Статті в журналах з теми "Membrane proteins and peptides"
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Schrul, Bianca, Katja Kapp, Irmgard Sinning, and Bernhard Dobberstein. "Signal peptide peptidase (SPP) assembles with substrates and misfolded membrane proteins into distinct oligomeric complexes." Biochemical Journal 427, no. 3 (April 14, 2010): 523–34. http://dx.doi.org/10.1042/bj20091005.
Повний текст джерелаMartin, Isabelle, and Jean-Marie Ruysschaert. "Common Properties of Fusion Peptides from Diverse Systems." Bioscience Reports 20, no. 6 (December 1, 2000): 483–500. http://dx.doi.org/10.1023/a:1010454803579.
Повний текст джерелаRöckendorf, Niels, Christian Nehls, and Thomas Gutsmann. "Design of Membrane Active Peptides Considering Multi-Objective Optimization for Biomedical Application." Membranes 12, no. 2 (February 2, 2022): 180. http://dx.doi.org/10.3390/membranes12020180.
Повний текст джерелаHamasaki, Naotaka, Hiroyuki Kuma, Kazuhisa Ota, Masao Sakaguchi, and Katsuyoshi Mihara. "A new concept in polytopic membrane proteins following from the study of band 3 protein." Biochemistry and Cell Biology 76, no. 5 (October 1, 1998): 729–33. http://dx.doi.org/10.1139/o98-085.
Повний текст джерелаKondrashov, Oleg V., Peter I. Kuzmin, and Sergey A. Akimov. "Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides." Membranes 12, no. 1 (January 13, 2022): 89. http://dx.doi.org/10.3390/membranes12010089.
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 джерелаBechinger, B., and S. U. Gorr. "Antimicrobial Peptides: Mechanisms of Action and Resistance." Journal of Dental Research 96, no. 3 (November 25, 2016): 254–60. http://dx.doi.org/10.1177/0022034516679973.
Повний текст джерелаMirsaliotis, Antonis, Daniel Lamb та David W. Brighty. "Nonhelical Leash and α-Helical Structures Determine the Potency of a Peptide Antagonist of Human T-Cell Leukemia Virus Entry". Journal of Virology 82, № 10 (27 лютого 2008): 4965–73. http://dx.doi.org/10.1128/jvi.02458-07.
Повний текст джерелаMartoglio, B. "Intramembrane proteolysis and post-targeting functions of signal peptides." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1243–47. http://dx.doi.org/10.1042/bst0311243.
Повний текст джерелаClément, B., B. Segui-Real, P. Savagner, H. K. Kleinman, and Y. Yamada. "Hepatocyte attachment to laminin is mediated through multiple receptors." Journal of Cell Biology 110, no. 1 (January 1, 1990): 185–92. http://dx.doi.org/10.1083/jcb.110.1.185.
Повний текст джерелаSCHRAW, Todd D., Paula P. LEMONS, William L. DEAN, and Sidney W. WHITEHEART. "A role for Sec1/Munc18 proteins in platelet exocytosis." Biochemical Journal 374, no. 1 (August 15, 2003): 207–17. http://dx.doi.org/10.1042/bj20030610.
Повний текст джерелаNg, Sandy Y. M., David J. VanDyke, Bonnie Chaban, John Wu, Yoshika Nosaka, Shin-Ichi Aizawa, and Ken F. Jarrell. "Different Minimal Signal Peptide Lengths Recognized by the Archaeal Prepilin-Like Peptidases FlaK and PibD." Journal of Bacteriology 191, no. 21 (August 28, 2008): 6732–40. http://dx.doi.org/10.1128/jb.00673-09.
Повний текст джерелаShmulevitz, Maya, Raquel F. Epand, Richard M. Epand, and Roy Duncan. "Structural and Functional Properties of an Unusual Internal Fusion Peptide in a Nonenveloped Virus Membrane Fusion Protein." Journal of Virology 78, no. 6 (March 15, 2004): 2808–18. http://dx.doi.org/10.1128/jvi.78.6.2808-2818.2004.
Повний текст джерелаEissa, N. G., E. J. Sayers, D. Birch, S. G. Patel, Y. H. Tsai, H. Mørck Nielsen, and A. T. Jones. "EJP18 peptide derived from the juxtamembrane domain of epidermal growth factor receptor represents a novel membrane-active cell-penetrating peptide." Biochemical Journal 477, no. 1 (January 8, 2020): 45–60. http://dx.doi.org/10.1042/bcj20190452.
Повний текст джерелаSkehel, J. J., K. Cross, D. Steinhauer, and D. C. Wiley. "Influenza fusion peptides." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 623–26. http://dx.doi.org/10.1042/bst0290623.
Повний текст джерелаDahiya, Sunita, and Rajiv Dahiya. "BIOAVAILABILITY ENHANCEMENT AND LIPID NANOCARRIER BASED DELIVERY OF PEPTIDES AND PROTEINS." Bulletin of Pharmaceutical Research 10, no. 1-3 (2020): 1–10. http://dx.doi.org/10.21276/bpr.2020.10.3.
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 джерелаŻyłka, Romuald, Justyna Kupiec, and Stanislaw Przestalski. "Peptides conformational changes of the erythrocyte membrane induced by organometallic tin compounds." Current Topics in Biophysics 34, no. 1 (January 1, 2011): 31–35. http://dx.doi.org/10.2478/v10214-011-0005-2.
Повний текст джерелаSzachowicz-Petelska, Barbara, Stanisław Sulkowski, and Zbigniew Figaszewski. "Altered membrane amino acids composition in human colorectal cancer tissue." Open Chemistry 10, no. 4 (August 1, 2012): 1245–52. http://dx.doi.org/10.2478/s11532-012-0050-1.
Повний текст джерелаReinhardt, Timothy A., and John D. Lippolis. "Bovine Milk Fat Globule Membrane Proteome." Journal of Dairy Research 73, no. 4 (July 12, 2006): 406–16. http://dx.doi.org/10.1017/s0022029906001889.
Повний текст джерелаWang, Guangshun. "NMR of Membrane-Associated Peptides and Proteins." Current Protein & Peptide Science 9, no. 1 (February 1, 2008): 50–69. http://dx.doi.org/10.2174/138920308783565714.
Повний текст джерелаClague, M. J., and R. J. Cherry. "Comparison of p25 presequence peptide and melittin. Red blood cell haemolysis and band 3 aggregation." Biochemical Journal 252, no. 3 (June 15, 1988): 791–94. http://dx.doi.org/10.1042/bj2520791.
Повний текст джерелаWang, P., G. Gyllner, and S. Kvist. "Selection and binding of peptides to human transporters associated with antigen processing and rat cim-a and -b." Journal of Immunology 157, no. 1 (July 1, 1996): 213–20. http://dx.doi.org/10.4049/jimmunol.157.1.213.
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 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 джерелаHiken, Jeffrey, Richard LeDuc, Petra Gilmore, Henry Rohrs, R. Reid Townsend, and Monica Bessler. "Global Differences in RBC Membrane Protein Expression Between Normal and PNH Individuals." Blood 114, no. 22 (November 20, 2009): 1986. http://dx.doi.org/10.1182/blood.v114.22.1986.1986.
Повний текст джерелаShai, Yechiel. "Functional Domains within Fusion Proteins: Prospectives for Development of Peptide Inhibitors of Viral Cell Fusion." Bioscience Reports 20, no. 6 (December 1, 2000): 535–55. http://dx.doi.org/10.1023/a:1010411021326.
Повний текст джерелаJeong, Sekyoo, Seokjeong Yoon, Sungwoo Kim, Juyeon Jung, Myungho Kor, Kayoung Shin, Chaejin Lim, et al. "Anti-Wrinkle Benefits of Peptides Complex Stimulating Skin Basement Membrane Proteins Expression." International Journal of Molecular Sciences 21, no. 1 (December 20, 2019): 73. http://dx.doi.org/10.3390/ijms21010073.
Повний текст джерелаLear, J. D., H. Gratkowski, and W. F. DeGrado. "De novo design, synthesis and characterization of membrane-active peptides." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 559–64. http://dx.doi.org/10.1042/bst0290559.
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 джерелаLee, Ernest Y., Benjamin M. Fulan, Gerard C. L. Wong, and Andrew L. Ferguson. "Mapping membrane activity in undiscovered peptide sequence space using machine learning." Proceedings of the National Academy of Sciences 113, no. 48 (November 14, 2016): 13588–93. http://dx.doi.org/10.1073/pnas.1609893113.
Повний текст джерелаBraunagel, Julia, Ann Junghans, and Ingo Köper. "Membrane-Based Sensing Approaches." Australian Journal of Chemistry 64, no. 1 (2011): 54. http://dx.doi.org/10.1071/ch10347.
Повний текст джерелаSiminovitch, David J. "Solid-state NMR studies of proteins: the view from static 2H NMR experiments." Biochemistry and Cell Biology 76, no. 2-3 (May 1, 1998): 411–22. http://dx.doi.org/10.1139/o98-054.
Повний текст джерелаChicz, R. M., D. F. Graziano, M. Trucco, J. L. Strominger, and J. C. Gorga. "HLA-DP2: self peptide sequences and binding properties." Journal of Immunology 159, no. 10 (November 15, 1997): 4935–42. http://dx.doi.org/10.4049/jimmunol.159.10.4935.
Повний текст джерелаLiu, Betty Revon, Shiow-Her Chiou, Yue-Wern Huang, and Han-Jung Lee. "Bio-Membrane Internalization Mechanisms of Arginine-Rich Cell-Penetrating Peptides in Various Species." Membranes 12, no. 1 (January 13, 2022): 88. http://dx.doi.org/10.3390/membranes12010088.
Повний текст джерелаPorotto, Matteo, Christine C. Yokoyama, Laura M. Palermo, Bruce Mungall, Mohamad Aljofan, Riccardo Cortese, Antonello Pessi, and Anne Moscona. "Viral Entry Inhibitors Targeted to the Membrane Site of Action." Journal of Virology 84, no. 13 (March 31, 2010): 6760–68. http://dx.doi.org/10.1128/jvi.00135-10.
Повний текст джерелаLee, Jung-Seok, Goran Mitulović, Layla Panahipour, and Reinhard Gruber. "Proteomic Analysis of Porcine-Derived Collagen Membrane and Matrix." Materials 13, no. 22 (November 17, 2020): 5187. http://dx.doi.org/10.3390/ma13225187.
Повний текст джерелаVolynsky, P. E., T. R. Galimzyanov, and S. A. Akimov. "Interaction of Peptides Containing CRAC Motifs with Lipids in Membranes of Various Composition." Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology 15, no. 2 (April 2021): 120–29. http://dx.doi.org/10.1134/s1990747821010074.
Повний текст джерелаMüller, W. E., C. Kirsch та G. P. Eckert. "Membrane-disordering effects of β-amyloid peptides". Biochemical Society Transactions 29, № 4 (1 серпня 2001): 617–23. http://dx.doi.org/10.1042/bst0290617.
Повний текст джерелаTao, Houchao, Sung Chang Lee, Arne Moeller, Rituparna Sinha Roy, Fai Yiu Siu, Jörg Zimmermann, Raymond C. Stevens, Clinton S. Potter, Bridget Carragher та Qinghai Zhang. "Engineered nanostructured β-sheet peptides protect membrane proteins". Nature Methods 10, № 8 (30 червня 2013): 759–61. http://dx.doi.org/10.1038/nmeth.2533.
Повний текст джерелаWenzel, M., A. I. Chiriac, A. Otto, D. Zweytick, C. May, C. Schumacher, R. Gust, et al. "Small cationic antimicrobial peptides delocalize peripheral membrane proteins." Proceedings of the National Academy of Sciences 111, no. 14 (March 24, 2014): E1409—E1418. http://dx.doi.org/10.1073/pnas.1319900111.
Повний текст джерелаKillian, J. Antoinette. "Synthetic peptides as models for intrinsic membrane proteins." FEBS Letters 555, no. 1 (October 15, 2003): 134–38. http://dx.doi.org/10.1016/s0014-5793(03)01154-2.
Повний текст джерелаKuchler, K., and J. Thorner. "Membrane translocation of proteins without hydrophobic signal peptides." Current Opinion in Cell Biology 2, no. 4 (August 1990): 617–24. http://dx.doi.org/10.1016/0955-0674(90)90102-k.
Повний текст джерелаMakkar, Sarbjeet, Rohana Liyanage, Lakshmi Kannan, Balamurugan Packialakshmi, Jack O. Lay, and Narayan C. Rath. "Chicken Egg Shell Membrane Associated Proteins and Peptides." Journal of Agricultural and Food Chemistry 63, no. 44 (October 28, 2015): 9888–98. http://dx.doi.org/10.1021/acs.jafc.5b04266.
Повний текст джерелаTakano, Mikihisa, and Yumoto Ryoko. "Transport of Proteins and Peptides and its Regulation in Alveolar Epithelial Cells." MEMBRANE 36, no. 4 (2011): 145–53. http://dx.doi.org/10.5360/membrane.36.145.
Повний текст джерелаEpand, Richard M. "Membrane Fusion." Bioscience Reports 20, no. 6 (December 1, 2000): 435–41. http://dx.doi.org/10.1023/a:1010498618600.
Повний текст джерелаUlmschneider, Martin. "Spontaneous Assembly of Functional Membrane Proteins from Soluble Membrane Active Peptides." Biophysical Journal 114, no. 3 (February 2018): 8a. http://dx.doi.org/10.1016/j.bpj.2017.11.080.
Повний текст джерелаSzabó, Zalán, Adriana Oliveira Stahl, Sonja-V. Albers, Jessica C. Kissinger, Arnold J. M. Driessen, and Mechthild Pohlschröder. "Identification of Diverse Archaeal Proteins with Class III Signal Peptides Cleaved by Distinct Archaeal Prepilin Peptidases." Journal of Bacteriology 189, no. 3 (November 17, 2006): 772–78. http://dx.doi.org/10.1128/jb.01547-06.
Повний текст джерелаRainey, Jan K., Larry Fliegel, and Brian D. Sykes. "Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptidesThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease." Biochemistry and Cell Biology 84, no. 6 (December 2006): 918–29. http://dx.doi.org/10.1139/o06-178.
Повний текст джерелаLi, Caroline M., Pouya Haratipour, Robert G. Lingeman, J. Jefferson P. Perry, Long Gu, Robert J. Hickey, and Linda H. Malkas. "Novel Peptide Therapeutic Approaches for Cancer Treatment." Cells 10, no. 11 (October 27, 2021): 2908. http://dx.doi.org/10.3390/cells10112908.
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