Статті в журналах з теми "OMP biogenesis"
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Ознайомтеся з топ-41 статей у журналах для дослідження на тему "OMP biogenesis".
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Costello, Shawn M., Ashlee M. Plummer, Patrick J. Fleming, and Karen G. Fleming. "Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins." Proceedings of the National Academy of Sciences 113, no. 33 (August 1, 2016): E4794—E4800. http://dx.doi.org/10.1073/pnas.1601002113.
Повний текст джерелаAlbrecht, Reinhard, Monika Schütz, Philipp Oberhettinger, Michaela Faulstich, Ivan Bermejo, Thomas Rudel, Kay Diederichs, and Kornelius Zeth. "Structure of BamA, an essential factor in outer membrane protein biogenesis." Acta Crystallographica Section D Biological Crystallography 70, no. 6 (May 30, 2014): 1779–89. http://dx.doi.org/10.1107/s1399004714007482.
Повний текст джерелаKonovalova, Anna, Marcin Grabowicz, Carl J. Balibar, Juliana C. Malinverni, Ronald E. Painter, Daniel Riley, Paul A. Mann та ін. "Inhibitor of intramembrane protease RseP blocks the σE response causing lethal accumulation of unfolded outer membrane proteins". Proceedings of the National Academy of Sciences 115, № 28 (25 червня 2018): E6614—E6621. http://dx.doi.org/10.1073/pnas.1806107115.
Повний текст джерелаVolokhina, Elena B., Frank Beckers, Jan Tommassen та Martine P. Bos. "The β-Barrel Outer Membrane Protein Assembly Complex of Neisseria meningitidis". Journal of Bacteriology 191, № 22 (18 вересня 2009): 7074–85. http://dx.doi.org/10.1128/jb.00737-09.
Повний текст джерелаHart, Elizabeth M., Angela M. Mitchell, Anna Konovalova, Marcin Grabowicz, Jessica Sheng, Xiaoqing Han, Frances P. Rodriguez-Rivera, et al. "A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier." Proceedings of the National Academy of Sciences 116, no. 43 (October 7, 2019): 21748–57. http://dx.doi.org/10.1073/pnas.1912345116.
Повний текст джерелаHorne, Jim E., та Sheena E. Radford. "A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis". Biochemical Society Transactions 44, № 3 (9 червня 2016): 802–9. http://dx.doi.org/10.1042/bst20160020.
Повний текст джерелаWeirich, Johanna, Cornelia Bräutigam, Melanie Mühlenkamp, Mirita Franz-Wachtel, Boris Macek, Ina Meuskens, Mikael Skurnik, et al. "Identifying components required for OMP biogenesis as novel targets for antiinfective drugs." Virulence 8, no. 7 (February 6, 2017): 1170–88. http://dx.doi.org/10.1080/21505594.2016.1278333.
Повний текст джерелаTata, Muralidhar, Santosh Kumar, Sarah R. Lach, Shreya Saha, Elizabeth M. Hart, and Anna Konovalova. "High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function." Proceedings of the National Academy of Sciences 118, no. 32 (August 4, 2021): e2100369118. http://dx.doi.org/10.1073/pnas.2100369118.
Повний текст джерелаSoltes, Garner R., Jaclyn Schwalm, Dante P. Ricci, and Thomas J. Silhavy. "The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain." Journal of Bacteriology 198, no. 6 (January 4, 2016): 921–29. http://dx.doi.org/10.1128/jb.00889-15.
Повний текст джерелаMarx, Dagan C., Ashlee M. Plummer, Anneliese M. Faustino, Taylor Devlin, Michaela A. Roskopf, Mathis J. Leblanc, Henry J. Lessen, et al. "SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins." Proceedings of the National Academy of Sciences 117, no. 45 (October 22, 2020): 28026–35. http://dx.doi.org/10.1073/pnas.2008175117.
Повний текст джерелаHorne, Jim E., David J. Brockwell, and Sheena E. Radford. "Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria." Journal of Biological Chemistry 295, no. 30 (June 4, 2020): 10340–67. http://dx.doi.org/10.1074/jbc.rev120.011473.
Повний текст джерелаRollauer, Sarah E., Moloud A. Sooreshjani, Nicholas Noinaj, and Susan K. Buchanan. "Outer membrane protein biogenesis in Gram-negative bacteria." Philosophical Transactions of the Royal Society B: Biological Sciences 370, no. 1679 (October 5, 2015): 20150023. http://dx.doi.org/10.1098/rstb.2015.0023.
Повний текст джерелаFardini, Yann, Jérôme Trotereau, Elisabeth Bottreau, Charlène Souchard, Philippe Velge, and Isabelle Virlogeux-Payant. "Investigation of the role of the BAM complex and SurA chaperone in outer-membrane protein biogenesis and type III secretion system expression in Salmonella." Microbiology 155, no. 5 (May 1, 2009): 1613–22. http://dx.doi.org/10.1099/mic.0.025155-0.
Повний текст джерелаMasi, Muriel, Guillaume Duret, Anne H. Delcour, and Rajeev Misra. "Folding and trimerization of signal sequence-less mature TolC in the cytoplasm of Escherichia coli." Microbiology 155, no. 6 (June 1, 2009): 1847–57. http://dx.doi.org/10.1099/mic.0.027219-0.
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 джерелаWu, Si, Xi Ge, Zhixin Lv, Zeyong Zhi, Zengyi Chang, and Xin Sheng Zhao. "Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism." Biochemical Journal 438, no. 3 (August 26, 2011): 505–11. http://dx.doi.org/10.1042/bj20110264.
Повний текст джерелаLuthra, Amit, Arvind Anand, Kelly L. Hawley, Morgan LeDoyt, Carson J. La Vake, Melissa J. Caimano, Adriana R. Cruz, Juan C. Salazar, and Justin D. Radolf. "A Homology Model Reveals Novel Structural Features and an Immunodominant Surface Loop/Opsonic Target in the Treponema pallidum BamA Ortholog TP_0326." Journal of Bacteriology 197, no. 11 (March 30, 2015): 1906–20. http://dx.doi.org/10.1128/jb.00086-15.
Повний текст джерелаChen, Ching-ju, Deborah M. Tobiason, Christopher E. Thomas, William M. Shafer, H. Steven Seifert, and P. Frederick Sparling. "A Mutant Form of the Neisseria gonorrhoeae Pilus Secretin Protein PilQ Allows Increased Entry of Heme and Antimicrobial Compounds." Journal of Bacteriology 186, no. 3 (February 1, 2004): 730–39. http://dx.doi.org/10.1128/jb.186.3.730-739.2004.
Повний текст джерелаFriedrich, V., C. Gruber, I. Nimeth, S. Pabinger, G. Sekot, G. Posch, F. Altmann, P. Messner, O. Andrukhov, and C. Schäffer. "Outer membrane vesicles of Tannerella forsythia : biogenesis, composition, and virulence." Molecular Oral Microbiology 30, no. 6 (June 16, 2015): 451–73. http://dx.doi.org/10.1111/omi.12104.
Повний текст джерелаXu, R., Q. Hu, Q. Ma, C. Liu та G. Wang. "The protease Omi regulates mitochondrial biogenesis through the GSK3β/PGC-1α pathway". Cell Death & Disease 5, № 8 (серпень 2014): e1373-e1373. http://dx.doi.org/10.1038/cddis.2014.328.
Повний текст джерелаKarakas, Umit, Ozlem Izci Ay, Mustafa Ertan Ay, Wei Wang, Mehmet Ali Sungur, Kenan Çevik, Gurbet Dogru, and Mehmet Emin Erdal. "Regulating the Regulators in Attention-Deficit/Hyperactivity Disorder: A Genetic Association Study of microRNA Biogenesis Pathways." OMICS: A Journal of Integrative Biology 21, no. 6 (June 2017): 352–58. http://dx.doi.org/10.1089/omi.2017.0048.
Повний текст джерелаCrowley, P. J., and L. J. Brady. "Evaluation of the effects ofStreptococcus mutanschaperones and protein secretion machinery components on cell surface protein biogenesis, competence, and mutacin production." Molecular Oral Microbiology 31, no. 1 (October 7, 2015): 59–77. http://dx.doi.org/10.1111/omi.12130.
Повний текст джерелаCuthbertson, Leslie, Iain L. Mainprize, James H. Naismith, and Chris Whitfield. "Pivotal Roles of the Outer Membrane Polysaccharide Export and Polysaccharide Copolymerase Protein Families in Export of Extracellular Polysaccharides in Gram-Negative Bacteria." Microbiology and Molecular Biology Reviews 73, no. 1 (March 2009): 155–77. http://dx.doi.org/10.1128/mmbr.00024-08.
Повний текст джерелаHao, Jiejie, Cui Hao, Lijuan Zhang, Xin Liu, Xiaolin Zhou, Yunlou Dun, Haihua Li та ін. "OM2, a Novel Oligomannuronate-Chromium(III) Complex, Promotes Mitochondrial Biogenesis and Lipid Metabolism in 3T3-L1 Adipocytes via the AMPK-PGC1α Pathway". PLOS ONE 10, № 7 (15 липня 2015): e0131930. http://dx.doi.org/10.1371/journal.pone.0131930.
Повний текст джерелаJohnston, Joanne L., Stephen J. Billington, Volker Haring, and Julian I. Rood. "Complementation Analysis of the Dichelobacter nodosus fimN, fimO, and fimP Genes inPseudomonas aeruginosa and Transcriptional Analysis of thefimNOP Gene Region." Infection and Immunity 66, no. 1 (January 1, 1998): 297–304. http://dx.doi.org/10.1128/iai.66.1.297-304.1998.
Повний текст джерелаAragon, Virginia, Sherry Kurtz, Antje Flieger, Birgid Neumeister, and Nicholas P. Cianciotto. "Secreted Enzymatic Activities of Wild-Type andpilD-Deficient Legionella pneumophila." Infection and Immunity 68, no. 4 (April 1, 2000): 1855–63. http://dx.doi.org/10.1128/iai.68.4.1855-1863.2000.
Повний текст джерелаRanava, David, Yiying Yang, Luis Orenday-Tapia, François Rousset, Catherine Turlan, Violette Morales, Lun Cui, et al. "Lipoprotein DolP supports proper folding of BamA in the bacterial outer membrane promoting fitness upon envelope stress." eLife 10 (April 13, 2021). http://dx.doi.org/10.7554/elife.67817.
Повний текст джерелаMamou, Gideon, Federico Corona, Ruth Cohen-Khait, Nicholas G. Housden, Vivian Yeung, Dawei Sun, Pooja Sridhar, et al. "Peptidoglycan maturation controls outer membrane protein assembly." Nature, June 15, 2022. http://dx.doi.org/10.1038/s41586-022-04834-7.
Повний текст джерелаSchiffrin, Bob, Jonathan M. Machin, Theodoros K. Karamanos, Anastasia Zhuravleva, David J. Brockwell, Sheena E. Radford, and Antonio N. Calabrese. "Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding." Communications Biology 5, no. 1 (June 8, 2022). http://dx.doi.org/10.1038/s42003-022-03502-w.
Повний текст джерелаHart, Elizabeth M., Meera Gupta, Martin Wühr та Thomas J. Silhavy. "The Synthetic Phenotype of ΔbamBΔbamEDouble Mutants Results from a Lethal Jamming of the Bam Complex by the Lipoprotein RcsF". mBio 10, № 3 (21 травня 2019). http://dx.doi.org/10.1128/mbio.00662-19.
Повний текст джерелаSoltes, Garner R., Nicholas R. Martin, Eunhae Park, Holly A. Sutterlin, and Thomas J. Silhavy. "Distinctive Roles for Periplasmic Proteases in the Maintenance of Essential Outer Membrane Protein Assembly." Journal of Bacteriology 199, no. 20 (August 7, 2017). http://dx.doi.org/10.1128/jb.00418-17.
Повний текст джерелаTata, Muralidhar, and Anna Konovalova. "Improper Coordination of BamA and BamD Results in Bam Complex Jamming by a Lipoprotein Substrate." mBio 10, no. 3 (May 21, 2019). http://dx.doi.org/10.1128/mbio.00660-19.
Повний текст джерелаAlvira, Sara, Daniel W. Watkins, Lucy Troman, William J. Allen, James S. Lorriman, Gianluca Degliesposti, Eli J. Cohen, et al. "Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis." eLife 9 (November 4, 2020). http://dx.doi.org/10.7554/elife.60669.
Повний текст джерелаRicci, Dante P., Jaclyn Schwalm, Michelle Gonzales-Cope, and Thomas J. Silhavy. "The Activity and Specificity of the Outer Membrane Protein Chaperone SurA Are Modulated by a Proline Isomerase Domain." mBio 4, no. 4 (August 13, 2013). http://dx.doi.org/10.1128/mbio.00540-13.
Повний текст джерела"Escherichia coli BepA has proteolytic and chaperone-like functions and acts in the degradation and biogenesis of β-barrel outer membrane proteins (OMP). The tetratricopeptide repeat (TPR) domain of BepA (orange) interacts with proteins of the β-barrel ass". Molecular Microbiology 106, № 5 (20 листопада 2017): i. http://dx.doi.org/10.1111/mmi.13522.
Повний текст джерелаAlaei, Sarah R., Jin Ho Park, Stephen G. Walker, and David G. Thanassi. "Peptide-Based Inhibitors of Fimbrial Biogenesis inPorphyromonas gingivalis." Infection and Immunity 87, no. 3 (January 14, 2019). http://dx.doi.org/10.1128/iai.00750-18.
Повний текст джерелаWen, Zezhang T., Ashton N. Jorgensen, Xiaochang Huang, Kassapa Ellepola, Lynne Chapman, Hui Wu, and L. Jeannine Brady. "Multiple factors are involved in regulation of extracellular membrane vesicle biogenesis in Streptococcus mutans." Molecular Oral Microbiology, December 3, 2020. http://dx.doi.org/10.1111/omi.12318.
Повний текст джерелаFilipović, Maša, Darja Flegar, Sara Aničić, Dino Šisl, Tomislav Kelava, Nataša Kovačić, Alan Šućur, and Danka Grčević. "Transcriptome profiling of osteoclast subsets associated with arthritis: A pathogenic role of CCR2hi osteoclast progenitors." Frontiers in Immunology 13 (December 15, 2022). http://dx.doi.org/10.3389/fimmu.2022.994035.
Повний текст джерелаColas, Vincent, Philippe Barre, Frederik van Parijs, Lukas Wolters, Yannick Quitté, Tom Ruttink, Isabel Roldán-Ruiz, Abraham J. Escobar Gutiérrez, and Hilde Muylle. "Seasonal Differences in Structural and Genetic Control of Digestibility in Perennial Ryegrass." Frontiers in Plant Science 12 (January 4, 2022). http://dx.doi.org/10.3389/fpls.2021.801145.
Повний текст джерелаJiang, Min, Zifan Liu, Junjie Shao, Jingjing Zhou, Haiming Wang, Chao Song, Xin Li та ін. "Estrogen receptor α regulates phenotypic switching and proliferation of vascular smooth muscle cells through the NRF1-OMI-mitophagy signaling pathway under simulated microgravity". Frontiers in Physiology 13 (10 листопада 2022). http://dx.doi.org/10.3389/fphys.2022.1039913.
Повний текст джерелаNelson, Cassandra E., Weiliang Huang, Luke K. Brewer, Angela T. Nguyen, Maureen A. Kane, Angela Wilks, and Amanda G. Oglesby-Sherrouse. "Proteomic Analysis of thePseudomonas aeruginosaIron Starvation Response Reveals PrrF Small Regulatory RNA-Dependent Iron Regulation of Twitching Motility, Amino Acid Metabolism, and Zinc Homeostasis Proteins." Journal of Bacteriology 201, no. 12 (April 8, 2019). http://dx.doi.org/10.1128/jb.00754-18.
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