, Boyko, IR, Bozson, AJ, Bracinik, J, Brahimi, N, Brandt, A, Brandt, G, Brandt, O, Braren, F, Bratzler, U, Brau, B, Brau, JE, Madden, WD Breaden, Brendlinger, K, Brennan, AJ, Brenner, L, Brenner, R, Bressler, S, Brickwedde, B, Briglin, DL, Britton, D, Britzger, D, Brock, I, Brock, R, Brooijmans, G, Brooks, T, Brooks, WK, Brost, E, Broughton, JH, de Renstrom, PA Brockman, Bruncko, D, Bruni, A, Bruni, G, Bruni, LS, Bruno, S, Brunt, BH, Bruschi, M, Bruscino, N, Bryant, P, Bryngemark, L, Buanes, T, Buat, Q, Buchholz, P, Buckley, AG, Budagov, IA, Buehrer, F, Bugge, MK, Bulekov, O, Bullock, D, Burch, TJ, Burdin, S, Burgard, CD, Burger, AM, Burghgrave, B, Burka, K, Burke, S, Burmeister, I, Burr, JTP, Buscher, D, Buscher, V, Buschmann, E, Bussey, P, Butler, JM, Buttar, CM, Butterworth, JM, Butti, P, Buttinger, W, Buzatu, A, Buzykaev, AR, Cabras, G, Urban, S Cabrera, Caforio, D, Cai, H, Cairo, VMM, Cakir, O, Calace, N, Calafiura, P, Calandri, A, Calderini, G, Calfayan, P, Callea, G, Caloba, LP, Lopez, S Calvente, Calvet, D, Calvet, S, Calvet, TP, Calvetti, M, Toro, R Camacho, Camarda, S, Camarri, P, Cameron, D, Armadans, R Caminal, Camincher, C, Campana, S, Campanelli, M, Camplani, A, Campoverde, A, Canale, V, Bret, M Cano, Cantero, J, Cao, T, Cao, Y, Garrido, MDM Capeans, Caprini, I, Caprini, M, Capua, M, Carbone, RM, Cardarelli, R, Cardillo, FC, Carli, I, Carli, T, Carlino, G, Carlson, BT, Carminati, L, Carney, RMA, Caron, S, Carquin, E, Carra, S, Carrillo-Montoya, GD, Casadei, D, Casado, MP, Casha, AF, Casolino, M, Casper, DW, Castelijn, R, Castillo, FL, Gimenez, V Castillo, Castro, NF, Catinaccio, A, Catmore, JR, Cattai, A, Caudron, J, Cavaliere, V, Cavallaro, E, Cavalli, D, Cavalli-Sforza, M, Cavasinni, V, Celebi, E, Ceradini, F, Alberich, L Cerda, Cerqueira, AS, Cerri, A, Cerrito, L, Cerutti, F, Cervelli, A, Cetin, SA, Chafaq, A, Chakraborty, D, Chan, SK, Chan, WS, Chan, YL, Chapman, JD, Charlton, DG, Chau, CC, Barajas, CA Chavez, Che, S, Chegwidden, A, Chekanov, S, Chekulaev, SV, Chelkov, GA, Chelstowska, MA, Chen, C, Chen, CH, Chen, H, Chen, J, Chen, S, Chen, SJ, Chen, X, Chen, Y, Chen, Y-H, Cheng, HC, Cheng, HJ, Cheplakov, A, Cheremushkina, E, El Moursli, R Cherkaoui, Cheu, E, Cheung, K, Chevalier, L, Chiarella, V, Chiarelli, G, Chiodini, G, Chisholm, AS, Chitan, A, Chiu, I, Chiu, YH, Chizhov, MV, Choi, K, Chomont, AR, Chouridou, S, Chow, YS, Christodoulou, V, Chu, MC, Chudoba, J, Chuinard, AJ, Chwastowski, JJ, Chytka, L, Cinca, D, Cindro, V, Cioara, IA, Ciocio, A, Cirotto, F, Citron, ZH, Citterio, M, Clark, A, Clark, MR, Clark, PJ, Clement, C, Coadou, Y, Cobal, M, Cochran, J, Coimbra, AEC, Colasurdo, L, Cole, B, Colijn, AP, Collot, J, Muino, P Conde, Coniavitis, E, Connell, SH, Connelly, IA, Constantinescu, S, Conventi, F, Cooper-Sarkar, AM, Cormier, F, Cormier, KJR, Corradi, M, Corrigan, EE, Corriveau, F, Cartes-Gonzalez, A, Costa, MJ, Costanzo, D, Cottin, G, Cowan, G, Cox, BE, Crane, J, Cranmer, K, Crawley, SJ, Creager, RA, Cree, G, Crepe-Renaudin, S, Crescioli, F, Cristinziani, M, Croft, V, Crosetti, G, Cueto, A, Donszelmann, T Cuhadar, Cukierman, AR, Cuth, J, Czekierda, S, Czodrowski, P, De Sousa, MJ Da Cunha Sargedas, Da Via, C, Dabrowski, W, Dado, T, Dahbi, S, Dai, T, Dallaire, F, Dallapiccola, C, Dam, M, D'amen, G, Damp, J, Dandoy, JR, Daneri, MF, Dang, NP, Dann, ND, Danninger, M, Dao, V, Darbo, G, Darmora, S, Dartsi, O, Dattagupta, A, Daubney, T, D'Auria, S, Davey, W, David, C, Davidek, T, Davis, DR, Dawe, E, Dawson, I, De, K, De Asmundis, R, De Benedetti, A, De Beurs, M, De Castro, S, De Cecco, S, De Groot, N, de Jong, P, De la Torre, H, De Lorenzi, F, De Maria, A, De Pedis, D, De Salvo, A, De Sanctis, U, De Santo, A, Corga, K De Vasconcelos, De Regie, JB De Vivie, Debenedetti, C, Dedovich, DV, Dehghanian, N, Del Gaudio, M, Del Peso, J, Diaz, Y Delabat, Delgove, D, Deliot, F, Delitzsch, CM, Della Pietra, M, Della Volpe, D, Dell'Acqua, A, Dell'Asta, L, Delmastro, M, Delporte, C, Delsart, PA, DeMarco, DA, Demers, S, Demichev, M, Denisov, SP, Denysiuk, D, D'Eramo, L, Derendarz, D, Derkaoui, JE, Derue, F, Dervan, P, Desch, K, Deterre, C, Dette, K, Devesa, MR, Deviveiros, PO, Dewhurst, A, Dhaliwal, S, Di Bello, FA, Di Ciaccio, A, Di Ciaccio, L, Di Clemente, WK, Di Donato, C, Di Girolamo, A, Di Micco, B, Di Nardo, R, Di Petrillo, KF, Di Simone, A, Di Sipio, R, Di Valentino, D, Diaconu, C, Diamond, M, Dias, FA, Do Vale, T Dias, Diaz, MA, Dickinson, J, Diehl, EB, Dietrich, J, Cornell, S Diez, Dimitrievska, A, Dingfelder, J, Dittus, F, Djama, F, Djobava, T, Djuvsland, JI, Do Vale, MAB, Dobre, M, Dodsworth, D, Doglioni, C, Dolejsi, J, Dolezal, Z, Donadelli, M, Donini, J, D'onofrio, A, D'Onofrio, M, Dopke, J, Doria, A, Dova, MT, Doyle, AT, Drechsler, E, Dreyer, E, Dreyer, T, Du, Y, Duarte-Campderros, J, Dubinin, F, Dubovsky, M, Dubreuil, A, Duchovni, E, Duckeck, G, Ducourthial, A, Ducu, OA, Duda, D, Dudarev, A, Dudder, AC, Duffield, EM, Dutlot, L, Duhrssen, M, Dulsen, C, Dumancic, M, Dumitriu, AE, Duncan, AK, Dunford, M, Duperrin, A, Yildiz, H Duran, Duren, M, Durglishvili, A, Duschinger, D, Dutta, B, Duvnjak, D, Dyndal, M, Dysch, S, Dziedzic, BS, Eckardt, C, Ecker, KM, Edgar, RC, Eifert, T, Eigen, G, Einsweiler, K, Ekelof, T, El Kacimi, M, El Kosseifi, R, Ellajosyula, V, Ellert, M, Ellinghaus, F, Elliot, AA, Ellis, N, Elmsheuser, J, Elsing, M, Emeliyanov, D, Enari, Y, Ennis, JS, Epland, MB, Erdmann, J, Ereditato, A, Errede, S, Escalier, M, Escobar, C, Pastor, O Estrada, Etienvre, AI, Etzion, E, Evans, H, Ezhilov, A, Ezzi, M, Fabbri, F, Fabbri, L, Fabiani, V, Facini, G, Faisca Rodrigues Pereira, RM, Fakhrutdinov, RM, Falciano, S, Falke, PJ, Falke, S, Faltova, J, Fang, Y, Fanti, M, Farbin, A, Farilla, A, Farina, EM, Farooque, T, Farrell, S, Farrington, SM, Farthouat, P, Fassi, F, Fassnacht, P, Fassouliotis, D, Giannelli, M Faucci, Favareto, A, Fawcett, WJ, Fayard, L, Fedin, OL, Fedorko, W, Feickert, M, Feigl, S, Feligioni, L, Feng, C, Feng, EJ, Feng, M, Fenton, MJ, Fenyuk, AB, Feremenga, L, Ferrando, J, Ferrari, A, Ferrari, P, Ferrari, R, de Lima, DE Ferreira, Ferrer, A, Ferrere, D, Ferretti, C, Fiedler, F, Filipcic, A, Filthaut, F, Finelli, KD, Fiolhais, MCN, Fiorini, L, Fischer, C, Fisher, WC, Flaschel, N, Fleck, I, Fleischmann, P, Fletcher, RRM, Flick, T, Flierl, BM, Flores, LM, Castillo, LR Flores, Fomin, N, Forcolin, GT, Formica, A, Forster, FA, Forti, AC, Foster, AG, Fournier, D, Fox, H, Fracchia, S, Francavilla, P, Franchini, M, Franchino, S, Francis, D, Franconi, L, Franklin, M, Frate, M, Fraternali, M, Freeborn, D, Fressard-Batraneanu, SM, Freund, B, Freund, WS, Froidevaux, D, Frost, JA, Fukunaga, C, Torregrosa, E Fullana, Fusayasu, T, Fuster, J, Gabizon, O, Gabrielli, A, Gach, GP, Gadatsch, S, Gadow, P, Gagliardi, G, Gagnon, LG, Galea, C, Galhardo, B, Gallas, EJ, Gallop, BJ, Gallus, P, Galster, G, Goni, R Gamboa, Gan, KK, Ganguly, S, Gao, Y, Gao, YS, Garcia, C, Navarro, JE Garcia, Pascual, JA Garcia, Garcia-Sciveres, M, Gardner, RW, Garelli, N, Garonne, V, Gasnikova, K, Gaudiello, A, Gaudio, G, Gavrilenko, IL, Gavrilyuk, A, Gay, C, Gaycken, G, Gazis, EN, Gee, CNP, Geisen, J, Geisen, M, Geisler, MP, Gellerstedt, K, Gemme, C, Genest, MH, Geng, C, Gentile, S, Gentsos, C, George, S, Gerbaudo, D, Gessner, G, Ghasemi, S, Bostanabad, M Ghasemi, Ghneimat, M, Giacobbe, B, Giagu, S, Giangiacomi, N, Giannetti, P, Giannini, A, Gibson, SM, Gignac, M, Gillberg, D, Gilles, G, Gingrich, DM, Giordani, MP, Giorgi, FM, Giraud, PF, Giromini, P, Giugliarelli, G, Giugni, D, Giuli, F, Giulini, M, Gkaitatzis, S, Gkialas, I, Gkougkousis, EL, Gkountoumis, P, Gladilin, LK, Glasman, C, Glatzer, J, Glaysher, PCF, Glazov, A, Goblirsch-Kolb, M, Godlewski, J, Goldfarb, S, Colling, T, Golubkov, D, Gomes, A, Gama, R Gonsalves, Goncalo, R, Gonella, G, Gonella, L, Gongadze, A, Gonnella, F, Gonski, JL, de la Hoz, S Gonzalez, Gonzalez-Sevilla, S, Goossens, L, Gorbounov, PA, Gordon, HA, Gorini, B, Gorini, E, Gorisek, A, Goshaw, AT, Gossling, C, Gostkin, MI, Gottardo, CA, Goudet, CR, Goujdami, D, Goussiou, AG, Govender, N, Goy, C, Gozani, E, Grabowska-Bold, I, Gradin, POJ, Graham, EC, Gramling, J, Gramstad, E, Grancagnolo, S, Gratchev, V, Gravila, PM, Gravili, FG, Gray, C, Gray, HM, Greenwood, ZD, Grefe, C, Gregersen, K, Gregor, IM, Grenier, P, Grevtsov, K, Griffiths, J, Grillo, AA, Grimm, K, Grinstein, S, Gris, Ph, Grivaz, J-F, Groh, S, Gross, E, Grosse-Knetter, J, Grossi, GC, Grout, ZJ, Crud, C, Grummer, A, Guan, L, Guan, W, Guenther, J, Guerguichon, A, Guescini, F, Guest, D, Gugel, R, Gui, B, Guillemin, T, Guindon, S, Gul, U, Gumpert, C, Guo, L, Guo, W, Guo, Y, Guo, Z, Gupta, R, Gurbuz, S, Gustavino, G, Gutelman, BJ, Gutierrez, P, Gutschow, C, Guyot, C, Guzik, MP, Gwenlan, C, Gwilliam, CB, Haas, A, Haber, C, Hadavand, HK, Haddad, N, Hadef, A, Hagebock, S, Hagihara, M, Hakobyan, H, Haleem, M, Haley, J, Halladjian, G, Hallewell, GD, Hamacher, K, Hamal, P, Hamano, K, Hamilton, A, Hamity, GN, Han, K, Han, L, Han, S, Hanagaki, K, Hance, M, Handl, DM, Haney, B, Hankache, R, Hanke, P, Hansen, E, Hansen, JB, Hansen, JD, Hansen, MC, Hansen, PH, Hara, K, Hard, AS, Harenberg, T, Harkusha, S, Harrison, PF, Hartmann, NM, Hasegawa, Y, Hasib, A, Hassani, S, Haug, S, Hauser, R, Hauswald, L, Havener, LB, Havranek, M, Hawkes, CM, Hawkings, RJ, Hayden, D, Hayes, C, Hays, CP, Hays, JM, Hayward, HS, Haywood, SJ, Heath, MP, Hedberg, V, Heelan, L, Heer, S, Heidegger, KK, Heilman, J, Heim, S, Heim, T, Heinemann, B, Heinrich, JJ, Fleinrich, L, Heinz, C, Hejbal, J, Helary, L, Held, A, Hellesund, S, Hellman, S, Helsens, C, Henderson, RCW, Heng, Y, Henkelmann, S, Correia, AM Henriques, Herbert, GH, Herde, H, Herget, V, Jimenez, Y Hernandez, Herr, H, Hellmann, MG, Herten, G, Hertenberger, R, Hervas, L, Herwig, TC, Hesketh, GG, Hessey, NP, Hetherly, JW, Higashino, S, Higon-Rodriguez, E, Hildebrand, K, Hill, E, Hill, JC, Hill, KK, Hiller, KH, Hillier, SJ, Hils, M, Hinchliffe, I, Hirose, M, Hirschbuehl, D, Hiti, B, Hladik, O, HIaluku, DR, Hoad, X, Hobbs, J, Hod, N, Hodgkinson, MC, Hoecker, A, Hoeferkamp, MR, Hoenig, F, Hohn, D, Hohov, D, Holmes, TR, Holzbock, M, Homann, M, Honda, S, Honda, T, Hong, TM, Honle, A, Hooberman, BH, Hopkins, WH, Horii, Y, Horn, P, Horton, AJ, Horyn, LA, Hostachy, J-Y, Hostiuc, A, Hou, S, Hoummada, A, Howarth, J, Hoya, J, Hrabovsky, M, Hrdinka, J, Hristova, I, Hrivnac, J, Hrynevich, A, Hryn'ova, T, Hsu, PJ, Hsu, S-C, Hu, Q, Hu, S, Huang, Y, Hubacek, Z, Hubaut, F, Huebner, M, Huegging, F, Huffman, TB, Hughes, EW, Huhtinen, M, Hunter, RFH, Huo, P, Hupe, AM, Huseynov, N, Huston, J, Huth, J, Hyneman, R, Iacobucci, G, Iakovidis, G, Ibragimov, I, Iconomidou-Fayard, L, Idrissi, Z, Iengo, P, Ignazzi, R, Igonkina, O, Iguchi, R, Iizawa, T, Ikegami, Y, Ikeno, M, Iliadis, D, Ilic, N, Iltzsche, F, Introzzi, G, Lodice, M, Iordanidou, K, Ippolito, V, Isacson, MF, Ishijima, N, Ishino, M, Ishitsuka, M, Islam, W, Issever, C, Istin, S, Ito, F, Ponce, JM Iturbe, Iuppa, R, Ivina, A, Iwasaki, H, Izen, JM, Izzo, V, Jabbar, S, Jacka, P, Jackson, P, Jacobs, RM, Jain, V, Jakel, G, Jakobi, KB, Jakobs, K, Jakobsen, S, Jakoubek, T, Jamin, DO, 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Soloshenko, A, Solovyanov, OV, Solovyev, V, Sommer, P, Son, H, Song, W, Sopczak, A, Sopkova, F, Sosa, D, Sotiropoulou, CL, Sottocornola, S, Soualah, R, Soukharev, AM, South, D, Sowden, BC, Spagnolo, S, Spalla, M, Spangenberg, M, Spano, F, Sperlich, D, Spettel, F, Spieker, TM, Spighi, R, Spigo, G, Spiller, LA, Spiteri, DP, Spousta, M, Stabile, A, Stamen, R, Stamm, S, Stanecka, E, Stanek, RW, Stanescu, C, Stanislaus, B, Stanitzki, MM, Stapf, B, Stapnes, S, Starchenko, EA, Stark, GH, Stark, J, Stark, SH, Staroba, P, Starovoitov, P, Starz, S, Staszewski, R, Stegler, M, Steinberg, P, Stelzer, B, Stelzer, HJ, Stelzer-Chilton, O, Stenzel, H, Stevenson, TJ, Stewart, GA, Stockton, MC, Stoicea, G, Stolte, P, Stonjek, S, Straessner, A, Strandberg, J, Strandberg, S, Strauss, M, Strizenec, P, Strohmer, R, Strom, DM, Stroynowski, R, Strubig, A, Stucci, SA, Stugu, B, Stupak, J, Styles, NA, Su, D, Su, J, Suchek, S, Sugaya, Y, Suk, M, Sulin, VV, Sultan, DMS, Sultansoy, S, Sumida, T, Sun, S, Sun, X, Suruliz, K, Suster, CJE, Sutton, MR, Suzuki, S, Svatos, M, Swiatlowski, M, Swift, SP, Sydorenko, A, Sykora, I, Sykora, T, Ta, D, Tackmann, K, Taenzer, J, Taffard, A, Tafirout, R, Tahirovic, E, Taiblum, N, Takai, H, Takashima, R, Takasugi, EH, Takeda, K, Takeshita, T, Takubo, Y, Talby, M, Talyshey, AA, Tanaka, J, Tanaka, M, Tanaka, R, Tanioka, R, Tannenwald, BB, Araya, S Tapia, Tapprogge, S, Mohamed, A Tarek Abouelfadl, Tarem, S, Tama, G, Tartarelli, GF, Tas, P, Tasevsky, M, Tashiro, T, Tassi, E, Delgado, A Tavares, Tayalati, Y, Taylor, AC, Taylor, AJ, Taylor, GN, Taylor, PTE, Taylor, W, Tee, AS, Teixeira-Dias, P, Ten Kate, H, Teng, PK, Teoh, JJ, Tepel, F, Terada, S, Terashi, K, Tenon, J, Terzo, S, Testa, M, Teuscher, RJ, Thais, SJ, Theveneaux-Pelzer, T, Thiele, F, Thomas, JP, Thompson, AS, Thompson, PD, Thomsen, LA, Thomson, E, Tian, Y, Torres, RE Ticse, Tikhomirov, VO, Tikhonov, Yu A, Timoshenko, S, Tipton, P, Tisserant, S, Todome, K, Todorova-Nova, S, Todt, S, Tojo, J, Tokar, S, Tokushuku, K, Tolley, E, Tomiwa, KG, Tomoto, M, Tompkins, L, Toms, K, Tong, B, Tomambe, P, Torrence, E, Torres, H, Pastor, E Torro, Tosciri, C, Toth, J, Touchard, F, Tovey, DR, Treado, CJ, Trefzger, T, Tresoldi, F, Tricoli, A, Trigger, IM, Trincaz-Duvoid, S, Tripiana, MF, Trischuk, W, Trocme, B, Trofymov, A, Troncon, C, Trovatelli, M, Trovato, F, Truong, L, Trzebinski, M, Trzupek, A, Tsai, F, Tseng, JC-L, Tsiareshka, PV, Tsirintanis, N, Tsiskaridze, V, Tskhadadze, EG, Tsukerman, II, Tsulaia, V, Tsuno, S, Tsybychev, D, Tu, Y, Tudorache, A, Tudorache, V, Tulbure, TT, Tuna, AN, Turchikhin, S, Turgeman, D, Cakir, I Turk, Turra, R, Tuts, PM, Tzovara, E, Ucchielli, G, Ueda, I, Ughetto, M, Ukegawa, F, Unal, G, Undrus, A, Unel, G, Ungaro, FC, Unno, Y, Uno, K, Urban, J, Urquijo, P, Urrejola, P, Usai, G, Usui, J, Vacavant, L, Vacek, V, Vachon, B, Vadla, KOH, Vaidya, A, Valderanis, C, Santurio, E Valdes, Valente, M, Valentinetti, S, Valero, A, Valery, L, Vallance, RA, Vallier, A, Ferrer, JA Valls, Van Daalen, TR, Van Den Wollenberg, W, Van der Graaf, H, Van Gemmeren, P, Van Nieuwkoop, J, Van Vulpen, I, Vanadia, M, Vandelli, W, Vaniachine, A, Vankov, P, Vari, R, Varnes, EW, Varni, C, Varo, T, Varouchas, D, Varvell, KE, Vasquez, GA, Vasquez, JG, Vazeille, F, Furelos, D Vazquez, Schroeder, T Vazquez, Veatch, J, Vecchio, V, Veloce, LM, Veloso, F, Veneziano, S, Ventura, A, Venturi, M, Venturi, N, Vercesi, V, Verducci, M, Infante, CM Vergel, Verkerke, W, Vermeulen, AT, Vermeulen, JC, Vetterli, MC, Maira, N Viaux, Pinto, M Vicente Barreto, Vichou, I, Vickey, T, Boeriu, OE Vickey, Viehhauser, GHA, Viel, S, Vigani, L, Villa, M, Perez, M Villaplana, Vilucchi, E, Vincter, MG, Vinogradov, VB, Vishwakarma, A, Vittori, C, Vivarelli, I, Vlachos, S, Vogel, M, Vokac, P, Vopi, G, von Buddenbrock, SE, Von Toerne, E, Vorobel, V, Vorobev, K, Vos, M, Vossebeld, JH, Vranjes, N, Milosavljevic, M Vranjes, Vrba, V, Vreeswijk, M, Sfiligoj, T, Vuillermet, R, Vukotic, I, Zenis, T, Zivkovic, L, Wagner, P, Wagner, W, Wagner-Kuhr, J, Wahlberg, H, Wahrmund, S, Wakamiya, K, Walbrecht, VM, Walder, J, Walker, R, Walker, SD, Walkowiak, W, Wallangen, V, Wang, AM, Wang, C, Wang, F, Wang, H, Wang, J, Wang, P, Wang, Q, Wang, R-J, Wang, R, Wang, SM, Wang, WT, Wang, W, Wang, WX, Wang, Y, Wang, Z, Wanotayaroj, C, Warburton, A, Ward, CP, Wardrope, DR, Washbrook, A, Watkins, PM, Watson, AT, Watson, MF, Watts, G, Watts, S, Waugh, BM, Webb, AF, Webb, S, Weber, C, Weber, MS, Weber, SA, Weber, SM, Webster, JS, Weidberg, AR, Weinert, B, Weingarten, J, Weirich, M, Weiser, C, Wells, PS, Wenaus, T, Wengler, T, Wenig, S, Wermes, N, Werner, MD, Werner, P, Wessels, M, Weston, TD, Whalen, K, Whallon, NL, Wharton, AM, White, AS, White, A, White, MJ, White, R, Whiteson, D, Whitmore, SW, Wickens, FJ, Wiedenmann, W, Wielers, M, Wiglesworth, C, Wiik-Fuchs, LAM, Wildauer, A, Wilk, F, Wilkens, HG, Wilkins, LJ, Williams, HH, Williams, S, Willis, C, Willocq, S, Wilson, JA, Wingerter-Seez, I, Winkels, E, Winklmeier, F, Winston, OJ, Winter, BT, Wihtgen, M, Wobisch, M, Wolf, A, Wolf, TMH, Wolff, R, Wolter, MW, Wolters, H, Wong, VWS, Woods, NL, Worm, SD, Wosiek, BK, Wozniak, KW, Wraight, K, Wu, M, Wu, SL, Wu, X, Wu, Y, Wyatt, TR, Wynne, BM, Xella, S, Xi, Z, Xia, L, Xu, D, Xu, H, Xu, L, Xu, T, Xu, W, Yabsley, B, Yacoob, S, Yajima, K, Yallup, DP, Yamaguchi, D, Yamaguchi, Y, Yamamoto, A, Yamanaka, T, Yamane, F, Yamatani, M, Yamazaki, T, Yamazaki, Y, Yan, Z, Yang, HJ, Yang, HT, Yang, S, Yang, Y, Yang, Z, Yao, W-M, Yap, YC, Yasu, Y, Yatsenko, E, Ye, J, Ye, S, Yeletskikh, I, Yigitbasi, E, Yildirim, E, Yorita, K, Yoshihara, K, Young, CJS, Young, C, Yu, J, Yue, X, Yuen, SPY, Zabinski, B, Zacharis, G, Zaffaroni, E, Zaidan, R, Zaitsev, AM, Zakharchuk, N, Zalieckas, J, Zambito, S, Zanzi, D, Zaripovas, DR, Zeissner, SV, Zeitnitz, C, Zemaityte, G, Zeng, JC, Zeng, Q, Zenin, O, Zerwas, D, Zgubic, M, Zhang, DF, Zhang, D, Zhang, F, Zhang, G, Zhang, H, Zhang, J, Zhang, L, Zhang, M, Zhang, P, Zhang, R, Zhang, X, Zhang, Y, Zhang, Z, Zhao, P, Zhao, X, Zhao, Y, Zhao, Z, Zhemchugov, A, Zhou, B, Zhou, C, Zhou, L, Zhou, MS, Zhou, M, Zhou, N, Zhou, Y, Zhu, CG, Zhu, HL, Zhu, H, Zhu, J, Zhu, Y, Zhuang, X, Zhukov, K, Zhulanov, V, Zibell, A, Zieminska, D, Zimine, NI, Zimmermann, S, Zinonos, Z, Zinser, M, Ziolkowski, M, Zobernig, G, Zoccoli, A, Zoch, K, Zorbas, TG, Zou, R, Nedden, M Zur, Zwalinski, L, and Collaboration, ATLAS

Published
2018

13. N-O-Isopropyl Sulfonamido-Based Hydroxamates as Matrix Metalloproteinase Inhibitors: Hit Selection and in Vivo Antiangiogenic Activity

Author

Nuti, E, Cantelmo, A, Gallo, C, Bruno, A, Bassani, B, Camodeca, C, Tuccinardi, T, Vera, L, Orlandini, E, Nencetti, S, Stura, E, Martinelli, A, Dive, V, Albini, A, Rossello, A, Nuti E, Cantelmo AR, Gallo C, Bruno A, Bassani B, Camodeca C, Tuccinardi T, Vera L, Orlandini E, Nencetti S, Stura EA, Martinelli A, Dive V, Albini A, Rossello A, Nuti, E, Cantelmo, A, Gallo, C, Bruno, A, Bassani, B, Camodeca, C, Tuccinardi, T, Vera, L, Orlandini, E, Nencetti, S, Stura, E, Martinelli, A, Dive, V, Albini, A, Rossello, A, Nuti E, Cantelmo AR, Gallo C, Bruno A, Bassani B, Camodeca C, Tuccinardi T, Vera L, Orlandini E, Nencetti S, Stura EA, Martinelli A, Dive V, Albini A, and Rossello A

Abstract

Matrix metalloproteinases (MMPs) have been shown to be involved in tumor-induced angiogenesis. In particular, MMP-2, MMP-9, and MMP-14 have been reported to be crucial for tumor angiogenesis and the formation of metastasis, thus becoming attractive targets in cancer therapy. Here, we report our optimization effort to identify novel N-isopropoxy-arylsulfonamide hydroxamates with improved inhibitory activity toward MMP-2, MMP-9, and MMP-14 with respect to the previously discovered compound 1. A new series of hydroxamates was designed, synthesized, and tested for their antiangiogenic activity using in vitro assays with human umbilical vein endothelial cells (HUVECs). A nanomolar MMP-2, MMP-9, and MMP-14 inhibitor was identified, compound 3, able to potently inhibit angiogenesis in vitro and also in vivo in the matrigel sponge assay in mice. Finally, X-ray crystallographic and docking studies were conducted for compound 3 in order to investigate its binding mode to MMP-9 and MMP-14.

Published
2015

14. HTA & MCDA In The Treatment of Macular Edema

Author

Ferrario, L, primary, Foglia, E, additional, Bandello, F, additional, Ferri, C, additional, Figini, I, additional, Franzin, M, additional, Gambaro, G, additional, Introini, U, additional, Staurenghi, G, additional, Tadini, P, additional, Zuppini, T, additional, Tessari, R, additional, Scarpa, G, additional, Urban, F, additional, Beltramini, S, additional, Tobaldi, RF, additional, Nicolò, M, additional, Ancona, C, additional, Moriconi, S, additional, Nuti, E, additional, Fusco, F, additional, and Croce, D, additional

Published
2017
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15. Synthesis and biological evaluation in U87MG glioma cells of (ethynylthiophene)sulfonamido-based hydroxamates as matrix metalloproteinase inhibitors

Author

Nuti E., Casalini F., Santamaria S., Gabelloni P., Bendinelli S., Da Pozzo E., Costa B., MARINELLI, LUCIANA, LA PIETRA, VALERIA, NOVELLINO, ETTORE, Margarida Bernardo M., Fridman R., Da Settimo F., Martini C., Rossello A., Nuti, E., Casalini, F., Santamaria, S., Gabelloni, P., Bendinelli, S., Da Pozzo, E., Costa, B., Marinelli, Luciana, LA PIETRA, Valeria, Novellino, Ettore, Margarida Bernardo, M., Fridman, R., Da Settimo, F., Martini, C., and Rossello, A.

Published
2011

17. In vivo imaging of matrix metalloproteinase 12 and matrix metalloproteinase 13 activities in the mouse model of collagen-induced arthritis

Author

Lim, N, Meinjohanns, E, Bou-Gharios, G, Gompels, L, Nuti, E, Rossello, A, Devel, L, Dive, V, Meldal, M, and Nagase, H

Abstract

OBJECTIVE: To develop enzyme-activatable Förster resonance energy transfer (FRET) substrate probes to detect matrix metalloproteinase 12 (MMP-12) and MMP-13 activities in vivo in mouse models of inflammatory arthritis. METHODS: Peptidic FRET probes activated by MMP-12 and MMP-13 were reverse designed from inhibitors selected from a phosphinic peptide inhibitor library. Selectivity of the probes was demonstrated in vitro using MMP-1, MMP-2, MMP-3, MMP-12, and MMP-13. In vivo activation of the probes was tested in the zymosan-induced mouse model of inflammation, and probe specificity was evaluated by the MMP inhibitor GM6001 and specific synthetic inhibitors of MMP-12 and MMP-13. The probes were used to monitor these enzyme activities in the collagen-induced arthritis (CIA) model in vivo. RESULTS: The MMP-12 and MMP-13 activity probes (MMP12ap and MMP13ap, respectively) discriminated between the activities of the 2 enzymes. The in vivo activation of these probes was inhibited by GM6001 and by their respective specific inhibitors. In the CIA model, MMP12ap activation peaked 5 days after disease onset and showed strong correlation with disease severity during this time (r = 0.85, P < 0.0001). MMP13ap activation increased gradually after disease onset and correlated with disease severity over a longer period of 15 days (r = 0.58, P < 0.0001). CONCLUSION: We generated two selective FRET probes that can be used to monitor MMP-12 and MMP-13 activities in live animals. MMP12ap follows the initial stage of inflammation in CIA, while MMP13ap follows the progression of the disease. The specificity of these probes is useful in monitoring the efficacy of MMP inhibitors.

Published
2014

18. In vivo imaging of matrix metalloprotease 12 and matrix metalloprotease 13 activities in the mouse model of collagen-induced arthritis

Author

Lim, N, Meinjohanns, E, Bou-Gharios, G, Gompels, L, Nuti, E, Rossello, A, Devel, L, Dive, V, Meldal, M, and Nagase, H

Abstract

Objective. To develop enzyme activatable Förster resonance energy transfer (FRET) substrate probes to detect MMP-12 and MMP-13 activities in vivo in mouse models of inflammatory arthritis Methods. Peptidic FRET probes activated by MMP-12 and MMP-13 were reverse designed from inhibitors selected from a peptide phosphinic inhibitor library. Selectivity of the probes was demonstrated in vitro using MMP-1, MMP-2, MMP-3, MMP-12, and MMP-13. In vivo activation of the probe was tested in the zymosan-induced mouse model of inflammation and probe specificity was evaluated by the metalloprotease inhibitor GM6001 and specific synthetic inhibitors of MMP-12 and MMP-13. The probes were used to follow these enzyme activities in the collagen-induced arthritis (CIA) model in vivo. Results. The MMP-12- and MMP-13-activity probes (MMP12ap and MMP13ap, respectively) discriminated between the two enzymatic activities. The in vivo activation of these probes was inhibited by GM6001 and by their respective specific inhibitors. In the CIA model, MMP12ap activation peaked 5 days after disease onset and showed strong correlation with disease severity during this time (r = 0.85; p

Published
2013

24. PSS54 - HTA & MCDA In The Treatment of Macular Edema

Author

Ferrario, L, Foglia, E, Bandello, F, Ferri, C, Figini, I, Franzin, M, Gambaro, G, Introini, U, Staurenghi, G, Tadini, P, Zuppini, T, Tessari, R, Scarpa, G, Urban, F, Beltramini, S, Tobaldi, RF, Nicolò, M, Ancona, C, Moriconi, S, Nuti, E, Fusco, F, and Croce, D

Published
2017
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28. Crisi economica e valorizzazione delle risorse: una lettura del nomos arghias

Author

Angiolillo, R., Clerico, L., Elia, E., Nuti, E., Loddo, Rita Laura, Angiolillo, R., Clerico, L., Elia, E., Nuti, E., and Loddo, Rita Laura

Abstract

At the beginning of VI century B.C. Athens was affected by a political, social and economic crisis, caused by a partisan management of the power and by radicalization of social struggles. As a concrete answer to the crisis, Athenians entrusted Solon – a wise man – with the difficult task of giving new life to the polis and putting an end to the endemic crisis which held it. In order to solve the crisis, Solon used the laws he had written, laws that he claimed were equal both for the noble and the poorest man. Between the laws that literary tradition credited him with, I will analyse the nomos arghias, idleness law. Two aspects will be considered: first of all law’s authorship and secondly the meaning of this law. If on one hand we have to deal with a complex and stratified tradition which points to Drakon, Solon and Peisistratus as potential authors of the law, I will propose that Solon is the one that introduced it. This is possible by analysing “the spirit of the law”, in my opinion Solonic, and studying the procedures that ancient sources attest. I will also review the meaning of the nomos arghias, by clarifying above all Athenian attitude about work and inactivity. I will refer this law to economic politics of Solon which aimed to boast economic activities, value the commerce and craftsmanship, redefining the concept of citizenship, unbound from this moment on from nobility of birth and extended beyond polis borders. This law seems to bring the new citizenship concept that Solon introduced, a citizenship which valued the individual contribution to the common good. Facing this crisis, VI century Athens didn’t withdraw into itself, but reacted by giving value to the human resources that were available within and without the ethnic group.

Published
2014

41. Identification of novel molecular scaffolds for the design of MMP-13 inhibitors: A first round of lead optimization

Author

Valeria La Pietra, Sabrina Taliani, Hideaki Nagase, Elisa Nuti, Robert Visse, Federico Da Settimo, Francesco Saverio Di Leva, Ettore Novellino, Luciana Marinelli, Concettina La Motta, Salvatore Santamaria, Sandro Cosconati, Matteo Morelli, Armando Rossello, F Casalini, Isabella Pugliesi, La Pietra, V, Marinelli, L, Cosconati, Sandro, Di Leva, F, Nuti, E, Santamaria, S, Pugliesi, I, Morelli, M, Casalini, F, Rossello, A, La Motta, C, Taliani, S, Visse, R, Nagase, H, da Settimo, F, Novellino, E., LA PIETRA, Valeria, Marinelli, Luciana, Cosconati, S., Di Leva, Francesco Saverio, Nuti, E., Santamaria, S., Pugliesi, I., Morelli, M., Casalini, F., Rossello, A., La Motta, C., Taliani, S., Visse, R., Nagase, H., da Settimo, F., and Novellino, Ettore

Subjects
Virtual screening, High selectivity, Drug Evaluation, Preclinical, Nanotechnology, Articular cartilage, Osteoarthritis, Matrix Metalloproteinase Inhibitors, Matrix metalloproteinase, Crystallography, X-Ray, Inhibitory Concentration 50, User-Computer Interface, Catalytic Domain, Matrix Metalloproteinase 13, Drug Discovery, medicine, Humans, Protease Inhibitors, IC50, Cancer, Pharmacology, MMP, Chemistry, Cartilage, Organic Chemistry, General Medicine, medicine.disease, medicine.anatomical_structure, Docking (molecular), Drug Design, Molecular docking, Cancer research, Osteoarthriti
Abstract

Osteoarthritis (OA) is the leading cause of joint pain and disability in middle-aged and elderly patients, and is characterized by progressive loss of articular cartilage. Among the various matrix metalloproteinases (MMPs), MMP-13 is specifically expressed in the cartilage of human OA patients and is not present in normal adult cartilage. Thus, MMP-13-selective inhibitors are promising candidates in osteoarthritis therapy. Recently, we designed an N-isopropoxy-arylsulfonamide-based hydroxamate inhibitor, which showed low nanomolar activity and high selectivity for MMP-13. In parallel to further studies aiming to assess the in vivo activity of our compound, we screened the Life Chemicals database through computational docking to seek for novel scaffolds as zinc-chelating non-hydroxamate inhibitors. Experimental evaluation of 20 selected candidate compounds verified five novel leads with IC 50 in the low μM range. These newly discovered inhibitors are structurally unrelated to the ones known so far and provide useful scaffolds to develop compounds with more desirable properties. Finally, a first round of structure-based optimization on lead 1 was accomplished and led to an increase in potency of more than 5 fold. © 2011 Elsevier Masson SAS. All rights reserved.

Published
2012
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42. Synthesis and antiangiogenic activity study of new hop chalcone Xanthohumol analogues

Author

Susanna Nencetti, Caterina Camodeca, Barbara Bassani, A.R. Cantelmo, Armando Rossello, Denisa Baci, Elisabetta Orlandini, Elisa Nuti, Douglas M. Noonan, Adriana Albini, Antonino Bruno, Cristina Gallo, Lea Rosalia, Nuti, E, Bassani, B, Camodeca, C, Rosalia, L, Cantelmo, A, Gallo, C, Baci, D, Bruno, A, Orlandini, E, Nencetti, S, Noonan, D, Albini, A, and Rossello, A

Subjects
0301 basic medicine, Chalcone, Xanthohumol analogues, Prenylated chalcones, Antiangiogenic activity, Chemopreventive agents, Stereochemistry, Angiogenesis, Prenylated chalcones, Neovascularization, Physiologic, Angiogenesis Inhibitors, Apoptosis, Antiangiogenic activity, Chemopreventive agents, Xanthohumol analogues, Pharmacology, Drug Discovery3003 Pharmaceutical Science, Organic Chemistry, Hop (networking), Structure-Activity Relationship, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Cell Movement, Drug Discovery, Cell Adhesion, Human Umbilical Vein Endothelial Cells, Humans, Structure–activity relationship, Cell adhesion, Cells, Cultured, Cell Proliferation, Flavonoids, Propiophenones, Dose-Response Relationship, Drug, Molecular Structure, Cell growth, General Medicine, 030104 developmental biology, chemistry, 030220 oncology & carcinogenesis, Xanthohumol
Abstract

Angiogenesis induction is a hallmark of cancer. Antiangiogenic properties of Xanthohumol (XN), a naturally occurring prenylated chalcone from hops, have been widely reported. Here we describe the synthesis and study the antiangiogenic activity in vitro of a series of XN derivatives, where different substituents on the B-ring of the chalcone scaffold were inserted. The new XN derivatives inhibited human umbilical-vein endothelial cell (HUVEC) proliferation, adhesion, migration, invasion and their ability to form capillary-like structures in vitro at 10 μM concentration. The preliminary results indicate that the phenolic OH group in R, present in natural XN, is not necessary for having antiangiogenic activity. In fact, the most effective compound from this series, 13 , was characterized by a para-methoxy group in R and a fluorine atom in R 2 on B-ring. This study paves the way for future development of synthetic analogues of XN to be used as cancer angiopreventive and chemopreventive agents.

Published
2017
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43. Discovery of 1,1′-Biphenyl-4-sulfonamides as a New Class of Potent and Selective Carbonic Anhydrase XIV Inhibitors

Author

Peiwen Pan, Giuseppe La Regina, Elisa Nuti, Ludovica Monti, Vincenzo Alterio, Antonio Coluccia, Sveva Pelliccia, Claudiu T. Supuran, Romano Silvestri, Seppo Parkkila, Simona Maria Monti, Valeria Famiglini, Giuseppina De Simone, Armando Rossello, Daniela Vullo, La Regina, G., Coluccia, A., Famiglini, V., Pelliccia, S., Monti, L., Vullo, D., Nuti, E., Alterio, V., De Simone, G., Monti, S. M., Pan, P., Parkkila, S., Supuran, C. T., Rossello, A., and Silvestri, R.

Subjects
Models, Molecular, Carbonic Anhydrase Inhibitor, Molecular model, drug design, Stereochemistry, Crystallography, X-Ray, Adduct, Carbonic Anhydrase, Structure-Activity Relationship, Carbonic anhydrase, Drug Discovery, medicine, Humans, Structure–activity relationship, Carbonic Anhydrase Inhibitors, cristallography, Carbonic Anhydrases, chemistry.chemical_classification, activators, Sulfonamides, biology, IX, targets, Biphenyl Compounds, Lyase, Biphenyl compound, Enzyme, chemistry, Biochemistry, Biphenyl Compound, biology.protein, Molecular Medicine, Acetazolamide, Human, medicine.drug
Abstract

New 1,1'-biphenylsulfonamides were synthesized and evaluated as inhibitors of the ubiquitous human carbonic anhydrase isoforms I, II, IX, XII, and XIV using acetazolamide (AAZ) as reference compound. The sulfonamides 1-21 inhibited all the isoforms, with Ki values in the nanomolar range of concentration, and were superior to AAZ against all of them. X-ray crystallography and molecular modeling studies on the adducts that compound 20, the most potent hCA XIV inhibitor of the series (Ki = 0.26 nM), formed with the five hCAs, provided insight into the molecular determinants responsible for the high affinity of this molecule toward the target enzymes. The results pave the way to the development of 1.1'-biphenylsulfonamides as a new class of highy potent hCA XIV inhibitors.

Published
2015
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44. N-O-Isopropyl sulfonamido-based hydroxamates: Kinetic characterisation of a series of MMP-12/MMP-13 dual target inhibitors

Author

Elisa Nuti, Salvatore Santamaria, Giovanni Cercignani, Valeria La Pietra, Armando Rossello, Ettore Novellino, Luciana Marinelli, Santamaria, S, Nuti, E, Cercignani, G, Marinelli, Luciana, LA PIETRA, Valeria, Novellino, Ettore, and Rossello, A.

Subjects
Models, Molecular, Stereochemistry, Protein Data Bank (RCSB PDB), Arthritis, Matrix Metalloproteinase Inhibitors, Matrix metalloproteinase, Hydroxamic Acids, Biochemistry, Structure-Activity Relationship, Matrix Metalloproteinase 12, Matrix Metalloproteinase 13, medicine, Humans, Pharmacology, chemistry.chemical_classification, Sulfonamides, biology, Chemistry, Active site, medicine.disease, Sulfonamide, Dissociation constant, Kinetics, biology.protein, Collagenase, Isopropyl, medicine.drug
Abstract

Matrix metalloproteinases (MMPs) are a family of zinc dependent endopeptidases known to play key roles in extracellular matrix (ECM) breakdown disorders, such as the two main forms of arthritis, rheumatoid arthritis (RA) and osteoarthritis (OA). MMP-13 (collagenase 3) is the leading MMP involved in cartilage degradation through its particular ability to cleave type-II collagen and as such plays a pivotal role in the pathogenesis of these diseases. Here we report the kinetic characterisation of N - O -isopropyl sulfonamido-based hydroxamates, potent inhibitors of MMP-13 and MMP-12, bearing different P1 and P1′ substituents. One of these compounds proved to be a potent (4 ≤ K i ≤ 5 nM) slow-binding inhibitor towards MMP-13 and MMP-12, with very favourable low association (10 4 M −1 s −1 ) and dissociation constants (10 −4 s −1 ). Moreover, this compound exhibited a good selectivity for MMP-13 and MMP-12 over MMP-1, MMP-3, MMP-7, MMP-8 and, even to a minor extent, MMP-2. A molecular-docking study carried out using the experimentally-derived X-ray crystal structure of MMP-12 (PDB ID: 3F17 ) revealed critical hydrogen bonding of the hydroxamate and the sulfonamide moieties with key active site residues. Since also MMP-12 is involved in RA, this MMP-13/MMP-12 dual target inhibitor could be a valid candidate for the treatment of this pathology.

Published
2012
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45. N-O-Isopropyl Sulfonamido-Based Hydroxamates as Matrix Metalloproteinase Inhibitors: Hit Selection and in Vivo Antiangiogenic Activity

Author

Adriana Albini, Antonino Bruno, Cristina Gallo, Barbara Bassani, Laura Vera, Enrico A. Stura, Vincent Dive, Armando Rossello, Tiziano Tuccinardi, Caterina Camodeca, Susanna Nencetti, Adriano Martinelli, Anna Rita Cantelmo, Elisabetta Orlandini, Elisa Nuti, Nuti, E, Cantelmo, A, Gallo, C, Bruno, A, Bassani, B, Camodeca, C, Tuccinardi, T, Vera, L, Orlandini, E, Nencetti, S, Stura, E, Martinelli, A, Dive, V, Albini, A, and Rossello, A

Subjects
Matrix metalloproteinase inhibitor, Angiogenesis, Cell Survival, Angiogenesis Inhibitors, Apoptosis, Matrix metalloproteinase, Matrix Metalloproteinase Inhibitors, Crystallography, X-Ray, Hydroxamic Acids, Mice, Structure-Activity Relationship, In vivo, Cell Movement, Drug Discovery, Human Umbilical Vein Endothelial Cells, Matrix Metalloproteinase 14, Structure–activity relationship, Animals, Humans, Matrigel, Sulfonamides, Chemistry, Angiogenesis Inhibitors/chemical synthesis/*chemistry/pharmacology Animals Apoptosis/drug effects Cell Movement/drug effects Cell Survival/drug effects Crystallography, X-Ray Human Umbilical Vein Endothelial Cells/cytology/drug effects/physiology Humans Hydroxamic Acids/chemical synthesis/*chemistry/pharmacology Matrix Metalloproteinase 14/chemistry/metabolism Matrix Metalloproteinase 2/chemistry/metabolism Matrix Metalloproteinase 9/chemistry/metabolism Matrix Metalloproteinase Inhibitors/chemical synthesis/*chemistry/pharmacology Mice Molecular Docking Simulation Stereoisomerism Structure-Activity Relationship Sulfonamides/chemical synthesis/*chemistry/pharmacology, Stereoisomerism, In vitro, Molecular Docking Simulation, Biochemistry, Matrix Metalloproteinase 9, Docking (molecular), Molecular Medicine, Matrix Metalloproteinase 2
Abstract

Matrix metalloproteinases (MMPs) have been shown to be involved in tumor-induced angiogenesis. In particular, MMP-2, MMP-9, and MMP-14 have been reported to be crucial for tumor angiogenesis and the formation of metastasis, thus becoming attractive targets in cancer therapy. Here, we report our optimization effort to identify novel N-isopropoxy-arylsulfonamide hydroxamates with improved inhibitory activity toward MMP-2, MMP-9, and MMP-14 with respect to the previously discovered compound 1. A new series of hydroxamates was designed, synthesized, and tested for their antiangiogenic activity using in vitro assays with human umbilical vein endothelial cells (HUVECs). A nanomolar MMP-2, MMP-9, and MMP-14 inhibitor was identified, compound 3, able to potently inhibit angiogenesis in vitro and also in vivo in the matrigel sponge assay in mice. Finally, X-ray crystallographic and docking studies were conducted for compound 3 in order to investigate its binding mode to MMP-9 and MMP-14.

Published
2015

46. Selective arylsulfonamide inhibitors of ADAM-17: hit optimization and activity in ovarian cancer cell models

Author

F Casalini, Ettore Novellino, Salvatore Santamaria, Silvano Ferrini, Marina Fabbi, Elisabetta Orlandini, Elisa Nuti, Susanna Nencetti, Armando Rossello, Luciana Marinelli, Caterina Camodeca, Valeria La Pietra, Grazia Carbotti, Nuti, E., Casalini, F., Santamaria, S., Fabbi, M., Carbotti, G., Ferrini, S., Marinelli, Luciana, LA PIETRA, Valeria, Novellino, Ettore, Camodeca, C., Orlandini, E., Nencetti, S., and Rossello, A.

Subjects
Models, Molecular, Cell Survival, Cell, ADAM17 Protein, Crystallography, X-Ray, Hydroxamic Acids, Cell Movement, Activated-Leukocyte Cell Adhesion Molecule, Cell Line, Tumor, Drug Discovery, medicine, Humans, Enzyme Inhibitors, ALCAM, Ovarian Neoplasms, Sulfonamides, Dose-Response Relationship, Drug, Molecular Structure, Chemistry, In vitro toxicology, Biological activity, medicine.disease, In vitro, Protein Structure, Tertiary, carbohydrates (lipids), ADAM Proteins, medicine.anatomical_structure, Models, Chemical, Cell culture, Immunology, Cancer research, Molecular Medicine, Female, Ovarian cancer, Protein Binding
Abstract

Activated leukocyte cell adhesion molecule (ALCAM) is expressed at the surface of epithelial ovarian cancer (EOC) cells and is released in a soluble form (sALCAM) by ADAM-17-mediated shedding. This process is relevant to EOC cell motility and invasiveness, which is reduced by inhibitors of ADAM-17. In addition, ADAM-17 plays a key role in EGFR signaling and thus may represent a useful target in anticancer therapy. Herein we report our hit optimization effort to identify potent and selective ADAM-17 inhibitors, starting with previously identified inhibitor 1. A new series of secondary sulfonamido-based hydroxamates was designed and synthesized. The biological activity of the newly synthesized compounds was tested in vitro on isolated enzymes and human EOC cell lines. The optimization process led to compound 21, which showed an IC50 of 1.9 nM on ADAM-17 with greatly increased selectivity. This compound maintained good inhibitory properties on sALCAM shedding in several in vitro assays.

Published
2013

47. Potent arylsulfonamide inhibitors of tumor necrosis factor-alpha converting enzyme able to reduce activated leukocyte cell adhesion molecule shedding in cancer cell models

Author

Salvatore Santamaria, Vittorio Limongelli, Susanna Nencetti, F Casalini, Ettore Novellino, Armando Rossello, Luciana Marinelli, Valeria La Pietra, Stanislava Ivanova Avramova, Elisabetta Orlandini, Elisa Nuti, Silvano Ferrini, Giovanni Cercignani, Marina Fabbi, Nuti, E., Casalini, F., Avramova, S. i., Santamaria, S., Fabbi, M., Ferrini, S., Marinelli, Luciana, LA PIETRA, Valeria, Limongelli, Vittorio, Novellino, Ettore, Cercignani, G., Orlandini, E., Nencetti, S., and Rossello, A.

Subjects
Models, Molecular, Blotting, Western, Motility, Enzyme-Linked Immunosorbent Assay, ADAM17 Protein, Hydroxamic Acids, Structure-Activity Relationship, Activated-Leukocyte Cell Adhesion Molecule, Cell Line, Tumor, Drug Discovery, Structure–activity relationship, Humans, Enzyme Inhibitors, ALCAM, Enzyme Assays, chemistry.chemical_classification, Ovarian Neoplasms, Sulfonamides, Dose-Response Relationship, Drug, Molecular Structure, Cell biology, carbohydrates (lipids), ADAM Proteins, Kinetics, Enzyme, chemistry, Models, Chemical, Cell culture, Cancer cell, Molecular Medicine, Female, Protein Binding
Abstract

Activated leukocyte cell adhesion molecule (ALCAM) plays a relevant role in tumor biology and progression. Our previous studies showed that ALCAM is expressed at the surface of epithelial ovarian cancer (EOC) cells and is released in a soluble form by ADAM-17-mediated shedding. This process is relevant to EOC cell motility and invasiveness, which is reduced by nonspecific inhibitors of ADAM-17. For this reason, ADAM-17 may represent a new useful target in anticancer therapy. Herein, we report the synthesis and biological evaluation of new ADAM-17 inhibitors containing an arylsulfonamidic scaffold. Among the new potential inhibitors, two very promising compounds 17 and 18 were discovered, with a nanomolar activity for ADAM-17 isolated enzyme. These compounds proved to be also the most potent in inhibiting soluble ALCAM release in cancer cells, showing a nanomolar activity on A2774 and SKOV3 cell lines.

Published
2010

48. N-O-Isopropyl Sulfonamido-Based Hydroxamates: Design, Synthesis and Biological Evaluation of Selective Matrix Metalloproteinase-13 Inhibitors as Potential Therapeutic Agents for Osteoarthritis

Author

Elisabetta Orlandini, Elisa Nuti, Stanislava Ivanova Avramova, Hideaki Nagase, Robert Visse, Salvatore Santamaria, Armando Rossello, Tiziano Tuccinardi, Ngee Han Lim, Luciana Marinelli, Valeria La Pietra, Adriano Martinelli, Ettore Novellino, F Casalini, Susanna Nencetti, Giovanni Cercignani, Nuti, E., Casalini, F., Avramora, S. I., Santamaria, S., Cercignani, G., Marinelli, Luciana, LA PIETRA, Valeria, Novellino, Ettore, Orlandini, E., Nencetti, S., Tuccinardi, T., Martinelli, A., Lim, N. H., Visse, R., Nagase, H., and Rossello, A.

Subjects
Models, Molecular, Matrix metalloproteinase, ADAM17 Protein, Matrix Metalloproteinase Inhibitors, Hydroxamic Acids, Chemical synthesis, chemistry.chemical_compound, Structure-Activity Relationship, Drug Discovery, Matrix Metalloproteinase 13, Osteoarthritis, Matrix Metalloproteinase 14, Protease Inhibitors, chemistry.chemical_classification, Hydroxamic acid, biology, Biological activity, In vitro, ADAM Proteins, Enzyme, Cartilage, Biochemistry, chemistry, Enzyme inhibitor, Docking (molecular), Drug Design, biology.protein, Molecular Medicine, Matrix Metalloproteinase 1
Abstract

Matrix metalloproteinase-13 (MMP-13) is a key enzyme implicated in the degradation of the extracellular matrix in osteoarthritis (OA). For this reason, MMP-13 synthetic inhibitors are being sought as potential therapeutic agents to prevent cartilage degradation and to halt the progression of OA. Herein, we report the synthesis and in vitro evaluation of a new series of selective MMP-13 inhibitors possessing an arylsulfonamidic scaffold. Among these potential inhibitors, a very promising compound was discovered exhibiting nanomolar activity for MMP-13 and was highly selective for this enzyme compared to MMP-1, -14, and TACE. This compound acted as a slow-binding inhibitor of MMP-13 and was demonstrated to be effective in an in vitro collagen assay and in a model of cartilage degradation. Furthermore, a docking study was conducted for this compound in order to investigate its binding interactions with MMP-13 and the reasons for its selectivity toward MMP-13 versus other MMPs.

Published
2009

49. A series of benzensulfonamide derivatives as new potent carbonic anhydrase IX and XII inhibitors.

Author

Nencetti S, Cuffaro D, Ciccone L, Nocentini A, Di Stefano M, Poli G, Macchia M, Tuccinardi T, Nuti E, Supuran CT, Rossello A, and Orlandini E

Subjects
Humans, Structure-Activity Relationship, Molecular Structure, Molecular Docking Simulation, Carbonic Anhydrase Inhibitors pharmacology, Carbonic Anhydrase Inhibitors chemistry, Carbonic Anhydrase Inhibitors chemical synthesis, Sulfonamides chemistry, Sulfonamides pharmacology, Sulfonamides chemical synthesis, Carbonic Anhydrase IX antagonists & inhibitors, Carbonic Anhydrase IX metabolism, Carbonic Anhydrases metabolism, Antigens, Neoplasm metabolism
Abstract

Aim: Human carbonic anhydrases (hCAs) are involved in many physiological processes including respiration, pH control, ion transport, bone resorption, and gastric fluid secretion. Recently, CA IX and CA XII have been studied for their role in cancer diseases, motivating the design of inhibitors of these isoforms., Material and Method: Here, we used the tail approach to design a new series of monoaryl ( 1a-i ) and bicyclic ( 1j-n ) benzensulfonamide derivatives CA IX and CA XII inhibitors. All synthesized compounds were investigated toward a panel of hCAs, and most of them exhibited potent CA inhibitory activity for CA II, CA IX and CA XII with K i values. In silico studies were performed to investigate the binding mode between inhibitors and CA., Results and Conclusion: The best compound was 1i that showed a low nanomolar range of K i value as CA inhibitor (K i  = 9.4, 5.6 and 6.3 nM hCA II, IX and XII, respectively).

Published
2025
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50. JG26 attenuates ADAM17 metalloproteinase-mediated ACE2 receptor processing and SARS-CoV-2 infection in vitro.

Author

Gentili V, Beltrami S, Cuffaro D, Cianci G, Maini G, Rizzo R, Macchia M, Rossello A, Bortolotti D, and Nuti E

Subjects
Humans, Cell Line, Imidazoles, Leucine analogs & derivatives, ADAM17 Protein metabolism, ADAM17 Protein antagonists & inhibitors, Angiotensin-Converting Enzyme 2 metabolism, SARS-CoV-2 drug effects, Antiviral Agents pharmacology, COVID-19 Drug Treatment, COVID-19 metabolism, COVID-19 virology
Abstract

Background: ADAM17 is a metalloprotease implicated in the proteolysis of angiotensin-converting enzyme 2 (ACE2), known to play a critical role in the entry and spread of SARS-CoV-2. In this context, ADAM17 results as a potential novel target for controlling SARS-CoV-2 infection., Methods: In this study, we investigated the impact on ACE2 surface expression and the antiviral efficacy against SARS-CoV-2 infection of the selective ADAM17 inhibitor JG26 and its dimeric (compound 1) and glycoconjugate (compound 2) derivatives using Calu-3 human lung cells., Results: None of the compounds exhibited cytotoxic effects on Calu-3 cells up to a concentration of 25 µM. Treatment with JG26 resulted in partial inhibition of both ACE2 receptor shedding and SARS-CoV-2 infection, followed by compound 1., Conclusion: JG26, an ADAM17 inhibitor, demonstrated promising antiviral activity against SARS-CoV-2 infection, likely attributed to reduced sACE2 availability, thus limiting viral dissemination., Competing Interests: Declarations. Competing interests: The authors declare no competing interests., (© 2024. The Author(s).)

Published
2025
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