Table of Contents Author Guidelines Submit a Manuscript
Journal of Biomedicine and Biotechnology
Volume 2012, Article ID 252049, 7 pages
http://dx.doi.org/10.1155/2012/252049
Research Article

Effect of αB-Crystallin on Protein Aggregation in Drosophila

1Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
2Insect Biomedical Research Center, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
3Center for Gene-Protein Research, Hanoi Medical University, No. 1, Ton That Tung Street, DongDa, Hanoi, Vietnam
4Department of Biomolecular Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan

Received 5 October 2011; Accepted 13 December 2011

Academic Editor: George Perry

Copyright © 2012 Nguyen Trong Tue et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Citations to this Article [14 citations]

The following is the list of published articles that have cited the current article.

  • Ali Chaari, Jessica Hoarau-Véchot, and Moncef Ladjimi, “Applying chaperones to protein-misfolding disorders: Molecular chaperones against alpha synuclein in Parkinson's disease,” International Journal of Biological Macromolecules, 2013. View at Publisher · View at Google Scholar
  • Heng B. Xie, Anthony Cammarato, Namakkal S. Rajasekaran, Huali Zhang, Jennifer A. Suggs, Ho-Chen Lin, Sanford I. Bernstein, Ivor J. Benjamin, and Kent G. Golic, “The NADPH Metabolic Network Regulates Human αB-crystallin Cardiomyopathy and Reductive Stress in Drosophila melanogaster,” PLoS Genetics, vol. 9, no. 6, 2013. View at Publisher · View at Google Scholar
  • R. A. Quinlan, and R. J. Ellis, “Chaperones: needed for both the good times and the bad times,” Philosophical Transactions of the Royal Society B: Biological Sciences, vol. 368, no. 1617, pp. 20130091–20130091, 2013. View at Publisher · View at Google Scholar
  • Dezerae Cox, John A. Carver, and Heath Ecroyd, “Preventing α-synuclein aggregation: The role of the small heat-shock molecular chaperone proteins,” Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2014. View at Publisher · View at Google Scholar
  • Vaishali Kakkar, Melanie Meister-Broekema, Melania Minoia, Serena Carra, and Harm H. Kampinga, “Barcoding heat shock proteins to human diseases: Looking beyond the heat shock response,” DMM Disease Models and Mechanisms, vol. 7, no. 4, pp. 421–434, 2014. View at Publisher · View at Google Scholar
  • Maria Jimenez-Sanchez, Wun Lam, Michael Hannus, Birte Sönnichsen, Sara Imarisio, Angeleen Fleming, Alessia Tarditi, Fiona Menzies, Teresa Ed Dami, Catherine Xu, Eduardo Gonzalez-Couto, Giulia Lazzeroni, Freddy Heitz, Daniela Diamanti, Luisa Massai, Venkata P Satagopam, Guido Marconi, Chiara Caramelli, Arianna Nencini, Matteo Andreini, Gian Luca Sardone, Nicola P Caradonna, Valentina Porcari, Carla Scali, Reinhard Schneider, Giuseppe Pollio, Cahir J O'Kane, Andrea Caricasole, and David C Rubinsztein, “siRNA screen identifies QPCT as a druggable target for Huntington's disease,” Nature Chemical Biology, 2015. View at Publisher · View at Google Scholar
  • Reddy, and Reddy, “Emerging role for αB-crystallin as a therapeutic agent: Pros and Cons,” Current Molecular Medicine, vol. 15, no. 1, pp. 47–61, 2015. View at Publisher · View at Google Scholar
  • Nikola Golenhofen, and Britta Bartelt-Kirbach, “HspB5/αB-Crystallin in the Brain,” The Big Book on Small Heat Shock Proteins, vol. 8, pp. 365–381, 2015. View at Publisher · View at Google Scholar
  • Nikola Golenhofen, and Britta Bartelt-Kirbach, “The impact of small heat shock proteins (HspBs) in Alzheimer’s and other neurological diseases,” Current Pharmaceutical Design, vol. 22, no. 26, pp. 4050–4062, 2016. View at Publisher · View at Google Scholar
  • Ana Osório Oliveira, Alexander Osmand, Tiago Fleming Outeiro, Paul Joseph Muchowski, and Steven Finkbeiner, “αB-Crystallin overexpression in astrocytes modulates the phenotype of the BACHD mouse model of Huntington's disease.,” Human molecular genetics, vol. 25, no. 9, pp. 1677–89, 2016. View at Publisher · View at Google Scholar
  • Britta Bartelt-Kirbach, Margarethe Moron, Maximilian Glomb, Marie-Pascale Weller, Nikola Golenhofen, and Clara-Maria Beck, “HspB5/αB-crystallin increases dendritic complexity and protects the dendritic arbor during heat shock in cultured rat hippocampal neurons,” Cellular and Molecular Life Sciences, vol. 73, no. 19, pp. 3761–3775, 2016. View at Publisher · View at Google Scholar
  • Justin J. Yerbury, Lezanne Ooi, Andrew Dillin, Darren N. Saunders, Danny M. Hatters, Philip M. Beart, Neil R. Cashman, Mark R. Wilson, and Heath Ecroyd, “Walking the tightrope: proteostasis and neurodegenerative disease,” Journal of Neurochemistry, vol. 137, no. 4, pp. 489–505, 2016. View at Publisher · View at Google Scholar
  • Sabrina Batonnet-Pichon, Anthony Behin, Eva Cabet, Florence Delort, Patrick Vicart, and Alain Lilienbaum, “Myofibrillar Myopathies: New Perspectives from Animal Models to Potential Therapeutic Approaches,” Journal of Neuromuscular Diseases, vol. 4, no. 1, pp. 1–15, 2017. View at Publisher · View at Google Scholar
  • Vibha Prasad, Yasmine Wasser, Friederike Hans, Anand Goswami, Istvan Katona, Tiago F. Outeiro, Philipp J. Kahle, Jörg B. Schulz, and Aaron Voigt, “ Monitoring α-synuclein multimerization in vivo ,” The FASEB Journal, vol. 33, no. 2, pp. 2116–2131, 2019. View at Publisher · View at Google Scholar