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ISRN Allergy
Volume 2011 (2011), Article ID 869647, 8 pages
http://dx.doi.org/10.5402/2011/869647
Review Article

Histone Deacetylase Inhibition and Dietary Short-Chain Fatty Acids

1Allergy and Immune Disorders, Murdoch Childrens Research Institute, Royal Children's Hospital, Flemington Road, Parkville, VIC 3052, Australia
2Department of Paediatrics, The University of Melbourne, Parkville, VIC 3010, Australia
3Epigenomic Medicine, Baker IDI Heart and Diabetes Institute, The Alfred Medical Research and Education Precinct, 75 Commercial Road, Melbourne, VIC 3004, Australia
4Department of Pathology, The University of Melbourne, Parkville, VIC 3010, Australia

Received 12 November 2011; Accepted 5 December 2011

Academic Editors: V. Calder, C. I. Ezeamuzie, E. A. García-Zepeda, and R. Paganelli

Copyright © 2011 Paul V. Licciardi 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.

Linked References

  1. P. A. Marks and R. Breslow, “Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug,” Nature Biotechnology, vol. 25, no. 1, pp. 84–90, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. C. Campàs-Moya, “Romidepsin for the treatment of cutaneous T-cell lymphoma,” Drugs of Today, vol. 45, no. 11, pp. 787–795, 2009.
  3. F. A.A. Kwa, A. Balcerczyk, P. Licciardi, A. El-Osta, and T. C. Karagiannis, “Chromatin modifying agents—the cutting edge of anticancer therapy,” Drug Discovery Today, vol. 16, no. 13-14, pp. 543–547, 2011. View at Publisher · View at Google Scholar
  4. P. A. Marks, “Histone deacetylase inhibitors: a chemical genetics approach to understanding cellular functions,” Biochimica et Biophysica Acta, vol. 1799, no. 10-12, pp. 717–725, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. P. A. Marks and W. S. Xu, “Histone deacetylase inhibitors: potential in cancer therapy,” Journal of Cellular Biochemistry, vol. 107, no. 4, pp. 600–608, 2009. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Dokmanovic, C. Clarke, and P. A. Marks, “Histone deacetylase inhibitors: overview and perspectives,” Molecular Cancer Research, vol. 5, no. 10, pp. 981–989, 2007. View at Publisher · View at Google Scholar · View at Scopus
  7. R. A. Blaheta and J. Cinatl Jr., “Anti-tumor mechanisms of valproate: a novel role for an old drug,” Medicinal Research Reviews, vol. 22, no. 5, pp. 492–511, 2002. View at Publisher · View at Google Scholar · View at Scopus
  8. G. Rosenberg, “The mechanisms of action of valproate in neuropsychiatric disorders: can we see the forest for the trees?” Cellular and Molecular Life Sciences, vol. 64, no. 16, pp. 2090–2103, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. C. U. Johannessen, “Mechanisms of action of valproate: a commentatory,” Neurochemistry International, vol. 37, no. 2-3, pp. 103–110, 2000. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Gottlicher, S. Minucci, P. Zhu et al., “Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells,” The EMBO Journal, vol. 20, no. 24, pp. 6969–6978, 2001.
  11. C. J. Phiel, F. Zhang, E. Y. Huang, M. G. Guenther, M. A. Lazar, and P. S. Klein, “Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen,” The Journal of Biological Chemistry, vol. 276, no. 39, pp. 36734–36741, 2001. View at Publisher · View at Google Scholar · View at Scopus
  12. O. H. Kramer, P. Zhu, H. P. Ostendorff et al., “The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2,” The EMBO Journal, vol. 22, no. 13, pp. 3411–3420, 2003. View at Publisher · View at Google Scholar · View at Scopus
  13. J. E. Shabason, P. J. Tofilon, and K. Camphausen, “Grand rounds at the National Institutes of Health: HDAC inhibitors as radiation modifiers, from bench to clinic,” Journal of Cellular and Molecular Medicine, vol. 15, no. 12, pp. 2735–2744, 2011. View at Publisher · View at Google Scholar
  14. T. Kouzarides, “Chromatin modifications and their function,” Cell, vol. 128, no. 4, pp. 693–705, 2007. View at Publisher · View at Google Scholar · View at Scopus
  15. A. R. Cyr and F. E. Domann, “The redox basis of epigenetic modifications: from mechanisms to functional consequences,” Antioxidants & Redox Signaling, vol. 15, no. 2, pp. 551–589, 2011. View at Publisher · View at Google Scholar
  16. M. H. Kuo and C. D. Allis, “Roles of histone acetyltransferases and deacetylases in gene regulation,” BioEssays, vol. 20, no. 8, pp. 615–626, 1998. View at Publisher · View at Google Scholar · View at Scopus
  17. P. A. Wade, D. Pruss, and A. P. Wolffe, “Histone acetylation: chromatin in action,” Trends in Biochemical Sciences, vol. 22, no. 4, pp. 128–132, 1997. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Y. Roth, J. M. Denu, and C. D. Allis, “Histone acetyltransferases,” Annual Review of Biochemistry, vol. 70, pp. 81–120, 2001. View at Publisher · View at Google Scholar · View at Scopus
  19. B. C. Smith and J. M. Denu, “Chemical mechanisms of histone lysine and arginine modifications,” Biochimica et Biophysica Acta, vol. 1789, no. 1, pp. 45–57, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. M. C. Haigis and L. P. Guarente, “Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction,” Genes & Development, vol. 20, no. 21, pp. 2913–2921, 2006. View at Publisher · View at Google Scholar · View at Scopus
  21. J. Landry, J. T. Slama, and R. Sternglanz, “Role of NAD+ in the deacetylase activity of the SIR2-like proteins,” Biochemical and Biophysical Research Communications, vol. 278, no. 3, pp. 685–690, 2000. View at Publisher · View at Google Scholar · View at Scopus
  22. J. Landry, A. Sutton, S. T. Tafrov et al., “The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 11, pp. 5807–5811, 2000. View at Publisher · View at Google Scholar · View at Scopus
  23. Y. Horio, T. Hayashi, A. Kuno, and R. Kunimoto, “Cellular and molecular effects of sirtuins in health and disease,” Clinical Science, vol. 121, no. 5, pp. 191–203, 2011. View at Publisher · View at Google Scholar
  24. G. S. Kelly, “A review of the sirtuin system, its clinical implications, and the potential role of dietary activators like resveratrol: part 2,” Alternative Medicine Review, vol. 15, pp. 313–328, 2010.
  25. A. J. M. de Ruijter, A. H. van Gennip, H. N. Caron, S. Kemp, and A. B. P. van Kuilenburg, “Histone deacetylases (HDACs): characterization of the classical HDAC family,” Biochemical Journal, vol. 370, no. 3, pp. 737–749, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. I. V. Gregoretti, Y. M. Lee, and H. V. Goodson, “Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis,” Journal of Molecular Biology, vol. 338, no. 1, pp. 17–31, 2004. View at Publisher · View at Google Scholar · View at Scopus
  27. J. E. Bolden, M. J. Peart, and R. W. Johnstone, “Anticancer activities of histone deacetylase inhibitors,” Nature Reviews Drug Discovery, vol. 5, no. 9, pp. 769–784, 2006. View at Publisher · View at Google Scholar · View at Scopus
  28. P. A. Marks, R. A. Rifkind, V. M. Richon, R. Breslow, T. Miller, and W. K. Kelly, “Histone deacetylases and cancer: causes and therapies,” Nature Reviews Cancer, vol. 1, no. 3, pp. 194–202, 2001. View at Scopus
  29. X. J. Yang and E. Seto, “Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression,” Current Opinion in Genetics & Development, vol. 13, no. 2, pp. 143–153, 2003. View at Publisher · View at Google Scholar · View at Scopus
  30. M. Martin, R. Kettmann, and F. Dequiedt, “Class IIa histone deacetylases: regulating the regulators,” Oncogene, vol. 26, no. 37, pp. 5450–5467, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. O. Witt, H. E. Deubzer, T. Milde, and I. Oehme, “HDAC family: what are the cancer relevant targets?” Cancer Letters, vol. 277, no. 1, pp. 8–21, 2009. View at Publisher · View at Google Scholar · View at Scopus
  32. A. Mai, D. Rotili, S. Valente, and A. G. Kazantsev, “Histone deacetylase inhibitors and neurodegenerative disorders: holding the promise,” Current Pharmaceutical Design, vol. 15, no. 34, pp. 3940–3957, 2009. View at Publisher · View at Google Scholar · View at Scopus
  33. S. Minucci and P. G. Pelicci, “Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer,” Nature Reviews Cancer, vol. 6, no. 1, pp. 38–51, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. W. S. Xu, R. B. Parmigiani, and P. A. Marks, “Histone deacetylase inhibitors: molecular mechanisms of action,” Oncogene, vol. 26, no. 37, pp. 5541–5552, 2007. View at Publisher · View at Google Scholar · View at Scopus
  35. A. Villagra, F. Cheng, H. W. Wang et al., “The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance,” Nature Immunology, vol. 10, no. 1, pp. 92–100, 2009. View at Publisher · View at Google Scholar · View at Scopus
  36. A. Villagra, E. M. Sotomayor, and E. Seto, “Histone deacetylases and the immunological network: implications in cancer and inflammation,” Oncogene, vol. 29, no. 2, pp. 157–173, 2010. View at Publisher · View at Google Scholar · View at Scopus
  37. H. H. Chang, C. P. Chiang, H. C. Hung, C. Y. Lin, Y. T. Deng, and M. Y. P. Kuo, “Histone deacetylase 2 expression predicts poorer prognosis in oral cancer patients,” Oral Oncology, vol. 45, no. 7, pp. 610–614, 2009. View at Publisher · View at Google Scholar · View at Scopus
  38. A. Gloghini, D. Buglio, N. M. Khaskhely et al., “Expression of histone deacetylases in lymphoma: implication for the development of selective inhibitors,” British Journal of Haematology, vol. 147, no. 4, pp. 515–525, 2009. View at Publisher · View at Google Scholar · View at Scopus
  39. M. Dokmanovic and P. A. Marks, “Prospects: histone deacetylase inhibitors,” Journal of Cellular Biochemistry, vol. 96, no. 2, pp. 293–304, 2005. View at Publisher · View at Google Scholar · View at Scopus
  40. J. R. Davie, “Inhibition of histone deacetylase activity by butyrate,” Journal of Nutrition, vol. 133, pp. 2485S–2493S, 2003. View at Scopus
  41. H.-J. Kim and S.-C. Bae, “Histone deacetylase inhibitors: molecular mechanisms of action and clinical trials as anti-cancer drugs,” American Journal of Translational Research, vol. 3, no. 2, pp. 166–179, 2011.
  42. M. Yoshida, M. Kijima, M. Akita, and T. Beppu, “Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A,” The Journal of Biological Chemistry, vol. 265, no. 28, pp. 17174–17179, 1990. View at Scopus
  43. C. M. Arundel, A. S. Glicksman, and J. T. Leith, “Enhancement of radiation injury in human colon tumor cells by the maturational agent sodium butyrate (NaB),” Radiation Research, vol. 104, no. 3, pp. 443–448, 1985. View at Scopus
  44. J. T. Leith, “Potentiation of X ray sensitivity by combinations of sodium butyrate and buthionine sulfoximine,” International Journal of Radiation Oncology Biology Physics, vol. 15, no. 4, pp. 949–951, 1988. View at Scopus
  45. Z. Nackerdien, J. Michie, and L. Bohm, “Chromatin decondensed by acetylation shows an elevated radiation response,” Radiation Research, vol. 117, no. 2, pp. 234–244, 1989. View at Scopus
  46. Y. L. Chung, Y. H. W. Lee, S. H. Yen, and K. H. Chi, “A novel approach for nasopharyngeal carcinoma treatment uses phenylbutyrate as a protein kinase C modulator: implications for radiosensitization and EBV-targeted therapy,” Clinical Cancer Research, vol. 6, no. 4, pp. 1452–1458, 2000. View at Scopus
  47. G. Musso, R. Gambino, and M. Cassader, “Obesity, diabetes, and gut microbiota: the hygiene hypothesis expanded?” Diabetes Care, vol. 33, no. 10, pp. 2277–2284, 2010. View at Publisher · View at Google Scholar
  48. J. Amar, C. Chabo, A. Waget et al., “Intestinal mucosal adherence and translocation of commensal bacteria at the early onset of type 2 diabetes: molecular mechanisms and probiotic treatment,” EMBO Molecular Medicine, vol. 3, no. 9, pp. 559–572, 2011. View at Publisher · View at Google Scholar
  49. F. Backhed, H. Ding, T. Wang et al., “The gut microbiota as an environmental factor that regulates fat storage,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 44, pp. 15718–15723, 2004. View at Publisher · View at Google Scholar · View at Scopus
  50. F. Backhed, J. K. Manchester, C. F. Semenkovich, and J. I. Gordon, “Mechanisms underlying the resistance to diet-induced obesity in germ-free mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 3, pp. 979–984, 2007. View at Publisher · View at Google Scholar · View at Scopus
  51. M. L. K. Tang, “Probiotics and prebiotics: immunological and clinical effects in allergic disease,” Nestle Nutrition Workshop Series: Pediatric Program, vol. 64, pp. 219–238, 2009. View at Publisher · View at Google Scholar · View at Scopus
  52. G. C. Yap, K. K. Chee, P.-Y. Hong et al., “Evaluation of stool microbiota signatures in two cohorts of Asian (Singapore and Indonesia) newborns at risk of atopy,” BMC Microbiology, vol. 11, article 193, 2011. View at Publisher · View at Google Scholar
  53. S. Mueller, K. Saunier, C. Hanisch et al., “Differences in fecal microbiota in different European study populations in relation to age, gender, and country: a cross-sectional study,” Applied and Environmental Microbiology, vol. 72, no. 2, pp. 1027–1033, 2006. View at Publisher · View at Google Scholar · View at Scopus
  54. V. Mai, Q. M. McCrary, R. Sinha, and M. Glei, “Associations between dietary habits and body mass index with gut microbiota composition and fecal water genotoxicity: an observational study in African American and Caucasian American volunteers,” Nutrition Journal, vol. 8, no. 1, article 49, 2009. View at Publisher · View at Google Scholar · View at Scopus
  55. D. W. Thomas and F. R. Greer, “Probiotics and prebiotics in pediatrics,” Pediatrics, vol. 126, pp. 1217–1231, 2010.
  56. B. Bjorksten, E. Sepp, K. Julge, T. Voor, and M. Mikelsaar, “Allergy development and the intestinal microflora during the first year of life,” The Journal of Allergy and Clinical Immunology, vol. 108, no. 4, pp. 516–520, 2001. View at Publisher · View at Google Scholar · View at Scopus
  57. S. Watanabe, Y. Narisawa, S. Arase et al., “Differences in fecal microflora between patients with atopic dermatitis and healthy control subjects,” The Journal of Allergy and Clinical Immunology, vol. 111, no. 3, pp. 587–591, 2003. View at Publisher · View at Google Scholar · View at Scopus
  58. M. Wang, C. Karlsson, C. Olsson et al., “Reduced diversity in the early fecal microbiota of infants with atopic eczema,” The Journal of Allergy and Clinical Immunology, vol. 121, no. 1, pp. 129–134, 2008. View at Publisher · View at Google Scholar
  59. R. E. Ley, P. J. Turnbaugh, S. Klein, and J. I. Gordon, “Microbial ecology: human gut microbes associated with obesity,” Nature, vol. 444, no. 7122, pp. 1022–1023, 2006. View at Publisher · View at Google Scholar · View at Scopus
  60. P. J. Turnbaugh, M. Hamady, T. Yatsunenko et al., “A core gut microbiome in obese and lean twins,” Nature, vol. 457, no. 7228, pp. 480–484, 2009. View at Publisher · View at Google Scholar · View at Scopus
  61. A. Sandin, L. Bråbäck, E. Norin, and B. Bjorksten, “Faecal short chain fatty acid pattern and allergy in early childhood,” Acta Paediatrica, vol. 98, no. 5, pp. 823–827, 2009. View at Publisher · View at Google Scholar · View at Scopus
  62. O. C. Thompson-Chagoyan, M. Fallani, J. Maldonado et al., “Faecal microbiota and short-chain fatty acid levels in faeces from infants with cow's milk protein allergy,” International Archives of Allergy and Immunology, vol. 156, no. 3, pp. 325–332, 2011. View at Publisher · View at Google Scholar
  63. M. Roberfroid, G. R. Gibson, L. Hoyles et al., “Prebiotic effects: metabolic and health benefits,” British Journal of Nutrition, vol. 104, supplement 2, pp. S1–S63, 1999. View at Publisher · View at Google Scholar · View at Scopus
  64. N. Huda-Faujan, A. S. Abdulamir, A. B. Fatimah, et al., “The impact of the level of the intestinal short chain Fatty acids in inflammatory bowel disease patients versus healthy subjects,” The Open Biochemistry Journal, vol. 4, pp. 53–58, 2010.
  65. G. D'Argenio and G. Mazzacca, “Short-chain fatty acid in the human colon: relation to inflammatory bowel diseases and colon cancer,” Advances in Experimental Medicine and Biology, vol. 472, pp. 149–158, 2000. View at Scopus
  66. K. M. Maslowski, A. T. Vieira, A. Ng et al., “Regulation of inflammatory responses by gut microbiota and chemoattractant receptor GPR43,” Nature, vol. 461, no. 7268, pp. 1282–1286, 2009. View at Publisher · View at Google Scholar · View at Scopus
  67. G. Musso, R. Gambino, M. Cassader, et al., “Interactions between gut microbiota and host metabolism predisposing to obesity and diabetes,” Annual Review of Medicine, vol. 62, pp. 361–380, 2011.
  68. M. Vijay-Kumar, J. D. Aitken, F. A. Carvalho et al., “Metabolie syndrome and altered gut microbiota in mice lacking toll-like receptor 5,” Science, vol. 328, no. 5975, pp. 228–231, 2010. View at Publisher · View at Google Scholar · View at Scopus
  69. R. Stienstra, J. A. van Diepen, C. J. Tack et al., “Inflammasome is a central player in the induction of obesity and insulin resistance,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 37, pp. 15324–15329, 2011. View at Publisher · View at Google Scholar
  70. B. Vandanmagsar, Y. H. Youm, A. Ravussin et al., “The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance,” Nature Medicine, vol. 17, pp. 179–188, 2011.
  71. G. Caramia, “Metchnikoff and the centenary of probiotics: an update of their use in gastroenteric pathology during the age of development,” Minerva Pediatrica, vol. 60, no. 6, pp. 1417–1435, 2008.
  72. M. G. Gareau, P. M. Sherman, and W. A. Walker, “Probiotics and the gut microbiota in intestinal health and disease,” Nature Reviews Gastroenterology and Hepatology, vol. 7, pp. 503–514, 2010.
  73. G. Reid, J. A. Younes, H. C. van der Mei, G. B. Gloor, R. Knight, and H. J. Busscher, “Microbiota restoration: natural and supplemented recovery of human microbial communities,” Nature Reviews Microbiology, vol. 9, no. 1, pp. 27–38, 2011. View at Publisher · View at Google Scholar · View at Scopus
  74. M. Kalliomäki, S. Salminen, H. Arvilommi, P. Kero, P. Koskinen, and E. Isolauri, “Probiotics in primary prevention of atopic disease: a randomised placebo-controlled trial,” The Lancet, vol. 357, no. 9262, pp. 1076–1079, 2001. View at Publisher · View at Google Scholar · View at Scopus
  75. H. Sokol, B. Pigneur, L. Watterlot et al., “Faecalibacterium prausnitzii is an anti-inflammatory commensal bacterium identified by gut microbiota analysis of Crohn disease patients,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 43, pp. 16731–16736, 2008. View at Publisher · View at Google Scholar · View at Scopus
  76. T. von der Weid, C. Bulliard, and E. J. Schiffrin, “Induction by a lactic acid bacterium of a population of CD4+ T cells with low proliferative capacity that produce transforming growth factor β and interleukin-10,” Clinical and Diagnostic Laboratory Immunology, vol. 8, no. 4, pp. 695–701, 2001. View at Publisher · View at Google Scholar · View at Scopus
  77. H. Braat, J. van den Brande, E. van Tol, D. Hommes, M. Peppelenbosch, and S. van Deventer, “Lactobacillus rhamnosus induces peripheral hyporesponsiveness in stimulated CD4+ T cells via modulation of dendritic cell function,” American Journal of Clinical Nutrition, vol. 80, no. 6, pp. 1618–1625, 2004. View at Scopus
  78. C. Di Giacinto, M. Marinaro, M. Sanchez, W. Strober, and M. Boirivant, “Probiotics ameliorate recurrent Th1-mediated murine colitis by inducing IL-10 and IL-10-dependent TGF-β-bearing regulatory cells,” The Journal of Immunology, vol. 174, no. 6, pp. 3237–3246, 2005. View at Scopus
  79. T. Pessi, Y. Sütas, M. Hurme, and E. Isolauri, “Interleukin-10 generation in atopic children following oral lactobacillus rhamnosus GG,” Clinical & Experimental Allergy, vol. 30, no. 12, pp. 1804–1808, 2000. View at Publisher · View at Google Scholar · View at Scopus
  80. C. Mullié, A. Yazourh, H. Thibault et al., “Increased poliovirus-specific intestinal antibody response coincides with promotion of Bifidobacterium longum-infantis and Bifidobacterium breve in infants: a randomized, double-blind, placebo-controlled trial,” Pediatric Research, vol. 56, no. 5, pp. 791–795, 2004. View at Publisher · View at Google Scholar · View at Scopus
  81. E. Isolauri, J. Joensuu, H. Suomalainen, M. Luomala, and T. Vesikari, “Improved immunogenicity of oral D x RRV reassortant rotavirus vaccine by Lactobacillus casei GG,” Vaccine, vol. 13, no. 3, pp. 310–312, 1995. View at Publisher · View at Google Scholar · View at Scopus
  82. H. Fang, T. Elina, A. Heikki, and S. Seppo, “Modulation of humoral immune response through probiotic intake,” FEMS Immunology & Medical Microbiology, vol. 29, no. 1, pp. 47–52, 2000. View at Publisher · View at Google Scholar · View at Scopus
  83. P. V. Licciardi, S.-S. Wong, M. L. Tang, and T. C. Karagiannis, “Epigenome targeting by probiotic metabolites,” Gut Pathogens, vol. 2, article 24, 2010. View at Publisher · View at Google Scholar
  84. S. Brand, R. Teich, T. Dicke et al., “Epigenetic regulation in murine offspring as a novel mechanism for transmaternal asthma protection induced by microbes,” The Journal of Allergy and Clinical Immunology, vol. 128, no. 3, pp. 618–625.e7, 2011. View at Publisher · View at Google Scholar