Academic literature on the topic 'Chaperone; fibril formation; phosphorylation'
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Journal articles on the topic "Chaperone; fibril formation; phosphorylation"
Mitra, Gopa, Suvroma Gupta, Asim Poddar, and Bhabatarak Bhattacharyya. "MAP2c prevents arachidonic acid-induced fibril formation of tau: Role of chaperone activity and phosphorylation." Biophysical Chemistry 205 (October 2015): 16–23. http://dx.doi.org/10.1016/j.bpc.2015.06.003.
Full textSelig, Emily E., Courtney O. Zlatic, Dezerae Cox, Yee-Foong Mok, Paul R. Gooley, Heath Ecroyd, and Michael D. W. Griffin. "N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation." Journal of Biological Chemistry 295, no. 29 (May 16, 2020): 9838–54. http://dx.doi.org/10.1074/jbc.ra120.012748.
Full textEcroyd, Heath, Sarah Meehan, Joseph Horwitz, J. Andrew Aquilina, Justin L. P. Benesch, Carol V. Robinson, Cait E. Macphee, and John A. Carver. "Mimicking phosphorylation of αB-crystallin affects its chaperone activity." Biochemical Journal 401, no. 1 (December 11, 2006): 129–41. http://dx.doi.org/10.1042/bj20060981.
Full textNakata, Yui, Yuuto Kitazaki, Hitomi Kanaoka, Erika Shingen, Rina Uehara, Kunihiro Hongo, Yasushi Kawata, and Tomohiro Mizobata. "Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from Escherichia coli." International Journal of Molecular Sciences 23, no. 21 (October 31, 2022): 13243. http://dx.doi.org/10.3390/ijms232113243.
Full textRaman, Bakthisaran, Tadato Ban, Miyo Sakai, Saloni Y. Pasta, Tangirala Ramakrishna, Hironobu Naiki, Yuji Goto, and Ch Mohan Rao. "αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin." Biochemical Journal 392, no. 3 (December 6, 2005): 573–81. http://dx.doi.org/10.1042/bj20050339.
Full textKulig, Melissa, and Heath Ecroyd. "The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin." Biochemical Journal 448, no. 3 (November 21, 2012): 343–52. http://dx.doi.org/10.1042/bj20121187.
Full textAkbari, Ali, Fatemeh Bamdad, and Jianping Wu. "Chaperone-like food components: from basic concepts to food applications." Food & Function 9, no. 7 (2018): 3597–609. http://dx.doi.org/10.1039/c7fo01902e.
Full textAbelein, Axel, Astrid Gräslund, and Jens Danielsson. "Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation." Proceedings of the National Academy of Sciences 112, no. 17 (March 30, 2015): 5407–12. http://dx.doi.org/10.1073/pnas.1421961112.
Full textXu, Li-Qiong, Si Wu, Alexander K. Buell, Samuel I. A. Cohen, Li-Jun Chen, Wan-Hui Hu, Sarah A. Cusack, et al. "Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1617 (May 5, 2013): 20110410. http://dx.doi.org/10.1098/rstb.2011.0410.
Full textTanaka, Naoki, Ryoji Tanaka, Mutsumi Tokuhara, Shigeru Kunugi, Yin-Fai Lee, and Daizo Hamada. "Amyloid Fibril Formation and Chaperone-like Activity of Peptides from αA-Crystallin†." Biochemistry 47, no. 9 (March 2008): 2961–67. http://dx.doi.org/10.1021/bi701823g.
Full textDissertations / Theses on the topic "Chaperone; fibril formation; phosphorylation"
Hemmingsson, Lovisa. "Bri2 BRICHOS domain : Eukaryotic expression and importance of strictly conserved cysteine residues." Thesis, Linköpings universitet, Institutionen för fysik, kemi och biologi, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-138401.
Full textKoudelka, Tomas. "Casein proteins: investigating their chaperone activity and amyloid fibril formation." Thesis, 2011. http://hdl.handle.net/2440/67197.
Full textThesis (Ph.D.) -- University of Adelaide, School of Chemistry and Physics, 2011
Conference papers on the topic "Chaperone; fibril formation; phosphorylation"
Saenger, Thorsten, Marten Schulte, Fabian Herrmann, Marius Pattberg, Stefan Vordenbäumen, Ellen Bleck, Matthias Schneider, and Joachim Jose. "Phosphorylation of breast-milk αS1-casein induced conformational changes and abolished TLR4-agonisticity as well as formation of fibril structure." In 5th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2019. http://dx.doi.org/10.3390/ecmc2019-06290.
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