Artículos de revistas sobre el tema "HSP18.5"
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Liu, Peng, Jundong Jia, Hanwen Wu, Zihan Song y Xi He. "Hsp from Lactobacillus plantarum Expression in Lactococcus lactis MG1363". BIO Web of Conferences 61 (2023): 01010. http://dx.doi.org/10.1051/bioconf/20236101010.
Texto completoKurre, Devanshu y Kaza Suguna. "Network of Entamoeba histolytica HSP18.5 dimers formed by two overlapping [IV]‐X‐[IV] motifs". Proteins: Structure, Function, and Bioinformatics 89, n.º 8 (8 de abril de 2021): 1039–54. http://dx.doi.org/10.1002/prot.26081.
Texto completoKokke, Bas P. A., Michel R. Leroux, E. Peter M. Candido, Wilbert C. Boelens y Wilfried W. de Jong. "Caenorhabditis eleganssmall heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity". FEBS Letters 433, n.º 3 (21 de agosto de 1998): 228–32. http://dx.doi.org/10.1016/s0014-5793(98)00917-x.
Texto completoOtani, Mieko, Toshiyuki Ueki, Satoshi Kozuka, Miki Segawa, Keiji Sano y Sumiko Inouye. "Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus". Journal of Bacteriology 187, n.º 15 (1 de agosto de 2005): 5236–41. http://dx.doi.org/10.1128/jb.187.15.5236-5241.2005.
Texto completoLöw, Daniela, Kurt Brändle, Lutz Nover y Christoph Forreiter. "Cytosolic heat-stress proteins Hsp17.7 class I and Hsp17.3 class II of tomato act as molecular chaperones in vivo". Planta 211, n.º 4 (15 de septiembre de 2000): 575–82. http://dx.doi.org/10.1007/s004250000315.
Texto completoZhang, Yanhao, Shanshan Li, Qianyi Liu, Ruiying Long, Jihong Feng, Huan Qin, Mao Li, Liping Liu y Junmin Luo. "Mycobacterium tuberculosis Heat-Shock Protein 16.3 Induces Macrophage M2 Polarization Through CCRL2/CX3CR1". Inflammation 43, n.º 2 (20 de noviembre de 2019): 487–506. http://dx.doi.org/10.1007/s10753-019-01132-9.
Texto completoMa, Pengfei, Jie Li, Lei Qi y Xiuzhu Dong. "The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation". International Journal of Molecular Sciences 22, n.º 5 (4 de marzo de 2021): 2591. http://dx.doi.org/10.3390/ijms22052591.
Texto completoWagner, Daniela, Jens Schneider-Mergener y Christoph Forreiter. "Analysis of Chaperone Function and Formation of Hetero-oligomeric Complexes of Hsp18.1 and Hsp17.7, Representing Two Different Cytoplasmic sHSP Classes in Pisum sativum". Journal of Plant Growth Regulation 24, n.º 3 (septiembre de 2005): 226–37. http://dx.doi.org/10.1007/s00344-005-0020-3.
Texto completoZhang, L., C. Lohmann, R. Prändl y F. Schöffl. "Heat Stress-Dependent DNA Binding of Arabidopsis Heat Shock Transcription Factor HSF1 to Heat Shock Gene Promoters in Arabidopsis Suspension Culture Cells in vivo". Biological Chemistry 384, n.º 6 (16 de junio de 2003): 959–63. http://dx.doi.org/10.1515/bc.2003.108.
Texto completoWANG, Z., B. LAI, J. CAO, Z. LI, L. QU, A. CAO y L. LAI. "Hierarchical Unfolding of Mj HSP16.5". Acta Physico-Chimica Sinica 24, n.º 10 (octubre de 2008): 1745–50. http://dx.doi.org/10.1016/s1872-1508(08)60070-4.
Texto completoSaha, Abhik, Archna Sharma, Amlanjyoti Dhar, Bhabatarak Bhattacharyya, Siddhartha Roy y Sujoy K. Das Gupta. "Antagonists of Hsp16.3, a Low-Molecular-Weight Mycobacterial Chaperone and Virulence Factor, Derived from Phage-Displayed Peptide Libraries". Applied and Environmental Microbiology 71, n.º 11 (noviembre de 2005): 7334–44. http://dx.doi.org/10.1128/aem.71.11.7334-7344.2005.
Texto completoMerewitz, Emily B., Thomas Gianfagna y Bingru Huang. "Effects of SAG12-ipt and HSP18.2-ipt Expression on Cytokinin Production, Root Growth, and Leaf Senescence in Creeping Bentgrass Exposed to Drought Stress". Journal of the American Society for Horticultural Science 135, n.º 3 (mayo de 2010): 230–39. http://dx.doi.org/10.21273/jashs.135.3.230.
Texto completoKim, Dong Ryoung, Ick Lee, Sung Chul Ha y Kyeong Kyu Kim. "Activation mechanism of HSP16.5 from Methanococcus jannaschii". Biochemical and Biophysical Research Communications 307, n.º 4 (agosto de 2003): 991–98. http://dx.doi.org/10.1016/s0006-291x(03)01302-0.
Texto completoChen, Ke-Jun, Feng-Zeng Li, Qian Ye, Meng Jia y Sheng Fang. "HSP105 expression in cutaneous malignant melanoma: Correlation with clinicopathological characteristics". PLOS ONE 16, n.º 10 (7 de octubre de 2021): e0258053. http://dx.doi.org/10.1371/journal.pone.0258053.
Texto completoFENG, Xiuguang, Sufang HUANG, Xinmiao FU, Abuduaini ABULIMITI y Zengyi CHANG. "The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein Hsp16.3 occurs via a stepwise mechanism". Biochemical Journal 363, n.º 2 (8 de abril de 2002): 329–34. http://dx.doi.org/10.1042/bj3630329.
Texto completoKozhabek, Zh, J. L. Үu y X. L. Wang. "Analysis of the HSP17.6 protein mechanism in BBSV infection". BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 135, n.º 2 (2021): 38–47. http://dx.doi.org/10.32523/2616-7034-2021-135-2-38-47.
Texto completoYu, Nancy, Michael Kakunda, Victoria Pham, Jennie R. Lill, Pan Du, Matthew Wongchenko, Yibing Yan, Ron Firestein y XiaoDong Huang. "HSP105 Recruits Protein Phosphatase 2A To Dephosphorylate β-Catenin". Molecular and Cellular Biology 35, n.º 8 (2 de febrero de 2015): 1390–400. http://dx.doi.org/10.1128/mcb.01307-14.
Texto completoZappasodi, Roberta, Italia Bongarzone, Gaia C. Ghedini, Lorenzo Castagnoli, Antonello D. Cabras, Antonella Messina, Monica Tortoreto et al. "Serological identification of HSP105 as a novel non-Hodgkin lymphoma therapeutic target". Blood 118, n.º 16 (20 de octubre de 2011): 4421–30. http://dx.doi.org/10.1182/blood-2011-06-364570.
Texto completoWang, Zheng, AoNeng Cao y LuHua Lai. "High activity of Mj HSP16.5 under acidic condition". Science in China Series B: Chemistry 52, n.º 3 (16 de diciembre de 2008): 325–31. http://dx.doi.org/10.1007/s11426-008-0158-5.
Texto completoZappasodi, Roberta, Alessandra Cavanè, Monica Tortoreto, Cristina Tringali, Giusi Ruggiero, Lorenzo Castagnoli, Bruno Venerando et al. "HSP105 Inhibition Counteracts Key Oncogenic Pathways and Hampers the Growth of Human Aggressive B-Cell Non-Hodgkin Lymphoma". Blood 120, n.º 21 (16 de noviembre de 2012): 1562. http://dx.doi.org/10.1182/blood.v120.21.1562.1562.
Texto completoPark, Hanseul y Yeh-Jin Ahn. "Development of Transgenic Escherichia coli with Improved Viability by Heterologous Expression of a Heat Shock Protein Gene from Carrot (Daucus carota L.)". HortScience 51, n.º 3 (marzo de 2016): 305–10. http://dx.doi.org/10.21273/hortsci.51.3.305.
Texto completoZappasodi, Roberta, Gaia C. Ghedini, Italia Bongarzone, Lorenzo Castagnoli, Maida de Bortoli, Piera Aiello, Alessandra Cavanè et al. "Serological Identification of HSP105 as a Novel Non-Hodgkin Lymphoma Therapeutic Target". Blood 116, n.º 21 (19 de noviembre de 2010): 463. http://dx.doi.org/10.1182/blood.v116.21.463.463.
Texto completoLiman, Narin y Murat Kuzkale. "Heat shock proteins exhibit distinct spatiotemporal expression patterns in the domestic cat (". Reproduction, Fertility and Development 34, n.º 6 (4 de febrero de 2022): 498–515. http://dx.doi.org/10.1071/rd21155.
Texto completoZhang, Yang, Xing-Hui Cai, Rong-Jun Zhang, Xiao-Rong Hou, Xiao-Ge Song, Sheng-Bing Wu, Shuang Yu y Jiang-Peng Cao. "Acupuncture Regulates the Unfolded Protein Response and Inhibits Apoptosis in a Rat Model of Heroin Relapse". Acupuncture in Medicine 34, n.º 6 (diciembre de 2016): 441–48. http://dx.doi.org/10.1136/acupmed-2015-010954.
Texto completoMchaourab, Hassane S., Yi-Lun Lin y Benjamin W. Spiller. "Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5". Biochemistry 51, n.º 25 (15 de junio de 2012): 5105–12. http://dx.doi.org/10.1021/bi300525x.
Texto completoVlachonasios, Konstantinos E., Dina K. Kadyrzhanova y David R. Dilley. "Application of Gene-specific mRNA Differential Display for Identification of cDNAs that Encode Small HSPs Correlated with the Heat-induced Chilling Tolerance of Tomato Fruit". HortScience 32, n.º 3 (junio de 1997): 498D—498. http://dx.doi.org/10.21273/hortsci.32.3.498d.
Texto completoAo-Neng, CAO, WANG Wei-Xue, YUWEN Tai-Ran, DENG Wei y LAI Lu-Hua. "Inhibition of Amyloid Fibrillization and Dissociation of Matured Amyloid Fibrils by Mj HSP16.5". Acta Physico-Chimica Sinica 26, n.º 07 (2010): 2015–20. http://dx.doi.org/10.3866/pku.whxb20100708.
Texto completoBettey, Mary y W. E. Finch-Savage. "Stress protein content of mature Brassica seeds and their germination performance". Seed Science Research 8, n.º 3 (septiembre de 1998): 347–55. http://dx.doi.org/10.1017/s096025850000427x.
Texto completoHan, Dong y Huang Xu. "Cloning, expression, purification and characterization of HSP105". Cell Biology International 34, n.º 8 (1 de agosto de 2010): S46. http://dx.doi.org/10.1042/cbi034s046a.
Texto completoXie, Jia, Xing‐Xing Hu, Meng‐Fan Zhai, Xiao‐Juan Yu, Xiao‐Wen Song, Shan‐Shan Gao, Wei Wu y Bin Li. "Characterization and functional analysis of hsp18.3 gene in the red flour beetle, Tribolium castaneum". Insect Science 26, n.º 2 (7 de diciembre de 2017): 263–73. http://dx.doi.org/10.1111/1744-7917.12543.
Texto completoNandi, Sandip Kumar, Ayon Chakraborty, Alok Kumar Panda y Ashis Biswas. "Conformational perturbation, hydrophobic interactions and oligomeric association are responsible for the enhanced chaperone function of Mycobacterium leprae HSP18 under pre-thermal condition". RSC Advances 6, n.º 67 (2016): 62146–56. http://dx.doi.org/10.1039/c6ra00167j.
Texto completoHayakawa, Toshihiko, Toru Kudo, Takashi Ito, Nobuyuki Takahashi y Tomoyuki Yamaya. "ACT Domain Repeat Protein 7, ACR7, Interacts with a Chaperone HSP18.0-CII in Rice Nuclei". Plant and Cell Physiology 47, n.º 7 (julio de 2006): 891–904. http://dx.doi.org/10.1093/pcp/pcj062.
Texto completoKoteiche, Hanane A. y Hassane S. Mchaourab. "The determinants of the oligomeric structure in Hsp16.5 are encoded in the α-crystallin domain". FEBS Letters 519, n.º 1-3 (19 de abril de 2002): 16–22. http://dx.doi.org/10.1016/s0014-5793(02)02688-1.
Texto completoXi, Dong, Ping Wei, Changsheng Zhang y Luhua Lai. "The minimal α-crystallin domain of Mj Hsp16.5 is functional at non-heat-shock conditions". Proteins: Structure, Function, and Bioinformatics 82, n.º 7 (6 de diciembre de 2013): 1156–67. http://dx.doi.org/10.1002/prot.24480.
Texto completoSavic, Jelena, Ivana Dragicevic, D. Pantelic, Jasmina Oljaca y Ivana Momcilovic. "Expression of small heat shock proteins and heat tolerance in potato (Solanum tuberosum L.)". Archives of Biological Sciences 64, n.º 1 (2012): 135–44. http://dx.doi.org/10.2298/abs1201135s.
Texto completoMangas, Kirstie M., Nicholas J. Tobias, Estelle Marion, Jérémie Babonneau, Laurent Marsollier, Jessica L. Porter, Sacha J. Pidot et al. "High antibody titres induced by protein subunit vaccines using Mycobacterium ulcerans antigens Hsp18 and MUL_3720 with a TLR-2 agonist fail to protect against Buruli ulcer in mice". PeerJ 8 (7 de agosto de 2020): e9659. http://dx.doi.org/10.7717/peerj.9659.
Texto completoLini, Nirmala, Nallakandy Panangadan Shankernarayan y Kuppamuthu Dharmalingam. "Quantitative real-time PCR analysis of Mycobacterium leprae DNA and mRNA in human biopsy material from leprosy and reactional cases". Journal of Medical Microbiology 58, n.º 6 (1 de junio de 2009): 753–59. http://dx.doi.org/10.1099/jmm.0.007252-0.
Texto completoZhao, Shanmin, Jieran Shi, Caiqin Zhang, Yong Zhao, Fengfeng Mao, Wei Yang, Bing Bai, Hai Zhang, Changhong Shi y Zhikai Xu. "Monoclonal Antibodies Against a Mycobacterium tuberculosis Ag85B-Hsp16.3 Fusion Protein". Hybridoma 30, n.º 5 (octubre de 2011): 427–32. http://dx.doi.org/10.1089/hyb.2011.0047.
Texto completoRauch, Jennifer N. y Jason E. Gestwicki. "Binding of Human Nucleotide Exchange Factors to Heat Shock Protein 70 (Hsp70) Generates Functionally Distinct Complexes in Vitro". Journal of Biological Chemistry 289, n.º 3 (5 de diciembre de 2013): 1402–14. http://dx.doi.org/10.1074/jbc.m113.521997.
Texto completoSaito, Youhei, Nobuyuki Yamagishi y Takumi Hatayama. "Different localization of Hsp105 family proteins in mammalian cells". Experimental Cell Research 313, n.º 17 (octubre de 2007): 3707–17. http://dx.doi.org/10.1016/j.yexcr.2007.06.009.
Texto completoXing, Jinpeng, Yan Xu, Jiang Tian, Thomas Gianfagna y Bingru Huang. "Suppression of Shade- or Heat-induced Leaf Senescence in Creeping Bentgrass through Transformation with the ipt Gene for Cytokinin Synthesis". Journal of the American Society for Horticultural Science 134, n.º 6 (noviembre de 2009): 602–9. http://dx.doi.org/10.21273/jashs.134.6.602.
Texto completoAtkinson, Burr G., Ling Liu, Ing Swie Goping y David B. Walden. "Expression of the genes encoding hsp73, hsp18, and ubiquitin in radicles of heat-shocked maize seedlings". Genome 31, n.º 2 (15 de enero de 1989): 698–704. http://dx.doi.org/10.1139/g89-127.
Texto completoMarmiroli, Nelson, Angelo Pavesi, Gabriella Di Cola, Hans Hartings, Giovanna Raho, Maria Rosaria Conte y Carla Perrotta. "Identification, characterization, and analysis of cDNA and genomic sequences encoding two different small heat shock proteins in Hordeum vulgare". Genome 36, n.º 6 (1 de diciembre de 1993): 1111–18. http://dx.doi.org/10.1139/g93-148.
Texto completoKorber, Philipp, Jennifer M. Stahl, Knud H. Nierhaus y James C. A. Bardwell. "Hsp15: a ribosome-associated heat shock protein". EMBO Journal 19, n.º 4 (15 de febrero de 2000): 741–48. http://dx.doi.org/10.1093/emboj/19.4.741.
Texto completoMaitre, Magali, Stéphanie Weidmann, Aurélie Rieu, Daphna Fenel, Guy Schoehn, Christine Ebel, Jacques Coves y Jean Guzzo. "The oligomer plasticity of the small heat-shock protein Lo18 from Oenococcus oeni influences its role in both membrane stabilization and protein protection". Biochemical Journal 444, n.º 1 (26 de abril de 2012): 97–104. http://dx.doi.org/10.1042/bj20120066.
Texto completoFodor, Dávid, Éva Pozsgai, Andrew V. Schally, Zoltán László, Éva Gömöri, Éva Szabó, László Rumi, Dorottya Lőcsei, Árpád Boronkai y Szabolcs Bellyei. "Expression Levels of GHRH-Receptor, pAkt and Hsp90 Predict 10-Year Overall Survival in Patients with Locally Advanced Rectal Cancer". Biomedicines 11, n.º 3 (27 de febrero de 2023): 719. http://dx.doi.org/10.3390/biomedicines11030719.
Texto completoHatayama, T., K. Ishihara y K. Yasuda. "Mammalian stress protein HSP105 is phosphorylated by casein kinase II". Biochemical Society Transactions 28, n.º 5 (1 de octubre de 2000): A411. http://dx.doi.org/10.1042/bst028a411.
Texto completoChen, Y., J. An, Y. Ding, H. Dai, Q. Mao, L. Feng, B. Liu et al. "Preliminary X-Ray Crystallographic Studies Of The Mycobacterium Tuberculosis Hsp16.3 Molecular Chaperone". Protein & Peptide Letters 8, n.º 6 (1 de diciembre de 2001): 499–502. http://dx.doi.org/10.2174/0929866013409111.
Texto completoChang, Yong, Xuemei Li y Zihe Rao. "A preliminary study on functional domains of small heat shock protein Hsp16.3 *". Progress in Natural Science 14, n.º 1 (1 de enero de 2004): 21–25. http://dx.doi.org/10.1080/10020070412331343081.
Texto completoPark, Hanseul, Joohee Lee y Yeh-Jin Ahn. "Heterologously expressed carrot Hsp17.7 was denatured by ATP treatment under abiotic stress". Biocatalysis and Agricultural Biotechnology 15 (julio de 2018): 240–44. http://dx.doi.org/10.1016/j.bcab.2018.06.020.
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