Статті в журналах з теми "Folded Peptides"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Folded Peptides".
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Venkatraman, Janani, Sasalu C. Shankaramma, and Padmanabhan Balaram. "Design of Folded Peptides†." Chemical Reviews 101, no. 10 (October 2001): 3131–52. http://dx.doi.org/10.1021/cr000053z.
Повний текст джерелаChatterjee, Sunanda, Rituparna Sinha Roy та P. Balaram. "Expanding the polypeptide backbone: hydrogen-bonded conformations in hybrid polypeptides containing the higher homologues of α-amino acids". Journal of The Royal Society Interface 4, № 15 (23 січня 2007): 587–606. http://dx.doi.org/10.1098/rsif.2006.0203.
Повний текст джерелаVenkatraman, Janani, Sasalu C. Shankaramma, and Padmanabhan Balaram. "ChemInform Abstract: Design of Folded Peptides." ChemInform 32, no. 52 (May 23, 2010): no. http://dx.doi.org/10.1002/chin.200152270.
Повний текст джерелаYuan, Xiushuang, Linhai Jiang, Weike Chen, Bo Song, Wei Chen, Xiaobing Zuo, Xiankai Sun, et al. "Self-assembly of chimeric peptides toward molecularly defined hexamers with controlled multivalent ligand presentation." Chemical Communications 56, no. 52 (2020): 7128–31. http://dx.doi.org/10.1039/d0cc02066d.
Повний текст джерелаSaini, Sunil Kumar, Katja Ostermeir, Venkat Raman Ramnarayan, Martin Zacharias, and Sebastian Springer. "Dipeptides enhance folding and peptide binding of “empty” MHC class I molecules (P5002)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 41.2. http://dx.doi.org/10.4049/jimmunol.190.supp.41.2.
Повний текст джерелаArai, Kenta, and Michio Iwaoka. "Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments." Molecules 26, no. 1 (January 2, 2021): 195. http://dx.doi.org/10.3390/molecules26010195.
Повний текст джерелаHuang, Sheng-Yu, Tin-Yu Wei, Bing-Shin Liu, Min-Han Lin, Sheng-Kuo Chiang, Sung-Fang Chen, and Wang-Chou Sung. "Monitoring the Disulfide Bonds of Folding Isomers of Synthetic CTX A3 Polypeptide Using MS-Based Technology." Toxins 11, no. 1 (January 17, 2019): 52. http://dx.doi.org/10.3390/toxins11010052.
Повний текст джерелаCalabrese, Antonio N., Lauren A. Speechley, and Tara L. Pukala. "Characterisation of Calmodulin Structural Transitions by Ion Mobility Mass Spectrometry." Australian Journal of Chemistry 65, no. 5 (2012): 504. http://dx.doi.org/10.1071/ch12047.
Повний текст джерелаMaurer, Carlo, Sascha Panahandeh, Anna-Carina Jungkamp, Michael Moser, and Matthias Müller. "TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins." Molecular Biology of the Cell 21, no. 23 (December 2010): 4151–61. http://dx.doi.org/10.1091/mbc.e10-07-0585.
Повний текст джерелаKraft, Jennifer R., Russell E. Vance, Jan Pohl, Amy M. Martin, David H. Raulet, and Peter E. Jensen. "Analysis of Qa-1bPeptide Binding Specificity and the Capacity of Cd94/Nkg2a to Discriminate between Qa-1–Peptide Complexes." Journal of Experimental Medicine 192, no. 5 (August 28, 2000): 613–24. http://dx.doi.org/10.1084/jem.192.5.613.
Повний текст джерелаFukugita, M., H. Kawai, T. Nakazawa, and Y. Okamoto. "Monte Carlo simulation for folded structure of peptides." Nuclear Physics B - Proceedings Supplements 20 (May 1991): 766–70. http://dx.doi.org/10.1016/0920-5632(91)91018-f.
Повний текст джерелаKelil, Abdellali, Emmanuel D. Levy, and Stephen W. Michnick. "Evolution of domain–peptide interactions to coadapt specificity and affinity to functional diversity." Proceedings of the National Academy of Sciences 113, no. 27 (June 17, 2016): E3862—E3871. http://dx.doi.org/10.1073/pnas.1518469113.
Повний текст джерелаHuang, Cheng-Hsin, Tong Wai Wong, Chen-Hsu Yu, Jing-Yuan Chang, Shing-Jong Huang, Shou-Ling Huang та Richard P. Cheng. "Swapping the Positions in a Cross-Strand Lateral Ion-Pairing Interaction between Ammonium- and Carboxylate-Containing Residues in a β-Hairpin". Molecules 26, № 5 (3 березня 2021): 1346. http://dx.doi.org/10.3390/molecules26051346.
Повний текст джерелаYap, Kuok, Junqiao Du, Fong Yang Looi, Shyn Ric Tang, Simon J. de Veer, Anuja R. Bony, Fabian B. H. Rehm, et al. "An environmentally sustainable biomimetic production of cyclic disulfide-rich peptides." Green Chemistry 22, no. 15 (2020): 5002–16. http://dx.doi.org/10.1039/d0gc01366h.
Повний текст джерелаHuang, Xueting, Chia-Hung Christine Hsiao, and Andrew J. Wiemer. "Discovery of TIGIT inhibitors by phage display." Journal of Immunology 210, no. 1_Supplement (May 1, 2023): 62.06. http://dx.doi.org/10.4049/jimmunol.210.supp.62.06.
Повний текст джерелаNiu, Hongyan, Meng-Ying Li, Yi-Lun Ying, and Yi-Tao Long. "An engineered third electrostatic constriction of aerolysin to manipulate heterogeneously charged peptide transport." Chemical Science 13, no. 8 (2022): 2456–61. http://dx.doi.org/10.1039/d1sc06459b.
Повний текст джерелаChakraborty, T. K., S. Jayaprakash, P. V. Diwan, R. Nagaraj, S. R. B. Jampani, and A. C. Kunwar. "Folded Conformation in Peptides Containing Furanoid Sugar Amino Acids." Journal of the American Chemical Society 120, no. 49 (December 1998): 12962–63. http://dx.doi.org/10.1021/ja9816685.
Повний текст джерелаCline, Lauren L., and Marcey L. Waters. "The structure of well-folded β-hairpin peptides promotes resistance to peptidase degradation." Biopolymers 92, no. 6 (2009): 502–7. http://dx.doi.org/10.1002/bip.21266.
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 джерелаSargent, F. "The twin-arginine transport system: moving folded proteins across membranes." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 835–47. http://dx.doi.org/10.1042/bst0350835.
Повний текст джерелаKotrba, Pavel, Lucie Dolečková, Víctor de Lorenzo, and Tomas Ruml. "Enhanced Bioaccumulation of Heavy Metal Ions by Bacterial Cells Due to Surface Display of Short Metal Binding Peptides." Applied and Environmental Microbiology 65, no. 3 (March 1, 1999): 1092–98. http://dx.doi.org/10.1128/aem.65.3.1092-1098.1999.
Повний текст джерелаChen, Charles H., Jakob P. Ulmschneider, and Martin B. Ulmschneider. "Mechanisms of a Small Membrane-Active Antimicrobial Peptide from Hyla punctata." Australian Journal of Chemistry 73, no. 3 (2020): 236. http://dx.doi.org/10.1071/ch19429.
Повний текст джерелаKhvotchev, Mikhail, and Mikhail Soloviev. "SNARE Modulators and SNARE Mimetic Peptides." Biomolecules 12, no. 12 (November 29, 2022): 1779. http://dx.doi.org/10.3390/biom12121779.
Повний текст джерелаLi, Nian-Zhi, Chen-Hsu Yu, Jhuan-Yu Wu, Shing-Jong Huang, Shou-Ling Huang та Richard P. Cheng. "Diagonal Interactions between Glutamate and Arginine Analogs with Varying Side-Chain Lengths in a β-Hairpin". Molecules 28, № 7 (23 березня 2023): 2888. http://dx.doi.org/10.3390/molecules28072888.
Повний текст джерелаWynn, Jessica E., and Webster L. Santos. "HIV-1 drug discovery: targeting folded RNA structures with branched peptides." Organic & Biomolecular Chemistry 13, no. 21 (2015): 5848–58. http://dx.doi.org/10.1039/c5ob00589b.
Повний текст джерелаPetkov, Peicho, Elena Lilkova, Nevena Ilieva, and Leandar Litov. "Self-Association of Antimicrobial Peptides: A Molecular Dynamics Simulation Study on Bombinin." International Journal of Molecular Sciences 20, no. 21 (November 1, 2019): 5450. http://dx.doi.org/10.3390/ijms20215450.
Повний текст джерелаNatarajan, Kannan, Jiansheng Jiang, Lisa F. Boyd, Giora I. Morozov, Michael G. Mage, and David H. Margulies. "Insights into MHC-I peptide loading obtained from the structure of a TAPBPR/MHC-I complex." Journal of Immunology 198, no. 1_Supplement (May 1, 2017): 146.25. http://dx.doi.org/10.4049/jimmunol.198.supp.146.25.
Повний текст джерелаChang, Jing-Yuan, Yen-Jin Pan, Pei-Yu Huang, Yi-Ting Sun, Chen-Hsu Yu, Zhi-Jun Ning, Shou-Ling Huang, Shing-Jong Huang та Richard P. Cheng. "The Effects of Charged Amino Acid Side-Chain Length on Diagonal Cross-Strand Interactions between Carboxylate- and Ammonium-Containing Residues in a β-Hairpin". Molecules 27, № 13 (29 червня 2022): 4172. http://dx.doi.org/10.3390/molecules27134172.
Повний текст джерелаBarre, Annick, Hervé Benoist та Pierre Rougé. "Impacts of Sourdough Technology on the Availability of Celiac Peptides from Wheat α- and γ-Gliadins: In Silico Approach". Allergies 3, № 1 (3 лютого 2023): 39–57. http://dx.doi.org/10.3390/allergies3010004.
Повний текст джерелаTaubert, Johannes, and Thomas Brüser. "Twin-arginine translocation-arresting protein regions contact TatA and TatB." Biological Chemistry 395, no. 7-8 (July 1, 2014): 827–36. http://dx.doi.org/10.1515/hsz-2014-0170.
Повний текст джерелаZhai, Luhan, Masayuki Nara, Yuko Otani та Tomohiko Ohwada. "Unexpectedly rigid short peptide foldamers in which NH–π and CH–π interactions are preserved in solution". Chemical Communications 57, № 67 (2021): 8344–47. http://dx.doi.org/10.1039/d1cc02998c.
Повний текст джерелаHuang, Qi, Felicity Alcock, Holger Kneuper, Justin C. Deme, Sarah E. Rollauer, Susan M. Lea, Ben C. Berks, and Tracy Palmer. "A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase." Proceedings of the National Academy of Sciences 114, no. 10 (February 21, 2017): E1958—E1967. http://dx.doi.org/10.1073/pnas.1615056114.
Повний текст джерелаByazrova, Maria, Pia Gattinger, Ekaterina Astakhova, Gerhard Hofer, Musa Khaitov, Alexander Filatov, and Rudolf Valenta. "Dissection of Antibody Responses of Gam-COVID-Vac-Vaccinated Subjects Suggests Involvement of Epitopes Outside RBD in SARS-CoV-2 Neutralization." International Journal of Molecular Sciences 24, no. 6 (March 7, 2023): 5104. http://dx.doi.org/10.3390/ijms24065104.
Повний текст джерелаMisra, Rajkumar, Rahi M. Reja, Lagumaddepalli V. Narendra, Gijo George, Srinivasarao Raghothama, and Hosahudya N. Gopi. "Exploring structural features of folded peptide architectures in the construction of nanomaterials." Chemical Communications 52, no. 61 (2016): 9597–600. http://dx.doi.org/10.1039/c6cc04502b.
Повний текст джерелаArdejani, Maziar S., Evan T. Powers, and Jeffery W. Kelly. "Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities." Accounts of Chemical Research 50, no. 8 (July 19, 2017): 1875–82. http://dx.doi.org/10.1021/acs.accounts.7b00195.
Повний текст джерелаSchröder, Bernd, and Paul Saftig. "Molecular insights into mechanisms of intramembrane proteolysis through signal peptide peptidase (SPP)." Biochemical Journal 427, no. 3 (April 14, 2010): e1-e3. http://dx.doi.org/10.1042/bj20100391.
Повний текст джерелаStroganova, Iuliia, Sjors Bakels, and Anouk M. Rijs. "Structural Properties of Phenylalanine-Based Dimers Revealed Using IR Action Spectroscopy." Molecules 27, no. 7 (April 6, 2022): 2367. http://dx.doi.org/10.3390/molecules27072367.
Повний текст джерелаZhang, Huixi Violet, Frank Polzer, Michael J. Haider, Yu Tian, Jose A. Villegas, Kristi L. Kiick, Darrin J. Pochan, and Jeffery G. Saven. "Computationally designed peptides for self-assembly of nanostructured lattices." Science Advances 2, no. 9 (September 2016): e1600307. http://dx.doi.org/10.1126/sciadv.1600307.
Повний текст джерелаNayar, Divya, and Charusita Chakravarty. "Sensitivity of local hydration behaviour and conformational preferences of peptides to choice of water model." Phys. Chem. Chem. Phys. 16, no. 21 (2014): 10199–213. http://dx.doi.org/10.1039/c3cp55147d.
Повний текст джерелаHallupp, M., F. Buck, and W. H. Strätling. "Structure analysis of purified histone H5 and of H5 in nuclei by limited proteolysis." Biochemical Journal 282, no. 2 (March 1, 1992): 435–41. http://dx.doi.org/10.1042/bj2820435.
Повний текст джерелаSOTERIADOU, Ketty P., Athina K. TZINIA, Evgenia PANOU-PAMONIS, Vassilias TSIKARIS, Maria SAKARELLOS-DAITSIOTIS, Constantinos SAKARELLOS, Youli PAPAPOULOU, and Rebecca MATSAS. "Antigenicity and conformational analysis of the Zn2+-binding sites of two Zn2+-metalloproteases: Leishmania gp63 and mammalian endopeptidase-24.11." Biochemical Journal 313, no. 2 (January 15, 1996): 455–66. http://dx.doi.org/10.1042/bj3130455.
Повний текст джерелаHaris, P. I. "Structural model of a voltage-gated potassium channel based on spectroscopic data." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 589–93. http://dx.doi.org/10.1042/bst0290589.
Повний текст джерелаvan der Ploeg, René, Carmine G. Monteferrante, Sjouke Piersma, James P. Barnett, Thijs R. H. M. Kouwen, Colin Robinson, and Jan Maarten van Dijl. "High-Salinity Growth Conditions Promote Tat-Independent Secretion of Tat Substrates in Bacillus subtilis." Applied and Environmental Microbiology 78, no. 21 (August 24, 2012): 7733–44. http://dx.doi.org/10.1128/aem.02093-12.
Повний текст джерелаWoodhead, Andrea, Andrew Church, Trevor Rapson, Holly Trueman, Jeffrey Church, and Tara Sutherland. "Confirmation of Bioinformatics Predictions of the Structural Domains in Honeybee Silk." Polymers 10, no. 7 (July 16, 2018): 776. http://dx.doi.org/10.3390/polym10070776.
Повний текст джерелаLukacik, Petra, C. David Owen, Gemma Harris, Jani Reddy Bolla, Sarah Picaud, Irfan Alibay, Joanne E. Nettleship, et al. "The structure of nontypeable Haemophilus influenzae SapA in a closed conformation reveals a constricted ligand-binding cavity and a novel RNA binding motif." PLOS ONE 16, no. 10 (October 15, 2021): e0256070. http://dx.doi.org/10.1371/journal.pone.0256070.
Повний текст джерелаLehmann, T. E., G. Kroon, H. J. Dyson, M. A. Lorenzo, H. Bermúdez, and H. Perez. "Plasmodium vivax CS peptides display conformational preferences for folded forms in solution." Journal of Peptide Research 61, no. 5 (March 28, 2003): 252–62. http://dx.doi.org/10.1034/j.1399-3011.2003.00055.x.
Повний текст джерелаHaridas, V., Sandhya Sadanandan, M. V. S. Gopalakrishna, M. B. Bijesh, Ram P. Verma, Srinivas Chinthalapalli, and Ashutosh Shandilya. "Bispidine as a helix inducing scaffold: examples of helically folded linear peptides." Chemical Communications 49, no. 93 (2013): 10980. http://dx.doi.org/10.1039/c3cc45649h.
Повний текст джерелаBhattacharjya, Surajit, Padmanabhan Balaram, Satish K. Awasthi, and P. Radhakantha Adiga. "Folded conformations of antigenic peptides from riboflavin carrier protein in aqueous hexafluoroacetone." Protein Science 7, no. 1 (January 1998): 123–31. http://dx.doi.org/10.1002/pro.5560070113.
Повний текст джерелаWani, Naiem Ahmad, Vivek Kumar Gupta, Umesh Prasad Singh, Subrayashastry Aravinda та Rajkishor Rai. "Folded Structure Stabilized by C7, C10and C12Hydrogen Bonds in αγ Hybrid Peptides". ChemistrySelect 1, № 8 (1 червня 2016): 1674–77. http://dx.doi.org/10.1002/slct.201600389.
Повний текст джерелаDröge, Melloney J., Ykelien L. Boersma, Peter G. Braun, Robbert Jan Buining, Mattijs K. Julsing, Karin G. A. Selles, Jan Maarten van Dijl, and Wim J. Quax. "Phage Display of an Intracellular Carboxylesterase of Bacillus subtilis: Comparison of Sec and Tat Pathway Export Capabilities." Applied and Environmental Microbiology 72, no. 7 (July 2006): 4589–95. http://dx.doi.org/10.1128/aem.02750-05.
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