Статті в журналах з теми "Bacterial Small Heat Shock Protein"
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Bepperling, A., F. Alte, T. Kriehuber, N. Braun, S. Weinkauf, M. Groll, M. Haslbeck, and J. Buchner. "Alternative bacterial two-component small heat shock protein systems." Proceedings of the National Academy of Sciences 109, no. 50 (November 26, 2012): 20407–12. http://dx.doi.org/10.1073/pnas.1209565109.
Повний текст джерелаVentura, Marco, Carlos Canchaya, Ziding Zhang, Gerald F. Fitzgerald, and Douwe van Sinderen. "Molecular Characterization of hsp20, Encoding a Small Heat Shock Protein of Bifidobacterium breve UCC2003." Applied and Environmental Microbiology 73, no. 14 (May 18, 2007): 4695–703. http://dx.doi.org/10.1128/aem.02496-06.
Повний текст джерелаWhiston, Emily A., Norito Sugi, Merideth C. Kamradt, Coralynn Sack, Susan R. Heimer, Michael Engelbert, Eric F. Wawrousek, Michael S. Gilmore, Bruce R. Ksander та Meredith S. Gregory. "αB-Crystallin Protects Retinal Tissue during Staphylococcus aureus- Induced Endophthalmitis". Infection and Immunity 76, № 4 (28 січня 2008): 1781–90. http://dx.doi.org/10.1128/iai.01285-07.
Повний текст джерелаLarge, Andrew T., Martin D. Goldberg, and Peter A. Lund. "Chaperones and protein folding in the archaea." Biochemical Society Transactions 37, no. 1 (January 20, 2009): 46–51. http://dx.doi.org/10.1042/bst0370046.
Повний текст джерелаYin, Huaqun, Min Tang, Zhijun Zhou, Xian Fu, Li Shen, Yili Liang, Qian Li, Hongwei Liu, and Xueduan Liu. "Distinctive heat-shock response of bioleaching microorganismAcidithiobacillus ferrooxidansobserved using genome-wide microarray." Canadian Journal of Microbiology 58, no. 5 (May 2012): 628–36. http://dx.doi.org/10.1139/w2012-023.
Повний текст джерелаZhang, Bo, Sean P. Leonard, Yiyuan Li, and Nancy A. Moran. "Obligate bacterial endosymbionts limit thermal tolerance of insect host species." Proceedings of the National Academy of Sciences 116, no. 49 (November 18, 2019): 24712–18. http://dx.doi.org/10.1073/pnas.1915307116.
Повний текст джерелаAvelange-Macherel, Marie-Hélène, Aurélia Rolland, Marie-Pierre Hinault, Dimitri Tolleter, and 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, no. 1 (December 21, 2019): 97. http://dx.doi.org/10.3390/ijms21010097.
Повний текст джерелаLaksanalamai, Pongpan, Dennis L. Maeder, and Frank T. Robb. "Regulation and Mechanism of Action of the Small Heat Shock Protein from the Hyperthermophilic ArchaeonPyrococcus furiosus." Journal of Bacteriology 183, no. 17 (September 1, 2001): 5198–202. http://dx.doi.org/10.1128/jb.183.17.5198-5202.2001.
Повний текст джерелаLupoli, Tania J., Allison Fay, Carolina Adura, Michael S. Glickman, and Carl F. Nathan. "Reconstitution of aMycobacterium tuberculosisproteostasis network highlights essential cofactor interactions with chaperone DnaK." Proceedings of the National Academy of Sciences 113, no. 49 (November 21, 2016): E7947—E7956. http://dx.doi.org/10.1073/pnas.1617644113.
Повний текст джерелаOliver, Cristian, Patricio Sánchez, Karla Valenzuela, Mauricio Hernández, Juan Pablo Pontigo, Maria C. Rauch, Rafael A. Garduño, Ruben Avendaño-Herrera, and Alejandro J. Yáñez. "Subcellular Location of Piscirickettsia salmonis Heat Shock Protein 60 (Hsp60) Chaperone by Using Immunogold Labeling and Proteomic Analysis." Microorganisms 8, no. 1 (January 15, 2020): 117. http://dx.doi.org/10.3390/microorganisms8010117.
Повний текст джерелаPiróg, Artur, Francesca Cantini, Łukasz Nierzwicki, Igor Obuchowski, Bartłomiej Tomiczek, Jacek Czub, and Krzysztof Liberek. "Two Bacterial Small Heat Shock Proteins, IbpA and IbpB, Form a Functional Heterodimer." Journal of Molecular Biology 433, no. 15 (July 2021): 167054. http://dx.doi.org/10.1016/j.jmb.2021.167054.
Повний текст джерелаFu, Xinmiao, Zengyi Chang, Xiaodong Shi, Dongbo Bu, and Chao Wang. "Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins." Protein Science 23, no. 2 (December 16, 2013): 229–37. http://dx.doi.org/10.1002/pro.2404.
Повний текст джерелаRasouly, Aviram, Chen Davidovich, and Eliora Z. Ron. "The Heat Shock Protein YbeY Is Required for Optimal Activity of the 30S Ribosomal Subunit." Journal of Bacteriology 192, no. 18 (July 16, 2010): 4592–96. http://dx.doi.org/10.1128/jb.00448-10.
Повний текст джерелаArvans, Donna L., Stephan R. Vavricka, Hongyu Ren, Mark W. Musch, Lisa Kang, Flavio G. Rocha, Alvaro Lucioni, Jerrold R. Turner, John Alverdy, and 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, no. 4 (April 2005): G696—G704. http://dx.doi.org/10.1152/ajpgi.00206.2004.
Повний текст джерелаKim, Hyesoon, and 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, no. 3 (June 2009): 866–69. http://dx.doi.org/10.21273/hortsci.44.3.866.
Повний текст джерелаIburg, Manuel, Dmytro Puchkov, Irving U. Rosas-Brugada, Linda Bergemann, Ulrike Rieprecht, and Janine Kirstein. "The noncanonical small heat shock protein HSP-17 from Caenorhabditis elegans is a selective protein aggregase." Journal of Biological Chemistry 295, no. 10 (January 30, 2020): 3064–79. http://dx.doi.org/10.1074/jbc.ra119.011185.
Повний текст джерелаFeng, Jinlin. "ITRAQ-Based Proteomic Analysis of The Response to Ralstonia solanacearum in Potato." Pakistan Journal of Agricultural Sciences 59, no. 02 (January 1, 2022): 165–71. http://dx.doi.org/10.21162/pakjas/22.1347.
Повний текст джерелаMaitre, Magali, Stéphanie Weidmann, Florence Dubois-Brissonnet, Vanessa David, Jacques Covès, and 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, no. 10 (February 28, 2014): 2973–80. http://dx.doi.org/10.1128/aem.04178-13.
Повний текст джерелаStuder, Sonja, and Franz Narberhaus. "Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock Proteins." Journal of Biological Chemistry 275, no. 47 (September 7, 2000): 37212–18. http://dx.doi.org/10.1074/jbc.m004701200.
Повний текст джерелаZav'yalov, Vladimir P., Galina A. Zav'yalova, Alexander I. Denesyuk, Matthias Gaestel, and Timo Korpela. "Structural and functional homology between periplasmic bacterial molecular chaperones and small heat shock proteins." FEMS Immunology & Medical Microbiology 11, no. 4 (July 1995): 265–72. http://dx.doi.org/10.1111/j.1574-695x.1995.tb00155.x.
Повний текст джерелаJobin, Michel-Philippe, Dominique Garmyn, Charles Diviès, and Jean Guzzo. "The Oenococcus oeni clpX Homologue Is a Heat Shock Gene Preferentially Expressed in Exponential Growth Phase." Journal of Bacteriology 181, no. 21 (November 1, 1999): 6634–41. http://dx.doi.org/10.1128/jb.181.21.6634-6641.1999.
Повний текст джерелаSriramulu, Dinesh Diraviam. "Small Heat Shock Proteins Produced by Pseudomonas Aeruginosa Clonal Variants Isolated from Diverse Niches." Proteomics Insights 2 (January 2009): PRI.S3760. http://dx.doi.org/10.4137/pri.s3760.
Повний текст джерелаQiu, Zhijun, and Thomas H. MacRae. "ArHsp21, a developmentally regulated small heat-shock protein synthesized in diapausing embryos of Artemia franciscana." Biochemical Journal 411, no. 3 (April 14, 2008): 605–11. http://dx.doi.org/10.1042/bj20071472.
Повний текст джерелаRajaram, Hema, Akhilesh Kumar Chaurasia, and Shree Kumar Apte. "Cyanobacterial heat-shock response: role and regulation of molecular chaperones." Microbiology 160, no. 4 (April 1, 2014): 647–58. http://dx.doi.org/10.1099/mic.0.073478-0.
Повний текст джерелаWasilah, Ummi, Dian A. G. Perwitasari, and Mukhamad Su'udi. "Peran Chaperone Pada Tumbuhan: Mini Review." JURNAL BIOLOGI PAPUA 11, no. 2 (October 31, 2019): 110–15. http://dx.doi.org/10.31957/jbp.880.
Повний текст джерелаMusch, Mark W., Elaine O. Petrof, Keishi Kojima, Hongyu Ren, Derek M. McKay, and 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, no. 6 (June 2004): 3187–94. http://dx.doi.org/10.1128/iai.72.6.3187-3194.2004.
Повний текст джерелаCocotl-Yañez, Miguel, Soledad Moreno, Sergio Encarnación, Liliana López-Pliego, Miguel Castañeda, and Guadalupe Espín. "A small heat-shock protein (Hsp20) regulated by RpoS is essential for cyst desiccation resistance in Azotobacter vinelandii." Microbiology 160, no. 3 (March 1, 2014): 479–87. http://dx.doi.org/10.1099/mic.0.073353-0.
Повний текст джерелаPlayford, Raymond J., Naheed Choudhry, Paul Kelly, and 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, no. 3 (March 22, 2021): 1024. http://dx.doi.org/10.3390/nu13031024.
Повний текст джерелаLee, Joohee, and Yeh-Jin Ahn. "Heterologous Expression of a Carrot Small Heat Shock Protein Increased Escherichia coli Viability under Lead and Arsenic Stresses." HortScience 48, no. 10 (October 2013): 1323–26. http://dx.doi.org/10.21273/hortsci.48.10.1323.
Повний текст джерелаAhn, Yeh-Jin, and 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, no. 1 (January 2012): 143–48. http://dx.doi.org/10.21273/hortsci.47.1.143.
Повний текст джерелаPetrof, Elaine O., Mark W. Musch, Mae Ciancio, Jun Sun, Michael E. Hobert, Erika C. Claud, Andrew Gewirtz, and 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, no. 3 (March 2008): G808—G818. http://dx.doi.org/10.1152/ajpgi.00362.2007.
Повний текст джерелаOchocka, Anna-Maria, Marzena Czyzewska, and Tadeusz Pawełczyk. "Expression in Escherichia coli of human ARHGAP6 gene and purification of His-tagged recombinant protein." Acta Biochimica Polonica 50, no. 1 (March 31, 2003): 239–47. http://dx.doi.org/10.18388/abp.2003_3732.
Повний текст джерелаTomoyasu, Toshifumi, Akiko Takaya, Tomomi Sasaki, Takahiro Nagase, Reiko Kikuno, Mizue Morioka, and 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, no. 21 (November 1, 2003): 6331–39. http://dx.doi.org/10.1128/jb.185.21.6331-6339.2003.
Повний текст джерелаObuchowski, Igor, Artur Piróg, Milena Stolarska, Bartłomiej Tomiczek, and Krzysztof Liberek. "Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates." PLOS Genetics 15, no. 10 (October 25, 2019): e1008479. http://dx.doi.org/10.1371/journal.pgen.1008479.
Повний текст джерелаNarberhaus, Franz. "α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network". Microbiology and Molecular Biology Reviews 66, № 1 (березень 2002): 64–93. http://dx.doi.org/10.1128/mmbr.66.1.64-93.2002.
Повний текст джерелаHenderson, Brian, and Andrew C. R. Martin. "Protein moonlighting: a new factor in biology and medicine." Biochemical Society Transactions 42, no. 6 (November 17, 2014): 1671–78. http://dx.doi.org/10.1042/bst20140273.
Повний текст джерелаMacario, Alberto J. L., Marianne Lange, Birgitte K. Ahring, and Everly Conway De Macario. "Stress Genes and Proteins in the Archaea." Microbiology and Molecular Biology Reviews 63, no. 4 (December 1, 1999): 923–67. http://dx.doi.org/10.1128/mmbr.63.4.923-967.1999.
Повний текст джерелаFasnacht, Michel, Stefano Gallo, Puneet Sharma, Maximilian Himmelstoß, Patrick A. Limbach, Jessica Willi, and Norbert Polacek. "Dynamic 23S rRNA modification ho5C2501 benefits Escherichia coli under oxidative stress." Nucleic Acids Research 50, no. 1 (December 14, 2021): 473–89. http://dx.doi.org/10.1093/nar/gkab1224.
Повний текст джерелаPaul, Deborupa, and 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, no. 1 (February 28, 2022): 190–200. http://dx.doi.org/10.18006/2022.10(1).190.200.
Повний текст джерелаLiebscher, Markus, Günther Jahreis, Christian Lücke, Susanne Grabley, Satish Raina, and Cordelia Schiene-Fischer. "Fatty Acyl Benzamido Antibacterials Based on Inhibition of DnaK-catalyzed Protein Folding." Journal of Biological Chemistry 282, no. 7 (December 14, 2006): 4437–46. http://dx.doi.org/10.1074/jbc.m607667200.
Повний текст джерелаGarbe, T. R., N. S. Hibler та 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, № 1 (1 січня 1999): 460–65. http://dx.doi.org/10.1128/iai.67.1.460-465.1999.
Повний текст джерелаEl Demerdash, Hassan A. M., Knut J. Heller, and 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, no. 8 (August 2003): 4408–12. http://dx.doi.org/10.1128/aem.69.8.4408-4412.2003.
Повний текст джерелаKönen-Waisman, S., M. Fridkin, and 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, no. 11 (June 1, 1995): 5977–85. http://dx.doi.org/10.4049/jimmunol.154.11.5977.
Повний текст джерелаFu, Xinmiao, Wangwang Jiao, and 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, no. 3 (February 10, 2006): 257–66. http://dx.doi.org/10.1007/s00239-005-0076-5.
Повний текст джерелаBaldridge, Gerald D., Nicole Y. Burkhardt, Roderick F. Felsheim, Timothy J. Kurtti, and Ulrike G. Munderloh. "Plasmids of the pRM/pRF Family Occur in Diverse Rickettsia Species." Applied and Environmental Microbiology 74, no. 3 (December 7, 2007): 645–52. http://dx.doi.org/10.1128/aem.02262-07.
Повний текст джерелаMurthy, Ashlesh K., Kelly Rae Keeler, Jennifer Do, Aravind Seetharaman, Kyle H. Ramsey, Mae Ciancio, and weidang Li. "Tissue Specific Overexpression of Human Heat Shock Protein 70 in Mouse Oviduct Epithelium Reduces Chlamydia Induced Immunopathology." Journal of Immunology 200, no. 1_Supplement (May 1, 2018): 114.20. http://dx.doi.org/10.4049/jimmunol.200.supp.114.20.
Повний текст джерелаReilly, Natasha, Vitaliy Poylin, Michael Menconi, Andrew Onderdonk, Stig Bengmark та 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, № 3 (вересень 2007): R1169—R1179. http://dx.doi.org/10.1152/ajpregu.00770.2006.
Повний текст джерелаInaba, Yuhei, Nobuhiro Ueno, Masatsugu Numata, Xiaorong Zhu, Jeannette S. Messer, David L. Boone, Mikihiro Fujiya, Yutaka Kohgo, Mark W. Musch, and 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, no. 4 (October 1, 2016): G634—G647. http://dx.doi.org/10.1152/ajpgi.00092.2016.
Повний текст джерелаDarsonval, Maud, Tarek Msadek, Hervé Alexandre, and 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, no. 1 (October 9, 2015): 18–26. http://dx.doi.org/10.1128/aem.02495-15.
Повний текст джерелаGregory, Meredith, Emily Whiston, Norito Sugi, Coralynn Sack, Merideth C. Kamradt, Susan Heimer, Michael S. Gilmore та Bruce R. Ksander. "αB-crystallin protects the retina during S. aureus induced endophthalmitis (45.2)". Journal of Immunology 178, № 1_Supplement (1 квітня 2007): S57. http://dx.doi.org/10.4049/jimmunol.178.supp.45.2.
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