Добірка наукової літератури з теми "HSP18.5"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся зі списками актуальних статей, книг, дисертацій, тез та інших наукових джерел 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.
Статті в журналах з теми "HSP18.5"
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 джерелаДисертації з теми "HSP18.5"
Saxena, Anita. "Role of Hsp105 in CFTR Biogenesis." University of Toledo Health Science Campus / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=mco1279120195.
Повний текст джерелаFang, Feng. "EXPRESSION OF HEAT SHOCK GENES HSP16.6 AND HTPG IN THE CYANOBACTERIUM, SYNECHOCYSTIS SP. PCC 6803." Miami University / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=miami1060835729.
Повний текст джерелаSERVANT, PASCALE. "La reponse au choc thermique chez streptomyces albus : etude des genes groe et caracterisation de la proteine hsp18." Paris 7, 1994. http://www.theses.fr/1994PA077303.
Повний текст джерелаBoehm, Christian Reiner. "Gene expression control for synthetic patterning of bacterial populations and plants." Thesis, University of Cambridge, 2017. https://www.repository.cam.ac.uk/handle/1810/267842.
Повний текст джерелаShih, Chung-Cheng, and 施駿成. "Cloning, Expression, Purification and Chaperone-like Activity of a Small Heat-shock Protein, HSP16.1, from Caenorhabditis elegans." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/17108316576923005625.
Повний текст джерела國立臺灣大學
生化科學研究所
92
Small heat shock proteins (sHSPs) form a diverse family of proteins that are produced under various stresses in all organisms. It has been shown that they have chaperone-like activity, which can bind unfolded or misfolded proteins and maintain them in a folding-competent state. The common structural features of small heat shock proteins comprise an N-terminal domain and a C-terminal tail, which flank the evolutionarily conserved α-crystallin domain. However, α-crystallin, a major protein class of most animal eye lenses, was also found to possess chaperone-like activity similar to small heat shock proteins. Thus sHSPs and α-crystallin constitute a superfamily of related molecular chaperones with similar chaperone-like activity and aggregation property. In this thesis, we cloned, overexpressed, and characterized the chaperone-like activity of HSP16.1 from Caenorhabditis elegans. The cDNA sequence encoding HSP16.1 was amplified using reverse transcriptase/ polymerase chain reaction (RT-PCR) based on the two primers designed according to the nucleotide sequences obtained from the database of C. elegans. After overexpression, HSP16.1 was purified by two different size-exclusion chromatographies. The result from gel-filtration showed that the molecular mass of native HSP16.1 is about 670 kDa, which is different from that estimated from native gradient-gel electrophoresis and analytical ultracentrifugation. Although the midpoint temperature for protein aggregation of HSP16.1 is about 86℃, the secondary structure gradually changes when the temperature is over 50℃, accompanied by the decrease of chaperone-like activity. In contrast to α-crystallin from mammalian eye lenses, the oligomeric complexes and chaperone-like activity of HSP16.1 do not change after preheating treatment. These results suggested that HSP16.1 may be a thermostable protein with refolding potential, and its secondary structure is important to its chaperone-like activity. It is also of interest to find that the increase of calcium ion causes the decrease of chaperone-like activity of HSP16.1. Detailed mechanistic study of this effect is currently in progress.
Частини книг з теми "HSP18.5"
Hatayama, Takumi. "Mammalian 105-kDa Heat-Shock Protein HSP105 and Its Biological Function." In Thermotherapy for Neoplasia, Inflammation, and Pain, 371–81. Tokyo: Springer Japan, 2001. http://dx.doi.org/10.1007/978-4-431-67035-3_42.
Повний текст джерелаSaito, Youhei, and Yuji Nakayama. "Mammalian Heat Shock Protein Hsp105: The Hsp70 Inducer and a Potent Target for Cancer Therapy." In HSP70 in Human Diseases and Disorders, 347–59. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89551-2_18.
Повний текст джерелаТези доповідей конференцій з теми "HSP18.5"
Pupa, Serenella M., Roberta Zappasodi, Italia Bongarzone, Antonello Cabras, Gaia C. Ghedini, Lorenzo Castagnoli, Francesca Micciché, Massimo A. Gianni, and Massimo Di Nicola. "Abstract 4785: Identification of HSP105 as a novel non-Hodgkin lymphoma (NHL) restricted antigen." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4785.
Повний текст джерелаЗвіти організацій з теми "HSP18.5"
Blum, Abraham, Henry T. Nguyen, and N. Y. Klueva. The Genetics of Heat Shock Proteins in Wheat in Relation to Heat Tolerance and Yield. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568105.bard.
Повний текст джерела