Статті в журналах з теми "Beta barrel membrane proteins"
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Solan, Ron, Joana Pereira, Andrei N. Lupas, Rachel Kolodny та Nir Ben-Tal. "Gram-negative outer-membrane proteins with multiple β-barrel domains". Proceedings of the National Academy of Sciences 118, № 31 (30 липня 2021): e2104059118. http://dx.doi.org/10.1073/pnas.2104059118.
Повний текст джерелаMiles, A. J., and B. A. Wallace. "Circular dichroism spectroscopy of membrane proteins." Chemical Society Reviews 45, no. 18 (2016): 4859–72. http://dx.doi.org/10.1039/c5cs00084j.
Повний текст джерелаNoinaj, Nicholas, Adam Kuszak, Curtis Balusek, JC Gumbart, Petra Lukacik, Hoshing Chang, Nicole Easley, Trevor Lithgow, and Susan Buchanan. "The role of BamA in the biogenesis of beta-barrel membrane proteins." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C578. http://dx.doi.org/10.1107/s2053273314094212.
Повний текст джерелаTian, Wei, Hammad Naveed, and Jie Liang. "Improving 3D Structure Prediction of Beta-Barrel Membrane Proteins." Biophysical Journal 112, no. 3 (February 2017): 55a. http://dx.doi.org/10.1016/j.bpj.2016.11.333.
Повний текст джерелаLessen, Henry J., Patrick Fleming, Karen G. Fleming, and Alexander J. Sodt. "Transmembrane Beta-Barrel Proteins Rigidify the Bacterial Outer Membrane." Biophysical Journal 116, no. 3 (February 2019): 327a. http://dx.doi.org/10.1016/j.bpj.2018.11.1774.
Повний текст джерелаRoterman, Irena, Katarzyna Stapor, Piotr Fabian, and Leszek Konieczny. "The Functional Significance of Hydrophobic Residue Distribution in Bacterial Beta-Barrel Transmembrane Proteins." Membranes 11, no. 8 (July 30, 2021): 580. http://dx.doi.org/10.3390/membranes11080580.
Повний текст джерелаKazemian, Hassan B., and Cedric Maxime Grimaldi. "Cascading classifier application for topology prediction of transmembrane beta-barrel proteins." Journal of Bioinformatics and Computational Biology 18, no. 06 (October 15, 2020): 2050034. http://dx.doi.org/10.1142/s0219720020500341.
Повний текст джерелаJain, Sumita, and Marcia B. Goldberg. "Requirement for YaeT in the Outer Membrane Assembly of Autotransporter Proteins." Journal of Bacteriology 189, no. 14 (May 18, 2007): 5393–98. http://dx.doi.org/10.1128/jb.00228-07.
Повний текст джерелаNaveed, Hammad, and Jie Liang. "Weakly Stable Regions and Protein-Protein Interactions in Beta-Barrel Membrane Proteins." Current Pharmaceutical Design 20, no. 8 (March 31, 2014): 1268–73. http://dx.doi.org/10.2174/13816128113199990071.
Повний текст джерелаColumbus, Linda, Daniel A. Fox, and Ryan H. Lo. "Strategies for the Solution NMR Structure Determination of Beta-Barrel Membrane Proteins." Biophysical Journal 102, no. 3 (January 2012): 422a—423a. http://dx.doi.org/10.1016/j.bpj.2011.11.2311.
Повний текст джерелаFischbarg, J., and J. C. Vera. "Multifunctional transporter models: lessons from the transport of water, sugars, and ring compounds by GLUTs." American Journal of Physiology-Cell Physiology 268, no. 5 (May 1, 1995): C1077—C1089. http://dx.doi.org/10.1152/ajpcell.1995.268.5.c1077.
Повний текст джерелаMcClean, Siobhan. "Eight Stranded β -Barrel and Related Outer Membrane Proteins: Role in Bacterial Pathogenesis." Protein & Peptide Letters 19, no. 10 (September 1, 2012): 1013–25. http://dx.doi.org/10.2174/092986612802762688.
Повний текст джерелаRigel, Nathan W., and Thomas J. Silhavy. "Making a beta-barrel: assembly of outer membrane proteins in Gram-negative bacteria." Current Opinion in Microbiology 15, no. 2 (April 2012): 189–93. http://dx.doi.org/10.1016/j.mib.2011.12.007.
Повний текст джерелаTsirigos, Konstantinos D., Arne Elofsson, and Pantelis G. Bagos. "PRED-TMBB2: improved topology prediction and detection of beta-barrel outer membrane proteins." Bioinformatics 32, no. 17 (September 1, 2016): i665—i671. http://dx.doi.org/10.1093/bioinformatics/btw444.
Повний текст джерелаLithgow, Trevor. "The Assembly of Beta-Barrel Proteins into Bacterial Outer Membranes." Biophysical Journal 112, no. 3 (February 2017): 329a. http://dx.doi.org/10.1016/j.bpj.2016.11.1781.
Повний текст джерелаTian, Wei, Meishan Lin, Hammad Naveed, and Jie Liang. "Efficient computation of transfer free energies of amino acids in beta-barrel membrane proteins." Bioinformatics 33, no. 11 (January 31, 2017): 1664–71. http://dx.doi.org/10.1093/bioinformatics/btx053.
Повний текст джерелаNaveed, Hammad, Ronald Jackups, and Jie Liang. "Accurate Ab Initio Prediction of Three Dimensional Structures of Beta-Barrel Membrane Proteins from Sequences." Biophysical Journal 98, no. 3 (January 2010): 644a. http://dx.doi.org/10.1016/j.bpj.2009.12.3529.
Повний текст джерелаJacoboni, I. "Prediction of the transmembrane regions of beta-barrel membrane proteins with a neural network-based predictor." Protein Science 10, no. 4 (April 1, 2001): 779–87. http://dx.doi.org/10.1110/ps.37201.
Повний текст джерелаPajón, R., D. Yero, A. Lage, A. Llanes, and C. J. Borroto. "Computational identification of beta-barrel outer-membrane proteins in Mycobacterium tuberculosis predicted proteomes as putative vaccine candidates." Tuberculosis 86, no. 3-4 (May 2006): 290–302. http://dx.doi.org/10.1016/j.tube.2006.01.005.
Повний текст джерелаMizianty, Marcin J., and Lukasz Kurgan. "Improved identification of outer membrane beta barrel proteins using primary sequence, predicted secondary structure, and evolutionary information." Proteins: Structure, Function, and Bioinformatics 79, no. 1 (November 9, 2010): 294–303. http://dx.doi.org/10.1002/prot.22882.
Повний текст джерелаCrowet, Jean, Mehmet Nasir, Nicolas Dony, Antoine Deschamps, Vincent Stroobant, Pierre Morsomme, Magali Deleu, Patrice Soumillion, and Laurence Lins. "Insight into the Self-Assembling Properties of Peptergents: A Molecular Dynamics Simulation Study." International Journal of Molecular Sciences 19, no. 9 (September 14, 2018): 2772. http://dx.doi.org/10.3390/ijms19092772.
Повний текст джерелаBurgess, Nancy K., and Karen G. Fleming. "Beta-barrel Proteins that Reside in the E. coli Outer Membrane In Vivo Demonstrate Varied Folding Behavior In Vitro." Biophysical Journal 96, no. 3 (February 2009): 79a. http://dx.doi.org/10.1016/j.bpj.2008.12.308.
Повний текст джерелаBelcher Dufrisne, Meagan, and Linda M. Columbus. "Strategy for optimized expression of beta-barrel proteins from pathogenic Gram-negative bacteria to the outer membrane of Escherichia coli." Biophysical Journal 121, no. 3 (February 2022): 470a. http://dx.doi.org/10.1016/j.bpj.2021.11.432.
Повний текст джерелаKonovalova, Anna, and Thomas J. Silhavy. "Outer membrane lipoprotein biogenesis: Lol is not the end." Philosophical Transactions of the Royal Society B: Biological Sciences 370, no. 1679 (October 5, 2015): 20150030. http://dx.doi.org/10.1098/rstb.2015.0030.
Повний текст джерелаNarita, S. i., C. Masui, T. Suzuki, N. Dohmae, and Y. Akiyama. "Protease homolog BepA (YfgC) promotes assembly and degradation of -barrel membrane proteins in Escherichia coli." Proceedings of the National Academy of Sciences 110, no. 38 (September 3, 2013): E3612—E3621. http://dx.doi.org/10.1073/pnas.1312012110.
Повний текст джерелаAckermann, Nikolaus, Maximilian Tiller, Gisela Anding, Andreas Roggenkamp, and Jürgen Heesemann. "Contribution of Trimeric Autotransporter C-Terminal Domains of Oligomeric Coiled-Coil Adhesin (Oca) Family Members YadA, UspA1, EibA, and Hia to Translocation of the YadA Passenger Domain and Virulence of Yersinia enterocolitica." Journal of Bacteriology 190, no. 14 (May 16, 2008): 5031–43. http://dx.doi.org/10.1128/jb.00161-08.
Повний текст джерелаTian, Wei, Jie Liang, and Hammad Naveed. "Improved 3D Structure Prediction of Beta-Barrel Membrane Proteins by using Evolutionary Coupling Constraints, Reduced State Space and an Empirical Potential Function." Biophysical Journal 110, no. 3 (February 2016): 56a. http://dx.doi.org/10.1016/j.bpj.2015.11.370.
Повний текст джерелаTurgeson, Andrew, Lucas Morley, David Giles, and Bradley Harris. "Simulated Docking Predicts Putative Channels for the Transport of Long-Chain Fatty Acids in Vibrio cholerae." Biomolecules 12, no. 9 (September 9, 2022): 1269. http://dx.doi.org/10.3390/biom12091269.
Повний текст джерелаRister, Alexander Bernhard, Thomas Gudermann, and Johann Schredelseker. "E as in Enigma: The Mysterious Role of the Voltage-Dependent Anion Channel Glutamate E73." International Journal of Molecular Sciences 24, no. 1 (December 23, 2022): 269. http://dx.doi.org/10.3390/ijms24010269.
Повний текст джерелаvan ‘t Hag, Leonie, Hsin-Hui Shen, Tsung-Wu Lin, Sally L. Gras, Calum J. Drummond, and Charlotte E. Conn. "Effect of Lipid-Based Nanostructure on Protein Encapsulation within the Membrane Bilayer Mimetic Lipidic Cubic Phase Using Transmembrane and Lipo-proteins from the Beta-Barrel Assembly Machinery." Langmuir 32, no. 47 (June 29, 2016): 12442–52. http://dx.doi.org/10.1021/acs.langmuir.6b01800.
Повний текст джерелаBatchelor, Eric, Don Walthers, Linda J. Kenney, and Mark Goulian. "The Escherichia coli CpxA-CpxR Envelope Stress Response System Regulates Expression of the Porins OmpF and OmpC." Journal of Bacteriology 187, no. 16 (August 15, 2005): 5723–31. http://dx.doi.org/10.1128/jb.187.16.5723-5731.2005.
Повний текст джерелаJiao, Yongqin, and Dianne K. Newman. "The pio Operon Is Essential for Phototrophic Fe(II) Oxidation in Rhodopseudomonas palustris TIE-1." Journal of Bacteriology 189, no. 5 (December 22, 2006): 1765–73. http://dx.doi.org/10.1128/jb.00776-06.
Повний текст джерелаTamposis, Ioannis A., Konstantinos D. Tsirigos, Margarita C. Theodoropoulou, Panagiota I. Kontou, and Pantelis G. Bagos. "Semi-supervised learning of Hidden Markov Models for biological sequence analysis." Bioinformatics 35, no. 13 (November 16, 2018): 2208–15. http://dx.doi.org/10.1093/bioinformatics/bty910.
Повний текст джерелаSchulz, Georg E. "β-Barrel membrane proteins". Current Opinion in Structural Biology 10, № 4 (серпень 2000): 443–47. http://dx.doi.org/10.1016/s0959-440x(00)00120-2.
Повний текст джерелаRoumia, Ahmed F., Margarita C. Theodoropoulou, Konstantinos D. Tsirigos, Henrik Nielsen, and Pantelis G. Bagos. "Landscape of Eukaryotic Transmembrane Beta Barrel Proteins." Journal of Proteome Research 19, no. 3 (February 1, 2020): 1209–21. http://dx.doi.org/10.1021/acs.jproteome.9b00740.
Повний текст джерелаAsamoto, DeeAnn. "Beta-Barrel Membrane Protein Folding into Nanodiscs." Biophysical Journal 118, no. 3 (February 2020): 366a—367a. http://dx.doi.org/10.1016/j.bpj.2019.11.2103.
Повний текст джерелаIshikawa, Daigo, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh та Toshiya Endo. "Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly". Journal of Cell Biology 166, № 5 (23 серпня 2004): 621–27. http://dx.doi.org/10.1083/jcb.200405138.
Повний текст джерелаUlrich, Thomas, and Doron Rapaport. "Biogenesis of beta-barrel proteins in evolutionary context." International Journal of Medical Microbiology 305, no. 2 (February 2015): 259–64. http://dx.doi.org/10.1016/j.ijmm.2014.12.009.
Повний текст джерелаMiyoshi, Taro, Yuhei Nagai, Tomoyasu Aizawa, Katsuki Kimura, and Yoshimasa Watanabe. "Proteins causing membrane fouling in membrane bioreactors." Water Science and Technology 72, no. 6 (June 2, 2015): 844–49. http://dx.doi.org/10.2166/wst.2015.282.
Повний текст джерелаRapaport, Doron. "How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?" Journal of Cell Biology 171, no. 3 (October 31, 2005): 419–23. http://dx.doi.org/10.1083/jcb.200507147.
Повний текст джерелаMohammad, Mohammad M., Khalil R. Howard, and Liviu Movileanu. "Rationale Membrane Protein Design of a Beta-Barrel." Biophysical Journal 102, no. 3 (January 2012): 624a. http://dx.doi.org/10.1016/j.bpj.2011.11.3401.
Повний текст джерелаGruss, Fabian, Franziska Zaehringer, Roman Jakob, Björn Burmann, Sebastian Hiller, and Timm Maier. "A lateral gate for autotransporter and outer membrane protein assembly." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1492. http://dx.doi.org/10.1107/s2053273314085076.
Повний текст джерелаBohnert, Maria, Lena-Sophie Wenz, Ralf M. Zerbes, Susanne E. Horvath, David A. Stroud, Karina von der Malsburg, Judith M. Müller, et al. "Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane." Molecular Biology of the Cell 23, no. 20 (October 15, 2012): 3948–56. http://dx.doi.org/10.1091/mbc.e12-04-0295.
Повний текст джерелаUrfer, Matthias, Jasmina Bogdanovic, Fabio Lo Monte, Kerstin Moehle, Katja Zerbe, Ulrich Omasits, Christian H. Ahrens, Gabriella Pessi, Leo Eberl, and John A. Robinson. "A Peptidomimetic Antibiotic Targets Outer Membrane Proteins and Disrupts Selectively the Outer Membrane in Escherichia coli." Journal of Biological Chemistry 291, no. 4 (December 1, 2015): 1921–32. http://dx.doi.org/10.1074/jbc.m115.691725.
Повний текст джерелаTomasek, David, та Daniel Kahne. "The assembly of β-barrel outer membrane proteins". Current Opinion in Microbiology 60 (квітень 2021): 16–23. http://dx.doi.org/10.1016/j.mib.2021.01.009.
Повний текст джерелаWenz, Lena-Sophie, Jian Qiu, Thomas Becker та Nils Wiedemann. "Biogenesis and folding of β-barrel membrane proteins". Cell Cycle 13, № 2 (15 листопада 2013): 169–70. http://dx.doi.org/10.4161/cc.27035.
Повний текст джерелаTian, Wei, Meishan Lin, Ke Tang, Jie Liang та Hammad Naveed. "High-resolution structure prediction ofβ-barrel membrane proteins". Proceedings of the National Academy of Sciences 115, № 7 (29 січня 2018): 1511–16. http://dx.doi.org/10.1073/pnas.1716817115.
Повний текст джерелаPaschen, Stefan A., Walter Neupert та Doron Rapaport. "Biogenesis of β-barrel membrane proteins of mitochondria". Trends in Biochemical Sciences 30, № 10 (жовтень 2005): 575–82. http://dx.doi.org/10.1016/j.tibs.2005.08.009.
Повний текст джерелаTamm, Lukas K., Heedeok Hong та Binyong Liang. "Folding and assembly of β-barrel membrane proteins". Biochimica et Biophysica Acta (BBA) - Biomembranes 1666, № 1-2 (листопад 2004): 250–63. http://dx.doi.org/10.1016/j.bbamem.2004.06.011.
Повний текст джерелаTamm, Lukas K., Ashish Arora та Jörg H. Kleinschmidt. "Structure and Assembly of β-Barrel Membrane Proteins". Journal of Biological Chemistry 276, № 35 (29 червня 2001): 32399–402. http://dx.doi.org/10.1074/jbc.r100021200.
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