Relevant bibliographies by topics / "potere conformativo"

Academic literature on the topic '"potere conformativo"'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic ""potere conformativo""

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Fauceglia, Domenico. "Nullità e conformazione dei contratti di impresa ad opera delle autorità indipendenti = Nullity and conformation of business contracts by authorities." CUADERNOS DE DERECHO TRANSNACIONAL 10, no. 2 (October 5, 2018): 306. http://dx.doi.org/10.20318/cdt.2018.4379.

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Riassunto: Sin dall’avvento nel sistema istituzionale italiano delle c.d. Autorità indipendenti, al-le quali è attribuito il potere di regolare settori sensibili del mercato (domain sensibles), si è posta l’attenzione sulla particolare interferenza tra regolazione del mercato e di-sciplina dei contratti. In parti­colare, le Autorità indipendenti godono di un potere re-golamentare abbastanza variegato: la legge attri­buisce alle Authorities i poteri di defi-nire i procedimenti di formazione e conclusione, nonché la forma e il contenuto mi-nimo dei contratti. In relazione a questi ultimi poteri, si cercherà, con tale contributo, di esaminare le ipotesi di nullità negoziale derivanti dalla difformità dei contratti ri-spetto ai regolamenti delle Autorità Indipendenti, nonché le ipotesi di eteroregola-mentazione dei contratti ad opera dei rego­lamenti delle Autorità Indipendenti.Parole chiavi: contratto, mercato, autorità indipendenti, nullità dei contratti, integrazione contrat-tuale, contratti d’impresa, contratti bancari, contratti finanziari.Abstract: Since the inclusion in the Italian institutional system of the c.d. Independent authori-ties, which are given the power to regulate sensitive sectors of the market (domain sensibles), attention has been focused on the particular interference between market regulation and contract discipline. In particular, the Authorities have quite a varied regulatory power: the law gives the Authorities the power to define the starting and conclusion procedures, as well as the form and minimum content of the con­tracts. In relation to these last powers, we will try, with this contribution, to examine the hy-pothesis of negotiation nullity deriving from the non-conformity of the contracts with the regulations of the Inde­pendent Authorities, as well as the hypothesis of external regulation of the contracts by the regulations of Independent Authorities.Keywords: contract, market, independent authorities, nullity of contracts, contractual inte-gration, business contract, banking contracts, financial contracts.
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Hu, Wei-Gang, Junfei Yin, Damon Chau, Charles Chen Hu, Dustin Lillico, Justin Yu, Laurel M. Negrych, and John W. Cherwonogrodzky. "Conformation-Dependent High-Affinity Potent Ricin-Neutralizing Monoclonal Antibodies." BioMed Research International 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/471346.

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Ricin is a potential biothreat agent with no approved antidote available for ricin poisoning. The aim of this study was to develop potent antibody-based antiricin antidotes. Four strong ricin resistant hybridoma clones secreting antiricin monoclonal antibodies (mAbs) were developed. All four mAbs are bound to conformational epitopes of ricin toxin B (RTB) with high affinity (KDvalues from 2.55 to 36.27 nM). RTB not only triggers cellular uptake of ricin, but also facilitates transport of the ricin toxin A (RTA) from the endoplasmic reticulum to the cytosol, where RTA exerts its toxic activity. The four mAbs were found to have potent ricin-neutralizing capacities and synergistic effects among them as determined by anin vitroneutralization assay.In vivoprotection assay demonstrated that all four mAbs had strong efficacy against ricin challenges. D9 was found to be exceptionally effective. Intraperitoneal (i.p.) administration of D9, at a dose of 5 μg, 6 weeks before or 6 hours after an i.p. challenge with 5 × LD50 of ricin was able to protect or rescue 100% of the mice, indicating that mAb D9 is an excellent candidate to be developed as a potent antidote against ricin poisoning for both prophylactic and therapeutic purposes.
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Pukin, Aliaksei V., Arwin J. Brouwer, Leonie Koomen, H. C. Quarles van Ufford, Johan Kemmink, Nico J. de Mol, and Roland J. Pieters. "Thiourea-based spacers in potent divalent inhibitors of Pseudomonas aeruginosa virulence lectin LecA." Organic & Biomolecular Chemistry 13, no. 44 (2015): 10923–28. http://dx.doi.org/10.1039/c5ob01452b.

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GURRATH, Marion, Gerhard MULLER, Horst KESSLER, Monique AUMAILLEY, and Rupert TIMPL. "Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides." European Journal of Biochemistry 210, no. 3 (December 1992): 911–21. http://dx.doi.org/10.1111/j.1432-1033.1992.tb17495.x.

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Houdai, Toshihiro, Shigeru Matsuoka, Nagy Morsy, Nobuaki Matsumori, Masayuki Satake, and Michio Murata. "Hairpin conformation of amphidinols possibly accounting for potent membrane permeabilizing activities." Tetrahedron 61, no. 11 (March 2005): 2795–802. http://dx.doi.org/10.1016/j.tet.2005.01.069.

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Naveen, S., Sridhar M. Anandalwar, J. Shashidhara Prasad, Dinesh Manvar, Arun Mishra, and Anamik Shah. "Synthesis and Structural Conformation Studies of a Potent Unsymmetrical 1,4-Dihydropyridine." Journal of Chemical Crystallography 38, no. 4 (January 29, 2008): 315–19. http://dx.doi.org/10.1007/s10870-008-9314-1.

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Rizo, Josep, R. Bryan Sutton, Joshua Breslau, Steven C. Koerber, John Porter, Arnold T. Hagler, Jean E. Rivier, and Lila M. Gierasch. "A Novel Conformation in a Highly Potent, Constrained Gonadotropin-Releasing Hormone Antagonist." Journal of the American Chemical Society 118, no. 5 (January 1996): 970–76. http://dx.doi.org/10.1021/ja953207e.

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Yamagat, Yuriko, Ken-ichi Tomita, Nobuhiro Marubayashi, Ikuhiko Ueda, Shinji Sakata, Akira Matsuda, Kenji Takenuki, and Tohru Ueda. "Molecular Conformation of 2′-Deoxy-2′-methylidene-cytidine: A Potent Antineoplastic Nucleoside." Nucleosides and Nucleotides 11, no. 2-4 (February 1992): 835–53. http://dx.doi.org/10.1080/07328319208021744.

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Maia, Angélica Faleiros da Silva, Felipe T. Martins, Leonardo da Silva Neto, Rosemeire Brondi Alves, and Ângelo De Fátima. "Cocaethylene, the in vivo product of cocaine and ethanol, is a narcotic more potent than its precursors." Acta Crystallographica Section C Structural Chemistry 73, no. 10 (September 20, 2017): 780–83. http://dx.doi.org/10.1107/s2053229617012852.

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The molecular conformation and supramolecular architecture of cocaethylene [systematic name: ethyl (1R,2R,3S,5S)-3-benzoyloxy-8-methyl-8-azabicyclo[3.2.1]octane-2-carboxylate], C18H23NO4, have been determined for the first time. Cocaethylene is a narcotic produced in vivo when cocaine and ethanol are administered concomitantly. The intra- and intermolecular features of cocaethylene and its less potent narcotic precursor cocaine are very similar. The only molecular difference is in the conformation of the methyl group of the ethoxycarbonyl group. Similar to cocaine, the carboxylate atoms and the α-C atom are coplanar in cocaethylene, but the methyl C atom of the ethyl group is bent by ca 90° away from this plane in the narcotic reported here. The main supramolecular motif is a one-dimensional chain stabilized by weak C—H...O contacts.
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Amorim-Carmo, Bruno, Alessandra Daniele-Silva, Adriana M. S. Parente, Allanny A. Furtado, Eneas Carvalho, Johny W. F. Oliveira, Elizabeth C. G. Santos, et al. "Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin." International Journal of Molecular Sciences 20, no. 3 (January 31, 2019): 623. http://dx.doi.org/10.3390/ijms20030623.

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Scorpion venom constitutes a rich source of biologically active compounds with high potential for therapeutic and biotechnological applications that can be used as prototypes for the design of new drugs. The aim of this study was to characterize the structural conformation, evaluate the antimicrobial activity, and gain insight into the possible action mechanism underlying it, for two new analog peptides of the scorpion peptide Stigmurin, named StigA25 and StigA31. The amino acid substitutions in the native sequence for lysine residues resulted in peptides with higher positive net charge and hydrophobicity, with an increase in the theoretical helical content. StigA25 and StigA31 showed the capacity to modify their structural conformation according to the environment, and were stable to pH and temperature variation—results similar to the native peptide. Both analog peptides demonstrated broad-spectrum antimicrobial activity in vitro, showing an effect superior to that of the native peptide, being non-hemolytic at the biologically active concentrations. Therefore, this study demonstrates the therapeutic potential of the analog peptides from Stigmurin and the promising approach of rational drug design based on scorpion venom peptide to obtain new anti-infective agents.
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Dissertations / Theses on the topic ""potere conformativo""

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Ahn, Jung-Mo. "Search for bioactive conformation of glucagon and development of potent glucagon antagonists." Diss., The University of Arizona, 2000. http://hdl.handle.net/10150/284301.

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In pursuit of the working model of how glucagon interacts with the glucagon receptor and how glucagon antagonists exert their different activities, 42 glucagon analogues were designed and synthesized. An attempt to determine the minimum sequence for binding affinity of glucagon analogues was carried out and resulted in several potent truncated glucagon antagonists with substantial binding affinity, such as phenylbutyryl-glucagon(10-29) amide. Furthermore, a new method for determining the bioactive conformations of peptide hormones has been designed. In a positional cyclization scanning study, several conformationally constrained glucagon analogues containing disulfide or lactam bridges were synthesized, and the biological assay results showed that the alpha-helical conformation is required for the maximal receptor recognition. This study resulted in two superpotent glucagon analogues, c[Lys⁵, Glu⁹]glucagon amide and c[Lys¹⁷, Glu²¹]glucagon amide, which have picomolar binding affinities. A structure-activity relationship study of glycine at position 4 was performed to determine the importance of flexibility in the N-terminal region of glucagon. Four glucagon analogues were designed and synthesized, and all showed extremely potent antagonistic activity with improved binding affinity. Also, the potent glucagon antagonist [desHis¹, desPhe⁶, Glu⁹] glucagon amide was synthesized on a large scale (ca. 1.5 g), and the effect of the glucagon antagonist on diabetic ketoacidosis was studied in vivo in alloxan-induced diabetic dogs. The glucagon antagonist clearly showed its effectiveness in controlling serum bicarbonate concentration, while the control experiment with saline demonstrated increased diabetic ketoacidosis. This study clearly showed the possibility of using glucagon antagonists as therapeutic agents for the treatment of diabetic ketoacidosis. The conformation of the potent glucagon antagonist [desHis¹, desPhe⁶, Glu⁹] glucagon amide was studied using 2D NMR spectroscopy, and deuterated dodecylphosphocholine micelles were utilized to imitate the membrane environment. In this investigation, TOCSY, DQF-COSY, and NOESY spectra of the glucagon antagonist in a deuterated DPC micelle solution were acquired at pH 6.0 and 37°C. Restrained molecular dynamics (simulated annealing) using 332 distance restraints and 16 torsion angle restraints resulted in a conformation which displayed a similar C-terminal conformation, but a distinctly different N-terminal region, as compared to the conformation of glucagon. The newly discovered salt bridge between Ser² and Glu⁹ presumably resulted from the increased flexibility of the N-terminal region by the deletion of Phe⁶ and substitution of Glu⁹, which may shed light on how small changes in the sequence of peptides can significantly modify the conformation.
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VICENZONI, Francesco. "Ipoteri conformativi della proprietà privata e l'autoamministrazione del privato nel godimento della proprietà conformata." Doctoral thesis, 2018. http://hdl.handle.net/11562/980280.

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Il potere pubblico di conformazione del diritto di proprietà fondiaria nella sua più dettagliata espressione consente l’arretramento del potere attivo dell’amministrazione che, nel controllo edilizio, si traduce nel rilascio del permesso di costruire, favorendo in tal modo il ricorso a forme di autoamministrazione dei privati nel godimento della proprietà conformata anche comportanti profonde ricadute sul territorio. Regolamentazione e liberalizzazione divengono così un'endiade perché al maggior dettaglio della prima (piano-progetto) corrisponde maggior spazio applicativo per la seconda.
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Book chapters on the topic ""potere conformativo""

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Nutt, R. F., S. F. Brady, J. T. Sisko, T. M. Ciccarone, C. D. Colton, M. R. Levy, R. J. Gould, G. Zhang, P. A. Friedman, and D. F. Veber. "Structure- and conformation-activity studies leading to potent fibrinogen receptor antagonists containing Arg-Gly-Asp." In Peptides 1990, 784–86. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_325.

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Bienstock, Rachelle J., Steven C. Koerber, Josep Rizo, Jean E. Rivier, Arnold T. Hagler, and Lila M. Gierasch. "Conformation of a highly potent bicyclic GnRH antagonist by combined molecular dynamics and two-dimensional NMR analyses." In Peptides, 262–64. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_93.

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Taber, Douglass F. "The Fuwa Synthesis of Didemnaketal B." In Organic Synthesis. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780190646165.003.0097.

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Didemnaketal B 3 may be an artifact of isolation, derived from didemnaketal C, in which one of the methyl esters is instead an ethylsulfonate. Nevertheless, it is B, not C, that is a potent inhibitor of HIV protease. Haruhiko Fuwa of Tohoku University has provided (Chem. Eur. J. 2014, 20, 1848) a detailed account of the synthesis of 3, including the necessary revision of the absolute configuration of seven of the stereo­genic centers. A central feature of the modular synthesis of 3 was the cyclization of 1 to the thermodynamically most favorable diastereomer of the spiroketal 2. Three components were combined for the synthesis of 3. The upper sidechain was prepared from commercial citronellal 4. Reduction followed by protection and ozon­olysis delivered the aldehyde 5, that was carried on to the alkyne 6. Hydroiodination using the method previously reported by the authors (OHL May 30, 2011) gave 7, that was oxidized to 8 and then to the ester 9. Lactone formation by ring-closing metathesis is difficult because of the substantial preference for the extended conformation of the ester. As illustrated by the conversion of 10 to 11, this can be overcome by complexation with a Lewis acid. Conjugate addi­tion followed by phosphorylation completed the preparation of the enol phosphate 12. The third component of 3 was the lactone 15, prepared by deprotonation/kinetic protonation with 14 of 13. This was carried on to the sulfone 16, that was coupled with 17. Although the Julia–Kocienski reaction usually strongly favors the E alkene, in this case it was necessary to optimize both the base and the solvent. Sharpless asym­metric dihydroxylation followed by coupling with the enol phosphate 12 then completed the preparation of the diol 1. Addition of the ketene silyl acetal 18 to the aldehyde derived from 2 proceeded to give the undesired diastereomer 19. This was overcome by oxidation to the ketone followed by enantioselective reduction. The iodide 9 was added to the aldehyde 20 to give a 1.8:1 mixture of diastereomers, the major one of which was didemnaketal B 3. This full paper is worth reading in detail. The work reported underlines the impor­tance of powerful protocols for carbon–carbon bond formation that maintain high diastereocontrol in stereochemically complex environments.
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Conference papers on the topic ""potere conformativo""

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Pareti, F. I., K. Nliya, P. J. Kostel, J. M. McPherson, T. S. Zimmerman, and Z. M. Ruggeri. "IDENTIFICATION OF A SECOND COLLAGEN-BINDING DOMAIN IN HUMAN VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642877.

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We have recently reported (Journal of Biological Chemistry 261: 15310-15315, 1986) that von Willebrand factor (vWF) possesses a collagen-binding domain localized in a reduced and alkylated tryptic fragment of apparent 52/48 kDa molecular weight extending between residues Val (449) and Lys (728) of the constituent subunit. This proteolytic fragment of vWF also contains a glycoprotein lb-binding domain and a heparin-binding domain. We have now identified a second collagen-binding domain in the Staphylococcus aureus V8 protease-generated fragment I that extends from residue Gly (911) to Glu (1365). The two binding domains exhibit different interaction with collagens of different origin. The reduced and alkylated 52/48 kDa tryptic fragment was a potent inhibitor of vWF binding to equine collagen type I, but had no effect on the binding to bovine collagen type I and III. In contrast, a purified fraction containing the unreduced 52/48 kDa domain inhibited vWF binding to all types of collagen, as did anti-52/48 kDa monoclonal antibodies. Some of these antibodies, however, were more effective in inhibiting binding to equine collagen. On the other hand, fragment I markedly inhibited the binding of vWF to bovine collagen type I and III, but was less effective with equine collagen type I. Direct binding studies using 425j_qabeled fragment I demonstrated that the association constant was 5 to 10 times greater with the bovine collagens than with the equine collagen. The Staphylococcus aureus V8 protease-generated fragment III, which extends from residue Ser (1) to Glu (1365) and contains both collagen-binding domains, was the most potent inhibitor of vWF binding to all types of collagen tested. Thus, vWF has at least two collagen-binding domains. Native conformation appears to be necessary for binding of the 52/48 kDa domain to bovine collagen type I and III, but not to the equine collagen type I tested. The two domains appear to function concurrently in mediating vWF binding to collagen.
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