Статті в журналах з теми "Pseudopeptidic molecules"
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Alfonso, Ignacio. "From simplicity to complex systems with bioinspired pseudopeptides." Chemical Communications 52, no. 2 (2016): 239–50. http://dx.doi.org/10.1039/c5cc07596c.
Повний текст джерелаBijesh, M. B., N. U. Dheepthi, Appa Rao Sapala, Ashutosh Shandilya, Kedar Khare, and V. Haridas. "Chiral and non-chiral assemblies from lipidated serine-based pseudopeptidic molecules." Molecular Systems Design & Engineering 1, no. 2 (2016): 163–68. http://dx.doi.org/10.1039/c6me00009f.
Повний текст джерелаOstankovitch, Marina, Gilles Guichard, Francine Connan, Sylviane Muller, Aude Chaboissier, Johan Hoebeke, Jeannine Choppin, Jean-Paul Briand, and Jean-Gérard Guillet. "A Partially Modified Retro-Inverso Pseudopeptide Modulates the Cytokine Profile of CTL Specific for an Influenza Virus Epitope." Journal of Immunology 161, no. 1 (July 1, 1998): 200–208. http://dx.doi.org/10.4049/jimmunol.161.1.200.
Повний текст джерелаFaggi, Enrico, Santiago V. Luis та Ignacio Alfonso. "Minimalistic amino amides as models to study N–H⋯π interactions and their implication in the side chain folding of pseudopeptidic molecules". RSC Advances 3, № 29 (2013): 11556. http://dx.doi.org/10.1039/c3ra41843j.
Повний текст джерелаMehrazma, Banafsheh, Anahit Petoyan, Stanley K. A. Opare та Arvi Rauk. "Interaction of the N-AcAβ(13–23)NH2 segment of the beta amyloid peptide with beta-sheet-blocking peptides: site and edge specificity". Canadian Journal of Chemistry 94, № 6 (червень 2016): 583–92. http://dx.doi.org/10.1139/cjc-2016-0033.
Повний текст джерелаEsteve, Ferran, Alexis Villanueva-Antolí, Belén Altava, Eduardo García-Verdugo, and Santiago V. Luis. "Unravelling the Supramolecular Driving Forces in the Formation of CO2-Responsive Pseudopeptidic Low-Molecular-Weight Hydrogelators." Gels 8, no. 6 (June 20, 2022): 390. http://dx.doi.org/10.3390/gels8060390.
Повний текст джерелаDharmashekar, Chandan, Bhargav Shreevatsa, Anisha S. Jain, Bhavana Harendra, Sushma Pradeep, Prashanth M. Vishwanath, Pranav Singh, et al. "Evaluating the Antimicrobial and Anti-Hemolytic Activity of Synthesized Pseudopeptide against Leptospiral Species: In Silico and In Vitro Approach." Molecules 28, no. 3 (January 22, 2023): 1106. http://dx.doi.org/10.3390/molecules28031106.
Повний текст джерелаCalbo, Sébastien, Gilles Guichard, Philippe Bousso, Sylviane Muller, Philippe Kourilsky, Jean-Paul Briand, and Jean-Pierre Abastado. "Role of Peptide Backbone in T Cell Recognition." Journal of Immunology 162, no. 8 (April 15, 1999): 4657–62. http://dx.doi.org/10.4049/jimmunol.162.8.4657.
Повний текст джерелаAmini, Zohreh, Mohammad Hossein Fatemi та Arvi Rauk. "Molecular dynamics studies of a β-sheet blocking peptide with the full-length amyloid beta peptide of Alzheimer’s disease". Canadian Journal of Chemistry 94, № 10 (жовтень 2016): 833–41. http://dx.doi.org/10.1139/cjc-2016-0267.
Повний текст джерелаMoure, Alejandra, Santiago V. Luis, and Ignacio Alfonso. "Efficient Synthesis of Pseudopeptidic Molecular Cages." Chemistry - A European Journal 18, no. 18 (March 29, 2012): 5496–500. http://dx.doi.org/10.1002/chem.201104045.
Повний текст джерелаFaggi, Enrico, Cristian Vicent, Santiago V. Luis, and Ignacio Alfonso. "Stereoselective recognition of the Ac-Glu-Tyr-OH dipeptide by pseudopeptidic cages." Organic & Biomolecular Chemistry 13, no. 48 (2015): 11721–31. http://dx.doi.org/10.1039/c5ob01889g.
Повний текст джерелаFaggi, Enrico, Santiago V. Luis, and Ignacio Alfonso. "Sensing, Transport and Other Potential Biomedical Applications of Pseudopeptides." Current Medicinal Chemistry 26, no. 21 (September 19, 2019): 4065–97. http://dx.doi.org/10.2174/0929867325666180301091040.
Повний текст джерелаSharma, Sakshi, Shridhar H. Thorat, Rajesh G. Gonnade, Jerry P. Jasinski, Ray Butcher, and V. Haridas. "Engineering Molecular Topology: A Pseudopeptidic Macrocyclic Figure-Eight Motif." European Journal of Organic Chemistry 2017, no. 7 (December 12, 2016): 1120–24. http://dx.doi.org/10.1002/ejoc.201601365.
Повний текст джерелаGiuri, Demetra, Nicola Zanna, and Claudia Tomasini. "Low Molecular Weight Gelators Based on Functionalized l-Dopa Promote Organogels Formation." Gels 5, no. 2 (May 14, 2019): 27. http://dx.doi.org/10.3390/gels5020027.
Повний текст джерелаMartí, Inés, M. Isabel Burguete, Philip A. Gale, and Santiago V. Luis. "Acyclic Pseudopeptidic Hosts as Molecular Receptors and Transporters for Anions." European Journal of Organic Chemistry 2015, no. 23 (July 3, 2015): 5150–58. http://dx.doi.org/10.1002/ejoc.201500390.
Повний текст джерелаKotynia, Aleksandra, Benita Wiatrak, Wojciech Kamysz, Damian Neubauer, Paulina Jawień, and Aleksandra Marciniak. "Cationic Peptides and Their Cu(II) and Ni(II) Complexes: Coordination and Biological Characteristics." International Journal of Molecular Sciences 22, no. 21 (November 6, 2021): 12028. http://dx.doi.org/10.3390/ijms222112028.
Повний текст джерелаKoistinen, Hannu, Erik Wallén, Henna Ylikangas, Kristian Meinander, Maija Lahtela-Kakkonen, Ale Närvänen, and Ulf-Håkan Stenman. "Development of molecules stimulating the activity of KLK3 – an update." Biological Chemistry 397, no. 12 (December 1, 2016): 1229–35. http://dx.doi.org/10.1515/hsz-2016-0189.
Повний текст джерелаAngulo-Pachón, César A., Diego Navarro-Barreda, Celia M. Rueda, Francisco Galindo, and Juan F. Miravet. "Deamidation of pseudopeptidic molecular hydrogelators and its application to controlled release." Journal of Colloid and Interface Science 505 (November 2017): 1111–17. http://dx.doi.org/10.1016/j.jcis.2017.07.003.
Повний текст джерелаAbdelbaky, Ahmed S., Ivan A. Prokhorov, Igor P. Smirnov, Kristina M. Koroleva, Vitaliy I. Shvets та Yulia G. Kirillova. "Synthesis of α-(R)-/γ-(S)-Dimethyl Substituted Peptide Nucleic Acid Submonomer Using Mitsunobu Reaction". Letters in Organic Chemistry 16, № 5 (1 квітня 2019): 437–46. http://dx.doi.org/10.2174/1570178616666190118155031.
Повний текст джерелаRobinson, Morgan, Jennifer Lou, Banafsheh Mehrazma, Arvi Rauk, Michael Beazely, and Zoya Leonenko. "Pseudopeptide Amyloid Aggregation Inhibitors: In Silico, Single Molecule and Cell Viability Studies." International Journal of Molecular Sciences 22, no. 3 (January 21, 2021): 1051. http://dx.doi.org/10.3390/ijms22031051.
Повний текст джерелаFormicola, Lucia, Xavier Maréchal, Nicolas Basse, Michelle Bouvier-Durand, Danièle Bonnet-Delpon, Thierry Milcent, Michèle Reboud-Ravaux, and Sandrine Ongeri. "Novel fluorinated pseudopeptides as proteasome inhibitors." Bioorganic & Medicinal Chemistry Letters 19, no. 1 (January 2009): 83–86. http://dx.doi.org/10.1016/j.bmcl.2008.11.012.
Повний текст джерелаMehrazma, Banafsheh, Stanley Opare, Anahit Petoyan, and Arvi Rauk. "d-Amino Acid Pseudopeptides as Potential Amyloid-Beta Aggregation Inhibitors." Molecules 23, no. 9 (September 18, 2018): 2387. http://dx.doi.org/10.3390/molecules23092387.
Повний текст джерелаGiuri, Demetra, Marianna Barbalinardo, Nicola Zanna, Paolo Paci, Marco Montalti, Massimiliano Cavallini, Francesco Valle, Matteo Calvaresi, and Claudia Tomasini. "Tuning Mechanical Properties of Pseudopeptide Supramolecular Hydrogels by Graphene Doping." Molecules 24, no. 23 (November 28, 2019): 4345. http://dx.doi.org/10.3390/molecules24234345.
Повний текст джерелаGraham, Samuel L., S. Jane deSolms, Elizabeth A. Giuliani, Nancy E. Kohl, Scott D. Mosser, Allen I. Oliff, David L. Pompliano, Elaine Rands, and Michael J. Breslin. "Pseudopeptide Inhibitors of Ras Farnesyl-Protein Transferase." Journal of Medicinal Chemistry 37, no. 6 (March 1994): 725–32. http://dx.doi.org/10.1021/jm00032a004.
Повний текст джерелаTen Brink, Ruth E., Donald T. Pals, Douglas W. Harris, and Garland A. Johnson. "Renin inhibitors containing .psi.[CH2O] pseudopeptide inserts." Journal of Medicinal Chemistry 31, no. 3 (March 1988): 671–77. http://dx.doi.org/10.1021/jm00398a029.
Повний текст джерелаGaléotti, Nathalie, Joël Poncet, and Patrick Jouin. "Post-Source Decay Analysis of Dolastatin 10 and Dolastatin 15 by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry." European Journal of Mass Spectrometry 8, no. 4 (August 2002): 311–21. http://dx.doi.org/10.1255/ejms.502.
Повний текст джерелаMavridis, George, Richa Arya, Alexander Domnick, Jerome Zoidakis, Manousos Makridakis, Antonia Vlahou, Anastasia Mpakali, et al. "A systematic re-examination of processing of MHCI-bound antigenic peptide precursors by endoplasmic reticulum aminopeptidase 1." Journal of Biological Chemistry 295, no. 21 (March 17, 2020): 7193–210. http://dx.doi.org/10.1074/jbc.ra120.012976.
Повний текст джерелаPispisa, B., L. Stella, M. Venanzi, and A. Palleschi. "A spectroscopic and molecular modeling study on novel pseudopeptides exhibiting biological activity." Journal of Peptide Research 54, no. 4 (October 1999): 353–60. http://dx.doi.org/10.1034/j.1399-3011.1999.00124.x.
Повний текст джерелаBalboni, Gianfranco, Severo Salvadori, Remo Guerrini, Clementina Bianchi, Vincenzo Santagada, Giuseppe Calliendo, Sharon D. Bryant, and Lawrence H. Lazarus. "Opioid pseudopeptides containing heteroaromatic or heteroaliphatic nuclei." Peptides 21, no. 11 (November 2000): 1663–71. http://dx.doi.org/10.1016/s0196-9781(00)00315-6.
Повний текст джерелаLiu, Keyuan, Long Ye, Yao Wang, Ganhong Du, and Liming Jiang. "A Pseudopeptide Polymer Micelle Used for Asymmetric Catalysis of the Aldol Reaction in Water." Polymers 10, no. 9 (September 10, 2018): 1004. http://dx.doi.org/10.3390/polym10091004.
Повний текст джерелаPerez, Juan J. "Designing Peptidomimetics." Current Topics in Medicinal Chemistry 18, no. 7 (July 9, 2018): 566–90. http://dx.doi.org/10.2174/1568026618666180522075258.
Повний текст джерелаPinnen, Francesco, Grazia Luisi, Gino Lucente, Enrico Gavuzzo та Silvio Cerrini. "Approaches to pseudopeptidic ergopeptines. Synthesis and molecular structure of an α-aza-phenylalanine-containing oxa-cyclol". J. Chem. Soc., Perkin Trans. 1, № 7 (1993): 819–24. http://dx.doi.org/10.1039/p19930000819.
Повний текст джерелаValls, Adriana, Adrián Castillo, Raúl Porcar, Sami Hietala, Belén Altava, Eduardo Garcı́a-Verdugo, and Santiago V. Luis. "Urea-Based Low-Molecular-Weight Pseudopeptidic Organogelators for the Encapsulation and Slow Release of (R)-Limonene." Journal of Agricultural and Food Chemistry 68, no. 26 (June 8, 2020): 7051–61. http://dx.doi.org/10.1021/acs.jafc.0c01184.
Повний текст джерелаPreviti, Santo, Roberta Ettari, Carla Di Chio, Rahul Ravichandran, Marta Bogacz, Ute A. Hellmich, Tanja Schirmeister, Sandro Cosconati, and Maria Zappalà. "Development of Reduced Peptide Bond Pseudopeptide Michael Acceptors for the Treatment of Human African Trypanosomiasis." Molecules 27, no. 12 (June 11, 2022): 3765. http://dx.doi.org/10.3390/molecules27123765.
Повний текст джерелаD'Angeli, Ferruccio, Paolo Marchetti, Severe Salvador, and Gianfranco Balboni. "2-Bromoamides as synthons for pseudopeptides containing aminodicarboxy units." Journal of the Chemical Society, Chemical Communications, no. 3 (1993): 304. http://dx.doi.org/10.1039/c39930000304.
Повний текст джерелаZaretsky, Serge, and Andrei K. Yudin. "Recent advances in the synthesis of cyclic pseudopeptides." Drug Discovery Today: Technologies 26 (December 2017): 3–10. http://dx.doi.org/10.1016/j.ddtec.2017.11.004.
Повний текст джерелаAbdelbaky, Ahmed S., Ivan A. Prokhorov, Elena V. Gnuskova, Olga V. Esipova, and Yulia G. Kirillova. "Convenient and Efficient Syntheses of Peptide Nucleic Acid Purine Monomers." Current Organic Chemistry 23, no. 19 (December 19, 2019): 2122–30. http://dx.doi.org/10.2174/1385272823666191014161442.
Повний текст джерелаByk, Gerardo, Marc Duchesne, Fabienne Parker, Yves Lelievre, Jean D. Guitton, François F. Clerc, Jérôme Becquart, Bruno Tocque, and Daniel Scherman. "Local constrained shifty pseudopeptides inhibitors of rasfarnesyl transferase." Bioorganic & Medicinal Chemistry Letters 5, no. 22 (November 1995): 2677–82. http://dx.doi.org/10.1016/0960-894x(95)00482-9.
Повний текст джерелаScognamiglio, Pasqualina Liana, Chiara Platella, Ettore Napolitano, Domenica Musumeci, and Giovanni Nicola Roviello. "From Prebiotic Chemistry to Supramolecular Biomedical Materials: Exploring the Properties of Self-Assembling Nucleobase-Containing Peptides." Molecules 26, no. 12 (June 10, 2021): 3558. http://dx.doi.org/10.3390/molecules26123558.
Повний текст джерелаGuichard, Gilles, Sébastien Calbo, Sylviane Muller, Philippe Kourilsky, Jean-Paul Briand, and Jean-Pierre Abastado. "Efficient Binding of Reduced Peptide Bond Pseudopeptides to Major Histocompatibility Complex Class I Molecule." Journal of Biological Chemistry 270, no. 44 (November 3, 1995): 26057–59. http://dx.doi.org/10.1074/jbc.270.44.26057.
Повний текст джерелаQian, J. M., D. H. Coy, N. Y. Jiang, J. D. Gardner, and R. T. Jensen. "Reduced Peptide Bond Pseudopeptide Analogues of Substance P." Journal of Biological Chemistry 264, no. 28 (October 1989): 16667–71. http://dx.doi.org/10.1016/s0021-9258(19)84757-9.
Повний текст джерелаSharma, Sakshi, Shridhar H. Thorat, Rajesh G. Gonnade, Jerry P. Jasinski, Ray Butcher, and V. Haridas. "Front Cover: Engineering Molecular Topology: A Pseudopeptidic Macrocyclic Figure-Eight Motif (Eur. J. Org. Chem. 7/2017)." European Journal of Organic Chemistry 2017, no. 7 (February 10, 2017): 1099. http://dx.doi.org/10.1002/ejoc.201700131.
Повний текст джерелаGiastas, Petros, Anastasia Mpakali, Athanasios Papakyriakou, Aggelos Lelis, Paraskevi Kokkala, Margarete Neu, Paul Rowland, John Liddle, Dimitris Georgiadis, and Efstratios Stratikos. "Mechanism for antigenic peptide selection by endoplasmic reticulum aminopeptidase 1." Proceedings of the National Academy of Sciences 116, no. 52 (December 16, 2019): 26709–16. http://dx.doi.org/10.1073/pnas.1912070116.
Повний текст джерелаShaaban, Saad, Florenz Sasse, Torsten Burkholz, and Claus Jacob. "Sulfur, selenium and tellurium pseudopeptides: Synthesis and biological evaluation." Bioorganic & Medicinal Chemistry 22, no. 14 (July 2014): 3610–19. http://dx.doi.org/10.1016/j.bmc.2014.05.019.
Повний текст джерелаZhao, Ming, Hynda K. Kleinman, and Michael Mokotoff. "Synthetic Laminin-like Peptides and Pseudopeptides as Potential Antimetastatic Agents." Journal of Medicinal Chemistry 37, no. 20 (September 1994): 3383–88. http://dx.doi.org/10.1021/jm00046a023.
Повний текст джерелаEwenson, Ariel, Ralph Laufer, Michael Chorev, Zvi Selinger, and Chaim Gilon. "Ketomethylene pseudopeptide analogs of substance P: synthesis and biological activity." Journal of Medicinal Chemistry 29, no. 2 (February 1986): 295–99. http://dx.doi.org/10.1021/jm00152a020.
Повний текст джерелаMarastoni, Mauro, Martina Bazzaro, Fabrizio Bortolotti, and Roberto Tomatis. "Synthesis and activity of N-Benzyl pseudopeptides HIV protease inhibitors." Bioorganic & Medicinal Chemistry 11, no. 11 (May 29, 2003): 2477–83. http://dx.doi.org/10.1016/s0968-0896(02)00563-1.
Повний текст джерелаHarrington, Edmund M., James J. Kowalczyk, Sharon L. Pinnow, Karen Ackermann, Ana Maria Garcia, and Michael D. Lewis. "Cysteine and methionine linked by carbon pseudopeptides inhibit farnesyl transferase." Bioorganic & Medicinal Chemistry Letters 4, no. 23 (December 1994): 2775–80. http://dx.doi.org/10.1016/s0960-894x(01)80593-x.
Повний текст джерелаSieńczyk, Marcin, Dawid Podgórski, Aleksandra Błażejewska, Julita Kulbacka, Jolanta Saczko, and Józef Oleksyszyn. "Phosphonic pseudopeptides as human neutrophil elastase inhibitors—a combinatorial approach." Bioorganic & Medicinal Chemistry 19, no. 3 (February 2011): 1277–84. http://dx.doi.org/10.1016/j.bmc.2010.12.008.
Повний текст джерелаGeorgsson, Jennie, Ulrika Rosenström, Charlotta Wallinder, Hélène Beaudry, Bianca Plouffe, Gunnar Lindeberg, Milad Botros, et al. "Short pseudopeptides containing turn scaffolds with high AT2 receptor affinity." Bioorganic & Medicinal Chemistry 14, no. 17 (September 2006): 5963–72. http://dx.doi.org/10.1016/j.bmc.2006.05.019.
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