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  • Selective clearance of aberrant tau proteins and rescue of neurotoxicity by transcription factor EB
    1. Vinicia A Polito1,,
    2. Hongmei Li1,,
    3. Heidi Martini‐Stoica1,2,3,,
    4. Baiping Wang1,4,
    5. Li Yang1,
    6. Yin Xu1,
    7. Daniel B Swartzlander1,
    8. Michela Palmieri4,5,
    9. Alberto di Ronza4,5,
    10. Virginia M‐Y Lee6,
    11. Marco Sardiello4,5,
    12. Andrea Ballabio4,5,7 and
    13. Hui Zheng*,1,3,4
    1. 1Huffington Center on Aging, Baylor College of Medicine, Houston, TX, USA
    2. 2Interdepartmental Program of Translational Biology and Molecular Medicine, Baylor College of Medicine, Houston, TX, USA
    3. 3Medical Scientist Training Program, Baylor College of Medicine, Houston, TX, USA
    4. 4Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA
    5. 5Dan and Jan Duncan Neurological Research Institute, Texas Children's Hospital, Houston, TX, USA
    6. 6Department of Pathology and Lab Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA, USA
    7. 7Department of Translational Medical Sciences, Section of Pediatrics, Telethon Institute of Genetics and Medicine Federico II University, Naples, Italy
    1. *Corresponding author. Tel: +1 713 798 1568; Fax: +1 713 798 1610; E‐mail: huiz{at}bcm.edu
    1. These authors contributed equally to this work

    The autophagy and lysosomal Transcription Factor EB (TFEB) reduces neurofibrillary tangle pathology and rescues behavioral and synaptic deficits and neurodegeneration in the Tau mouse model. This effect requires lysosomal activity and in vitro evidence highlight PTEN as a TFEB‐target.

    Synopsis

    The autophagy and lysosomal Transcription Factor EB (TFEB) reduces neurofibrillary tangle pathology and rescues behavioral and synaptic deficits and neurodegeneration in the Tau mouse model. This effect requires lysosomal activity and in vitro evidence highlight PTEN as a TFEB‐target.

    • TFEB specifically targets aberrant tau proteins.

    • TFEB potently clears NFT pathology and rescues neurotoxicity in a tauopathy mouse model.

    • PTEN is a novel target of TFEB.

    • Upregulation of PTEN and lysosomal activity may underlie the TFEB effects.

    • Alzheimer's disease
    • tauopathy
    • TFEB
    • PTEN
    • autophagy‐lysosomal pathway
    • Received November 14, 2013.
    • Revision received June 26, 2014.
    • Accepted June 30, 2014.

    This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

    Vinicia A Polito, Hongmei Li, Heidi Martini‐Stoica, Baiping Wang, Li Yang, Yin Xu, Daniel B Swartzlander, Michela Palmieri, Alberto di Ronza, Virginia M‐Y Lee, Marco Sardiello, Andrea Ballabio, Hui Zheng
  • Principles of targeting endothelial cell metabolism to treat angiogenesis and endothelial cell dysfunction in disease
    1. Jermaine Goveia1,2,
    2. Peter Stapor1,2 and
    3. Peter Carmeliet*,1,2
    1. 1Laboratory of Angiogenesis and Neurovascular Link, Vesalius Research Center, Department of Oncology, University of Leuven, Leuven, Belgium
    2. 2Laboratory of Angiogenesis and Neurovascular Link, Vesalius Research Center VIB, Leuven, Belgium
    1. *Corresponding author. Tel: +32 16 37 32 02; Fax: +32 16 37 25 85; E‐mail: peter.carmeliet{at}vib-kuleuven.be

    An comprehensive overview of the alterations of endothelial cell metabolism in disease, and of the potential metabolic targets and strategies to reverse their dysfunction and inhibit angiogenesis.

    • angiogenesis
    • endothelial cell dysfunction
    • metabolism
    • Received April 8, 2014.
    • Revision received June 14, 2014.
    • Accepted July 3, 2014.

    This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

    Jermaine Goveia, Peter Stapor, Peter Carmeliet
  • The inwardly rectifying K+ channel KIR7.1 controls uterine excitability throughout pregnancy
    1. Conor McCloskey1,
    2. Cara Rada2,
    3. Elizabeth Bailey1,
    4. Samantha McCavera1,
    5. Hugo A van den Berg3,
    6. Jolene Atia1,
    7. David A Rand3,
    8. Anatoly Shmygol1,
    9. Yi‐Wah Chan1,
    10. Siobhan Quenby1,
    11. Jan J Brosens1,
    12. Manu Vatish1,
    13. Jie Zhang1,
    14. Jerod S Denton4,
    15. Michael J Taggart5,
    16. Catherine Kettleborough6,
    17. David Tickle6,
    18. Jeff Jerman6,
    19. Paul Wright6,
    20. Timothy Dale7,
    21. Srinivasan Kanumilli7,
    22. Derek J Trezise7,
    23. Steve Thornton8,
    24. Pamela Brown9,
    25. Roberto Catalano9,
    26. Nan Lin10,
    27. Sarah K England2 and
    28. Andrew M Blanks*,1
    1. 1Division of Reproductive Health, Clinical Sciences Research Laboratories, Warwick Medical School University of Warwick, Coventry, UK
    2. 2Division of Basic Science Research, Department of Obstetrics and Gynecology, School of Medicine Washington University in St. Louis,, St. Louis, MO, USA
    3. 3Warwick Systems Biology & Mathematics Institute University of Warwick, Coventry, UK
    4. 4Vanderbilt Institute of Chemical Biology, Vanderbilt Institute for Global Health Vanderbilt University School of Medicine Medical Center North, Nashville, TN, USA
    5. 5Institute of Cellular Medicine, Newcastle University, Newcastle upon Tyne, UK
    6. 6Centre for Therapeutics and Discovery, Medical Research Council Technologies, London, UK
    7. 7BioPark, Essen BioScience Ltd, Welwyn Garden City, Hertfordshire, UK
    8. 8Exeter Medical School, Exeter, UK
    9. 9MRC Centre for Reproductive Health (CRH), Queen's Medical Research Institute University of Edinburgh, Edinburgh, UK
    10. 10Department of Mathematics, Washington University, St. Louis, MO, USA
    1. *Corresponding author. Tel: +44 2476968703; Fax: +44 2476968653; E‐mail: andrew.blanks{at}warwick.ac.uk

    Only few effective treatments can manipulate uterine contractility for the prevention of dystocia, preterm labor or post‐partum hemorrhage. This study reveals Kir7.1 channel as a potential target for increasing uterine contractions and identifies novel Kir7.1 inhibitors.

    Synopsis

    Only few effective treatments can manipulate uterine contractility for the prevention of dystocia, preterm labor or post‐partum hemorrhage. This study reveals Kir7.1 channel as a potential target for increasing uterine contractions and identifies novel Kir7.1 inhibitors.

    • A genome‐wide scan of all known potassium channels combined with computational modeling identified Kir7.1 as a potentially useful therapeutic target.

    • Kir7.1 expression increases in mid gestation and declines towards the onset of labor in mice and humans.

    • Kir7.1 inhibition in vitro and in vivo increases uterine contractility.

    • Novel inhibitors of Kir7.1 induce contractions of greater magnitude than a commonly used uterine stimulant oxytocin.

    • pregnancy
    • parturition
    • potassium channels
    • uterus
    • myometrium
    • Received February 6, 2014.
    • Revision received June 13, 2014.
    • Accepted July 2, 2014.

    This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

    Conor McCloskey, Cara Rada, Elizabeth Bailey, Samantha McCavera, Hugo A van den Berg, Jolene Atia, David A Rand, Anatoly Shmygol, Yi‐Wah Chan, Siobhan Quenby, Jan J Brosens, Manu Vatish, Jie Zhang, Jerod S Denton, Michael J Taggart, Catherine Kettleborough, David Tickle, Jeff Jerman, Paul Wright, Timothy Dale, Srinivasan Kanumilli, Derek J Trezise, Steve Thornton, Pamela Brown, Roberto Catalano, Nan Lin, Sarah K England, Andrew M Blanks
  • Long‐term therapeutic silencing of miR‐33 increases circulating triglyceride levels and hepatic lipid accumulation in mice
    1. Leigh Goedeke1,2,3,4,,
    2. Alessandro Salerno3,4,,
    3. Cristina M Ramírez1,2,3,4,
    4. Liang Guo3,4,
    5. Ryan M Allen5,
    6. Xiaoke Yin6,
    7. Sarah R Langley6,
    8. Christine Esau7,
    9. Amarylis Wanschel3,4,
    10. Edward A Fisher3,4,
    11. Yajaira Suárez1,2,3,4,
    12. Angel Baldán5,
    13. Manuel Mayr6 and
    14. Carlos Fernández‐Hernando*,1,2,3,4
    1. 1Vascular Biology and Therapeutics Program, Yale University School of Medicine, New Haven, CT, USA
    2. 2Integrative Cell Signaling and Neurobiology of Metabolism Program, Section of Comparative Medicine Yale University School of Medicine, New Haven, CT, USA
    3. 3Leon H. Charney Division of Cardiology, Department of Medicine, New York University School of Medicine, New York, NY, USA
    4. 4Marc and Ruti Bell Vascular Biology and Disease Program, New York University School of Medicine, New York, NY, USA
    5. 5Edward A. Doisy Department of Biochemistry and Molecular Biology, Center for Cardiovascular Research, Saint Louis University School of Medicine, Saint Louis, MO, USA
    6. 6King's British Heart Foundation Centre, King's College London, London, UK
    7. 7Regulus Therapeutics, San Diego, CA, USA
    1. *Corresponding author. Tel: +1 203 737 4615; Fax: +1 203 737 2290; E‐mail: carlos.fernandez{at}yale.edu
    1. These authors contributed equally to this work.

    Although short‐term anti‐miR‐33 therapy was reported to increase circulating HDL‐cholesterol and reduce atherosclerosis, long‐term adverse effects are here shown for the 1st time in mice fed a high‐fat‐diet to result in hypertriglyerimedia and moderate hepatic steatosis.

    Synopsis

    Although short‐term anti‐miR‐33 therapy was reported to increase circulating HDL‐cholesterol and reduce atherosclerosis, long‐term adverse effects are here shown for the first time in mice fed a high‐fat diet to result in hypertriglyceridemia and moderate hepatic steatosis.

    • The effect of long‐term inhibition of miR‐33 was determined in mice fed a chow diet and high‐fat diet.

    • Chronic therapeutic silencing of miR‐33 increased circulating triglycerides and lipid accumulation in the livers of mice fed a high‐fat diet.

    • miR‐33 inhibition raised the expression of genes involved in fatty acid synthesis and lipid metabolism.

    • Further studies are warranted to understand the complex gene regulatory network controlled by miR‐33.

    • cholesterol
    • fatty acids
    • hepatic steatosis
    • microRNA
    • Received March 8, 2014.
    • Revision received June 18, 2014.
    • Accepted June 26, 2014.

    This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

    Leigh Goedeke, Alessandro Salerno, Cristina M Ramírez, Liang Guo, Ryan M Allen, Xiaoke Yin, Sarah R Langley, Christine Esau, Amarylis Wanschel, Edward A Fisher, Yajaira Suárez, Angel Baldán, Manuel Mayr, Carlos Fernández‐Hernando
  • Heat shock factor 2 is a stress‐responsive mediator of neuronal migration defects in models of fetal alcohol syndrome
    1. Rachid El Fatimy1,2,3,413,
    2. Federico Miozzo1,2,3,4,,
    3. Anne Le Mouël1,2,,
    4. Ryma Abane1,2,3,4,
    5. Leslie Schwendimann5,6,
    6. Délara Sabéran‐Djoneidi1,2,
    7. Aurélie de Thonel7,8,
    8. Illiasse Massaoudi1,2,
    9. Liliana Paslaru9,
    10. Kazue Hashimoto‐Torii101415,
    11. Elisabeth Christians11,12,
    12. Pasko Rakic10,
    13. Pierre Gressens5,6 and
    14. Valérie Mezger*,1,2
    1. 1CNRS UMR7216 Épigénétique et Destin Cellulaire, Paris Cedex 13, France
    2. 2Univ Paris Diderot Sorbonne Paris Cité, Paris Cedex 13, France
    3. 3ED 387 iViv UPMC Univ Paris 06, Paris, France
    4. 4Univ Paris Diderot, Paris Cedex 13, France
    5. 5INSERM U1141, Hôpital Robert Debré, Paris, France
    6. 6Faculté de Médecine Denis Diderot, Univ Paris Diderot Sorbonne Paris Cité, Paris, France
    7. 7INSERM UMR 866, Dijon, France
    8. 8Faculty of Medicine and Pharmacy, Univ Burgundy, Dijon, France
    9. 9Carol Davila University of Medicine and Pharmacy Fundeni Hospital, Bucharest, Romania
    10. 10Department of Neurobiology and Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT, USA
    11. 11Laboratoire de Biologie du Développement de Villefranche‐sur‐mer, Observatoire Océanologique, CNRS, Villefranche‐sur‐mer, France
    12. 12Sorbonne Universités UPMC Univ Paris 06, Villefranche‐sur‐mer, France
    13. 13Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School Harvard Institutes of Medicine, Boston, MA, USA
    14. 14Center for Neuroscience Research, Children's National Medical Center, Washington, DC, USA
    15. 15Department of Pediatrics, Pharmacology and Physiology, The George Washington University School of Medicine and Health Sciences, Washington, DC, USA
    1. *Corresponding author. Tel: +33 1 57 27 89 14; +33 6 75 77 11 98; Fax: +33 1 57 27 89 11; E‐mail: valerie.mezger{at}univ-paris-diderot.fr
    1. These authors contributed equally to the work.

    Foetal Alcohol Spectrum Disorders (FASD) is the most frequent cause of non‐genetic mental retardation induced by mothers consuming alcohol during pregnancy. HSF2‐induced activation of HSF1 and formation of alcohol‐specific HSF1/HSF2 heterotrimers leads to cortical neuronal positioning defects in the foetus brain.

    Synopsis

    Foetal Alcohol Spectrum Disorders (FASD) is the most frequent cause of non‐genetic mental retardation induced by mothers consuming alcohol during pregnancy. HSF2‐induced activation of HSF1 and formation of alcohol‐specific HSF1/HSF2 heterotrimers leads to cortical neuronal positioning defects in the foetus brain.

    • HSF2 fine‐tunes neuronal migration in control conditions.

    • Upon foetal alcohol exposure, HSF2 drives the activation of HSF1.

    • The alcohol‐induced formation of HSF1‐HSF2 heterotrimers disturbs the expression of genes controlling radial neuronal migration in the cortex (including MAP genes).

    • In the absence of HSF2, the perturbation in radial neuronal migration and in the expression of MAP genes is less severe.

    • HSF2 is a mediator of radial neuronal migration aspects of Foetal Alcohol Syndrome.

    • fetal alcohol syndrome
    • heat shock factors
    • microtubule‐associated proteins
    • radial neuronal migration
    • transcription
    • Received July 23, 2013.
    • Revision received June 1, 2014.
    • Accepted June 2, 2014.

    This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

    Rachid El Fatimy, Federico Miozzo, Anne Le Mouël, Ryma Abane, Leslie Schwendimann, Délara Sabéran‐Djoneidi, Aurélie de Thonel, Illiasse Massaoudi, Liliana Paslaru, Kazue Hashimoto‐Torii, Elisabeth Christians, Pasko Rakic, Pierre Gressens, Valérie Mezger
  • Targeting macrophage Histone deacetylase 3 stabilizes atherosclerotic lesions
    1. Marten A Hoeksema1,
    2. Marion JJ Gijbels1,2,3,
    3. Jan Van den Bossche1,
    4. Saskia van der Velden1,
    5. Ayestha Sijm1,
    6. Annette E Neele1,
    7. Tom Seijkens1,
    8. J Lauran Stöger1,
    9. Svenja Meiler1,
    10. Marieke CS Boshuizen1,
    11. Geesje M Dallinga‐Thie4,
    12. Johannes HM Levels4,
    13. Louis Boon5,
    14. Shannon E Mullican6,
    15. Nathanael J Spann7,
    16. Jack P Cleutjens2,
    17. Chris K Glass7,
    18. Mitchell A Lazar6,
    19. Carlie JM de Vries1,
    20. Erik AL Biessen2,
    21. Mat JAP Daemen8,
    22. Esther Lutgens1,9 and
    23. Menno PJ de Winther*,1
    1. 1Department of Medical Biochemistry, Experimental Vascular Biology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands
    2. 2Department of Pathology, Maastricht University, Maastricht, The Netherlands
    3. 3Department of Molecular Genetics, Maastricht University, Maastricht, The Netherlands
    4. 4Department of Vascular and Experimental Vascular Medicine, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands
    5. 5Bioceros BV, Utrecht, The Netherlands
    6. 6Division of Endocrinology, Diabetes and Metabolism, Department of Medicine, Institute for Diabetes, Obesity and Metabolism, Perelman School of Medicine, University of Pennsylvania, Philadelphia, USA
    7. 7Department of Cellular and Molecular Medicine, University of California, San Diego, CA, USA
    8. 8Department of Pathology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands
    9. 9Institute for Cardiovascular Prevention (IPEK), Ludwig Maximilian's University, Munich, Germany
    1. *Corresponding author. Tel: +31 20 5666762; E‐mail: m.dewinther{at}amc.uva.nl

    Hdac3 is shown to be an important modulator of the fibrotic phenotype of macrophages in atherosclerosis and, in humans, the expression of Hdac3 is linked to plaque vulnerability to rupture.

    Synopsis

    Hdac3 is shown to be an important modulator of the fibrotic phenotype of macrophages in atherosclerosis and, in humans, the expression of Hdac3 is linked to plaque vulnerability to rupture.

    • Myeloid Hdac3 deficiency promotes collagen deposition in atherosclerosis

    • Macrophage Hdac3 deletion enhances TGF‐β secretion thereby increasing collagen production by vascular smooth muscle cells and results in improved lipid handling by de‐repression of PPARγ and LXR responses

    • In humans, Hdac3 is upregulated in ruptured atherosclerotic lesions and is associated with inflammatory macrophages

    • Fine‐tuning of the macrophage phenotype by altering the epigenetic landscape can be applied to affect atherosclerotic disease outcome

    • atherosclerosis
    • epigenetics
    • fibrosis
    • lipids
    • macrophages
    • Received April 14, 2014.
    • Revision received June 6, 2014.
    • Accepted June 10, 2014.

    This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

    Marten A Hoeksema, Marion JJ Gijbels, Jan Van den Bossche, Saskia van der Velden, Ayestha Sijm, Annette E Neele, Tom Seijkens, J Lauran Stöger, Svenja Meiler, Marieke CS Boshuizen, Geesje M Dallinga‐Thie, Johannes HM Levels, Louis Boon, Shannon E Mullican, Nathanael J Spann, Jack P Cleutjens, Chris K Glass, Mitchell A Lazar, Carlie JM de Vries, Erik AL Biessen, Mat JAP Daemen, Esther Lutgens, Menno PJ de Winther
  • Molecular pathogenesis of Spondylocheirodysplastic Ehlers‐Danlos syndrome caused by mutant ZIP13 proteins
    1. Bum‐Ho Bin1,2,,
    2. Shintaro Hojyo3,4,,
    3. Toshiaki Hosaka5,6,
    4. Jinhyuk Bhin7,
    5. Hiroki Kano8,
    6. Tomohiro Miyai9,10,
    7. Mariko Ikeda5,6,
    8. Tomomi Kimura‐Someya5,6,
    9. Mikako Shirouzu5,6,
    10. Eun‐Gyung Cho1,
    11. Kazuhisa Fukue11,
    12. Taiho Kambe11,
    13. Wakana Ohashi3,
    14. Kyu‐Han Kim1,
    15. Juyeon Seo1,
    16. Dong‐Hwa Choi12,
    17. Yeon‐Ju Nam12,
    18. Daehee Hwang13,
    19. Ayako Fukunaka14,
    20. Yoshio Fujitani14,
    21. Shigeyuki Yokoyama5,15,
    22. Andrea Superti‐Furga16,
    23. Shiro Ikegawa8,
    24. Tae Ryong Lee*,1 and
    25. Toshiyuki Fukada*,2,3
    1. 1Bioscience Research Institute, Amorepacific Corporation R&D Center, Yongin, Republic of Korea
    2. 2Division of Pathology, Department of Oral Diagnostic Sciences, School of Dentistry Showa University, Shinagawa, Japan
    3. 3Laboratory for Homeostatic Network, RIKEN Center for Integrative Medical Sciences, Yokohama, Japan
    4. 4Deutsches Rheuma‐Forschungszentrum, Berlin, Osteoimmunology, Berlin, Germany
    5. 5RIKEN Systems and Structural Biology Center, Yokohama, Japan
    6. 6Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Japan
    7. 7Department of Chemical Engineering, POSTECH, Pohang, Republic of Korea
    8. 8Laboratory for Bone and Joint Diseases, RIKEN Center for Integrative Medical Sciences, Tokyo, Japan
    9. 9Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan
    10. 10Laboratory for Immune Regeneration, RIKEN Center for Integrative Medical Sciences, Yokohama, Japan
    11. 11Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, Japan
    12. 12Gyeonggi Bio Center, Gyeonggi Institute of Science & Technology Promotion, Suwon, Republic of Korea
    13. 13Center for Systems Biology of Plant Senescence and Life History, Institute for Basic Science, Daegu, Republic of Korea
    14. 14Center for Beta‐Cell Biology and Regeneration, Department of Metabolism and Endocrinology, Juntendo University Graduate School of Medicine, Tokyo, Japan
    15. 15RIKEN Structural Biology Laboratory, Yokohama, Japan
    16. 16Department of Pediatrics, Centre Hospitalier Universitaire Vaudois University of Lausanne, Lausanne, Switzerland
    1. * Corresponding author. Tel: +82 31 280 5850; Fax: +82 31 899 2595; E‐mail: trlee{at}amorepacific.com

      Corresponding author. Tel: +81 45 503 9273; Fax: +81 45 503 9271; E‐mail: fukada{at}rcai.riken.jp

    1. These authors contributed equally to this work.

    The Spondylocheirodysplastic Ehlers‐Danlos syndrome pathogenic ZIP13 mutants are degraded by the ubiquitin‐proteasome pathway. Inhibition of this pathway restores ZIP13 levels with consequent improvement of intracellular Zn homeostasis.

    Synopsis

    The Spondylocheirodysplastic Ehlers‐Danlos syndrome pathogenic ZIP13 mutants are degraded by the ubiquitin‐proteasome pathway. Inhibition of this pathway restores ZIP13 levels with consequent improvement of intracellular Zn homeostasis.

    • The Spondylocheirodysplastic Ehlers‐Danlos syndrome pathogenic ZIP13 mutant proteins: ZIP13G64D and ZIP13ΔFLA, are degraded by the ubiquitin‐proteasome pathway.

    • Valosin‐containing protein (VCP) is involved in the degradation of the pathogenic mutant ZIP13 proteins.

    • The reduced expression levels of the ZIP13 mutant proteins are rescued by inhibition of the degradation pathways, resulting in improved intracellular zinc homeostasis.

    • Proteasome
    • SCD‐EDS
    • VCP
    • zinc transporter
    • ZIP13
    • Received December 29, 2013.
    • Revision received May 26, 2014.
    • Accepted May 27, 2014.

    This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

    Bum‐Ho Bin, Shintaro Hojyo, Toshiaki Hosaka, Jinhyuk Bhin, Hiroki Kano, Tomohiro Miyai, Mariko Ikeda, Tomomi Kimura‐Someya, Mikako Shirouzu, Eun‐Gyung Cho, Kazuhisa Fukue, Taiho Kambe, Wakana Ohashi, Kyu‐Han Kim, Juyeon Seo, Dong‐Hwa Choi, Yeon‐Ju Nam, Daehee Hwang, Ayako Fukunaka, Yoshio Fujitani, Shigeyuki Yokoyama, Andrea Superti‐Furga, Shiro Ikegawa, Tae Ryong Lee, Toshiyuki Fukada