Artículos de revistas sobre el tema "Bacterial Small Heat Shock Protein"
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Bepperling, A., F. Alte, T. Kriehuber, N. Braun, S. Weinkauf, M. Groll, M. Haslbeck y J. Buchner. "Alternative bacterial two-component small heat shock protein systems". Proceedings of the National Academy of Sciences 109, n.º 50 (26 de noviembre de 2012): 20407–12. http://dx.doi.org/10.1073/pnas.1209565109.
Texto completoVentura, Marco, Carlos Canchaya, Ziding Zhang, Gerald F. Fitzgerald y Douwe van Sinderen. "Molecular Characterization of hsp20, Encoding a Small Heat Shock Protein of Bifidobacterium breve UCC2003". Applied and Environmental Microbiology 73, n.º 14 (18 de mayo de 2007): 4695–703. http://dx.doi.org/10.1128/aem.02496-06.
Texto completoWhiston, Emily A., Norito Sugi, Merideth C. Kamradt, Coralynn Sack, Susan R. Heimer, Michael Engelbert, Eric F. Wawrousek, Michael S. Gilmore, Bruce R. Ksander y Meredith S. Gregory. "αB-Crystallin Protects Retinal Tissue during Staphylococcus aureus- Induced Endophthalmitis". Infection and Immunity 76, n.º 4 (28 de enero de 2008): 1781–90. http://dx.doi.org/10.1128/iai.01285-07.
Texto completoLarge, Andrew T., Martin D. Goldberg y Peter A. Lund. "Chaperones and protein folding in the archaea". Biochemical Society Transactions 37, n.º 1 (20 de enero de 2009): 46–51. http://dx.doi.org/10.1042/bst0370046.
Texto completoYin, Huaqun, Min Tang, Zhijun Zhou, Xian Fu, Li Shen, Yili Liang, Qian Li, Hongwei Liu y Xueduan Liu. "Distinctive heat-shock response of bioleaching microorganismAcidithiobacillus ferrooxidansobserved using genome-wide microarray". Canadian Journal of Microbiology 58, n.º 5 (mayo de 2012): 628–36. http://dx.doi.org/10.1139/w2012-023.
Texto completoZhang, Bo, Sean P. Leonard, Yiyuan Li y Nancy A. Moran. "Obligate bacterial endosymbionts limit thermal tolerance of insect host species". Proceedings of the National Academy of Sciences 116, n.º 49 (18 de noviembre de 2019): 24712–18. http://dx.doi.org/10.1073/pnas.1915307116.
Texto completoAvelange-Macherel, Marie-Hélène, Aurélia Rolland, Marie-Pierre Hinault, Dimitri Tolleter y David Macherel. "The Mitochondrial Small Heat Shock Protein HSP22 from Pea is a Thermosoluble Chaperone Prone to Co-Precipitate with Unfolding Client Proteins". International Journal of Molecular Sciences 21, n.º 1 (21 de diciembre de 2019): 97. http://dx.doi.org/10.3390/ijms21010097.
Texto completoLaksanalamai, Pongpan, Dennis L. Maeder y Frank T. Robb. "Regulation and Mechanism of Action of the Small Heat Shock Protein from the Hyperthermophilic ArchaeonPyrococcus furiosus". Journal of Bacteriology 183, n.º 17 (1 de septiembre de 2001): 5198–202. http://dx.doi.org/10.1128/jb.183.17.5198-5202.2001.
Texto completoLupoli, Tania J., Allison Fay, Carolina Adura, Michael S. Glickman y Carl F. Nathan. "Reconstitution of aMycobacterium tuberculosisproteostasis network highlights essential cofactor interactions with chaperone DnaK". Proceedings of the National Academy of Sciences 113, n.º 49 (21 de noviembre de 2016): E7947—E7956. http://dx.doi.org/10.1073/pnas.1617644113.
Texto completoOliver, Cristian, Patricio Sánchez, Karla Valenzuela, Mauricio Hernández, Juan Pablo Pontigo, Maria C. Rauch, Rafael A. Garduño, Ruben Avendaño-Herrera y Alejandro J. Yáñez. "Subcellular Location of Piscirickettsia salmonis Heat Shock Protein 60 (Hsp60) Chaperone by Using Immunogold Labeling and Proteomic Analysis". Microorganisms 8, n.º 1 (15 de enero de 2020): 117. http://dx.doi.org/10.3390/microorganisms8010117.
Texto completoPiróg, Artur, Francesca Cantini, Łukasz Nierzwicki, Igor Obuchowski, Bartłomiej Tomiczek, Jacek Czub y Krzysztof Liberek. "Two Bacterial Small Heat Shock Proteins, IbpA and IbpB, Form a Functional Heterodimer". Journal of Molecular Biology 433, n.º 15 (julio de 2021): 167054. http://dx.doi.org/10.1016/j.jmb.2021.167054.
Texto completoFu, Xinmiao, Zengyi Chang, Xiaodong Shi, Dongbo Bu y Chao Wang. "Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins". Protein Science 23, n.º 2 (16 de diciembre de 2013): 229–37. http://dx.doi.org/10.1002/pro.2404.
Texto completoRasouly, Aviram, Chen Davidovich y Eliora Z. Ron. "The Heat Shock Protein YbeY Is Required for Optimal Activity of the 30S Ribosomal Subunit". Journal of Bacteriology 192, n.º 18 (16 de julio de 2010): 4592–96. http://dx.doi.org/10.1128/jb.00448-10.
Texto completoArvans, Donna L., Stephan R. Vavricka, Hongyu Ren, Mark W. Musch, Lisa Kang, Flavio G. Rocha, Alvaro Lucioni, Jerrold R. Turner, John Alverdy y Eugene B. Chang. "Luminal bacterial flora determines physiological expression of intestinal epithelial cytoprotective heat shock proteins 25 and 72". American Journal of Physiology-Gastrointestinal and Liver Physiology 288, n.º 4 (abril de 2005): G696—G704. http://dx.doi.org/10.1152/ajpgi.00206.2004.
Texto completoKim, Hyesoon y Yeh-Jin Ahn. "Expression of a Gene Encoding the Carrot HSP17.7 in Escherichia coli Enhances Cell Viability and Protein Solubility Under Heat Stress". HortScience 44, n.º 3 (junio de 2009): 866–69. http://dx.doi.org/10.21273/hortsci.44.3.866.
Texto completoIburg, Manuel, Dmytro Puchkov, Irving U. Rosas-Brugada, Linda Bergemann, Ulrike Rieprecht y Janine Kirstein. "The noncanonical small heat shock protein HSP-17 from Caenorhabditis elegans is a selective protein aggregase". Journal of Biological Chemistry 295, n.º 10 (30 de enero de 2020): 3064–79. http://dx.doi.org/10.1074/jbc.ra119.011185.
Texto completoFeng, Jinlin. "ITRAQ-Based Proteomic Analysis of The Response to Ralstonia solanacearum in Potato". Pakistan Journal of Agricultural Sciences 59, n.º 02 (1 de enero de 2022): 165–71. http://dx.doi.org/10.21162/pakjas/22.1347.
Texto completoMaitre, Magali, Stéphanie Weidmann, Florence Dubois-Brissonnet, Vanessa David, Jacques Covès y Jean Guzzo. "Adaptation of the Wine Bacterium Oenococcus oeni to Ethanol Stress: Role of the Small Heat Shock Protein Lo18 in Membrane Integrity". Applied and Environmental Microbiology 80, n.º 10 (28 de febrero de 2014): 2973–80. http://dx.doi.org/10.1128/aem.04178-13.
Texto completoStuder, Sonja y Franz Narberhaus. "Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock Proteins". Journal of Biological Chemistry 275, n.º 47 (7 de septiembre de 2000): 37212–18. http://dx.doi.org/10.1074/jbc.m004701200.
Texto completoZav'yalov, Vladimir P., Galina A. Zav'yalova, Alexander I. Denesyuk, Matthias Gaestel y Timo Korpela. "Structural and functional homology between periplasmic bacterial molecular chaperones and small heat shock proteins". FEMS Immunology & Medical Microbiology 11, n.º 4 (julio de 1995): 265–72. http://dx.doi.org/10.1111/j.1574-695x.1995.tb00155.x.
Texto completoJobin, Michel-Philippe, Dominique Garmyn, Charles Diviès y Jean Guzzo. "The Oenococcus oeni clpX Homologue Is a Heat Shock Gene Preferentially Expressed in Exponential Growth Phase". Journal of Bacteriology 181, n.º 21 (1 de noviembre de 1999): 6634–41. http://dx.doi.org/10.1128/jb.181.21.6634-6641.1999.
Texto completoSriramulu, Dinesh Diraviam. "Small Heat Shock Proteins Produced by Pseudomonas Aeruginosa Clonal Variants Isolated from Diverse Niches". Proteomics Insights 2 (enero de 2009): PRI.S3760. http://dx.doi.org/10.4137/pri.s3760.
Texto completoQiu, Zhijun y Thomas H. MacRae. "ArHsp21, a developmentally regulated small heat-shock protein synthesized in diapausing embryos of Artemia franciscana". Biochemical Journal 411, n.º 3 (14 de abril de 2008): 605–11. http://dx.doi.org/10.1042/bj20071472.
Texto completoRajaram, Hema, Akhilesh Kumar Chaurasia y Shree Kumar Apte. "Cyanobacterial heat-shock response: role and regulation of molecular chaperones". Microbiology 160, n.º 4 (1 de abril de 2014): 647–58. http://dx.doi.org/10.1099/mic.0.073478-0.
Texto completoWasilah, Ummi, Dian A. G. Perwitasari y Mukhamad Su'udi. "Peran Chaperone Pada Tumbuhan: Mini Review". JURNAL BIOLOGI PAPUA 11, n.º 2 (31 de octubre de 2019): 110–15. http://dx.doi.org/10.31957/jbp.880.
Texto completoMusch, Mark W., Elaine O. Petrof, Keishi Kojima, Hongyu Ren, Derek M. McKay y Eugene B. Chang. "Bacterial Superantigen-Treated Intestinal Epithelial Cells Upregulate Heat Shock Proteins 25 and 72 and Are Resistant to Oxidant Cytotoxicity". Infection and Immunity 72, n.º 6 (junio de 2004): 3187–94. http://dx.doi.org/10.1128/iai.72.6.3187-3194.2004.
Texto completoCocotl-Yañez, Miguel, Soledad Moreno, Sergio Encarnación, Liliana López-Pliego, Miguel Castañeda y Guadalupe Espín. "A small heat-shock protein (Hsp20) regulated by RpoS is essential for cyst desiccation resistance in Azotobacter vinelandii". Microbiology 160, n.º 3 (1 de marzo de 2014): 479–87. http://dx.doi.org/10.1099/mic.0.073353-0.
Texto completoPlayford, Raymond J., Naheed Choudhry, Paul Kelly y Tania Marchbank. "Effects of Bovine Colostrum with or without Egg on In Vitro Bacterial-Induced Intestinal Damage with Relevance for SIBO and Infectious Diarrhea". Nutrients 13, n.º 3 (22 de marzo de 2021): 1024. http://dx.doi.org/10.3390/nu13031024.
Texto completoLee, Joohee y Yeh-Jin Ahn. "Heterologous Expression of a Carrot Small Heat Shock Protein Increased Escherichia coli Viability under Lead and Arsenic Stresses". HortScience 48, n.º 10 (octubre de 2013): 1323–26. http://dx.doi.org/10.21273/hortsci.48.10.1323.
Texto completoAhn, Yeh-Jin y Na-Hyun Song. "A Cytosolic Heat Shock Protein Expressed in Carrot (Daucus carota L.) Enhances Cell Viability under Oxidative and Osmotic Stress Conditions". HortScience 47, n.º 1 (enero de 2012): 143–48. http://dx.doi.org/10.21273/hortsci.47.1.143.
Texto completoPetrof, Elaine O., Mark W. Musch, Mae Ciancio, Jun Sun, Michael E. Hobert, Erika C. Claud, Andrew Gewirtz y Eugene B. Chang. "Flagellin is required for salmonella-induced expression of heat shock protein Hsp25 in intestinal epithelium". American Journal of Physiology-Gastrointestinal and Liver Physiology 294, n.º 3 (marzo de 2008): G808—G818. http://dx.doi.org/10.1152/ajpgi.00362.2007.
Texto completoOchocka, Anna-Maria, Marzena Czyzewska y Tadeusz Pawełczyk. "Expression in Escherichia coli of human ARHGAP6 gene and purification of His-tagged recombinant protein." Acta Biochimica Polonica 50, n.º 1 (31 de marzo de 2003): 239–47. http://dx.doi.org/10.18388/abp.2003_3732.
Texto completoTomoyasu, Toshifumi, Akiko Takaya, Tomomi Sasaki, Takahiro Nagase, Reiko Kikuno, Mizue Morioka y Tomoko Yamamoto. "A New Heat Shock Gene, agsA, Which Encodes a Small Chaperone Involved in Suppressing Protein Aggregation in Salmonella enterica Serovar Typhimurium". Journal of Bacteriology 185, n.º 21 (1 de noviembre de 2003): 6331–39. http://dx.doi.org/10.1128/jb.185.21.6331-6339.2003.
Texto completoObuchowski, Igor, Artur Piróg, Milena Stolarska, Bartłomiej Tomiczek y Krzysztof Liberek. "Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates". PLOS Genetics 15, n.º 10 (25 de octubre de 2019): e1008479. http://dx.doi.org/10.1371/journal.pgen.1008479.
Texto completoNarberhaus, Franz. "α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network". Microbiology and Molecular Biology Reviews 66, n.º 1 (marzo de 2002): 64–93. http://dx.doi.org/10.1128/mmbr.66.1.64-93.2002.
Texto completoHenderson, Brian y Andrew C. R. Martin. "Protein moonlighting: a new factor in biology and medicine". Biochemical Society Transactions 42, n.º 6 (17 de noviembre de 2014): 1671–78. http://dx.doi.org/10.1042/bst20140273.
Texto completoMacario, Alberto J. L., Marianne Lange, Birgitte K. Ahring y Everly Conway De Macario. "Stress Genes and Proteins in the Archaea". Microbiology and Molecular Biology Reviews 63, n.º 4 (1 de diciembre de 1999): 923–67. http://dx.doi.org/10.1128/mmbr.63.4.923-967.1999.
Texto completoFasnacht, Michel, Stefano Gallo, Puneet Sharma, Maximilian Himmelstoß, Patrick A. Limbach, Jessica Willi y Norbert Polacek. "Dynamic 23S rRNA modification ho5C2501 benefits Escherichia coli under oxidative stress". Nucleic Acids Research 50, n.º 1 (14 de diciembre de 2021): 473–89. http://dx.doi.org/10.1093/nar/gkab1224.
Texto completoPaul, Deborupa y Sanmitra Ghosh. "An overview of heat-stress response regulation in Gram-negative bacteria considering Escherichia coli as a model organism". Journal of Experimental Biology and Agricultural Sciences 10, n.º 1 (28 de febrero de 2022): 190–200. http://dx.doi.org/10.18006/2022.10(1).190.200.
Texto completoLiebscher, Markus, Günther Jahreis, Christian Lücke, Susanne Grabley, Satish Raina y Cordelia Schiene-Fischer. "Fatty Acyl Benzamido Antibacterials Based on Inhibition of DnaK-catalyzed Protein Folding". Journal of Biological Chemistry 282, n.º 7 (14 de diciembre de 2006): 4437–46. http://dx.doi.org/10.1074/jbc.m607667200.
Texto completoGarbe, T. R., N. S. Hibler y V. Deretic. "Response to Reactive Nitrogen Intermediates inMycobacterium tuberculosis: Induction of the 16-Kilodalton α-Crystallin Homolog by Exposure to Nitric Oxide Donors". Infection and Immunity 67, n.º 1 (1 de enero de 1999): 460–65. http://dx.doi.org/10.1128/iai.67.1.460-465.1999.
Texto completoEl Demerdash, Hassan A. M., Knut J. Heller y Arnold Geis. "Application of the shsp Gene, Encoding a Small Heat Shock Protein, as a Food-Grade Selection Marker for Lactic Acid Bacteria". Applied and Environmental Microbiology 69, n.º 8 (agosto de 2003): 4408–12. http://dx.doi.org/10.1128/aem.69.8.4408-4412.2003.
Texto completoKönen-Waisman, S., M. Fridkin y I. R. Cohen. "Self and foreign 60-kilodalton heat shock protein T cell epitope peptides serve as immunogenic carriers for a T cell-independent sugar antigen." Journal of Immunology 154, n.º 11 (1 de junio de 1995): 5977–85. http://dx.doi.org/10.4049/jimmunol.154.11.5977.
Texto completoFu, Xinmiao, Wangwang Jiao y Zengyi Chang. "Phylogenetic and Biochemical Studies Reveal a Potential Evolutionary Origin of Small Heat Shock Proteins of Animals from Bacterial Class A". Journal of Molecular Evolution 62, n.º 3 (10 de febrero de 2006): 257–66. http://dx.doi.org/10.1007/s00239-005-0076-5.
Texto completoBaldridge, Gerald D., Nicole Y. Burkhardt, Roderick F. Felsheim, Timothy J. Kurtti y Ulrike G. Munderloh. "Plasmids of the pRM/pRF Family Occur in Diverse Rickettsia Species". Applied and Environmental Microbiology 74, n.º 3 (7 de diciembre de 2007): 645–52. http://dx.doi.org/10.1128/aem.02262-07.
Texto completoMurthy, Ashlesh K., Kelly Rae Keeler, Jennifer Do, Aravind Seetharaman, Kyle H. Ramsey, Mae Ciancio y weidang Li. "Tissue Specific Overexpression of Human Heat Shock Protein 70 in Mouse Oviduct Epithelium Reduces Chlamydia Induced Immunopathology". Journal of Immunology 200, n.º 1_Supplement (1 de mayo de 2018): 114.20. http://dx.doi.org/10.4049/jimmunol.200.supp.114.20.
Texto completoReilly, Natasha, Vitaliy Poylin, Michael Menconi, Andrew Onderdonk, Stig Bengmark y Per-Olof Hasselgren. "Probiotics potentiate IL-6 production in IL-1β-treated Caco-2 cells through a heat shock-dependent mechanism". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 293, n.º 3 (septiembre de 2007): R1169—R1179. http://dx.doi.org/10.1152/ajpregu.00770.2006.
Texto completoInaba, Yuhei, Nobuhiro Ueno, Masatsugu Numata, Xiaorong Zhu, Jeannette S. Messer, David L. Boone, Mikihiro Fujiya, Yutaka Kohgo, Mark W. Musch y Eugene B. Chang. "Soluble bioactive microbial mediators regulate proteasomal degradation and autophagy to protect against inflammation-induced stress". American Journal of Physiology-Gastrointestinal and Liver Physiology 311, n.º 4 (1 de octubre de 2016): G634—G647. http://dx.doi.org/10.1152/ajpgi.00092.2016.
Texto completoDarsonval, Maud, Tarek Msadek, Hervé Alexandre y Cosette Grandvalet. "The Antisense RNA Approach: a New Application forIn VivoInvestigation of the Stress Response of Oenococcus oeni, a Wine-Associated Lactic Acid Bacterium". Applied and Environmental Microbiology 82, n.º 1 (9 de octubre de 2015): 18–26. http://dx.doi.org/10.1128/aem.02495-15.
Texto completoGregory, Meredith, Emily Whiston, Norito Sugi, Coralynn Sack, Merideth C. Kamradt, Susan Heimer, Michael S. Gilmore y Bruce R. Ksander. "αB-crystallin protects the retina during S. aureus induced endophthalmitis (45.2)". Journal of Immunology 178, n.º 1_Supplement (1 de abril de 2007): S57. http://dx.doi.org/10.4049/jimmunol.178.supp.45.2.
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