Name

SAWAMURA, Naoya

Official Title

Senior Researcher(Professor)

AffiliationResearch Council (Research Organization)/Affiliated organization

(Research Organization for Nano & Life Innovation)

Contact Information

URL

Web Page URL

http://asahi-lab.jp/member/staff/sawamura.html

Grant-in-aids for Scientific Researcher Number
40449351

Sub-affiliation

Affiliated Institutes

欧州バイオメディカルサイエンス研究所

研究所員 2009-2011

ライフサポートイノベーション研究所

研究所員 2014-2014

欧州バイオメディカルサイエンス研究所

研究所員 2011-2012

欧州バイオメディカルグリーンサイエンス研究所

研究所員 2012-2014

欧州バイオメディカルグリーンサイエンス研究所

研究所員 2015-2016

グローバルバイオメディカルグリーンサイエンス研究所

研究所員 2016-2017

Educational background・Degree

Educational background

-1994 Tokyo University of Science Faculty of Science and Engineering
-1996 University of Tsukuba Graduate School, Division of Medical Science
-2000 University of Tokyo Graduate School, Division of Medical Sciences

Academic Society Joined

Society for Neuroscience

The Japanece Society for Neurochemistry

Research Field

Grants-in-Aid for Scientific Research classification

Biological Sciences / Neuroscience / Neurochemistry/Neuropharmacology

Technology Seeds

Paper

Antioxidant Activity of Ge-132, a Synthetic Organic Germanium, on Cultured Mammalian Cells.

Wada Takeyoshi;Hanyu Takashi;Nozaki Kota;Kataoka Kosuke;Kawatani Tomoro;Asahi Toru;Sawamura Naoya

Biological & pharmaceutical bulletin 41(5) 2018-2018

PubMedDOI

Detail

ISSN:1347-5215

Outline::Ge-132 is a synthetic organic germanium that is used as a dietary supplement. The antioxidant activity of Ge-132 on cultured mammalian cells was investigated in this study. First, Ge-132 cytotoxicity on mammalian cultured cells was determined by measuring lactate dehydrogenase (LDH) levels. Ge-132 had no cytotoxic effect on three different cell lines. Second, the cell proliferative effect of Ge-132 was determined by measuring ATP content of whole cells and counting them. Ge-132 treatment of Chinese hamster ovary (CHO-K1) and SH-SY5Y cells promoted cell proliferation in a dose-dependent manner. Finally, antioxidant activity of Ge-132 against hydrogen peroxide-induced oxidative stress was determined by measuring the levels of intracellular reactive oxygen species (ROS) and carbonylated proteins. Pre-incubation of CHO-K1 and SH-SY5Y cells with Ge-132 suppressed intracellular ROS production and carbonylated protein levels induced by hydrogen peroxide. Our results suggest that Ge-132 has antioxidant activity against hydrogen peroxide-induced oxidative stress.

The Neuroprotective Effect of Thalidomide against Ischemia through the Cereblon-mediated Repression of AMPK Activity.

Sawamura Naoya;Yamada Mariko;Fujiwara Miku;Yamada Haruka;Hayashi Hideki;Takagi Norio;Asahi Toru

Scientific reports 8(1) 2018-2018

PubMedDOI

Detail

ISSN:2045-2322

Outline::Thalidomide was originally used as a sedative and found to be a teratogen, but now thalidomide and its derivatives are widely used to treat haematologic malignancies. Accumulated evidence suggests that thalidomide suppresses nerve cell death in neurologic model mice. However, detailed molecular mechanisms are unknown. Here we examined the molecular mechanism of thalidomide's neuroprotective effects, focusing on its target protein, cereblon (CRBN), and its binding protein, AMP-activated protein kinase (AMPK), which plays an important role in maintaining intracellular energy homeostasis in the brain. We used a cerebral ischemia rat model of middle cerebral artery occlusion/reperfusion (MCAO/R). Thalidomide treatment significantly decreased the infarct volume and neurological deficits of MCAO/R rats. AMPK was the key signalling protein in this mechanism. Furthermore, we considered that the AMPK-CRBN interaction was altered when neuroprotective action by thalidomide occurred in cells under ischemic conditions. Binding was strong between AMPK and CRBN in normal SH-SY5Y cells, but was weakened by the addition of H2O2. However, when thalidomide was administered at the same time as H2O2, the binding of AMPK and CRBN was partly restored. These results suggest that thalidomide inhibits the activity of AMPK via CRBN under oxidative stress and suppresses nerve cell death.

Arctic Aβ40 blocks the nicotine-induced neuroprotective effect of CHRNA7 by inhibiting the ERK1/2 pathway in human neuroblastoma cells.

Ju Ye;Asahi Toru;Sawamura Naoya

Neurochemistry international 110p.49 - 562017-2017

PubMedDOIScopus

Detail

ISSN:1872-9754

Outline::Amyloid β protein (Aβ) plays a central role in Alzheimer's disease (AD) pathogenesis. Point mutations in the Aβ sequence, which cluster around the central hydrophobic core of the peptide, are associated with familial AD (FAD). Several mutations have been identified, with the Arctic mutation exhibiting a purely cognitive phenotype that is typical of AD. Our previous findings suggest that Arctic Aβ40 binds to and aggregates with CHRNA7, thereby inhibiting the calcium response and signaling pathways downstream of the receptor. Activation of CHRNA7 is neuroprotective both in vitro and in vivo. Therefore, in the present study, we investigated whether Arctic Aβ40 affects neuronal survival and/or death via CHRNA7. Using human neuroblastoma SH-SY5Y cells, we found that the neuroprotective function of CHRNA7 is blocked by CHRNA7 knockdown using RNA interference. Furthermore, Arctic Aβ40 blocked the neuroprotective effect of nicotine by inhibiting the ERK1/2 pathway downstream of CHRNA7. Moreover, we show that ERK1/2 activation mediates the neuroprotective effect of nicotine against oxidative stress. Collectively, our findings further our understanding of the molecular pathogenesis of Arctic FAD.

Ohgata, the single Drosophila ortholog of human cereblon, regulates insulin signaling-dependent organismic growth

Wakabayashi, Satoru; Sawamura, Naoya; Sawamura, Naoya; Voelzmann, André; Broemer, Meike; Asahi, Toru; Asahi, Toru; Hoch, Michael

Journal of Biological Chemistry Peer Review Yes 291(48) p.25120 - 251322016/11-2016/11

PubMedDOIScopusWoS

Detail

ISSN:00219258

Outline:© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.Cereblon (CRBN) is a substrate receptor of the E3 ubiquitin ligase complex that is highly conserved in animals and plants. CRBN proteins have been implicated in various biological processes such as development, metabolism, learning, and memory formation, and their impairment has been linked to autosomal recessive non-syndromic intellectual disability and cancer. Furthermore, human CRBN was identified as the primary target of thalidomide teratogenicity. Data on functional analysis of CRBN family members in vivo, however, are still scarce. Here we identify Ohgata (OHGT), the Drosophila ortholog of CRBN, as a regulator of insulin signaling-mediated growth. Using ohgt mutants that we generated by targeted mutagenesis, we show that its loss results in increased body weight and organ size without changes of the body proportions. We demonstrate that ohgt knockdown in the fat body, an organ analogous to mammalian liver and adipose tissue, phenocopies the growth phenotypes. We further show that overgrowth is due to an elevation of insulin signaling in ohgt mutants and to the down-regulation of inhibitory cofactors of circulating Drosophila insulin-like peptides (DILPs), named acid-labile subunit and imaginal morphogenesis protein-late 2. The two inhibitory proteins were previously shown to be components of a heterotrimeric complex with growth-promoting DILP2 and DILP5. Our study reveals OHGT as a novel regulator of insulin-dependent organismic growth in Drosophila.

Nuclear cereblon modulates transcriptional activity of Ikaros and regulates its downstream target, enkephalin, in human neuroblastoma cells

Takeyoshi Wada, Toru Asahi, Naoya Sawamura

Biochemical and Biophysical Research Communications 477(3) p.388 - 3942016/08-2016/08

PubMedDOIScopus

Detail

ISSN:0006291X

Outline:© 2016 Elsevier Inc.The gene coding cereblon (CRBN) was originally identified in genetic linkage analysis of mild autosomal recessive nonsyndromic intellectual disability. CRBN has broad localization in both the cytoplasm and nucleus. However, the significance of nuclear CRBN remains unknown. In the present study, we aimed to elucidate the role of CRBN in the nucleus. First, we generated a series of CRBN deletion mutants and determined the regions responsible for the nuclear localization. Only CRBN protein lacking the N-terminal region was localized outside of the nucleus, suggesting that the N-terminal region is important for its nuclear localization. CRBN was also identified as a thalidomide-binding protein and component of the cullin-4-containing E3 ubiquitin ligase complex. Thalidomide has been reported to be involved in the regulation of the transcription factor Ikaros by CRBN-mediated degradation. To investigate the nuclear functions of CRBN, we performed co-immunoprecipitation experiments and evaluated the binding of CRBN to Ikaros. As a result, we found that CRBN was associated with Ikaros protein, and the N-terminal region of CRBN was required for Ikaros binding. In luciferase reporter gene experiments, CRBN modulated transcriptional activity of Ikaros. Furthermore, we found that CRBN modulated Ikaros-mediated transcriptional repression of the proenkephalin gene by binding to its promoter region. These results suggest that CRBN binds to Ikaros via its N-terminal region and regulates transcriptional activities of Ikaros and its downstream target, enkephalin.

Mitochondrial cereblon functions as a Lon-type protease

Kosuke Kataoka, China Nakamura, Toru Asahi, Naoya Sawamura

Scientific Reports Peer Review Yes 6p.299862016/07-2016/07

PubMedDOIScopus

Detail

ISSN:2045-2322

Outline:Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix, and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. However, whether CRBN has Lon protease-like function remains unknown. Here, we determined if CRBN has a protective function against oxidative stress, similar to Lon protease. We report that CRBN partially distributes in mitochondria, suggesting it has a mitochondrial function. To specify the mitochondrial role of CRBN, we mitochondrially expressed CRBN in human neuroblastoma SH-SY5Y cells. The resulting stable SH-SY5Y cell line showed no apparent effect on the mitochondrial functions of fusion, fission, and membrane potential. However, mitochondrially expressed CRBN exhibited protease activity, and was induced by oxidative stress. In addition, stably expressed cells exhibited suppressed neuronal cell death induced by hydrogen peroxide. These results suggest that CRBN functions specifically as a Lon-type protease in mitochondria.

Cereblon is recruited to aggresome and shows cytoprotective effect against ubiquitin-proteasome system dysfunction.

Sawamura N., Wakabayashi S., Matsumoto K.,Yamada H., Asahi T.

Biochemical and biophysical research communications 464(4) p.1054 - 10592015-2015

PubMedDOIScopusWoS

Detail

ISSN:1090-2104

Outline::Cereblon (CRBN) is encoded by a candidate gene for autosomal recessive nonsyndromic intellectual disability (ID). The nonsense mutation, R419X, causes deletion of 24 amino acids at the C-terminus of CRBN, leading to mild ID. Although abnormal CRBN function may be associated with ID disease onset, its cellular mechanism is still unclear. Here, we examine the role of CRBN in aggresome formation and cytoprotection. In the presence of a proteasome inhibitor, exogenous CRBN formed perinuclear inclusions and co-localized with aggresome markers. Endogenous CRBN also formed perinuclear inclusions under the same condition. Treatment with a microtubule destabilizer or an inhibitor of the E3 ubiquitin ligase activity of CRBN blocked formation of CRBN inclusions. Biochemical analysis showed CRBN containing inclusions were high-molecular weight, ubiquitin-positive. CRBN overexpression in cultured cells suppressed cell death induced by proteasome inhibitor. Furthermore, knockdown of endogenous CRBN in cultured cells increased cell death induced by proteasome inhibitor, compared with control cells. Our results show CRBN is recruited to aggresome and has functional roles in cytoprotection against ubiquitin-proteasome system impaired condition.

Arctic mutant Aß40 aggregates on α7 nicotinic acetylcholine receptors and inhibits their functions

Ye Ju, Toru Asahi and Naoya Sawamura

Journal of Neurochemistry 131(5) p.667 - 6742014/12-2014

PubMedDOIWoS

Detail

ISSN:0022-3042

Outline::Amyloid β protein (Aβ) plays a central role in the pathogenesis of Alzheimer's disease (AD). Point mutations within the Aβ sequence associated with familial AD (FAD) are clustered around the central hydrophobic core of Aβ. Several types of mutations within the Aβ sequence have been identified, and the 'Arctic' mutation (E22G) has a purely cognitive phenotype typical of AD. Previous studies have shown that the primary result of the 'Arctic' mutation is increased formation of Aβ protofibrils. However, the molecular mechanism underlying this effect remains unknown. Aβ42 binds to a neuronal nicotinic acetylcholine receptor subunit, neuronal acetylcholine receptor subunit alpha-7 (CHRNA7), with high affinity and, thus, may be involved in the pathogenesis of AD. Therefore, to clarify the molecular mechanism of Arctic mutation-mediated FAD, we focused on CHRNA7 as a target molecule of Arctic Aβ. We performed an in vitro binding assay using purified CHRNA7 and synthetic Arctic Aβ40, and demonstrated that Arctic Aβ40 specifically bound to CHRNA7. The aggregation of Arctic Aβ40 was enhanced with the addition of CHRNA7. Furthermore, the function of CHRNA7 was detected by measuring Ca(2+) flux and phospho-p44/42 MAPK (ERK1/2) activation. Our results indicated that Arctic Aβ40 aggregation was enhanced by the addition of CHRNA7, which destabilized the function of CHRNA7 via inhibition of Ca(2+) responses and activation of ERK1/2. These findings indicate that Arctic Aβ mutation may be involved in the mechanism underlying FAD. This mechanism may involve binding and aggregation, leading to the inhibition of CHRNA7 functions.

A label-free electrical assay of fibrous amyloid β based on semiconductor biosensing.

Hideshima, S., Kobayashi, M., Wada, T., Kuroiwa, S., Nakanishi, T., Sawamura, N., Asahi T., Osaka, T.

Chemical Communications 50(26) p.3476 - 34792014-2014

DOIWoS

Detail

ISSN:1359-7345

Construction of photoenergetic mitochondria in cultured mammalian cells

Hara, K. Y., Wada, T., Kino, K., Asahi, T., Sawamura, N.

Scientific Reports 3p.16352013-2013

DOIWoS

Detail

ISSN:2045-2322

Cereblon accumulates in aggresomes due to proteasome impairment

Wakabayashi, S., Yamada, H., Asahi, T., Sawamura, N.

Journal of Neurochemistry 123p.25 - 252012-

Construction of new energy synthesis system in SH-SY5Y cells: application for the treatment of Parkinson's disease.

Wada, T., Hara, K., Asahi, T., Sawamura, N.

Journal of Neurochemistry 123p.24 - 252012-

The fruitfly Drosophila melanogaster: a promising model to explore molecular psychiatry

Sawamura, N., Ishida, N., Tomoda, T., Hai, T., Furukubo-Tokunaga, K., Sawa, A.

Molecular Psychiatry 13p.1069 - 10692008-

Nuclear DISC1 regulates CRE-mediated gene transcription and sleep homeostasis in the fruit fly

Sawamura N, Ando T, Maruyama Y, Fujimuro M, Mochizuki H, Honjo K, Shimoda M, Toda H, Sawamura-Yamamoto T, Makuch LA, Hayashi A, Ishizuka K, Cascella NG, Kamiya A, Ishida N, Tomoda T, Hai T, Furukubo-Tokunaga K, Sawa A.

Molecular Psychiatry 13p.1138 - 11482008-

Molecules regulated by patterns of electrical activity

Ozaki, M. Sawamura, N. Ichikawa, M.

Neuroscience Research 58p.S1422007-

DOI

Disrupted-In-Schizophrenia (DISC1): a key susceptibility factor for major mental illnesses

Sawamura N and Sawa A

Annals of the New York Academy of Sciences 1086p.126 - 1332006-

Primate disrupted-in-schizophrenia-1 (DISC1): High divergence of a gene for major mental illnesses in recent evolutionary history.

Bord L., Wheeler J., Paek M., Saleh M., Lyons-Warren A., Ross C.A., Sawamura N., Sawa A.

Neuroscience Research 56p.286 - 2932006-

DISC1からみた統合失調症の分子病態 (特集 統合失調症の分子医学)

疋田 貴俊, 澤村 直哉, 尾関 祐二

細胞 37(14) p.573 - 5762005/12-

Production of DISC1 transgenic and knockout mice

Hikida, T., Sawamura, N., Paek, M., Cascio, M., Sawa, A.

American Journal of Medical Genetics Part B-Neuropsychiatric Genetics 138B(1) p.134 - 1352005/09-

A form of Disrupted-In-Schizophrenia-1 (DISC1) enriched in the nucleus has altered subcellular distribution in schizophrenia brains.

Sawamura N., Sawamura-Yamamoto T., Ozeki Y., Ross C.A., Sawa A

Proceedings of the National Academy of Sciences 102p.1187 - 11922005-

A schizophrenia-associated mutation of DISC1 perturbs cerebral cortex development.

Kamiya A., Kubo K., Tomoda T., Takaki M., Youn R., Ozeki Y., Sawamura N., Park U., Kubo C., Okawa M., Ross C.A., Hatten M.E., Nakajima K., Sawa A

Nature Cell Biology 7p.1167 - 11782005-

Disrupted-In-Schizophrenia-1 (DISC1): A promising lead in molecular analyzes of schizophrenia

Sawa A., Sawamura N., Balkissoon R

Clinical Neuroscience Research 5p.23 - 302005-

Modulation of amyloid precursor protein cleavage by cellular sphingolipids

Sawamura N., Ko M., Yu W., Zou K., Hanada K., Suzuki T., Gong J.S., Yanagisawa K., Michikawa M

Journal of Biological Chemistry 279p.11984 - 119912004-

Amyloid beta-protein (Aß)1-40 protects neurons from damage induced by Aß1-42 in culture and in rat brain

Zou K., Kim D., Kakio A., Byun K., Gong J.S., Kim J., Kim M., Sawamura N., Nishimoto S., Matsuzaki K., Lee B., Yanagisawa K., Michikawa M

Journal of Neurochemistry 87p.609 - 6192003-

Promotion of tau phosphorylation by MAP kinase Erk1/2 is accompanied by reduced cholesterol level in detergent-insoluble membrane fraction in Niemann-Pick C1-deficient cells.

Sawamura N., Gong J.S., Chang T.Y., Yanagisawa K., Michikawa M

Journal of Neurochemistry 84p.1086 - 10962003-

統合失調症とDISC1

澤村 直哉、澤 明

実験医学 -脳・神経研究2004, 増刊- 21p.2469 - 24732003-

Amyloid ß-protein affects cholesterol metabolism in cultured neurons: Implications for pivotal role of choleterol in the amyloid cascade.

Gong J.S., Sawamura N., Zou K., Sakai J., Yanagisawa K., Michikawa M.

Neuroscience Research 70p.438 - 4462002-

Apolipoprotein E (apoE)-Isoform-Dependent Lipid Release from Astrocytes Prepared from Human-apoE3- and apoE4-Knock-in Mice

Gong J.S., Kobayashi M., Hayashi H., Zou K., Sawamura N., Fujita S.C., Yanagisawa K., Michikawa M

Journal of Biological Chemsistry 277p.29919 - 299262002-

Cholesterol-dependent modulation of dendrite outgrowth and microtubule stability in cultured neurons

Fan Q.W., Yu W., Gong J.S., Zou K., Sawamura N., Senda T., Yanagisawa K., Michikawa M

Journal of Neurochemistry 80p.178 - 1902002-

A novel action of alzheimer's amyloid beta-protein (Aß): oligomeric Aß promotes lipid release

Michikawa M., Gong J.S., Fan Q.W., Sawamura N., Yanagisawa K

Journal of Neuroscience 21p.7226 - 72352001-

Site-specific phosphorylation of tau accompanied by activation of mitogen-activated protein kinase (MAPK) in brains of Niemann-Pick type C mice

Sawamura N., Gong J.S., Garver W.S., Heidenreich R.A., Ninomiya H., Ohno K., Yanagisawa K. Michikawa M

Journal of Biological Chemistry 276p.10314 - 103192001-

Mutant presenilin 2 transgenic mice: A large increase in the levels of Aß42 is presumably associated with the low density membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin

Sawamura N., Morishima-Kawashima M., Waki H., Kobayashi K., Kuramochi T., Frosch M.P., Ding K., Ito M., Kim T.W., Tanzi R.E., Oyama F., Tabira T., Ando S., Ihara Y

Journal of Biological Chemistry 275p.27901 - 279082000-

Mutant presenilin 2 transgenic mouse: Effect on an age-dependent increase of amyloid ß-protein (Aß) 42 in the brain

Sawamura N., Oyama F., Kobayashi K., Morishima-Kawashima M., Kuramochi T., Ito M., Tomita T., Maruyama K., Saido T.C., Iwatsubo T., Capell A., Walter J., Grunberg J., Ueyama Y., Haass C., Ihara Y (The first three authors contributed equally to this study)

Journal of Neurochemistry 71p.313 - 3221998-

Amyloid ß protein 42(43) in cerebrospinal fluid of patients with Alzheimer's disease

Tamaoka A., Sawamura N., Fukushima T., Shoji S., Matsubara E., Shoji M., Hirai S., Furiya Y., Endoh R., Mori H

Journal of Neurological Sciences 148p.41 - 451997-

Characterization of amyloid ß protein species in cerebral amyloid angiopathy of a cynomolgous monkey by immunocytochemistry and enzyme-linked immunosorbent assay

Sawamura N., Tamaoka A., Shoji S., Koo E.H., Walker L.C., Mori H

Brain Research 764p.225 - 2291997-

Deposition of amyloid ß protein (Aß) subtypes [Aß40 and Aß42(43)] in canine senile plaques and cerebral amyloid angiopathy

Nakamura S., Tamaoka A., Sawamura N., Kiatipattanasakul W., Nakayama H., Shoji S., Yoshikawa Y., Doi K

Acta Neuropathol (Berl) 94p.323 - 3281997-

Amyloid ß protein in plasma from patients with sporadic Alzheimer's disease

Tamaoka A., Fukushima T., Sawamura N., Ishikawa K., Oguni E., Komatsuzaki Y., Shoji S

Journal of the Neurological Sciences 151p.65 - 681996-

Amyloid ß protein 1-42/43 (Aß1-42/43) in cerebellar diffuse plaques: enzyme-linked immunosorbent assay and immunocytochemical study

Tamaoka A., Sawamura N., Odaka A., Suzuki N., Mizusawa H., Shoji S., Mori H

Brain Research 679p.151 - 1561995-

Carboxyl end-specific monoclonal antibodies to Amyloid ß protein (Aß) subtypes (Aß40 and Aß42(43)) differentiate Aß in senile plaques and amyloid angiopathy in brains of aged cynomolgus monkeys

Nakamura S., Tamaoka A., Sawamura N., Shoji S., Nakayama H., Ono F., Sakakibara I., Yoshikawa Y., Mori H., Goto N., Doi K

Neuroscience Letters 201p.151 - 1541995-

Biochemical evidence for the long-tail form (Aß1-42/43) of amyloid ß protein as a seed molecule in cerebral deposits of Alzheimer's disease

Tamaoka A., Kondo T., Odaka A., Sahara N., Sawamura N., Ozawa K., Suzuki N., Shoji S., Mori H

Biochemical and Biophysical Research Communications 205p.834 - 8421994-

Books And Publication

KEYWORD 精神第4版

澤村 直哉, 尾崎美和子 他

先端医学社2007-

生命科学概論

澤村直哉, 朝日透 他

朝倉書店2012/04-

Research Grants & Projects

Grant-in-aids for Scientific Research Adoption Situation

Research Classification:

Functional analysis of CHRNA7, a candidate gene product for schizophrenia

2009-2011

Allocation Class:¥4290000

Lecture Course

Course TitleSchoolYearTerm
Molecular Biology 51School of International Liberal Studies2018fall semester
Frontier of Solid State BioscienceSchool of Advanced Science and Engineering2018spring quarter
Introduction to Biomaterial AnalysisSchool of Advanced Science and Engineering2018spring semester
Advanced Solid State BioscienceGraduate School of Advanced Science and Engineering2018spring semester
Advanced Solid State BioscienceGraduate School of Advanced Science and Engineering2018spring semester
Advanced Solid State BioscienceGraduate School of Advanced Science and Engineering2018spring semester
Introduction to Nano-Chiral ScienceGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Introduction to Nano-Chiral ScienceGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)
Science Communication and Research IntegrityGraduate School of Advanced Science and Engineering2018an intensive course(fall)