Статті в журналах з теми "HSP18.5"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-50 статей у журналах для дослідження на тему "HSP18.5".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Переглядайте статті в журналах для різних дисциплін та оформлюйте правильно вашу бібліографію.
Liu, Peng, Jundong Jia, Hanwen Wu, Zihan Song, and 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.
Повний текст джерелаKurre, Devanshu, and Kaza Suguna. "Network of Entamoeba histolytica HSP18.5 dimers formed by two overlapping [IV]‐X‐[IV] motifs." Proteins: Structure, Function, and Bioinformatics 89, no. 8 (April 8, 2021): 1039–54. http://dx.doi.org/10.1002/prot.26081.
Повний текст джерелаKokke, Bas P. A., Michel R. Leroux, E. Peter M. Candido, Wilbert C. Boelens, and 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, no. 3 (August 21, 1998): 228–32. http://dx.doi.org/10.1016/s0014-5793(98)00917-x.
Повний текст джерелаOtani, Mieko, Toshiyuki Ueki, Satoshi Kozuka, Miki Segawa, Keiji Sano, and Sumiko Inouye. "Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus." Journal of Bacteriology 187, no. 15 (August 1, 2005): 5236–41. http://dx.doi.org/10.1128/jb.187.15.5236-5241.2005.
Повний текст джерелаLöw, Daniela, Kurt Brändle, Lutz Nover, and 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, no. 4 (September 15, 2000): 575–82. http://dx.doi.org/10.1007/s004250000315.
Повний текст джерелаZhang, Yanhao, Shanshan Li, Qianyi Liu, Ruiying Long, Jihong Feng, Huan Qin, Mao Li, Liping Liu, and Junmin Luo. "Mycobacterium tuberculosis Heat-Shock Protein 16.3 Induces Macrophage M2 Polarization Through CCRL2/CX3CR1." Inflammation 43, no. 2 (November 20, 2019): 487–506. http://dx.doi.org/10.1007/s10753-019-01132-9.
Повний текст джерелаMa, Pengfei, Jie Li, Lei Qi, and Xiuzhu Dong. "The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation." International Journal of Molecular Sciences 22, no. 5 (March 4, 2021): 2591. http://dx.doi.org/10.3390/ijms22052591.
Повний текст джерелаWagner, Daniela, Jens Schneider-Mergener, and 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, no. 3 (September 2005): 226–37. http://dx.doi.org/10.1007/s00344-005-0020-3.
Повний текст джерелаZhang, L., C. Lohmann, R. Prändl, and 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, no. 6 (June 16, 2003): 959–63. http://dx.doi.org/10.1515/bc.2003.108.
Повний текст джерелаWANG, Z., B. LAI, J. CAO, Z. LI, L. QU, A. CAO, and L. LAI. "Hierarchical Unfolding of Mj HSP16.5." Acta Physico-Chimica Sinica 24, no. 10 (October 2008): 1745–50. http://dx.doi.org/10.1016/s1872-1508(08)60070-4.
Повний текст джерелаSaha, Abhik, Archna Sharma, Amlanjyoti Dhar, Bhabatarak Bhattacharyya, Siddhartha Roy, and 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, no. 11 (November 2005): 7334–44. http://dx.doi.org/10.1128/aem.71.11.7334-7344.2005.
Повний текст джерелаMerewitz, Emily B., Thomas Gianfagna, and 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, no. 3 (May 2010): 230–39. http://dx.doi.org/10.21273/jashs.135.3.230.
Повний текст джерелаKim, Dong Ryoung, Ick Lee, Sung Chul Ha, and Kyeong Kyu Kim. "Activation mechanism of HSP16.5 from Methanococcus jannaschii." Biochemical and Biophysical Research Communications 307, no. 4 (August 2003): 991–98. http://dx.doi.org/10.1016/s0006-291x(03)01302-0.
Повний текст джерелаChen, Ke-Jun, Feng-Zeng Li, Qian Ye, Meng Jia, and Sheng Fang. "HSP105 expression in cutaneous malignant melanoma: Correlation with clinicopathological characteristics." PLOS ONE 16, no. 10 (October 7, 2021): e0258053. http://dx.doi.org/10.1371/journal.pone.0258053.
Повний текст джерелаFENG, Xiuguang, Sufang HUANG, Xinmiao FU, Abuduaini ABULIMITI, and Zengyi CHANG. "The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein Hsp16.3 occurs via a stepwise mechanism." Biochemical Journal 363, no. 2 (April 8, 2002): 329–34. http://dx.doi.org/10.1042/bj3630329.
Повний текст джерелаKozhabek, Zh, J. L. Үu, and 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, no. 2 (2021): 38–47. http://dx.doi.org/10.32523/2616-7034-2021-135-2-38-47.
Повний текст джерелаYu, Nancy, Michael Kakunda, Victoria Pham, Jennie R. Lill, Pan Du, Matthew Wongchenko, Yibing Yan, Ron Firestein та XiaoDong Huang. "HSP105 Recruits Protein Phosphatase 2A To Dephosphorylate β-Catenin". Molecular and Cellular Biology 35, № 8 (2 лютого 2015): 1390–400. http://dx.doi.org/10.1128/mcb.01307-14.
Повний текст джерелаZappasodi, 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, no. 16 (October 20, 2011): 4421–30. http://dx.doi.org/10.1182/blood-2011-06-364570.
Повний текст джерелаWang, Zheng, AoNeng Cao, and LuHua Lai. "High activity of Mj HSP16.5 under acidic condition." Science in China Series B: Chemistry 52, no. 3 (December 16, 2008): 325–31. http://dx.doi.org/10.1007/s11426-008-0158-5.
Повний текст джерелаZappasodi, 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, no. 21 (November 16, 2012): 1562. http://dx.doi.org/10.1182/blood.v120.21.1562.1562.
Повний текст джерелаPark, Hanseul, and 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, no. 3 (March 2016): 305–10. http://dx.doi.org/10.21273/hortsci.51.3.305.
Повний текст джерелаZappasodi, 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, no. 21 (November 19, 2010): 463. http://dx.doi.org/10.1182/blood.v116.21.463.463.
Повний текст джерелаLiman, Narin, and Murat Kuzkale. "Heat shock proteins exhibit distinct spatiotemporal expression patterns in the domestic cat (." Reproduction, Fertility and Development 34, no. 6 (February 4, 2022): 498–515. http://dx.doi.org/10.1071/rd21155.
Повний текст джерелаZhang, Yang, Xing-Hui Cai, Rong-Jun Zhang, Xiao-Rong Hou, Xiao-Ge Song, Sheng-Bing Wu, Shuang Yu, and Jiang-Peng Cao. "Acupuncture Regulates the Unfolded Protein Response and Inhibits Apoptosis in a Rat Model of Heroin Relapse." Acupuncture in Medicine 34, no. 6 (December 2016): 441–48. http://dx.doi.org/10.1136/acupmed-2015-010954.
Повний текст джерелаMchaourab, Hassane S., Yi-Lun Lin, and Benjamin W. Spiller. "Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5." Biochemistry 51, no. 25 (June 15, 2012): 5105–12. http://dx.doi.org/10.1021/bi300525x.
Повний текст джерелаVlachonasios, Konstantinos E., Dina K. Kadyrzhanova, and 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, no. 3 (June 1997): 498D—498. http://dx.doi.org/10.21273/hortsci.32.3.498d.
Повний текст джерелаAo-Neng, CAO, WANG Wei-Xue, YUWEN Tai-Ran, DENG Wei, and LAI Lu-Hua. "Inhibition of Amyloid Fibrillization and Dissociation of Matured Amyloid Fibrils by Mj HSP16.5." Acta Physico-Chimica Sinica 26, no. 07 (2010): 2015–20. http://dx.doi.org/10.3866/pku.whxb20100708.
Повний текст джерелаBettey, Mary, and W. E. Finch-Savage. "Stress protein content of mature Brassica seeds and their germination performance." Seed Science Research 8, no. 3 (September 1998): 347–55. http://dx.doi.org/10.1017/s096025850000427x.
Повний текст джерелаHan, Dong, and Huang Xu. "Cloning, expression, purification and characterization of HSP105." Cell Biology International 34, no. 8 (August 1, 2010): S46. http://dx.doi.org/10.1042/cbi034s046a.
Повний текст джерелаXie, Jia, Xing‐Xing Hu, Meng‐Fan Zhai, Xiao‐Juan Yu, Xiao‐Wen Song, Shan‐Shan Gao, Wei Wu, and Bin Li. "Characterization and functional analysis of hsp18.3 gene in the red flour beetle, Tribolium castaneum." Insect Science 26, no. 2 (December 7, 2017): 263–73. http://dx.doi.org/10.1111/1744-7917.12543.
Повний текст джерелаNandi, Sandip Kumar, Ayon Chakraborty, Alok Kumar Panda, and 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, no. 67 (2016): 62146–56. http://dx.doi.org/10.1039/c6ra00167j.
Повний текст джерелаHayakawa, Toshihiko, Toru Kudo, Takashi Ito, Nobuyuki Takahashi, and Tomoyuki Yamaya. "ACT Domain Repeat Protein 7, ACR7, Interacts with a Chaperone HSP18.0-CII in Rice Nuclei." Plant and Cell Physiology 47, no. 7 (July 2006): 891–904. http://dx.doi.org/10.1093/pcp/pcj062.
Повний текст джерелаKoteiche, Hanane A., та Hassane S. Mchaourab. "The determinants of the oligomeric structure in Hsp16.5 are encoded in the α-crystallin domain". FEBS Letters 519, № 1-3 (19 квітня 2002): 16–22. http://dx.doi.org/10.1016/s0014-5793(02)02688-1.
Повний текст джерелаXi, Dong, Ping Wei, Changsheng Zhang та Luhua Lai. "The minimal α-crystallin domain of Mj Hsp16.5 is functional at non-heat-shock conditions". Proteins: Structure, Function, and Bioinformatics 82, № 7 (6 грудня 2013): 1156–67. http://dx.doi.org/10.1002/prot.24480.
Повний текст джерелаSavic, Jelena, Ivana Dragicevic, D. Pantelic, Jasmina Oljaca, and Ivana Momcilovic. "Expression of small heat shock proteins and heat tolerance in potato (Solanum tuberosum L.)." Archives of Biological Sciences 64, no. 1 (2012): 135–44. http://dx.doi.org/10.2298/abs1201135s.
Повний текст джерелаMangas, 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 (August 7, 2020): e9659. http://dx.doi.org/10.7717/peerj.9659.
Повний текст джерелаLini, Nirmala, Nallakandy Panangadan Shankernarayan, and 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, no. 6 (June 1, 2009): 753–59. http://dx.doi.org/10.1099/jmm.0.007252-0.
Повний текст джерелаZhao, Shanmin, Jieran Shi, Caiqin Zhang, Yong Zhao, Fengfeng Mao, Wei Yang, Bing Bai, Hai Zhang, Changhong Shi, and Zhikai Xu. "Monoclonal Antibodies Against a Mycobacterium tuberculosis Ag85B-Hsp16.3 Fusion Protein." Hybridoma 30, no. 5 (October 2011): 427–32. http://dx.doi.org/10.1089/hyb.2011.0047.
Повний текст джерелаRauch, Jennifer N., and 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, no. 3 (December 5, 2013): 1402–14. http://dx.doi.org/10.1074/jbc.m113.521997.
Повний текст джерелаSaito, Youhei, Nobuyuki Yamagishi, and Takumi Hatayama. "Different localization of Hsp105 family proteins in mammalian cells." Experimental Cell Research 313, no. 17 (October 2007): 3707–17. http://dx.doi.org/10.1016/j.yexcr.2007.06.009.
Повний текст джерелаXing, Jinpeng, Yan Xu, Jiang Tian, Thomas Gianfagna, and 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, no. 6 (November 2009): 602–9. http://dx.doi.org/10.21273/jashs.134.6.602.
Повний текст джерелаAtkinson, Burr G., Ling Liu, Ing Swie Goping, and David B. Walden. "Expression of the genes encoding hsp73, hsp18, and ubiquitin in radicles of heat-shocked maize seedlings." Genome 31, no. 2 (January 15, 1989): 698–704. http://dx.doi.org/10.1139/g89-127.
Повний текст джерелаMarmiroli, Nelson, Angelo Pavesi, Gabriella Di Cola, Hans Hartings, Giovanna Raho, Maria Rosaria Conte, and Carla Perrotta. "Identification, characterization, and analysis of cDNA and genomic sequences encoding two different small heat shock proteins in Hordeum vulgare." Genome 36, no. 6 (December 1, 1993): 1111–18. http://dx.doi.org/10.1139/g93-148.
Повний текст джерелаKorber, Philipp, Jennifer M. Stahl, Knud H. Nierhaus, and James C. A. Bardwell. "Hsp15: a ribosome-associated heat shock protein." EMBO Journal 19, no. 4 (February 15, 2000): 741–48. http://dx.doi.org/10.1093/emboj/19.4.741.
Повний текст джерелаMaitre, Magali, Stéphanie Weidmann, Aurélie Rieu, Daphna Fenel, Guy Schoehn, Christine Ebel, Jacques Coves, and 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, no. 1 (April 26, 2012): 97–104. http://dx.doi.org/10.1042/bj20120066.
Повний текст джерелаFodor, Dávid, Éva Pozsgai, Andrew V. Schally, Zoltán László, Éva Gömöri, Éva Szabó, László Rumi, Dorottya Lőcsei, Árpád Boronkai, and Szabolcs Bellyei. "Expression Levels of GHRH-Receptor, pAkt and Hsp90 Predict 10-Year Overall Survival in Patients with Locally Advanced Rectal Cancer." Biomedicines 11, no. 3 (February 27, 2023): 719. http://dx.doi.org/10.3390/biomedicines11030719.
Повний текст джерелаHatayama, T., K. Ishihara, and K. Yasuda. "Mammalian stress protein HSP105 is phosphorylated by casein kinase II." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A411. http://dx.doi.org/10.1042/bst028a411.
Повний текст джерелаChen, 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, no. 6 (December 1, 2001): 499–502. http://dx.doi.org/10.2174/0929866013409111.
Повний текст джерелаChang, Yong, Xuemei Li, and Zihe Rao. "A preliminary study on functional domains of small heat shock protein Hsp16.3 *." Progress in Natural Science 14, no. 1 (January 1, 2004): 21–25. http://dx.doi.org/10.1080/10020070412331343081.
Повний текст джерелаPark, Hanseul, Joohee Lee, and Yeh-Jin Ahn. "Heterologously expressed carrot Hsp17.7 was denatured by ATP treatment under abiotic stress." Biocatalysis and Agricultural Biotechnology 15 (July 2018): 240–44. http://dx.doi.org/10.1016/j.bcab.2018.06.020.
Повний текст джерела