Search Results - (Author, Cooperation:T. Nishiyama)
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1Nakamura, Y., Nishi, T., Noguchi, R., Ito, Y., Watanabe, T., Nishiyama, T., Aikawa, S., Hasunuma, T., Ishii, J., Okubo, Y., Kondo, A.
The American Society for Microbiology (ASM)
Published 2018Staff ViewPublication Date: 2018-07-18Publisher: The American Society for Microbiology (ASM)Print ISSN: 0099-2240Electronic ISSN: 1098-5336Topics: BiologyPublished by: -
2J. A. Banks ; T. Nishiyama ; M. Hasebe ; J. L. Bowman ; M. Gribskov ; C. dePamphilis ; V. A. Albert ; N. Aono ; T. Aoyama ; B. A. Ambrose ; N. W. Ashton ; M. J. Axtell ; E. Barker ; M. S. Barker ; J. L. Bennetzen ; N. D. Bonawitz ; C. Chapple ; C. Cheng ; L. G. Correa ; M. Dacre ; J. DeBarry ; I. Dreyer ; M. Elias ; E. M. Engstrom ; M. Estelle ; L. Feng ; C. Finet ; S. K. Floyd ; W. B. Frommer ; T. Fujita ; L. Gramzow ; M. Gutensohn ; J. Harholt ; M. Hattori ; A. Heyl ; T. Hirai ; Y. Hiwatashi ; M. Ishikawa ; M. Iwata ; K. G. Karol ; B. Koehler ; U. Kolukisaoglu ; M. Kubo ; T. Kurata ; S. Lalonde ; K. Li ; Y. Li ; A. Litt ; E. Lyons ; G. Manning ; T. Maruyama ; T. P. Michael ; K. Mikami ; S. Miyazaki ; S. Morinaga ; T. Murata ; B. Mueller-Roeber ; D. R. Nelson ; M. Obara ; Y. Oguri ; R. G. Olmstead ; N. Onodera ; B. L. Petersen ; B. Pils ; M. Prigge ; S. A. Rensing ; D. M. Riano-Pachon ; A. W. Roberts ; Y. Sato ; H. V. Scheller ; B. Schulz ; C. Schulz ; E. V. Shakirov ; N. Shibagaki ; N. Shinohara ; D. E. Shippen ; I. Sorensen ; R. Sotooka ; N. Sugimoto ; M. Sugita ; N. Sumikawa ; M. Tanurdzic ; G. Theissen ; P. Ulvskov ; S. Wakazuki ; J. K. Weng ; W. W. Willats ; D. Wipf ; P. G. Wolf ; L. Yang ; A. D. Zimmer ; Q. Zhu ; T. Mitros ; U. Hellsten ; D. Loque ; R. Otillar ; A. Salamov ; J. Schmutz ; H. Shapiro ; E. Lindquist ; S. Lucas ; D. Rokhsar ; I. V. Grigoriev
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-05-10Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Angiosperms/chemistry/genetics ; *Biological Evolution ; Bryopsida/genetics ; Chlamydomonas/chemistry/genetics ; DNA Transposable Elements ; Evolution, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; *Genome, Plant ; MicroRNAs/genetics ; Molecular Sequence Data ; Phylogeny ; Plant Proteins/genetics/metabolism ; Proteome/analysis ; RNA Editing ; RNA, Plant/genetics ; Repetitive Sequences, Nucleic Acid ; Selaginellaceae/*genetics/growth & development/metabolism ; Sequence Analysis, DNAPublished by: -
3A. Tedeschi ; G. Wutz ; S. Huet ; M. Jaritz ; A. Wuensche ; E. Schirghuber ; I. F. Davidson ; W. Tang ; D. A. Cisneros ; V. Bhaskara ; T. Nishiyama ; A. Vaziri ; A. Wutz ; J. Ellenberg ; J. M. Peters
Nature Publishing Group (NPG)
Published 2013Staff ViewPublication Date: 2013-08-27Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Cell Cycle/genetics ; Cell Cycle Proteins/metabolism ; Chromatids/genetics/metabolism ; Chromatin/*chemistry/genetics/*metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; *Chromosome Segregation/genetics ; Chromosomes, Mammalian/chemistry/genetics/metabolism ; DNA/genetics/metabolism ; DNA-Binding Proteins/deficiency/genetics/metabolism ; Embryonic Development/genetics ; Endopeptidases/metabolism ; Gene Expression Regulation/genetics ; Genes, myc/genetics ; Interphase ; Mice ; Mitosis ; Prophase ; Proteins/genetics/*metabolism ; SeparasePublished by: -
4Staff View
Publication Date: 2018-12-11Publisher: Institute of Physics (IOP)Print ISSN: 1757-8981Electronic ISSN: 1757-899XTopics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision MechanicsPublished by: -
5Staff View
Publication Date: 2018-12-18Publisher: Institute of Physics Publishing (IOP)Electronic ISSN: 1748-0221Topics: PhysicsPublished by: -
6Staff View
ISSN: 1525-1314Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: GeosciencesNotes: Abstract Chromian omphacite which contains up to 4 wt % Cr2O3 has been identified from low-grade metamorphic rocks in Nishisonogi, Kyushu, Japan. It occurs as aggregates, forming a thin horizon ([20 mm thick) in alayered metagabbro within a serpentinite melange zone, together with Cr-free omphacite, actino-lite, epidote and sphene. It may have been formed by the metasomatic introduction of Cr into the metagabbro from the serpentinite rather than by reaction with chromite. The structural formula, based on EPMA analyses, and the optical absorption spectrum of the chromian omphacite show that the Cr is positioned in the octahedral site.Type of Medium: Electronic ResourceURL: -
7WADA, N. ; OHARA, N. ; KAMEOKA, M. ; NISHINO, Y. ; MATSUMOTO, S. ; NISHIYAMA, T. ; NAITO, M. ; YUKITAKE, H. ; OKADA, Y. ; IKUTA, K. ; YAMADA, T.
Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
Published 1996Staff ViewISSN: 1365-3083Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: The recombinant bacillus Calmette–Guérin (rBCG) secretion system utilizing an extracellular α antigen of Mycobacterium kansasii (α-K) was characterized biochemically and immunologically. The human immunodeficiency virus type1 (HIV-1) p17gag B cell epitope fused to α-K was secreted in extremely large amounts. At least three mice out of seven inoculated with rBCG generated high titres of antibody to the epitope. The long-lasting antibody production persisted more than 14 months.Type of Medium: Electronic ResourceURL: -
8OHARA, N. ; KITAURA, H. ; HOTOKEZAKA, H. ; NISHIYAMA, T. ; WADA, N. ; MATSUMOTO, S. ; MATSUO, T. ; NAITO, M. ; YAMADA, T.
Oxford, UK : Blackwell Publishing Ltd
Published 1995Staff ViewISSN: 1365-3083Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: The secreted protein MPB51 is one of the major proteins in the culture filtrate of Mycobacterium bovis BCG (BCG) and is a protein immunologically cross-reacting with the fibronectin binding 85 complex secreted by this bacterium. The gene encoding MPB51 (mpb51) was cloned, sequenced, and expressed in Escherichia coll. The mpb51 gene was mapped downstream of the gene for 85A component with 179 bp spaces. The mpb51 gene encoded 299 amino acids, including 33 amino acids for the signal peptide, followed by 266 amino acids for the mature protein with a molecular mass of 27807.37 Da. This is the first complete sequence of MPB51. MPB51 showed 37–43% homology to the components of 85 complex. Two-dimensional electrophoresis of culture fluids of BCG and Western blotting indicated the existence of the other novel protein(s) which strongly cross-reacted with the α antigen (85B) and MPB51.Type of Medium: Electronic ResourceURL: -
9Akutsu, N. ; Milbury, C. M. ; Burgeson, R. E. ; Nishiyama, T.
Oxford, UK : Blackwell Publishing Ltd
Published 1999Staff ViewISSN: 1600-0625Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Type XII and XIV collagens localize near the surface of banded collagen fibrils and most likely work as a molecular bridge between collagen fibrils. We have shown that both collagens can modulate the interactions between collagen fibrils, allowing fibroblasts to act upon the fibrils to vary the deformability. In the present study the effect of the globular domains (collagenase-resistant domains) of type XII and XIV collagens (XII-NC-3 and XIV-NC-3) on the migration of fibroblasts into the reconstituted type I collagen gel was investigated. Cell attachment and proliferation on the collagen gel were unaffected. The migration of fibroblasts into the gel was increased proportionally to the concentration of collagen. We found that XII-NC-3 and XIV-NC-3 domains caused decreases in the numbers of fibroblasts that migrated into the gel. Heat treatment of XII-NC-3 and XIV-NC-3 or the addition of polyclonal antibodies eliminated the suppressive activity on fibroblast migration, showing that the intact conformation of NC-3 domain is important for suppression of migration. The results suggest that both NC-3 domains influence the deformability of type I collagen fibril networks, which may cause the change in fibroblast migration.Type of Medium: Electronic ResourceURL: -
10Staff View
ISSN: 1095-8649Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Measurements of dry weight (wt), carbon (C), nitrogen (N) and calories were made on walleye pollock eggs (0.24 mg, 35.3% C, 8.3% N, and 4.6 kcal g−1 dry wt), larvae (0.16 g, 42.9% C, 11.1% N and 5.1 kcal g−1 dry wt) and juveniles (22.4 g, 47.2% C, 9.0% N and 5.6 kcal g−1 dry wt). For juvenile fish (9–360 g wet wt) the measured values were related to dry weight and Fulton's condition factor index (CFI) by regression models. The CFI was a better predictor of body composition than dry weight. As CFI improved from a minimum starvation level of 0.42 to a maximum of 1.16, body caloric content, percentage C, and the C/N ratio increased (kcal g−1 dry wt = 4.4 CFI + 1.7, percentage carbon = 49.7 CFI0.5, C/N ratio = 5.0 CFI + 0.9), while percentage N and percentage ash decreased (percentage N =−3.5 CFI + 12.1; percentage ash = 9.1 CFI−1.4). The results of this study suggest that seasonal C, N and caloric content of young pollock can be estimated from measurements of Fulton's condition factor index.Type of Medium: Electronic ResourceURL: -
11Nishiyama, T. ; Tsumagari, S. ; Ito, M. ; Kimura, J. ; Watanabe, G. ; Taya, K. ; Takeishi, M.
Oxford, UK : Blackwell Science, Ltd
Published 1999Staff ViewISSN: 1439-0264Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Using the immunohistochemical technique, we attempted to identify the source of secretion of steroid hormones between the mid- and late-terms of gestation in dogs by investigating steroid converting enzymes such as cholesterol side-chain cleavage enzyme (SCC), 3 β-hydroxysteroid dehydrogenase/isomerase (3 β-HSD), 17 α-hydroxylase/C17, 20lyase (c17), and aromatase in the ovaries and placenta. Aromatase positive cells were slightly confirmed in luteal cells in the mid-term of gestation (day 40), whereas, in the late-stage (day 50 and 60), the number of aromatase positive cells had increased. However, the oestrogen precursor (c-17 positive cells), could barely be identified in the marginal regions of the corpora lutea (CL) and completely disappeared in the late-stage of gestation. The androgen precursors, convertase SCC and 3 β-HSD, were confirmed in all regions of the CL during the mid-stage of gestation (day 40), showing particularly strong cell reactions in the marginal region of the CL. Yet, these positive reactions of SCC and 3 β-HSD in the marginal region of the CL disappeared in the late-stage of gestation. Moreover, it was discovered that the number of SCC and 3 β-HSD positive cells had decreased in all regions of the CL. None of the enzymes were detected in the placenta. The above results indicated that the source of oestrogen secretion in pregnant dogs is considered to be the CL, and that, compared with the mid-stage of gestation, there was an increased number of oestrogen synthesizing cells within the CL in the late-stage. However, the biosynthetic site of oestrogen precursors from the luteal cells during the late-stage of gestation is still unknown.Type of Medium: Electronic ResourceURL: -
12Isomoto, H. ; Furusu, H. ; Morikawa, T. ; Mizuta, Y. ; Nishiyama, T. ; Omagari, K. ; Murase, K. ; Inoue, K. ; Murata, I. ; Kohno, S.
Oxford UK : Blackwell Science Ltd
Published 2000Staff ViewISSN: 1365-2036Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: To determine whether a 5-day regimen with rabeprazole, clarithromycin and amoxicillin (RCA) was as effective as a 7-day regimen.〈section xml:id="abs1-2"〉〈title type="main"〉Methods:A total of 139 H. pylori-infected patients were randomized to receive either a 5-day or 7-day course of rabeprazole 10 mg b.d., clarithromycin 400 mg b.d. and amoxicillin 750 mg b.d. Eradication was assessed by CLO test, histology and 13C-urea breath test.〈section xml:id="abs1-3"〉〈title type="main"〉Results:On the intention-to-treat basis, eradication rates were 66% (46 out of 70) and 84% (58 out of 69) for the 5- and 7-day regimens, respectively (P 〈 0.05). Using per protocol analysis, eradication rates were 70% (46 out of 66) and 91% (58 out of 64) for the 5- and 7-day regimens, respectively (P 〈 0.01). Adverse events, which were observed in 14 patients from each group, caused discontinuation of treatment in only two patients, resulting in excellent compliance.〈section xml:id="abs1-4"〉〈title type="main"〉Conclusions:Our 5-day regimen of RCA yielded inferior results, whereas the 7-day regimen achieved an eradication rate exceeding 90% on the per protocol basis. Therefore, treatment regimens of less than 7 days for proton pump inhibitor–clarithromycin–amoxicillin therapies cannot be recommended.Type of Medium: Electronic ResourceURL: -
13Kadoya, K. ; Sasaki, T. ; Kostka, G. ; Timpl, R. ; Matsuzaki, K. ; Kumagai, N. ; Sakai, L.Y. ; Nishiyama, T. ; Amano, S.
Oxford, UK : Blackwell Science Ltd
Published 2005Staff ViewISSN: 1365-2133Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Background Fibulin-5 was recently found as a secreted extracellular matrix protein that functions as a scaffold for elastic fibres. However, the distribution of fibulin-5 in human skin and its changes during the ageing process are not known.Objectives To explore the involvement of fibulin-5 in skin ageing, the age-dependent changes in fibulin-5 localization in human skin were examined compared with those of other elastic fibre components including elastin, fibrillin-1 and fibulin-2.Methods The distribution of elastin, fibrillin-1, fibrillin-2, fibulin-2 and fibulin-5 was investigated by means of immunohistochemistry using their specific antibodies. Skin samples were recovered from 12 healthy subjects undergoing plastic surgery. Ultraviolet (UV) B-irradiated or control nonirradiated buttock skin samples were obtained from two healthy volunteers at 2 days after the irradiation at 2 minimal erythemal doses.Results In the reticular dermis of young sun-protected skin from the upper arm, fibulin-5 colocalized with the other elastic fibre components, while in the papillary dermis fibulin-5 showed candelabra-like structures perpendicular to the epidermis with an unstained area just beneath the epidermis, which was similar to that of elastin but not fibrillin-1. Fibulin-5 in the reticular dermis decreased and disappeared with age even in sun-protected skin from the thigh, abdomen and upper arm. In sun-exposed skin, fibulin-5 was extremely reduced in the dermis of cheek skin even from a 20-year-old man. UVB irradiation reduced fibulin-5, fibulin-2 and elastin markedly, moderately and weakly, respectively, compared with levels in control nontreated skin. Interestingly, the deposition of fibulin-5 was increased in solar elastosis, like that of other elastic fibre components.Conclusions These results suggest that fibulin-5 is a good marker of skin ageing and that the earlier loss of fibulin-5 may involve age-dependent changes in other elastic fibre components.Type of Medium: Electronic ResourceURL: -
14Kadoya, K. ; Amano, S. ; Inomata, S. ; Tsunenaga, M. ; Matsuzaki, K. ; Oshima, H. ; Tanabe, M. ; Kumagai, N. ; Nishiyama, T.
Oxford, UK : Blackwell Science Ltd
Published 2003Staff ViewISSN: 1365-2133Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Summary Background Cultured epidermal autographs (CEAs) are currently used as a coverage treatment for burn wounds, for disfiguring burn scars involving depigmentation and in restoring the elasticity of the skin. The advantage of CEAs is that epidermal sheets prepared from small skin pieces can be enlarged sufficiently to cover large burn areas. Objectives We examined the correlation between recovery of skin texture, and elastic fibre formation and keratinocyte differentiation (assessed by immunohistochemistry) in CEAs used as replacement skin after tattoo excision in a Japanese patient. Methods The tattooed skin was excised down to the deep dermal layer and then CEA was transplanted onto the patient. The skin textures were evaluated by taking replicas of the skin surface, and histological changes of filaggrin, transglutaminase, involucrin, fibrillin and elastin in the autograft skin were examined by immunohistochemistry. Results The skin texture improved with time after grafting the CEA, and appeared similar to that of normal skin at 39 months. Among keratinocyte differentiation markers, filaggrin recovered to a normal pattern at around 6 months, and transglutaminase did so at 39 months, whereas involucrin expression remained abnormal at 39 months. Fibrillin expression appeared similar to that of normal skin by 39 months, except for sparse candelabra-like structures of short fibres. Elastin expression remained at a low level throughout. Conclusions Our results show that the recovery of skin texture after application of CEAs following tattoo excision is associated with the normalization of epidermal differentiation markers, except involucrin, and with the regeneration of elastic fibres in the dermis.Type of Medium: Electronic ResourceURL: -
15Amano, S. ; Akutsu, N. ; Ogura, Y. ; Nishiyama, T.
Oxford, UK : Blackwell Science Ltd
Published 2004Staff ViewISSN: 1365-2133Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Background Laminin 5 is known to induce the adhesion, spreading and migration of human keratinocytes. In skin wound healing, laminin 5 deposition beneath migrating keratinocytes occurs early and is followed by the formation of hemidesmosomes and then basement membrane.Objectives To identify factors that regulate the synthesis and secretion of laminin 5 by human keratinocytes during acute wound healing.Methods Laminin 5 synthesis by human keratinocytes was determined by a specific sandwich enzyme-linked immunosorbent assay. To determine the total amount of laminin 5 synthesized, laminin 5 deposited on culture dishes and inside cells was solubilized by detergent solution and determined separately from conditioned medium, and the total laminin 5 synthesis was calculated. A quantitative polymerase chain reaction method was used to measure the expression levels of laminin 5 genes, LAMA3, LAMB3 and LAMC2, which correspond to the α3, β3 and γ2 chains of laminin 5. We also examined the effects of lysophospholipids, proinflammatory cytokines and growth factors, which are components in acute wound fluids, on laminin 5 synthesis in keratinocytes.Results Human acute wound fluid at days 1, 2 and 3 stimulated laminin 5 synthesis in cultured human keratinocytes in a concentration-dependent manner, although findings are restricted to one case. Human serum also increased laminin 5 production by human keratinocytes as strongly as the wound fluid did, suggesting that the major active components in acute wound fluid may be derived from those in human serum. Lysophospholipids such as lysophosphatidic acid (LPA), lysophosphatidylcholines (LPCs) and sphingosine-1-phosphate (S1P) increased laminin 5 synthesis in a concentration-dependent manner. Among growth factors, epidermal growth factor, insulin-like growth factor-1, interferon-γ and keratinocyte growth factor increased laminin 5 production in keratinocytes, while platelet-derived growth factor, hepatocyte growth factor and basic fibroblast growth factor were ineffective. Although interleukin-1α had no effect, transforming growth factor (TGF)-α, tumour necrosis factor (TNF)-α and TGF-β1 also stimulated laminin 5 synthesis, and TGF-α and TGF-β1 showed a synergistic effect. Neutralizing antibodies to TGF-α and TGF-β1 markedly inhibited the enhanced laminin 5 synthesis by human serum, suggesting that TGF-α and TGF-β1 are important components to increase laminin 5 in human serum. In line with the increase of laminin 5 synthesis, the expression levels of all three laminin 5 genes were also augmented by TGF-α and TGF-β1.Conclusions Laminin 5 synthesis in human keratinocytes was augmented by inflammatory cytokines and growth factors such as TGF-α, TGF-β1 and TNF-α, and lysophospholipids such as S1P, LPA and LPCs, which are supposed to be present in acute wound fluid. The increased laminin 5 protein in the wound area presumably enhances wound repair by stimulating adhesion and migration of keratinocytes on the wound bed and by facilitating basement membrane formation at the dermal–epidermal junction.Type of Medium: Electronic ResourceURL: -
16Amano, S. ; Ogura, Y. ; Akutsu, N. ; Matsunaga, Y. ; Kadoya, K. ; Adachi, E. ; Nishiyama, T.
Oxford, UK : Blackwell Publishing Ltd
Published 2005Staff ViewISSN: 1365-2133Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Background The epidermal basement membrane (BM) plays important roles in adhesion between epidermis and dermis, and in controlling epidermal differentiation. The BM has been reported to be damaged in sun-exposed skin. Although matrix metalloproteinases (MMPs) are believed to be involved in the BM damage, there is no good in vitro model for examining BM damage by MMPs or for exploring methods to protect the BM.Objectives To examine the involvement of MMPs in BM damage and approaches to protect the BM from such damage by using an in vitro skin-equivalent (SE) model.Method SE was prepared by culturing human keratinocytes on contracted collagen gel including human fibroblasts. MMP-1, -2, -3 and -9, laminin 5 and type IV and VII collagens were determined by specific sandwich ELISAs, and MMP-2 and MMP-9 were analysed by gelatin zymography. Histological examination of SE was also carried out.Results Despite production of BM components such as laminin 5 and type IV and VII collagens in SEs, BM was rarely observed at the dermal–epidermal junction. Several MMPs, such as MMP-1, -2, -3 and -9, were observed to be present in conditioned media and some of them were in active forms. Tissue inhibitor of metalloproteinase (TIMP)-2 was not detected, although TIMP-1 was present. Synthetic MMP inhibitors, CGS27023A and MMP-inhibitor I, which inhibit MMP-1, -2, -3 and -9, markedly augmented deposition of laminin 5 and type IV and VII collagens at the dermal–epidermal junction, resulting in the formation of continuous epidermal BM.Conclusions Our results indicate that MMPs are involved in the degradation of BM in SEs, and that MMP inhibitors exert a protective effect against BM damage.Type of Medium: Electronic ResourceURL: -
17Staff View
ISSN: 0006-291XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
18Hiratsuka, A. ; Okada, T. ; Nishiyama, T. ; Fujikawa, M. ; Ogura, K. ; Okuda, H. ; Watabe, T.
Amsterdam : ElsevierStaff ViewISSN: 0006-291XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
19Staff View
ISSN: 0006-291XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
20Otofuji, Y.-i. ; Funahara, S. ; Matsuo, J. ; Murata, F. ; Nishiyama, T. ; Xilan Zheng ; Yaskawa, K.
Amsterdam : ElsevierStaff ViewISSN: 0012-821XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: GeosciencesPhysicsType of Medium: Electronic ResourceURL: