Статті в журналах з теми "Peptide resonance"
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Martin, Aline, Valentin David, Jennifer S. Laurence, Patricia M. Schwarz, Eileen M. Lafer, Anne-Marie Hedge, and Peter S. N. Rowe. "Degradation of MEPE, DMP1, and Release of SIBLING ASARM-Peptides (Minhibins): ASARM-Peptide(s) Are Directly Responsible for Defective Mineralization in HYP." Endocrinology 149, no. 4 (December 27, 2007): 1757–72. http://dx.doi.org/10.1210/en.2007-1205.
Повний текст джерелаTsybin, Youri O., Per Håkansson, Magnus Wetterhall, Karin E. Markides, and Jonas Bergquist. "Capillary Electrophoresis and Electron Capture Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for Peptide Mixture and Protein Digest Analysis." European Journal of Mass Spectrometry 8, no. 5 (October 2002): 389–95. http://dx.doi.org/10.1255/ejms.514.
Повний текст джерелаVernen, Felicitas, Peta J. Harvey, Susana A. Dias, Ana Salomé Veiga, Yen-Hua Huang, David J. Craik, Nicole Lawrence, and Sónia Troeira Henriques. "Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties." International Journal of Molecular Sciences 20, no. 17 (August 26, 2019): 4184. http://dx.doi.org/10.3390/ijms20174184.
Повний текст джерелаWilson, David, and Norelle L. Daly. "Nuclear Magnetic Resonance seq (NMRseq): A New Approach to Peptide Sequence Tags." Toxins 10, no. 11 (October 28, 2018): 437. http://dx.doi.org/10.3390/toxins10110437.
Повний текст джерелаSyryamina, Victoria N., Alvaro S. Siano, Fernando Formaggio, and Marta De Zotti. "A Peptide-Based Trap for Metal Ions Studied by Electron Paramagnetic Resonance." Chemosensors 10, no. 2 (February 10, 2022): 71. http://dx.doi.org/10.3390/chemosensors10020071.
Повний текст джерелаPark, Sunghyouk, Michael E. Johnson, and Leslie W. M. Fung. "Nuclear magnetic resonance studies of mutations at the tetramerization region of human alpha spectrin." Blood 100, no. 1 (July 1, 2002): 283–88. http://dx.doi.org/10.1182/blood.v100.1.283.
Повний текст джерелаXia, Ning, Gang Liu, and Xinyao Yi. "Surface Plasmon Resonance for Protease Detection by Integration of Homogeneous Reaction." Biosensors 11, no. 10 (September 29, 2021): 362. http://dx.doi.org/10.3390/bios11100362.
Повний текст джерелаLupaescu, Ancuta-Veronica, Cosmin Stefan Mocanu, Gabi Drochioiu, and Catalina-Ionica Ciobanu. "Zinc Binding to NAP-Type Neuroprotective Peptides: Nuclear Magnetic Resonance Studies and Molecular Modeling." Pharmaceuticals 14, no. 10 (October 1, 2021): 1011. http://dx.doi.org/10.3390/ph14101011.
Повний текст джерелаNagaraj, G., M. V. Uma, M. S. Shivayogi, and Hemalatha Balaram. "Antimalarial Activities of Peptide Antibiotics Isolated from Fungi." Antimicrobial Agents and Chemotherapy 45, no. 1 (January 1, 2001): 145–49. http://dx.doi.org/10.1128/aac.45.1.145-149.2001.
Повний текст джерелаKim, Minseon, and Yongae Kim. "Structural Studies of Expressed tIK, Anti-Inflammatory Peptide." International Journal of Molecular Sciences 24, no. 1 (December 30, 2022): 636. http://dx.doi.org/10.3390/ijms24010636.
Повний текст джерелаGudivada, Vijaya Narasimha, Chen-Ji Huang, Yueh-Hsia Luo, and Guo-Chung Dong. "A Cyclic BMP-2 Peptide Upregulates BMP-2 Protein-Induced Cell Signaling in Myogenic Cells." Polymers 13, no. 15 (July 31, 2021): 2549. http://dx.doi.org/10.3390/polym13152549.
Повний текст джерелаBierzyński, A. "Methods of peptide conformation studies." Acta Biochimica Polonica 48, no. 4 (December 31, 2001): 1091–99. http://dx.doi.org/10.18388/abp.2001_3870.
Повний текст джерелаJaswal, JASWINDER S., and Alan S. Tracey. "Stereochemical requirements for the formation of vanadate complexes with peptides." Canadian Journal of Chemistry 69, no. 10 (October 1, 1991): 1600–1607. http://dx.doi.org/10.1139/v91-235.
Повний текст джерелаCROSS, Keith J., N. Laila HUQ, Wendy BICKNELL та Eric C. REYNOLDS. "Cation-dependent structural features of β-casein-(1–25)". Biochemical Journal 356, № 1 (8 травня 2001): 277–86. http://dx.doi.org/10.1042/bj3560277.
Повний текст джерелаMishra, Vinod K., та Gattadahalli M. Anantharamaiah. "High-Resolution Structural Studies Elucidate Antiatherogenic and Anti-Inflammatory Properties of Peptides Designed to Mimic Amphipathic α-Helical Domains of Apolipoprotein A-I". Natural Product Communications 14, № 5 (травень 2019): 1934578X1984913. http://dx.doi.org/10.1177/1934578x19849131.
Повний текст джерелаNatarajan, Kannan, Giora Morozov, Jiansheng Jiang, Lisa F. Boyd, Michael G. Mage, and David H. Margulies. "TAPBPR, a Peptide Editor – interactions with MHC complexes and SAXS structural studies." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 116.5. http://dx.doi.org/10.4049/jimmunol.196.supp.116.5.
Повний текст джерелаYoung, John K., Donghui Li, Matthew C. Abramowitz, and Trudy G. Morrison. "Interaction of Peptides with Sequences from the Newcastle Disease Virus Fusion Protein Heptad Repeat Regions." Journal of Virology 73, no. 7 (July 1, 1999): 5945–56. http://dx.doi.org/10.1128/jvi.73.7.5945-5956.1999.
Повний текст джерелаKim, Young Soo, and Hyung Joon Cha. "High-Throughput and Facile Assay of Antimicrobial Peptides Using pH-Controlled Fluorescence Resonance Energy Transfer." Antimicrobial Agents and Chemotherapy 50, no. 10 (October 2006): 3330–35. http://dx.doi.org/10.1128/aac.00455-06.
Повний текст джерелаMorozov, Giora, Huaying Zhao, Michael Mage, Lisa Boyd, Ramesh Venna, Michael Norcross, Curtis McMurtrey, et al. "Direct interaction of recombinant TAPBPR with MHC-I molecules: stabilization of peptide-free MHC-I promotes high affinity peptide loading (APP5P.102)." Journal of Immunology 194, no. 1_Supplement (May 1, 2015): 183.4. http://dx.doi.org/10.4049/jimmunol.194.supp.183.4.
Повний текст джерелаKakizuka, Taishi, Akira Takai, Keiko Yoshizawa, Yasushi Okada, and Tomonobu M. Watanabe. "An improved fluorescent protein-based expression reporter system that utilizes bioluminescence resonance energy transfer and peptide-assisted complementation." Chemical Communications 56, no. 25 (2020): 3625–28. http://dx.doi.org/10.1039/c9cc08664a.
Повний текст джерелаLau, Tong-Lay, Kevin J. Barnham, Cyril C. Curtain, Colin L. Masters та Frances Separovic. "Magnetic Resonance Studies of β-Amyloid Peptides". Australian Journal of Chemistry 56, № 5 (2003): 349. http://dx.doi.org/10.1071/ch02268.
Повний текст джерелаGalzitskaya, O. V., O. M. Selivanova, U. F. Dzhus, V. V. Marchenkov, M. Yu Suvorina та A. K. Surin. "Influence of Chaperones on Amyloid Formation of Аβ Peptide". Current Protein & Peptide Science 23, № 1 (січень 2022): 44–51. http://dx.doi.org/10.2174/1389203723666220127152545.
Повний текст джерелаYin, Liusong, Peter Trenh, and Lawrence Stern. "MHC II-peptide complex conformation constrained by interactions throughout the peptide binding groove determines HLA-DM susceptibility (P5014)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 41.8. http://dx.doi.org/10.4049/jimmunol.190.supp.41.8.
Повний текст джерелаKurepa, Zoran, Charles A. Hasemann, and James Forman. "Qa-1b Binds Conserved Class I Leader Peptides Derived from Several Mammalian Species." Journal of Experimental Medicine 188, no. 5 (September 7, 1998): 973–78. http://dx.doi.org/10.1084/jem.188.5.973.
Повний текст джерелаRibeiro, Ana R. M., Helena P. Felgueiras, Susana P. G. Costa, and Sílvia M. M. A. Pereira-Lima. "Synthesis of Peptaibolin, an Antimicrobial Peptide." Proceedings 78, no. 1 (December 1, 2020): 47. http://dx.doi.org/10.3390/iecp2020-08654.
Повний текст джерелаSgourakis, Nikolaos, Andrew C. McShan, Kannan Natarajan, Vlad K. Kumirov, David Flores-Solis, Jiansheng Jiang, Mareike Badstuebner, Evgenii L. Kovrigin, and David H. Margulies. "Chaperone-assisted peptide exchange on MHC-I is driven by a negative allostery release cycle: Implications for a role of peptide-editing Molecular Chaperones in scrutinizing the peptide repertoire." Journal of Immunology 200, no. 1_Supplement (May 1, 2018): 99.23. http://dx.doi.org/10.4049/jimmunol.200.supp.99.23.
Повний текст джерелаTan, Ying, Ling Jiang, Manli Wang, Feifei Yin, Fei Deng, Maili Liu, Zhihong Hu, and Hualin Wang. "Mutagenesis and Nuclear Magnetic Resonance Analyses of the Fusion Peptide of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein." Journal of Virology 82, no. 16 (June 4, 2008): 8138–48. http://dx.doi.org/10.1128/jvi.00368-08.
Повний текст джерелаKim, Seongsoo, Sang-Myung Lee, Je Pil Yoon, Namhun Lee, Jinhyo Chung, Woo-Jae Chung, and Dong-Sik Shin. "Robust Magnetized Graphene Oxide Platform for In Situ Peptide Synthesis and FRET-Based Protease Detection." Sensors 20, no. 18 (September 15, 2020): 5275. http://dx.doi.org/10.3390/s20185275.
Повний текст джерелаPoluektov, Yuri, AeRyon Kim, and Scheherazade Sadegh-Nasseri. "HLA-DO and its effect on peptide binding to MHC Class II (106.29)." Journal of Immunology 188, no. 1_Supplement (May 1, 2012): 106.29. http://dx.doi.org/10.4049/jimmunol.188.supp.106.29.
Повний текст джерелаBrunel, Florence M., Michael B. Zwick, Rosa M. F. Cardoso, Josh D. Nelson, Ian A. Wilson, Dennis R. Burton, and Philip E. Dawson. "Structure-Function Analysis of the Epitope for 4E10, a Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody." Journal of Virology 80, no. 4 (February 15, 2006): 1680–87. http://dx.doi.org/10.1128/jvi.80.4.1680-1687.2006.
Повний текст джерелаCarmona, Adriana K., Maria Aparecida Juliano, and Luiz Juliano. "The use of Fluorescence Resonance Energy Transfer (FRET) peptidesfor measurement of clinically important proteolytic enzymes." Anais da Academia Brasileira de Ciências 81, no. 3 (September 2009): 381–92. http://dx.doi.org/10.1590/s0001-37652009000300005.
Повний текст джерелаMarsh, D. "Application of electron spin resonance for investigating peptide-lipid interactions, and correlation with thermodynamics." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 582–89. http://dx.doi.org/10.1042/bst0290582.
Повний текст джерелаFischer, Sebastian Nils, та Armin Geyer. "Assembly of synthetic Aβ miniamyloids on polyol templates". Beilstein Journal of Organic Chemistry 11 (17 грудня 2015): 2646–53. http://dx.doi.org/10.3762/bjoc.11.284.
Повний текст джерелаSHE, Wenchuan, Kui LUO, Bin HE, Hua AI, and ZHongwei GU. "FUNCTIONAL PEPTIDE DENDRIMERS AS MAGNETIC RESONANCE IMAGING PROBES." Acta Polymerica Sinica 011, no. 2 (February 18, 2011): 157–65. http://dx.doi.org/10.3724/sp.j.1105.2011.10027.
Повний текст джерелаJiJi, Renee D., Jian Xiong, and Mingjuan Wang. "Ultraviolet Resonance Raman Studies of a Disordered Peptide." Biophysical Journal 100, no. 3 (February 2011): 202a. http://dx.doi.org/10.1016/j.bpj.2010.12.1316.
Повний текст джерелаGorbenko, Galyna, Hiroyuki Saito, Julian Molotkovsky, Masafumi Tanaka, Masashi Egashira, Minoru Nakano, and Tetsurou Handa. "Resonance energy transfer study of peptide–lipid complexes." Biophysical Chemistry 92, no. 3 (September 2001): 155–68. http://dx.doi.org/10.1016/s0301-4622(01)00195-8.
Повний текст джерелаKaras, John A., David W. Keizer, and Marc-Antoine Sani. "Nuclear Magnetic Resonance Study of the Peptide FRANCESSEPAROVIC." Australian Journal of Chemistry 73, no. 3 (2020): 158. http://dx.doi.org/10.1071/ch19357.
Повний текст джерелаKota, S., C. Coito, G. Mousseau, J. P. Lavergne, and A. D. Strosberg. "Peptide inhibitors of hepatitis C virus core oligomerization and virus production." Journal of General Virology 90, no. 6 (June 1, 2009): 1319–28. http://dx.doi.org/10.1099/vir.0.008565-0.
Повний текст джерелаHunter, Howard N., A. Ross Demcoe, Håvard Jenssen, Tore J. Gutteberg, and Hans J. Vogel. "Human Lactoferricin Is Partially Folded in Aqueous Solution and Is Better Stabilized in a Membrane Mimetic Solvent." Antimicrobial Agents and Chemotherapy 49, no. 8 (August 2005): 3387–95. http://dx.doi.org/10.1128/aac.49.8.3387-3395.2005.
Повний текст джерелаKim, Minseon, Jinyoung Son, and Yongae Kim. "Structural and Mechanismic Studies of Lactophoricin Analog, Novel Antibacterial Peptide." International Journal of Molecular Sciences 22, no. 7 (April 2, 2021): 3734. http://dx.doi.org/10.3390/ijms22073734.
Повний текст джерелаCantisani, Marco, Marilisa Leone, Eleonora Mignogna, Katerina Kampanaraki, Annarita Falanga, Giancarlo Morelli, Massimiliano Galdiero, and Stefania Galdiero. "Structure-Activity Relations of Myxinidin, an Antibacterial Peptide Derived from the Epidermal Mucus of Hagfish." Antimicrobial Agents and Chemotherapy 57, no. 11 (September 3, 2013): 5665–73. http://dx.doi.org/10.1128/aac.01341-13.
Повний текст джерелаPastori, Claudia, Alberto Clivio, Lorenzo Diomede, Roberto Consonni, Giacomo M. S. De Mori, Renato Longhi, Giorgio Colombo, and Lucia Lopalco. "Two Amino Acid Substitutions within the First External Loop of CCR5 Induce Human Immunodeficiency Virus-Blocking Antibodies in Mice and Chickens." Journal of Virology 82, no. 8 (February 6, 2008): 4125–34. http://dx.doi.org/10.1128/jvi.02232-07.
Повний текст джерелаHosseinzadeh, Parisa, Gaurav Bhardwaj, Vikram Khipple Mulligan, Matthew D. Shortridge, Timothy W. Craven, Fátima Pardo-Avila, Stephen A. Rettie, et al. "Comprehensive computational design of ordered peptide macrocycles." Science 358, no. 6369 (December 14, 2017): 1461–66. http://dx.doi.org/10.1126/science.aap7577.
Повний текст джерелаTkach, Igor, Ulf Diederichsen, and Marina Bennati. "Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels." European Biophysics Journal 50, no. 2 (February 28, 2021): 143–57. http://dx.doi.org/10.1007/s00249-021-01508-6.
Повний текст джерелаWentink, Madelon Q., Tilman M. Hackeng, Sebastien P. Tabruyn, Wouter C. Puijk, Klaus Schwamborn, Daniele Altschuh, Rob H. Meloen, Teun Schuurman, Arjan W. Griffioen, and Peter Timmerman. "Targeted vaccination against the bevacizumab binding site on VEGF using 3D-structured peptides elicits efficient antitumor activity." Proceedings of the National Academy of Sciences 113, no. 44 (October 17, 2016): 12532–37. http://dx.doi.org/10.1073/pnas.1610258113.
Повний текст джерелаWohlhueter, R. M., K. Parekh, V. Udhayakumar, S. Fang, and A. A. Lal. "Analysis of binding of monoclonal antibody to a malarial peptide by surface plasmon resonance biosensor and integrated rate equations." Journal of Immunology 153, no. 1 (July 1, 1994): 181–89. http://dx.doi.org/10.4049/jimmunol.153.1.181.
Повний текст джерелаLu, Hongyan, Li Fang, Xiyan Wang, Dan Wu, Chunlei Liu, Xiaoting Liu, Ji Wang, Yawen Gao, and Weihong Min. "Structure-Activity Relationship of Pine Nut-Derived Peptides and Their Protective Effect on Nerve-Cell Mitochondria." Foods 11, no. 10 (May 15, 2022): 1428. http://dx.doi.org/10.3390/foods11101428.
Повний текст джерелаYoo, Jingon, Soobin Han, Bumjun Park, Sonam Sonwal, Munirah Alhammadi, Eunsu Kim, Sheik Aliya, et al. "Highly Specific Peptide-Mediated Cuvette-Form Localized Surface Plasmon Resonance (LSPR)-Based Fipronil Detection in Egg." Biosensors 12, no. 11 (October 23, 2022): 914. http://dx.doi.org/10.3390/bios12110914.
Повний текст джерелаSon, Woo-Sung, Ji-Sun Kim, Hyung-Eun Kim, Sang-Ho Park, and Bong-Jin Lee. "Structural studies on the antimicrobial peptide Brevinin 1E by spectroscopic methods." Spectroscopy 17, no. 2-3 (2003): 127–38. http://dx.doi.org/10.1155/2003/650369.
Повний текст джерелаLarive, Cynthia K., Dimuthu Jayawickrama, and Laszlo Orfi. "Quantitative Analysis of Peptides with NMR Spectroscopy." Applied Spectroscopy 51, no. 10 (October 1997): 1531–36. http://dx.doi.org/10.1366/0003702971939055.
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