Статті в журналах з теми "Hybrid Peptide Helices"
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Misra, Rajkumar, Gijo George, Rahi M. Reja, Sanjit Dey, Srinivasarao Raghothama та Hosahudya N. Gopi. "Structural insight into hybrid peptide ε-helices". Chemical Communications 56, № 14 (2020): 2171–73. http://dx.doi.org/10.1039/c9cc07413a.
Повний текст джерелаAnanda, Kuppanna, Prema G. Vasudev, Anindita Sengupta, K. Muruga Poopathi Raja, Narayanaswamy Shamala, and Padmanabhan Balaram. "Polypeptide Helices in Hybrid Peptide Sequences." Journal of the American Chemical Society 127, no. 47 (November 2005): 16668–74. http://dx.doi.org/10.1021/ja055799z.
Повний текст джерелаSastry, Mallika, Christopher Brown, Gerhard Wagner та Thomas D. Clark. "Cyclic Peptide Helices: A Hybrid β-Hairpin/β-Helical Supersecondary Structure". Journal of the American Chemical Society 128, № 33 (серпень 2006): 10650–51. http://dx.doi.org/10.1021/ja062737f.
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 джерелаBandyopadhyay, Anupam, та Hosahudya N. Gopi. "Hybrid Peptides: Direct Transformation of α/α, β-Unsaturated γ-Hybrid Peptides to α/γ-Hybrid Peptide 12-Helices". Organic Letters 14, № 11 (18 травня 2012): 2770–73. http://dx.doi.org/10.1021/ol300987d.
Повний текст джерелаSchramm, Peter, Gangavaram V. M. Sharma та Hans-Jörg Hofmann. "Helix formation in β/δ-hybrid peptides: Correspondence between helices of different peptide foldamer classes". Biopolymers 94, № 3 (14 жовтня 2009): 279–91. http://dx.doi.org/10.1002/bip.21325.
Повний текст джерелаPullen, J. K., M. D. Tallquist, R. W. Melvold, and L. R. Pease. "Recognition of a single amino acid change on the surface of a major transplantation antigen is in the context of self peptide." Journal of Immunology 152, no. 7 (April 1, 1994): 3445–52. http://dx.doi.org/10.4049/jimmunol.152.7.3445.
Повний текст джерелаBandyopadhyay, Anupam, Sandip V. Jadhav та Hosahudya N. Gopi. "α/γ4-Hybrid peptide helices: synthesis, crystal conformations and analogy with the α-helix". Chemical Communications 48, № 57 (2012): 7170. http://dx.doi.org/10.1039/c2cc32911e.
Повний текст джерелаSmirnova, Evgeniya V., Tatiana V. Rakitina, George A. Saratov, Anna A. Kudriaeva, and Alexey A. Belogurov. "Deconvolution of the MBP-Bri2 Interaction by a Yeast Two Hybrid System and Synergy of the AlphaFold2 and High Ambiguity Driven Protein-Protein Docking." Crystals 12, no. 2 (January 28, 2022): 197. http://dx.doi.org/10.3390/cryst12020197.
Повний текст джерелаMisra, Rajkumar, Abhijith Saseendran, Gijo George, Kuruva Veeresh, K. Muruga Poopathi Raja, Srinivasarao Raghothama, Hans-Jörg Hofmann та Hosahudya N. Gopi. "Structural Dimorphism of Achiral α,γ-Hybrid Peptide Foldamers: Coexistence of 12- and 15/17-Helices". Chemistry - A European Journal 23, № 15 (14 лютого 2017): 3764–72. http://dx.doi.org/10.1002/chem.201605753.
Повний текст джерелаJadhav, Sandip V., Anupam Bandyopadhyay та Hosahudya N. Gopi. "Protein secondary structure mimetics: crystal conformations of α/γ4-hybrid peptide12-helices with proteinogenic side chains and their analogy with α- and β-peptide helices". Org. Biomol. Chem. 11, № 3 (2013): 509–14. http://dx.doi.org/10.1039/c2ob26805a.
Повний текст джерелаGanesh Kumar, Mothukuri, Varsha J. Thombare, Mona M. Katariya, Kuruva Veeresh, K. Muruga Poopathi Raja та Hosahudya N. Gopi. "Non-classical Helices withcisCarbon-Carbon Double Bonds in the Backbone: Structural Features of α,γ-Hybrid Peptide Foldamers". Angewandte Chemie International Edition 55, № 27 (6 червня 2016): 7847–51. http://dx.doi.org/10.1002/anie.201602861.
Повний текст джерелаGanesh Kumar, Mothukuri, Varsha J. Thombare, Mona M. Katariya, Kuruva Veeresh, K. Muruga Poopathi Raja та Hosahudya N. Gopi. "Non-classical Helices withcisCarbon-Carbon Double Bonds in the Backbone: Structural Features of α,γ-Hybrid Peptide Foldamers". Angewandte Chemie 128, № 27 (6 червня 2016): 7978–82. http://dx.doi.org/10.1002/ange.201602861.
Повний текст джерелаJadhav, Sandip V., Rajkumar Misra та Hosahudya N. Gopi. "Foldamers to Nanotubes: Influence of Amino Acid Side Chains in the Hierarchical Assembly of α,γ4-Hybrid Peptide Helices". Chemistry - A European Journal 20, № 50 (24 жовтня 2014): 16523–28. http://dx.doi.org/10.1002/chem.201404961.
Повний текст джерелаJagadeesh, Bharatam, Anabathula Prabhakar, Ganti Dattatreya Sarma, Srivari Chandrasekhar, Gudise Chandrashekar, Marepally Srinivasa Reddy та Bulusu Jagannadh. "Formation of left-handed helices in hybrid peptide oligomers with cis β-sugar amino acid and l-Ala as building blocks". Chem. Commun., № 4 (2007): 371–73. http://dx.doi.org/10.1039/b612058j.
Повний текст джерелаBeckers, W., L. Villa, S. Gonfloni, L. Castagnoli, S. M. Newton, G. Cesareni, and P. Ghiara. "Increasing the immunogenicity of protein antigens through the genetic insertion of VQGEESNDK sequence of human IL-1 beta into their sequence." Journal of Immunology 151, no. 4 (August 15, 1993): 1757–64. http://dx.doi.org/10.4049/jimmunol.151.4.1757.
Повний текст джерелаGuzzo-Pernell, Nancy, and Geoffrey W. Tregear. "Triple helical DNA formation by a hydrophobic oligonucleotide-peptide hybrid molecule." Australian Journal of Chemistry 53, no. 8 (2000): 699. http://dx.doi.org/10.1071/ch00114.
Повний текст джерелаMessaoudi, Ilhem, Joël LeMaoult, and Janko Nikolić-Z̆ugić. "The Mode of Ligand Recognition by Two Peptide:MHC Class I-Specific Monoclonal Antibodies." Journal of Immunology 163, no. 6 (September 15, 1999): 3286–94. http://dx.doi.org/10.4049/jimmunol.163.6.3286.
Повний текст джерелаJadhav, Sandip V., Rajkumar Misra, Sumeet K. Singh та Hosahudya N. Gopi. "Efficient Access to Enantiopure γ4-Amino Acids with Proteinogenic Side-Chains and Structural Investigation of γ4-Asn and γ4-Ser in Hybrid Peptide Helices". Chemistry - A European Journal 19, № 48 (21 жовтня 2013): 16256–62. http://dx.doi.org/10.1002/chem.201302732.
Повний текст джерелаBolger, Graeme B., George S. Baillie, Xiang Li, Martin J. Lynch, Pawel Herzyk, Ahmed Mohamed, Lisa High Mitchell та ін. "Scanning peptide array analyses identify overlapping binding sites for the signalling scaffold proteins, β-arrestin and RACK1, in cAMP-specific phosphodiesterase PDE4D5". Biochemical Journal 398, № 1 (27 липня 2006): 23–36. http://dx.doi.org/10.1042/bj20060423.
Повний текст джерелаSheppard, Hilary M., Janet C. Harries, Sagair Hussain, Charlotte Bevan, and David M. Heery. "Analysis of the Steroid Receptor Coactivator 1 (SRC1)-CREB Binding Protein Interaction Interface and Its Importance for the Function of SRC1." Molecular and Cellular Biology 21, no. 1 (January 1, 2001): 39–50. http://dx.doi.org/10.1128/mcb.21.1.39-50.2001.
Повний текст джерелаFalord, Mélanie, Gouzel Karimova, Aurélia Hiron, and Tarek Msadek. "GraXSR Proteins Interact with the VraFG ABC Transporter To Form a Five-Component System Required for Cationic Antimicrobial Peptide Sensing and Resistance in Staphylococcus aureus." Antimicrobial Agents and Chemotherapy 56, no. 2 (November 28, 2011): 1047–58. http://dx.doi.org/10.1128/aac.05054-11.
Повний текст джерелаDengler, Sebastian, Pradeep K. Mandal, Lars Allmendinger, Céline Douat, and Ivan Huc. "Conformational interplay in hybrid peptide–helical aromatic foldamer macrocycles." Chemical Science 12, no. 33 (2021): 11004–12. http://dx.doi.org/10.1039/d1sc03640h.
Повний текст джерелаLondoño, J. A., H. Gras-Masse, C. Dubeaux, A. Tartar, and P. Druilhe. "Secondary structure and immunogenicity of hybrid synthetic peptides derived from two Plasmodium falciparum pre-erythrocytic antigens." Journal of Immunology 145, no. 5 (September 1, 1990): 1557–63. http://dx.doi.org/10.4049/jimmunol.145.5.1557.
Повний текст джерелаFriedrich, Cornelius G., Armin Quentmeier, Frank Bardischewsky, Dagmar Rother, Regine Kraft, Susanne Kostka, and Heino Prinz. "Novel Genes Coding for Lithotrophic Sulfur Oxidation of Paracoccus pantotrophus GB17." Journal of Bacteriology 182, no. 17 (September 1, 2000): 4677–87. http://dx.doi.org/10.1128/jb.182.17.4677-4687.2000.
Повний текст джерелаParry, Christian, Guelaguetza Vazquez-meves, Andrey Ivanov, Xionghao Lin, Namita Kumari, and Sergei Nekhai. "Structure of human ferroportin (SLC40A1) inferred from mass spectrometry restraints." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 187.35. http://dx.doi.org/10.4049/jimmunol.202.supp.187.35.
Повний текст джерелаLane, Andrew N., and Terence C. Jenkins. "Thermodynamics of nucleic acids and their interactions with ligands." Quarterly Reviews of Biophysics 33, no. 3 (August 2000): 255–306. http://dx.doi.org/10.1017/s0033583500003632.
Повний текст джерелаKilgore, Nicole R., Karl Salzwedel, Mary Reddick, Graham P. Allaway, and Carl T. Wild. "Direct Evidence that C-Peptide Inhibitors of Human Immunodeficiency Virus Type 1 Entry Bind to the gp41 N-Helical Domain in Receptor-Activated Viral Envelope." Journal of Virology 77, no. 13 (July 1, 2003): 7669–72. http://dx.doi.org/10.1128/jvi.77.13.7669-7672.2003.
Повний текст джерелаFriedrich, Carol, Monisha G. Scott, Nedra Karunaratne, Hong Yan, and Robert E. W. Hancock. "Salt-Resistant Alpha-Helical Cationic Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 43, no. 7 (July 1, 1999): 1542–48. http://dx.doi.org/10.1128/aac.43.7.1542.
Повний текст джерелаArrighi, Romanico B. G., Chikashi Nakamura, Jun Miyake, Hilary Hurd, and J. Grant Burgess. "Design and Activity of Antimicrobial Peptides against Sporogonic-Stage Parasites Causing Murine Malarias." Antimicrobial Agents and Chemotherapy 46, no. 7 (July 2002): 2104–10. http://dx.doi.org/10.1128/aac.46.7.2104-2110.2002.
Повний текст джерелаYang, Yang, Di Wu, Chenxi Wang, Anshan Shan, Chongpeng Bi, Yanbing Li, and Wenping Gan. "Hybridization with Insect Cecropin A (1–8) Improve the Stability and Selectivity of Naturally Occurring Peptides." International Journal of Molecular Sciences 21, no. 4 (February 21, 2020): 1470. http://dx.doi.org/10.3390/ijms21041470.
Повний текст джерелаMarine, Jeannette E., Shuang Song, Xiaoli Liang, Matthew D. Watson та Jonathan G. Rudick. "Bundle-forming α-helical peptide–dendron hybrid". Chemical Communications 51, № 76 (2015): 14314–17. http://dx.doi.org/10.1039/c5cc05468k.
Повний текст джерелаGrammer, S. F., A. Sette, S. Colón, L. Walker, and R. Chesnut. "Identification of an HSV-1/HSV-2 cross-reactive T cell determinant." Journal of Immunology 145, no. 7 (October 1, 1990): 2249–53. http://dx.doi.org/10.4049/jimmunol.145.7.2249.
Повний текст джерелаBateman, J. F., S. Lamande, D. Chan, and W. G. Cole. "Peptide analysis of collagen produced from cDNA by transcription and translation in vitro." Biochemical Journal 245, no. 2 (July 15, 1987): 393–98. http://dx.doi.org/10.1042/bj2450393.
Повний текст джерелаHonisch, Claudia, Eugenio Ragazzi, Rohanah Hussain, John Brazier, Giuliano Siligardi, and Paolo Ruzza. "Interaction of a Short Peptide with G-Quadruplex-Forming Sequences: An SRCD and CD Study." Pharmaceutics 13, no. 8 (July 21, 2021): 1104. http://dx.doi.org/10.3390/pharmaceutics13081104.
Повний текст джерелаGoch, G., H. Kozłowska, A. Wójtowicz, and A. Bierzyński. "A comparative CD and fluorescence study of a series of model calcium-binding peptides." Acta Biochimica Polonica 46, no. 3 (September 30, 1999): 673–77. http://dx.doi.org/10.18388/abp.1999_4139.
Повний текст джерелаKubo, T., and M. Fujii. "Interaction of cationic -helical peptide with phoshporothioate DNA hybrid." Nucleic Acids Symposium Series 42, no. 1 (November 1, 1999): 167–68. http://dx.doi.org/10.1093/nass/42.1.167.
Повний текст джерелаJohnsborg, Ola, Per Eugen Kristiansen, Trinelise Blomqvist, and Leiv Sigve Håvarstein. "A Hydrophobic Patch in the Competence-Stimulating Peptide, a Pneumococcal Competence Pheromone, Is Essential for Specificity and Biological Activity." Journal of Bacteriology 188, no. 5 (March 1, 2006): 1744–49. http://dx.doi.org/10.1128/jb.188.5.1744-1749.2006.
Повний текст джерелаJohansson, J., G. Nilsson, R. Strömberg, B. Robertson, H. Jörnvall, and T. Curstedt. "Secondary structure and biophysical activity of synthetic analogues of the pulmonary surfactant polypeptide SP-C." Biochemical Journal 307, no. 2 (April 15, 1995): 535–41. http://dx.doi.org/10.1042/bj3070535.
Повний текст джерелаDutta, Arpita, Suven Das, Purak Das, Suvendu Maity, Prasanta Ghosh та Soumya Shankha Biswas. "Unique supramolecular assembly of a synthetic achiral α, γ-hybrid tripeptide". Zeitschrift für Kristallographie - Crystalline Materials 237, № 1-3 (1 березня 2022): 77–81. http://dx.doi.org/10.1515/zkri-2022-0002.
Повний текст джерелаSmith, Jessica M., John R. Frost та Rudi Fasan. "Designer macrocyclic organo-peptide hybrids inhibit the interaction between p53 and HDM2/X by accommodating a functional α-helix". Chem. Commun. 50, № 39 (2014): 5027–30. http://dx.doi.org/10.1039/c4cc01199f.
Повний текст джерелаRogers, Joseph M., Sunbum Kwon, Simon J. Dawson, Pradeep K. Mandal, Hiroaki Suga, and Ivan Huc. "Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids." Nature Chemistry 10, no. 4 (March 19, 2018): 405–12. http://dx.doi.org/10.1038/s41557-018-0007-x.
Повний текст джерелаAhmadi, Samaneh, Mohammad Bagher Shahsavani, Zohreh Tavaf, Rawayh Muslim Albaghlany, Ashutosh Kumar, Ali Akbar Moosavi-Movahedi, and Reza Yousefi. "A novel strategy for production of liraglutide precursor peptide and development of a new long-acting incretin mimic." PLOS ONE 17, no. 5 (May 2, 2022): e0266833. http://dx.doi.org/10.1371/journal.pone.0266833.
Повний текст джерелаMalik, Ankita, Mothukuri Ganesh Kumar, Anupam Bandyopadhyay та Hosahudya N. Gopi. "Helices with additional H-bonds: crystallographic conformations of α,γ-hybrid peptides helices composed of β-hydroxy γ-amino acids (statines)". Biopolymers 108, № 1 (січень 2017): e22978. http://dx.doi.org/10.1002/bip.22978.
Повний текст джерелаTomizaki, Kin-ya, Yuichi Yamaguchi, Naoyuki Tsukamoto та Takahito Imai. "α-Helical Peptide-Gold Nanoparticle Hybrids: Synthesis, Characterization, and Catalytic Activity". Protein & Peptide Letters 25, № 1 (18 квітня 2018): 56–63. http://dx.doi.org/10.2174/0929866525666171214113324.
Повний текст джерелаBarkley, Deborah A., Yekaterina Rokhlenko, Jeannette E. Marine, Rachelle David, Dipankar Sahoo, Matthew D. Watson, Tadanori Koga, Chinedum O. Osuji та Jonathan G. Rudick. "Hexagonally Ordered Arrays of α-Helical Bundles Formed from Peptide-Dendron Hybrids". Journal of the American Chemical Society 139, № 44 (24 жовтня 2017): 15977–83. http://dx.doi.org/10.1021/jacs.7b09737.
Повний текст джерелаMarine, Jeannette E., Shuang Song, Xiaoli Liang та Jonathan G. Rudick. "Synthesis and Self-Assembly of Bundle-Forming α-Helical Peptide–Dendron Hybrids". Biomacromolecules 17, № 1 (23 грудня 2015): 336–44. http://dx.doi.org/10.1021/acs.biomac.5b01452.
Повний текст джерелаRogers, Joseph M., Sunbum Kwon, Simon J. Dawson, Pradeep K. Mandal, Hiroaki Suga, and Ivan Huc. "Publisher Correction: Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids." Nature Chemistry 10, no. 7 (May 31, 2018): 795. http://dx.doi.org/10.1038/s41557-018-0086-8.
Повний текст джерелаZhang, Licong, Dandan Wei, Na Zhan, Taotao Sun, Bingdong Shan та Anshan Shan. "Heterologous expression of the novel α-helical hybrid peptide PR-FO in Bacillus subtilis". Bioprocess and Biosystems Engineering 43, № 9 (29 квітня 2020): 1619–27. http://dx.doi.org/10.1007/s00449-020-02353-1.
Повний текст джерелаBalamurugan, Dhayalan, та Kannoth M. Muraleedharan. "Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β2,3-Hybrid Peptides". Chemistry - A European Journal 21, № 26 (15 травня 2015): 9332–38. http://dx.doi.org/10.1002/chem.201501198.
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