Artículos de revistas sobre el tema "Hélice polyproline de type II"
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Zagrovic, B., J. Lipfert, E. J. Sorin, et al. "Unusual compactness of a polyproline type II structure." Proceedings of the National Academy of Sciences 102, no. 33 (2005): 11698–703. http://dx.doi.org/10.1073/pnas.0409693102.
Texto completovan Holst, G. J., S. R. Martin, A. K. Allen, D. Ashford, N. N. Desai, and A. Neuberger. "Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism." Biochemical Journal 233, no. 3 (1986): 731–36. http://dx.doi.org/10.1042/bj2330731.
Texto completoKubyshkin, Vladimir, and Nediljko Budisa. "Construction of a polyproline structure with hydrophobic exterior using octahydroindole-2-carboxylic acid." Organic & Biomolecular Chemistry 15, no. 3 (2017): 619–27. http://dx.doi.org/10.1039/c6ob02306a.
Texto completoLam, Sik Lok, and Victor L. Hsu. "NMR identification of left-handed polyproline type II helices." Biopolymers 69, no. 2 (2003): 270–81. http://dx.doi.org/10.1002/bip.10354.
Texto completoSong, Jikui, Jered V. McGivern, Karl W. Nichols, John L. Markley, and Michael D. Sheets. "Structural basis for RNA recognition by a type II poly(A)-binding protein." Proceedings of the National Academy of Sciences 105, no. 40 (2008): 15317–22. http://dx.doi.org/10.1073/pnas.0801274105.
Texto completoVlasov, Peter K., Anna V. Vlasova, Vladimir G. Tumanyan, and Natalia G. Esipova. "A tetrapeptide-based method for polyproline II-type secondary structure prediction." Proteins: Structure, Function, and Bioinformatics 61, no. 4 (2005): 763–68. http://dx.doi.org/10.1002/prot.20670.
Texto completoDoose, S., H. Neuweiler, H. Barsch, and M. Sauer. "Probing polyproline structure and dynamics by photoinduced electron transfer provides evidence for deviations from a regular polyproline type II helix." Proceedings of the National Academy of Sciences 104, no. 44 (2007): 17400–17405. http://dx.doi.org/10.1073/pnas.0705605104.
Texto completoSrinivasan, Mythily, and A. Keith Dunker. "Proline Rich Motifs as Drug Targets in Immune Mediated Disorders." International Journal of Peptides 2012 (May 16, 2012): 1–14. http://dx.doi.org/10.1155/2012/634769.
Texto completoVlasov, P. K., A. V. Budzko, M. A. Rubin, V. G. Tumanyan, A. A. Makarov, and N. G. Esipova. "Left-handed helix of polyproline ii type in linker regions of DNA-binding proteins." Biophysics 53, no. 6 (2008): 663–64. http://dx.doi.org/10.1134/s0006350908060353.
Texto completoMazuryk, Jarosław, Izabela Puchalska, Kamil Koziński, et al. "PTD4 Peptide Increases Neural Viability in an In Vitro Model of Acute Ischemic Stroke." International Journal of Molecular Sciences 22, no. 11 (2021): 6086. http://dx.doi.org/10.3390/ijms22116086.
Texto completoSiermala, Markku, Martti Juhola, and Mauno Vihinen. "On preprocessing of protein sequences for neural network prediction of polyproline type II secondary structures." Computers in Biology and Medicine 31, no. 5 (2001): 385–98. http://dx.doi.org/10.1016/s0010-4825(01)00013-0.
Texto completoSchweitzer-Stenner, Reinhard, Bridget Milorey, and Harald Schwalbe. "Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues." Biomolecules 12, no. 5 (2022): 684. http://dx.doi.org/10.3390/biom12050684.
Texto completoFeng, Chuang, Zhen Wang, Guokun Li, Xiaohan Yang, Nannan Wu, and Lei Wang. "BERT-PPII: The Polyproline Type II Helix Structure Prediction Model Based on BERT and Multichannel CNN." BioMed Research International 2022 (August 24, 2022): 1–14. http://dx.doi.org/10.1155/2022/9015123.
Texto completoPilpel, Yair, Oren Bogin, Vlad Brumfeld, and Ziv Reich. "Polyproline Type II Conformation in the C-Terminal Domain of the Nuclear Pore Complex Protein gp210†." Biochemistry 42, no. 12 (2003): 3519–26. http://dx.doi.org/10.1021/bi0266176.
Texto completoCutini, Michele, Marta Corno, Dominique Costa, and Piero Ugliengo. "How Does Collagen Adsorb on Hydroxyapatite? Insights From Ab Initio Simulations on a Polyproline Type II Model." Journal of Physical Chemistry C 123, no. 13 (2017): 7540–50. http://dx.doi.org/10.1021/acs.jpcc.7b10013.
Texto completoPerczel, András, Ödön Farkas, Imre G. Csizmadia, and Attila G. Császar. "Peptide models XX. Aromatic side-chain–backbone interaction in phenylalanine-containing diamide model system. A systematic search for the identification of all the ab initio conformers of N-formyl-L-phenylalanine-amide." Canadian Journal of Chemistry 75, no. 8 (1997): 1120–30. http://dx.doi.org/10.1139/v97-134.
Texto completoRenugopalakrishnan, V., L. A. Carreira, T. W. Collette, J. C. Dobbs, G. Chandraksasan, and R. C. Lord. "Non-Uniform Triple Helical Structure in Chick Skin Type I Collagen on Thermal Denaturation: Raman Spectroscopic Study." Zeitschrift für Naturforschung C 53, no. 5-6 (1998): 383–88. http://dx.doi.org/10.1515/znc-1998-5-613.
Texto completoSiermala, M., M. Juhola, and M. Vihinen. "On Postprocessing of Neural Network Prediction of Polyproline Type II Secondary Structures: Network Spectrum, Response Analysis, and Scattering." Neural Computing & Applications 11, no. 3-4 (2003): 238–43. http://dx.doi.org/10.1007/s00521-003-0360-5.
Texto completoReuter, Cédric, Robert Opitz, Arne Soicke, et al. "Design and Stereoselective Synthesis of ProM-2: A Spirocyclic Diproline Mimetic with Polyproline Type II (PPII) Helix Conformation." Chemistry - A European Journal 21, no. 23 (2015): 8464–70. http://dx.doi.org/10.1002/chem.201406493.
Texto completoPazderková, Markéta, Eva Kočišová, Tomáš Pazderka, et al. "Antimicrobial Peptide from the Eusocial BeeHalictus sexcinctusInteracting with Model Membranes." Spectroscopy: An International Journal 27 (2012): 497–502. http://dx.doi.org/10.1155/2012/840956.
Texto completoAlte, F., A. Stengel, J. P. Benz, et al. "Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner." Proceedings of the National Academy of Sciences 107, no. 45 (2010): 19260–65. http://dx.doi.org/10.1073/pnas.1009124107.
Texto completoIshijima, J., N. Nagasaki, M. Maeshima, and M. Miyano. "RVCaB, a Calcium-binding Protein in Radish Vacuoles, is Predominantly an Unstructured Protein with a Polyproline Type II Helix." Journal of Biochemistry 142, no. 2 (2007): 201–11. http://dx.doi.org/10.1093/jb/mvm130.
Texto completoBhagwanth, Swapna, Ram K. Mishra, and Rodney L. Johnson. "Development of peptidomimetic ligands of Pro-Leu-Gly-NH2 as allosteric modulators of the dopamine D2 receptor." Beilstein Journal of Organic Chemistry 9 (January 30, 2013): 204–14. http://dx.doi.org/10.3762/bjoc.9.24.
Texto completoScholl, Connor L., Sakae Tsuda, Laurie A. Graham, and Peter L. Davies. "Crystal waters on the nine polyproline type II helical bundle springtail antifreeze protein from Granisotoma rainieri match the ice lattice." FEBS Journal 288, no. 14 (2021): 4332–47. http://dx.doi.org/10.1111/febs.15717.
Texto completoEsipova, N. G., L. E. Ragulina, L. I. Davydova та ін. "Left helix of polyproline II type and genesis of β-structures in spidroins 1 and 2 and their recombinant analogs". Biophysics 54, № 3 (2009): 271–74. http://dx.doi.org/10.1134/s0006350909030014.
Texto completoReuter, Cédric, Peter Huy, Jörg-Martin Neudörfl, Ronald Kühne, and Hans-Günther Schmalz. "Exercises in Pyrrolidine Chemistry: Gram Scale Synthesis of a Pro-Pro Dipeptide Mimetic with a Polyproline Type II Helix Conformation." Chemistry - A European Journal 17, no. 43 (2011): 12037–44. http://dx.doi.org/10.1002/chem.201101704.
Texto completoMeirson, Tomer, David Bomze, Gal Markel та Abraham O. Samson. "κ-helix and the helical lock and key model: a pivotal way of looking at polyproline II". Bioinformatics 36, № 12 (2020): 3726–32. http://dx.doi.org/10.1093/bioinformatics/btaa186.
Texto completoMacDougall, Lindsay K., Mary Elizabeth Gagou, Sally J. Leevers, Ernst Hafen, and Michael D. Waterfield. "Targeted Expression of the Class II Phosphoinositide 3-Kinase in Drosophila melanogaster Reveals Lipid Kinase-Dependent Effects on Patterning and Interactions with Receptor Signaling Pathways." Molecular and Cellular Biology 24, no. 2 (2004): 796–808. http://dx.doi.org/10.1128/mcb.24.2.796-808.2004.
Texto completoRaghavan, Bhooma, Kevin J. Skoblenick, Swapna Bhagwanth, Niran Argintaru, Ram K. Mishra та Rodney L. Johnson. "Allosteric Modulation of the Dopamine D2Receptor by Pro-Leu-Gly-NH2Peptidomimetics Constrained in Either a Polyproline II Helix or a Type II β-Turn Conformation". Journal of Medicinal Chemistry 52, № 7 (2009): 2043–51. http://dx.doi.org/10.1021/jm801575w.
Texto completoBhatnagar, Rajendra S., Mark B. Shattuck, Jing Jing Qian, Craig A. Gough, and Steven B. Nicoll. "Theoretical and Experimental Approaches to Identification of a Fiber Surface Cell Binding Domain in Collagen and its Application in Tissue Engineering." Microscopy and Microanalysis 6, S2 (2000): 986–87. http://dx.doi.org/10.1017/s1431927600037429.
Texto completoGautam, Gunjan, Syed Arif Abdul Rehman, Preeti Pandey, and Samudrala Gourinath. "Crystal structure of the PEG-bound SH3 domain of myosin IB fromEntamoeba histolyticareveals its mode of ligand recognition." Acta Crystallographica Section D Structural Biology 73, no. 8 (2017): 672–82. http://dx.doi.org/10.1107/s2059798317009639.
Texto completoBeausoleil, Eric, and William D. Lubell. "An examination of the steric effects of 5-tert-butylproline on the conformation of polyproline and the cooperative nature of type II to type I helical interconversion." Biopolymers 53, no. 3 (2000): 249–56. http://dx.doi.org/10.1002/(sici)1097-0282(200003)53:3<249::aid-bip4>3.0.co;2-j.
Texto completoRowińska-Żyrek, Magdalena, Anna Wiȩch, Joanna Wa̧tły, et al. "Copper(II)-Binding Induces a Unique Polyproline Type II Helical Structure within the Ion-Binding Segment in the Intrinsically Disordered F-Domain of Ecdysteroid Receptor from Aedes aegypti." Inorganic Chemistry 58, no. 17 (2019): 11782–92. http://dx.doi.org/10.1021/acs.inorgchem.9b01826.
Texto completoSrinivasan, Mythily, Richard M. Wardrop, Ingrid E. Gienapp, Scott S. Stuckman, Caroline C. Whitacre, and Pravin T. P. Kaumaya. "A Retro-Inverso Peptide Mimic of CD28 Encompassing the MYPPPY Motif Adopts a Polyproline Type II Helix and Inhibits Encephalitogenic T Cells In Vitro." Journal of Immunology 167, no. 1 (2001): 578–85. http://dx.doi.org/10.4049/jimmunol.167.1.578.
Texto completoBrown, Alaina M., and Neal J. Zondlo. "A Propensity Scale for Type II Polyproline Helices (PPII): Aromatic Amino Acids in Proline-Rich Sequences Strongly Disfavor PPII Due to Proline–Aromatic Interactions." Biochemistry 51, no. 25 (2012): 5041–51. http://dx.doi.org/10.1021/bi3002924.
Texto completoAhmed, Shubbir, Anshuman Shukla та Purnananda Guptasarma. "Folding behavior of a backbone-reversed protein: Reversible polyproline type II to β-sheet thermal transitions in retro-GroES multimers with GroES-like features". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784, № 6 (2008): 916–23. http://dx.doi.org/10.1016/j.bbapap.2008.02.009.
Texto completoBatkhishig, Dashdavaa, Khurelbaatar Bilguun, Purevjav Enkhbayar, Hiroki Miyashita, Robert H. Kretsinger та Norio Matsushima. "Super Secondary Structure Consisting of a Polyproline II Helix and a β-Turn in Leucine Rich Repeats in Bacterial Type III Secretion System Effectors". Protein Journal 37, № 3 (2018): 223–36. http://dx.doi.org/10.1007/s10930-018-9767-9.
Texto completoKurz, E. M., T. W. Holstein, B. M. Petri, J. Engel, and C. N. David. "Mini-collagens in hydra nematocytes." Journal of Cell Biology 115, no. 4 (1991): 1159–69. http://dx.doi.org/10.1083/jcb.115.4.1159.
Texto completoCaporale, Andrea, Simone Adorinni, Doriano Lamba, and Michele Saviano. "Peptide–Protein Interactions: From Drug Design to Supramolecular Biomaterials." Molecules 26, no. 5 (2021): 1219. http://dx.doi.org/10.3390/molecules26051219.
Texto completoTop, Deniz, Jolene A. Read, Sandra J. Dawe, Raymond T. Syvitski, and Roy Duncan. "Cell-Cell Membrane Fusion Induced by p15 Fusion-associated Small Transmembrane (FAST) Protein Requires a Novel Fusion Peptide Motif Containing a Myristoylated Polyproline Type II Helix." Journal of Biological Chemistry 287, no. 5 (2011): 3403–14. http://dx.doi.org/10.1074/jbc.m111.305268.
Texto completoAdolph, Dörte, Nadine Flach, Katharina Mueller, Dirk H. Ostareck, and Antje Ostareck-Lederer. "Deciphering the Cross Talk between hnRNP K and c-Src: the c-Src Activation Domain in hnRNP K Is Distinct from a Second Interaction Site." Molecular and Cellular Biology 27, no. 5 (2006): 1758–70. http://dx.doi.org/10.1128/mcb.02014-06.
Texto completoStoddart, Cheryl A., Romas Geleziunas, Sharon Ferrell, et al. "Human Immunodeficiency Virus Type 1 Nef-Mediated Downregulation of CD4 Correlates with Nef Enhancement of Viral Pathogenesis." Journal of Virology 77, no. 3 (2003): 2124–33. http://dx.doi.org/10.1128/jvi.77.3.2124-2133.2003.
Texto completoNobuhisa, Ikuo, Ryu Takeya, Kenji Ogura та ін. "Activation of the superoxide-producing phagocyte NADPH oxidase requires co-operation between the tandem SH3 domains of p47phox in recognition of a polyproline type II helix and an adjacent α-helix of p22phox". Biochemical Journal 396, № 1 (2006): 183–92. http://dx.doi.org/10.1042/bj20051899.
Texto completoMucha, Piotr, Emilia Sikorska, Piotr Rekowski, and Jarosław Ruczyński. "Interaction of Arginine-Rich Cell-Penetrating Peptides with an Artificial Neuronal Membrane." Cells 11, no. 10 (2022): 1638. http://dx.doi.org/10.3390/cells11101638.
Texto completoTahoun, Amin, Gabriella Siszler, Kevin Spears, et al. "Comparative Analysis of EspF Variants in Inhibition of Escherichia coli Phagocytosis by Macrophages and Inhibition of E. coli Translocation through Human- and Bovine-Derived M Cells." Infection and Immunity 79, no. 11 (2011): 4716–29. http://dx.doi.org/10.1128/iai.00023-11.
Texto completoLewitzky, Marc, Maria Harkiolaki, Marie-Charlotte Domart, E. Yvonne Jones, and Stephan M. Feller. "Mona/Gads SH3C Binding to Hematopoietic Progenitor Kinase 1 (HPK1) Combines an Atypical SH3 Binding Motif, R/KXXK, with a Classical PXXP Motif Embedded in a Polyproline Type II (PPII) Helix." Journal of Biological Chemistry 279, no. 27 (2004): 28724–32. http://dx.doi.org/10.1074/jbc.m402745200.
Texto completoKeller, Rob C. A., and Wolf Frits A. de. "Physical-chemical characterization of thermoreversible gelatin helices." Industrial Proteins 4 (January 1, 1997): 14–15. https://doi.org/10.5281/zenodo.3229208.
Texto completoLokes, K. P., D. S. Avetikov, S. O. Stavitsky, O. O. Rozkolupa, and N. S. Lutsenko. "THE FEATURES OF THE FACE SKIN CONSTRUCTION THAT INFLUENCE ON THE FORMATION OF CICATRICAL TISSUES DURING SUGICAL INTERVENTIONS." Ukrainian Dental Almanac, no. 4 (December 26, 2019): 19–23. http://dx.doi.org/10.31718/2409-0255.4.2019.03.
Texto completoPanjarian, Shoghag, Shugui Chen, John Engen, and Thomas Smithgall. "Enhanced SH3:Linker Interaction Suppresses Activating Mutations of the c-Abl Protein-Tyrosine Kinase." Blood 116, no. 21 (2010): 1208. http://dx.doi.org/10.1182/blood.v116.21.1208.1208.
Texto completoCayrou, Chloé, Astrid Walrant, Delphine Ravault, et al. "Incorporation of CF3-pseudoprolines into polyproline type II foldamers confers promising biophysical features." Chemical Communications, 2024. http://dx.doi.org/10.1039/d4cc02895c.
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