Статті в журналах з теми "Hsp31"
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Rasouly, Aviram, Yotam Shenhar, and Eliora Z. Ron. "Thermoregulation of Escherichia coli hchA Transcript Stability." Journal of Bacteriology 189, no. 15 (May 25, 2007): 5779–81. http://dx.doi.org/10.1128/jb.00453-07.
Повний текст джерелаMujacic, Mirna, and Fran�ois Baneyx. "Chaperone Hsp31 Contributes to Acid Resistance in Stationary-Phase Escherichia coli." Applied and Environmental Microbiology 73, no. 3 (December 8, 2006): 1014–18. http://dx.doi.org/10.1128/aem.02429-06.
Повний текст джерелаSubedi, Krishna P., Dongwook Choi, Insook Kim, Bumchan Min, and Chankyu Park. "Hsp31 of Escherichia coli K-12 is glyoxalase III." Molecular Microbiology 81, no. 4 (July 6, 2011): 926–36. http://dx.doi.org/10.1111/j.1365-2958.2011.07736.x.
Повний текст джерелаHansberg, Wilhelm, Teresa Nava-Ramírez, Pablo Rangel-Silva, Adelaida Díaz-Vilchis, and Aydé Mendoza-Oliva. "Large-Size Subunit Catalases Are Chimeric Proteins: A H2O2 Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity." Antioxidants 11, no. 5 (May 17, 2022): 979. http://dx.doi.org/10.3390/antiox11050979.
Повний текст джерелаZhang, Kai, Kuikui Jiang, Ruoxi Hong, Fei Xu, Wen Xia, Ge Qin, Kaping Lee, et al. "Identification and characterization of critical genes associated with tamoxifen resistance in breast cancer." PeerJ 8 (December 4, 2020): e10468. http://dx.doi.org/10.7717/peerj.10468.
Повний текст джерелаKim, Jihong, Dongwook Choi, Chankyu Park, and Kyoung-Seok Ryu. "Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31." Biomolecular NMR Assignments 11, no. 2 (March 3, 2017): 159–63. http://dx.doi.org/10.1007/s12104-017-9739-6.
Повний текст джерелаKim, Jihong, Dongwook Choi, So-Young Cha, Young-Mee Oh, Eunha Hwang, Chankyu Park, and Kyoung-Seok Ryu. "Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone." Journal of Molecular Biology 430, no. 12 (June 2018): 1760–72. http://dx.doi.org/10.1016/j.jmb.2018.04.029.
Повний текст джерелаChoi, Dongwook, Kyoung-Seok Ryu, and Chankyu Park. "Structural alteration of Escherichia coli Hsp31 by thermal unfolding increases chaperone activity." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834, no. 2 (February 2013): 621–28. http://dx.doi.org/10.1016/j.bbapap.2012.11.006.
Повний текст джерелаHasim, Sahar, Nur Ahmad Hussin, Fadhel Alomar, Keshore R. Bidasee, Kenneth W. Nickerson, and Mark A. Wilson. "A Glutathione-independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans." Journal of Biological Chemistry 289, no. 3 (December 3, 2013): 1662–74. http://dx.doi.org/10.1074/jbc.m113.505784.
Повний текст джерелаNava-Ramírez, Teresa, Sammy Gutiérrez-Terrazas, and Wilhelm Hansberg. "The Molecular Chaperone Mechanism of the C-Terminal Domain of Large-Size Subunit Catalases." Antioxidants 12, no. 4 (March 30, 2023): 839. http://dx.doi.org/10.3390/antiox12040839.
Повний текст джерелаMujacic, Mirna, and Francois Baneyx. "Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31." Molecular Microbiology 60, no. 6 (June 2006): 1576–89. http://dx.doi.org/10.1111/j.1365-2958.2006.05207.x.
Повний текст джерелаTsai, Chai-jui, Kiran Aslam, Holli M. Drendel, Josephat M. Asiago, Kourtney M. Goode, Lake N. Paul, Jean-Christophe Rochet, and Tony R. Hazbun. "Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process." Journal of Biological Chemistry 290, no. 41 (August 25, 2015): 24816–34. http://dx.doi.org/10.1074/jbc.m115.678367.
Повний текст джерелаAslam, Kiran, Chai-jui Tsai, and Tony R. Hazbun. "The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation." Prion 10, no. 6 (October 3, 2016): 444–65. http://dx.doi.org/10.1080/19336896.2016.1234574.
Повний текст джерелаMihoub, Mouadh, Jad Abdallah, Brigitte Gontero, Julien Dairou, and Gilbert Richarme. "The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal." Biochemical and Biophysical Research Communications 463, no. 4 (August 2015): 1305–10. http://dx.doi.org/10.1016/j.bbrc.2015.06.111.
Повний текст джерелаKim, Jihong, Dongwook Choi, Chankyu Park, and Kyoung-Seok Ryu. "Per-deuteration and NMR experiments for the backbone assignment of 62 kDa protein, Hsp31." Journal of the Korean Magnetic Resonance Society 19, no. 3 (December 20, 2015): 112–18. http://dx.doi.org/10.6564/jkmrs.2015.19.3.112.
Повний текст джерелаSastry, M. S. R., Weibin Zhou, and François Baneyx. "Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity." Protein Science 18, no. 7 (May 13, 2009): 1439–47. http://dx.doi.org/10.1002/pro.158.
Повний текст джерелаAslam, Kiran, and Tony R. Hazbun. "Hsp31, a member of the DJ-1 superfamily, is a multitasking stress responder with chaperone activity." Prion 10, no. 2 (March 3, 2016): 103–11. http://dx.doi.org/10.1080/19336896.2016.1141858.
Повний текст джерелаGraille, Marc, Sophie Quevillon-Cheruel, Nicolas Leulliot, Cong-Zhao Zhou, Ines Li de La Sierra Gallay, Lilian Jacquamet, Jean-Luc Ferrer, et al. "Crystal Structure of the YDR533c S. cerevisiae Protein, a Class II Member of the Hsp31 Family." Structure 12, no. 5 (May 2004): 839–47. http://dx.doi.org/10.1016/j.str.2004.02.030.
Повний текст джерелаLee, Sun-Joo, So Jung Kim, In-Kwon Kim, Junsang Ko, Chang-Sook Jeong, Gyung-Hwa Kim, Chankyu Park, et al. "Crystal Structures of Human DJ-1 and Escherichia coli Hsp31, Which Share an Evolutionarily Conserved Domain." Journal of Biological Chemistry 278, no. 45 (August 25, 2003): 44552–59. http://dx.doi.org/10.1074/jbc.m304517200.
Повний текст джерелаde Miguel, N., P. C. Echeverria, and S. O. Angel. "Differential Subcellular Localization of Members of the Toxoplasma gondii Small Heat Shock Protein Family." Eukaryotic Cell 4, no. 12 (December 2005): 1990–97. http://dx.doi.org/10.1128/ec.4.12.1990-1997.2005.
Повний текст джерелаDas, Samir, Sanghati Roy Chowdhury, Sanjay Dey, and Udayaditya Sen. "Structural and biochemical studies on Vibrio cholerae Hsp31 reveals a novel dimeric form and Glutathione-independent Glyoxalase activity." PLOS ONE 12, no. 2 (February 24, 2017): e0172629. http://dx.doi.org/10.1371/journal.pone.0172629.
Повний текст джерелаSastry, M. S. R., Konstantin Korotkov, Yan Brodsky, and François Baneyx. "Hsp31, theEscherichia coli yedUGene Product, Is a Molecular Chaperone Whose Activity Is Inhibited by ATP at High Temperatures." Journal of Biological Chemistry 277, no. 48 (September 15, 2002): 46026–34. http://dx.doi.org/10.1074/jbc.m205800200.
Повний текст джерелаPadilla, C. A., J. A. Bárcena, M. J. López-Grueso, and R. Requejo-Aguilar. "The regulation of TORC1 pathway by the yeast chaperones Hsp31 is mediated by SFP1 and affects proteasomal activity." Biochimica et Biophysica Acta (BBA) - General Subjects 1863, no. 3 (March 2019): 534–46. http://dx.doi.org/10.1016/j.bbagen.2018.12.011.
Повний текст джерелаGraf, Paul C. F., Maria Martinez-Yamout, Stephen VanHaerents, Hauke Lilie, H. Jane Dyson, and Ursula Jakob. "Activation of the Redox-regulated Chaperone Hsp33 by Domain Unfolding." Journal of Biological Chemistry 279, no. 19 (March 15, 2004): 20529–38. http://dx.doi.org/10.1074/jbc.m401764200.
Повний текст джерелаQuigley, P. M., K. Korotkov, F. Baneyx, and W. G. J. Hol. "The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad." Proceedings of the National Academy of Sciences 100, no. 6 (March 5, 2003): 3137–42. http://dx.doi.org/10.1073/pnas.0530312100.
Повний текст джерелаAmm, Ingo, Derrick Norell, and Dieter H. Wolf. "Absence of the Yeast Hsp31 Chaperones of the DJ-1 Superfamily Perturbs Cytoplasmic Protein Quality Control in Late Growth Phase." PLOS ONE 10, no. 10 (October 14, 2015): e0140363. http://dx.doi.org/10.1371/journal.pone.0140363.
Повний текст джерелаCarlin, Aaron F., Sinem Beyhan, Jesús F. Peña, Jason E. Stajich, Suganya Viriyakosol, Joshua Fierer, and Theo N. Kirkland. "Transcriptional Analysis of Coccidioides immitis Mycelia and Spherules by RNA Sequencing." Journal of Fungi 7, no. 5 (May 7, 2021): 366. http://dx.doi.org/10.3390/jof7050366.
Повний текст джерелаHansberg, Wilhelm. "Monofunctional Heme-Catalases." Antioxidants 11, no. 11 (November 2, 2022): 2173. http://dx.doi.org/10.3390/antiox11112173.
Повний текст джерелаBoudreault, Julien, Ni Wang, Gang Yan, Meiou Dai, Sophie Poulet, Girija Daliah, and Jean-Jacques Lebrun. "Abstract 3938: In vivo genome-wide CRISPR screen in pancreatic ductal adenocarcinoma defines HSPE1 as a potential oncogene by acting through G2/M cell cycle arrest." Cancer Research 83, no. 7_Supplement (April 4, 2023): 3938. http://dx.doi.org/10.1158/1538-7445.am2023-3938.
Повний текст джерелаGalai, Geut, Hila Ben-David, Liron Levin, Martin F. Orth, Thomas G. P. Grünewald, Shai Pilosof, Shimon Bershtein, and Barak Rotblat. "Pan-Cancer Analysis of Mitochondria Chaperone-Client Co-Expression Reveals Chaperone Functional Partitioning." Cancers 12, no. 4 (March 30, 2020): 825. http://dx.doi.org/10.3390/cancers12040825.
Повний текст джерелаScieglinska, Dorota, Zdzisław Krawczyk, Damian Robert Sojka, and Agnieszka Gogler-Pigłowska. "Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes." Cell Stress and Chaperones 24, no. 6 (November 2019): 1027–44. http://dx.doi.org/10.1007/s12192-019-01044-5.
Повний текст джерелаBankapalli, Kondalarao, SreeDivya Saladi, Sahezeel S. Awadia, Arvind Vittal Goswami, Madhuja Samaddar, and Patrick D'Silva. "Robust Glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI Family Member Protein, Is Critical for Oxidative Stress Resistance inSaccharomyces cerevisiae." Journal of Biological Chemistry 290, no. 44 (September 14, 2015): 26491–507. http://dx.doi.org/10.1074/jbc.m115.673624.
Повний текст джерелаSeibert, Jacob T., Malavika K. Adur, Ronald B. Schultz, Porsha Q. Thomas, Zoe E. Kiefer, Aileen F. Keating, Lance H. Baumgard, and Jason W. Ross. "Differentiating between the effects of heat stress and lipopolysaccharide on the porcine ovarian heat shock protein response1." Journal of Animal Science 97, no. 12 (November 29, 2019): 4965–73. http://dx.doi.org/10.1093/jas/skz343.
Повний текст джерелаSastry, M. S. R., P. M. Quigley, W. G. J. Hol, and F. Baneyx. "The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures." Proceedings of the National Academy of Sciences 101, no. 23 (June 1, 2004): 8587–92. http://dx.doi.org/10.1073/pnas.0403033101.
Повний текст джерелаRicharme, Gilbert, Jad Abdallah, Nicolas Mathas, Valérie Gautier, and Julien Dairou. "Further characterization of the Maillard deglycase DJ-1 and its prokaryotic homologs, deglycase 1/Hsp31, deglycase 2/YhbO, and deglycase 3/YajL." Biochemical and Biophysical Research Communications 503, no. 2 (September 2018): 703–9. http://dx.doi.org/10.1016/j.bbrc.2018.06.064.
Повний текст джерелаAndrade, Warne Pedro, Bryan Ôrtero Perez Gonçalves, Luciana Maria Silva, and Agnaldo Lopes Dasilva Filho. "Upregulation of HSPB1 heat shock gene and ERCC1 gene on serous ovarian cancer cell line in HIPEC in vitro model." Journal of Clinical Oncology 39, no. 15_suppl (May 20, 2021): e17559-e17559. http://dx.doi.org/10.1200/jco.2021.39.15_suppl.e17559.
Повний текст джерелаZaitsev, M. S., T. N. Kiseleva, K. V. Lugovkina, N. V. Balatskaya, E. V. Jani, and K. E. Seliverstova. "Experimental assessment of the impact of high acoustic power ultrasound diagnostics on animal eyes." Russian Ophthalmological Journal 15, no. 3 (September 23, 2022): 92–98. http://dx.doi.org/10.21516/2072-0076-2022-15-3-92-98.
Повний текст джерелаDavis, R. E., and M. L. King. "The developmental expression of the heat-shock response in Xenopus laevis." Development 105, no. 2 (February 1, 1989): 213–22. http://dx.doi.org/10.1242/dev.105.2.213.
Повний текст джерелаAlabi, Mutiu A., Olugbenga O. Adebawo, Oluwole A. Daini, Stella B. Somiari, and Richard I. Somiari. "HSPD1, HSPB1 and VDAC1 are Over-expressed in Invasive Ductal Carcinoma of the Breast." International Journal of Cancer Research 12, no. 2 (March 15, 2016): 82–91. http://dx.doi.org/10.3923/ijcr.2016.82.91.
Повний текст джерелаMujacic, Mirna, Martin W. Bader, and François Baneyx. "Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions." Molecular Microbiology 51, no. 3 (December 15, 2003): 849–59. http://dx.doi.org/10.1046/j.1365-2958.2003.03871.x.
Повний текст джерелаRehman, Saif ur, Asif Nadeem, Maryam Javed, Faiz-ul Hassan, Xier Luo, Ruqayya Bint Khalid, and Qingyou Liu. "Genomic Identification, Evolution and Sequence Analysis of the Heat-Shock Protein Gene Family in Buffalo." Genes 11, no. 11 (November 23, 2020): 1388. http://dx.doi.org/10.3390/genes11111388.
Повний текст джерелаRen, Juanhui, Bo Ren, Qiuwen Zhang, and Xiuqing Zheng. "A Novel Hybrid Extreme Learning Machine Approach Improved by K Nearest Neighbor Method and Fireworks Algorithm for Flood Forecasting in Medium and Small Watershed of Loess Region." Water 11, no. 9 (September 5, 2019): 1848. http://dx.doi.org/10.3390/w11091848.
Повний текст джерелаLi, Junwei, Jiufu Wen, Ruiping Hu, Surui Pei, Ting Li, Binbin Shan, Honghui Huang, and Changbo Zhu. "Transcriptome Responses to Different Environments in Intertidal Zones in the Peanut Worm Sipunculus nudus." Biology 12, no. 9 (August 29, 2023): 1182. http://dx.doi.org/10.3390/biology12091182.
Повний текст джерелаChen, Keqin, Changmiao Hou, Lei Xu, Hanwu Peng, Chaogui He, Jing Liu, Guoqing Wang, Shaoshuai Huang, and Xiehong Liu. "HSPB1 Regulates Autophagy and Apoptosis in Vascular Smooth Muscle Cells in Arteriosclerosis Obliterans." Cardiovascular Therapeutics 2022 (November 14, 2022): 1–11. http://dx.doi.org/10.1155/2022/3889419.
Повний текст джерелаZhao, Sida, Bin Li, Yiyuan Chen, Chuzhong Li, and Yazhuo Zhang. "Analysis of the Prognostic and Immunological Role of HSPB1 in Pituitary Adenoma: A Potential Target for Therapy." Medicina 59, no. 5 (May 5, 2023): 885. http://dx.doi.org/10.3390/medicina59050885.
Повний текст джерелаCai, Qiaoyan, Jing Lin, Ling Zhang, Jiumao Lin, Lili Wang, Daxin Chen, and Jun Peng. "Comparative proteomics—network analysis of proteins responsible for ursolic acid–induced cytotoxicity in colorectal cancer cells." Tumor Biology 39, no. 3 (March 2017): 101042831769501. http://dx.doi.org/10.1177/1010428317695015.
Повний текст джерелаWang, Yana, Jiali Liu, Qiuyue Kong, Hao Cheng, Fei Tu, Peng Yu, Ying Liu та ін. "Cardiomyocyte-specific deficiency of HSPB1 worsens cardiac dysfunction by activating NFκB-mediated leucocyte recruitment after myocardial infarction". Cardiovascular Research 115, № 1 (2 липня 2018): 154–67. http://dx.doi.org/10.1093/cvr/cvy163.
Повний текст джерелаJundra, Nuntawat, Aksarakorn Kummasook, and Monsicha Pongpom. "Expression of Heat Shock Protein 30 in Talaromyces marneffei during Phase Transition and in Response to Heat and Oxidative Stresses." Biomedical Sciences and Clinical Medicine 62, no. 2 (June 29, 2023): 63–72. http://dx.doi.org/10.12982/bscm.2023.07.
Повний текст джерелаGibert, Benjamin, Stéphanie Simon, Valeriya Dimitrova, Chantal Diaz-Latoud, and André-Patrick Arrigo. "Peptide aptamers: tools to negatively or positively modulate HSPB1(27) function." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1617 (May 5, 2013): 20120075. http://dx.doi.org/10.1098/rstb.2012.0075.
Повний текст джерелаKovács, Árpád Ferenc, Nóra Fekete, Lilla Turiák, András Ács, László Kőhidai, Edit I. Buzás, and Éva Pállinger. "Unravelling the Role of Trophoblastic-Derived Extracellular Vesicles in Regulatory T Cell Differentiation." International Journal of Molecular Sciences 20, no. 14 (July 14, 2019): 3457. http://dx.doi.org/10.3390/ijms20143457.
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