Artículos de revistas sobre el tema "Folded Peptides"
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Venkatraman, Janani, Sasalu C. Shankaramma y Padmanabhan Balaram. "Design of Folded Peptides†". Chemical Reviews 101, n.º 10 (octubre de 2001): 3131–52. http://dx.doi.org/10.1021/cr000053z.
Texto completoChatterjee, Sunanda, Rituparna Sinha Roy y 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, n.º 15 (23 de enero de 2007): 587–606. http://dx.doi.org/10.1098/rsif.2006.0203.
Texto completoVenkatraman, Janani, Sasalu C. Shankaramma y Padmanabhan Balaram. "ChemInform Abstract: Design of Folded Peptides". ChemInform 32, n.º 52 (23 de mayo de 2010): no. http://dx.doi.org/10.1002/chin.200152270.
Texto completoYuan, 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, n.º 52 (2020): 7128–31. http://dx.doi.org/10.1039/d0cc02066d.
Texto completoSaini, Sunil Kumar, Katja Ostermeir, Venkat Raman Ramnarayan, Martin Zacharias y Sebastian Springer. "Dipeptides enhance folding and peptide binding of “empty” MHC class I molecules (P5002)". Journal of Immunology 190, n.º 1_Supplement (1 de mayo de 2013): 41.2. http://dx.doi.org/10.4049/jimmunol.190.supp.41.2.
Texto completoArai, Kenta y Michio Iwaoka. "Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments". Molecules 26, n.º 1 (2 de enero de 2021): 195. http://dx.doi.org/10.3390/molecules26010195.
Texto completoHuang, Sheng-Yu, Tin-Yu Wei, Bing-Shin Liu, Min-Han Lin, Sheng-Kuo Chiang, Sung-Fang Chen y Wang-Chou Sung. "Monitoring the Disulfide Bonds of Folding Isomers of Synthetic CTX A3 Polypeptide Using MS-Based Technology". Toxins 11, n.º 1 (17 de enero de 2019): 52. http://dx.doi.org/10.3390/toxins11010052.
Texto completoCalabrese, Antonio N., Lauren A. Speechley y Tara L. Pukala. "Characterisation of Calmodulin Structural Transitions by Ion Mobility Mass Spectrometry". Australian Journal of Chemistry 65, n.º 5 (2012): 504. http://dx.doi.org/10.1071/ch12047.
Texto completoMaurer, Carlo, Sascha Panahandeh, Anna-Carina Jungkamp, Michael Moser y Matthias Müller. "TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins". Molecular Biology of the Cell 21, n.º 23 (diciembre de 2010): 4151–61. http://dx.doi.org/10.1091/mbc.e10-07-0585.
Texto completoKraft, Jennifer R., Russell E. Vance, Jan Pohl, Amy M. Martin, David H. Raulet y 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, n.º 5 (28 de agosto de 2000): 613–24. http://dx.doi.org/10.1084/jem.192.5.613.
Texto completoFukugita, M., H. Kawai, T. Nakazawa y Y. Okamoto. "Monte Carlo simulation for folded structure of peptides". Nuclear Physics B - Proceedings Supplements 20 (mayo de 1991): 766–70. http://dx.doi.org/10.1016/0920-5632(91)91018-f.
Texto completoKelil, Abdellali, Emmanuel D. Levy y Stephen W. Michnick. "Evolution of domain–peptide interactions to coadapt specificity and affinity to functional diversity". Proceedings of the National Academy of Sciences 113, n.º 27 (17 de junio de 2016): E3862—E3871. http://dx.doi.org/10.1073/pnas.1518469113.
Texto completoHuang, Cheng-Hsin, Tong Wai Wong, Chen-Hsu Yu, Jing-Yuan Chang, Shing-Jong Huang, Shou-Ling Huang y 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, n.º 5 (3 de marzo de 2021): 1346. http://dx.doi.org/10.3390/molecules26051346.
Texto completoYap, 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, n.º 15 (2020): 5002–16. http://dx.doi.org/10.1039/d0gc01366h.
Texto completoHuang, Xueting, Chia-Hung Christine Hsiao y Andrew J. Wiemer. "Discovery of TIGIT inhibitors by phage display". Journal of Immunology 210, n.º 1_Supplement (1 de mayo de 2023): 62.06. http://dx.doi.org/10.4049/jimmunol.210.supp.62.06.
Texto completoNiu, Hongyan, Meng-Ying Li, Yi-Lun Ying y Yi-Tao Long. "An engineered third electrostatic constriction of aerolysin to manipulate heterogeneously charged peptide transport". Chemical Science 13, n.º 8 (2022): 2456–61. http://dx.doi.org/10.1039/d1sc06459b.
Texto completoChakraborty, T. K., S. Jayaprakash, P. V. Diwan, R. Nagaraj, S. R. B. Jampani y A. C. Kunwar. "Folded Conformation in Peptides Containing Furanoid Sugar Amino Acids". Journal of the American Chemical Society 120, n.º 49 (diciembre de 1998): 12962–63. http://dx.doi.org/10.1021/ja9816685.
Texto completoCline, Lauren L. y Marcey L. Waters. "The structure of well-folded β-hairpin peptides promotes resistance to peptidase degradation". Biopolymers 92, n.º 6 (2009): 502–7. http://dx.doi.org/10.1002/bip.21266.
Texto completoHunter, Howard N., A. Ross Demcoe, Håvard Jenssen, Tore J. Gutteberg y 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, n.º 8 (agosto de 2005): 3387–95. http://dx.doi.org/10.1128/aac.49.8.3387-3395.2005.
Texto completoSargent, F. "The twin-arginine transport system: moving folded proteins across membranes". Biochemical Society Transactions 35, n.º 5 (25 de octubre de 2007): 835–47. http://dx.doi.org/10.1042/bst0350835.
Texto completoKotrba, Pavel, Lucie Dolečková, Víctor de Lorenzo y 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, n.º 3 (1 de marzo de 1999): 1092–98. http://dx.doi.org/10.1128/aem.65.3.1092-1098.1999.
Texto completoChen, Charles H., Jakob P. Ulmschneider y Martin B. Ulmschneider. "Mechanisms of a Small Membrane-Active Antimicrobial Peptide from Hyla punctata". Australian Journal of Chemistry 73, n.º 3 (2020): 236. http://dx.doi.org/10.1071/ch19429.
Texto completoKhvotchev, Mikhail y Mikhail Soloviev. "SNARE Modulators and SNARE Mimetic Peptides". Biomolecules 12, n.º 12 (29 de noviembre de 2022): 1779. http://dx.doi.org/10.3390/biom12121779.
Texto completoLi, Nian-Zhi, Chen-Hsu Yu, Jhuan-Yu Wu, Shing-Jong Huang, Shou-Ling Huang y Richard P. Cheng. "Diagonal Interactions between Glutamate and Arginine Analogs with Varying Side-Chain Lengths in a β-Hairpin". Molecules 28, n.º 7 (23 de marzo de 2023): 2888. http://dx.doi.org/10.3390/molecules28072888.
Texto completoWynn, Jessica E. y Webster L. Santos. "HIV-1 drug discovery: targeting folded RNA structures with branched peptides". Organic & Biomolecular Chemistry 13, n.º 21 (2015): 5848–58. http://dx.doi.org/10.1039/c5ob00589b.
Texto completoPetkov, Peicho, Elena Lilkova, Nevena Ilieva y Leandar Litov. "Self-Association of Antimicrobial Peptides: A Molecular Dynamics Simulation Study on Bombinin". International Journal of Molecular Sciences 20, n.º 21 (1 de noviembre de 2019): 5450. http://dx.doi.org/10.3390/ijms20215450.
Texto completoNatarajan, Kannan, Jiansheng Jiang, Lisa F. Boyd, Giora I. Morozov, Michael G. Mage y David H. Margulies. "Insights into MHC-I peptide loading obtained from the structure of a TAPBPR/MHC-I complex". Journal of Immunology 198, n.º 1_Supplement (1 de mayo de 2017): 146.25. http://dx.doi.org/10.4049/jimmunol.198.supp.146.25.
Texto completoChang, Jing-Yuan, Yen-Jin Pan, Pei-Yu Huang, Yi-Ting Sun, Chen-Hsu Yu, Zhi-Jun Ning, Shou-Ling Huang, Shing-Jong Huang y 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, n.º 13 (29 de junio de 2022): 4172. http://dx.doi.org/10.3390/molecules27134172.
Texto completoBarre, Annick, Hervé Benoist y Pierre Rougé. "Impacts of Sourdough Technology on the Availability of Celiac Peptides from Wheat α- and γ-Gliadins: In Silico Approach". Allergies 3, n.º 1 (3 de febrero de 2023): 39–57. http://dx.doi.org/10.3390/allergies3010004.
Texto completoTaubert, Johannes y Thomas Brüser. "Twin-arginine translocation-arresting protein regions contact TatA and TatB". Biological Chemistry 395, n.º 7-8 (1 de julio de 2014): 827–36. http://dx.doi.org/10.1515/hsz-2014-0170.
Texto completoZhai, Luhan, Masayuki Nara, Yuko Otani y Tomohiko Ohwada. "Unexpectedly rigid short peptide foldamers in which NH–π and CH–π interactions are preserved in solution". Chemical Communications 57, n.º 67 (2021): 8344–47. http://dx.doi.org/10.1039/d1cc02998c.
Texto completoHuang, Qi, Felicity Alcock, Holger Kneuper, Justin C. Deme, Sarah E. Rollauer, Susan M. Lea, Ben C. Berks y 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, n.º 10 (21 de febrero de 2017): E1958—E1967. http://dx.doi.org/10.1073/pnas.1615056114.
Texto completoByazrova, Maria, Pia Gattinger, Ekaterina Astakhova, Gerhard Hofer, Musa Khaitov, Alexander Filatov y 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, n.º 6 (7 de marzo de 2023): 5104. http://dx.doi.org/10.3390/ijms24065104.
Texto completoMisra, Rajkumar, Rahi M. Reja, Lagumaddepalli V. Narendra, Gijo George, Srinivasarao Raghothama y Hosahudya N. Gopi. "Exploring structural features of folded peptide architectures in the construction of nanomaterials". Chemical Communications 52, n.º 61 (2016): 9597–600. http://dx.doi.org/10.1039/c6cc04502b.
Texto completoArdejani, Maziar S., Evan T. Powers y Jeffery W. Kelly. "Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities". Accounts of Chemical Research 50, n.º 8 (19 de julio de 2017): 1875–82. http://dx.doi.org/10.1021/acs.accounts.7b00195.
Texto completoSchröder, Bernd y Paul Saftig. "Molecular insights into mechanisms of intramembrane proteolysis through signal peptide peptidase (SPP)". Biochemical Journal 427, n.º 3 (14 de abril de 2010): e1-e3. http://dx.doi.org/10.1042/bj20100391.
Texto completoStroganova, Iuliia, Sjors Bakels y Anouk M. Rijs. "Structural Properties of Phenylalanine-Based Dimers Revealed Using IR Action Spectroscopy". Molecules 27, n.º 7 (6 de abril de 2022): 2367. http://dx.doi.org/10.3390/molecules27072367.
Texto completoZhang, Huixi Violet, Frank Polzer, Michael J. Haider, Yu Tian, Jose A. Villegas, Kristi L. Kiick, Darrin J. Pochan y Jeffery G. Saven. "Computationally designed peptides for self-assembly of nanostructured lattices". Science Advances 2, n.º 9 (septiembre de 2016): e1600307. http://dx.doi.org/10.1126/sciadv.1600307.
Texto completoNayar, Divya y Charusita Chakravarty. "Sensitivity of local hydration behaviour and conformational preferences of peptides to choice of water model". Phys. Chem. Chem. Phys. 16, n.º 21 (2014): 10199–213. http://dx.doi.org/10.1039/c3cp55147d.
Texto completoHallupp, M., F. Buck y W. H. Strätling. "Structure analysis of purified histone H5 and of H5 in nuclei by limited proteolysis". Biochemical Journal 282, n.º 2 (1 de marzo de 1992): 435–41. http://dx.doi.org/10.1042/bj2820435.
Texto completoSOTERIADOU, Ketty P., Athina K. TZINIA, Evgenia PANOU-PAMONIS, Vassilias TSIKARIS, Maria SAKARELLOS-DAITSIOTIS, Constantinos SAKARELLOS, Youli PAPAPOULOU y 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, n.º 2 (15 de enero de 1996): 455–66. http://dx.doi.org/10.1042/bj3130455.
Texto completoHaris, P. I. "Structural model of a voltage-gated potassium channel based on spectroscopic data". Biochemical Society Transactions 29, n.º 4 (1 de agosto de 2001): 589–93. http://dx.doi.org/10.1042/bst0290589.
Texto completovan der Ploeg, René, Carmine G. Monteferrante, Sjouke Piersma, James P. Barnett, Thijs R. H. M. Kouwen, Colin Robinson y Jan Maarten van Dijl. "High-Salinity Growth Conditions Promote Tat-Independent Secretion of Tat Substrates in Bacillus subtilis". Applied and Environmental Microbiology 78, n.º 21 (24 de agosto de 2012): 7733–44. http://dx.doi.org/10.1128/aem.02093-12.
Texto completoWoodhead, Andrea, Andrew Church, Trevor Rapson, Holly Trueman, Jeffrey Church y Tara Sutherland. "Confirmation of Bioinformatics Predictions of the Structural Domains in Honeybee Silk". Polymers 10, n.º 7 (16 de julio de 2018): 776. http://dx.doi.org/10.3390/polym10070776.
Texto completoLukacik, 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, n.º 10 (15 de octubre de 2021): e0256070. http://dx.doi.org/10.1371/journal.pone.0256070.
Texto completoLehmann, T. E., G. Kroon, H. J. Dyson, M. A. Lorenzo, H. Bermúdez y H. Perez. "Plasmodium vivax CS peptides display conformational preferences for folded forms in solution". Journal of Peptide Research 61, n.º 5 (28 de marzo de 2003): 252–62. http://dx.doi.org/10.1034/j.1399-3011.2003.00055.x.
Texto completoHaridas, V., Sandhya Sadanandan, M. V. S. Gopalakrishna, M. B. Bijesh, Ram P. Verma, Srinivas Chinthalapalli y Ashutosh Shandilya. "Bispidine as a helix inducing scaffold: examples of helically folded linear peptides". Chemical Communications 49, n.º 93 (2013): 10980. http://dx.doi.org/10.1039/c3cc45649h.
Texto completoBhattacharjya, Surajit, Padmanabhan Balaram, Satish K. Awasthi y P. Radhakantha Adiga. "Folded conformations of antigenic peptides from riboflavin carrier protein in aqueous hexafluoroacetone". Protein Science 7, n.º 1 (enero de 1998): 123–31. http://dx.doi.org/10.1002/pro.5560070113.
Texto completoWani, Naiem Ahmad, Vivek Kumar Gupta, Umesh Prasad Singh, Subrayashastry Aravinda y Rajkishor Rai. "Folded Structure Stabilized by C7, C10and C12Hydrogen Bonds in αγ Hybrid Peptides". ChemistrySelect 1, n.º 8 (1 de junio de 2016): 1674–77. http://dx.doi.org/10.1002/slct.201600389.
Texto completoDröge, Melloney J., Ykelien L. Boersma, Peter G. Braun, Robbert Jan Buining, Mattijs K. Julsing, Karin G. A. Selles, Jan Maarten van Dijl y 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, n.º 7 (julio de 2006): 4589–95. http://dx.doi.org/10.1128/aem.02750-05.
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