83 results on '"Morozumi Y"'
Search Results
2. Communication support project for patients with an intractable neurological disease
- Author
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Hineno, A., primary, Shikata, Y., additional, Morozumi, Y., additional, Nakamura, A., additional, and Ikeda, S.I., additional
- Published
- 2017
- Full Text
- View/download PDF
3. Muonium reaction with nitrogen dioxide
- Author
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Morozumi, Y., Suzuki, T., Nagamine, K., and Kondow, T.
- Published
- 1984
- Full Text
- View/download PDF
4. Muon spin relaxation for Ar+NO2 systems in transverse and longitudinal magnetic fields
- Author
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Kondow, T., Matsushita, A., Kuchitsu, K., Nishiyama, K., Morozumi, Y., and Nagamine, K.
- Published
- 1986
- Full Text
- View/download PDF
5. Zero-field spin relaxation of positive muon in Al-Mg
- Author
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Sato, E., Hatano, T., Suzuki, Y., Imafuku, M., Sunaga, M., Doyama, M., Morozumi, Y., Suzuki, T., and Nagamine, K.
- Published
- 1984
- Full Text
- View/download PDF
6. μ +SR studies on cis- and transpolyacetylene
- Author
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Nagamine, K., Ishida, K., Matsuzaki, T., Nishiyama, K., Kuno, Y., Morozumi, Y., Suzuki, T., Yamazaki, T., and Shirakawa, H.
- Published
- 1984
- Full Text
- View/download PDF
7. Experimental Comparison at KEK of High Gradient Performance Different Single Cell Superconducting Cavity Designs
- Author
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Furuta, F., Higashi, Y., Higo, T., Inoue, H., Kazakov, S., Kobayashi, Y., Matsumoto, H., Morozumi, Y., Orr, R., Saeki, T., Saito, K., Ueno, K., Yamaoka, H., and Sekutowicz, J.
- Published
- 2006
8. High Performance Normally-off GaN MOSFETs on Si Substrates
- Author
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Kambayashi, Hiroshi, primary, Ikeda, Nariaki, additional, Nomura, Takehiko, additional, Ueda, Hirokazu, additional, Morozumi, Y., additional, Harada, Katsushige, additional, Hasebe, Kazuhide, additional, Teramoto, Akinobu, additional, Sugawa, Shigetoshi, additional, and Ohmi, Tadahiro, additional
- Published
- 2013
- Full Text
- View/download PDF
9. Beam test of the pre-injector and the 3-MeV $H^{-}$ RFQ with a new field stabilizer PISL
- Author
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Ueno, A, Fujimura, S, Yamashita, Y, Tanaka, M, Kubota, C, Yoshino, K, Morozumi, Y, Kawamura, M, Kudo, K, Ono, M, Anami, S, Igarashi, Z E, Takasaki, E, Takagi, A, and Yamazaki, Y
- Subjects
Accelerators and Storage Rings - Published
- 1996
10. High Quality SiO2/Al2O3 Gate Stack for GaN MOSFET
- Author
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Kambayashi, H., primary, Nomura, T., additional, Ueda, H., additional, Harada, K., additional, Morozumi, Y., additional, Hasebe, K., additional, Teramoto, A., additional, Sugawa, S., additional, and Ohmi, T., additional
- Published
- 2012
- Full Text
- View/download PDF
11. First operation of a 432-MHz, 3-MeV RFQ stabilized with PISLs
- Author
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Ueno, A, Yamazaki, Y, Fujimura, S, Kubota, C, Yoshino, K, Morozumi, Y, Kawamura, M, Kudo, K, Ono, M, Anami, S, Igarashi, Z E, Takasaki, E, Takagi, A, Mori, Y, and Kihara, M
- Subjects
Engineering - Published
- 1995
12. High-power test of a 432-MHz, 3-MeV RFQ stabilized with PISLs
- Author
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Ueno, A, Yamazaki, Y, Kubota, C, Yoshino, K, Morozumi, Y, Kawamura, M, Kudo, K, Ono, M, Anami, S, Igarashi, Z E, Takasaki, E, Takagi, A, Mori, Y, and Kihara, M
- Subjects
Engineering - Published
- 1995
13. rf characteristics of a high-power model of the 432 MHz DTL
- Author
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Naito, F, Anami, S, Igarashi, Z E, Kato, T, Kawamura, M, Kubota, T, Kubo, T, Kudo, K, Morozumi, Y, Nanmo, K, Ono, M, Takasaki, E, Takenaka, T, Yoshino, K, and Yamazaki, Y
- Subjects
Engineering - Published
- 1995
14. Human PSF binds to RAD51 and modulates its homologous-pairing and strand-exchange activities
- Author
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Morozumi, Y., primary, Takizawa, Y., additional, Takaku, M., additional, and Kurumizaka, H., additional
- Published
- 2009
- Full Text
- View/download PDF
15. HIGH ACCELERATING FIELD SUPERCONDUCTING RADIO FREQUENCY CAVITIES
- Author
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ORR, R. S., primary, SAITO, K., additional, FURUTA, F., additional, SAEKI, T., additional, INOUE, H., additional, MOROZUMI, Y., additional, HIGO, T., additional, HIGASHI, Y., additional, MATSUMOTO, H., additional, KAZAKOV, S., additional, YAMAOKA, H., additional, UENO, K., additional, and SATO, M., additional
- Published
- 2008
- Full Text
- View/download PDF
16. An application of a homogenization method to the estimation of effective thermal conductivity of a hydrogen storage alloy bed considering variation of contact conditions between alloy particles
- Author
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UEOKA, K, primary, MIYAUCHI, S, additional, ASAKUMA, Y, additional, HIROSAWA, T, additional, MOROZUMI, Y, additional, AOKI, H, additional, and MIURA, T, additional
- Published
- 2007
- Full Text
- View/download PDF
17. Test operation of ball-screw-type tuner for low-los high-gradient superconducting cavity at 77 K
- Author
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Higo, T., primary, Higashi, Y., additional, Araoka, O., additional, Furuta, F., additional, Morozumi, Y., additional, Saeki, T., additional, Saito, K., additional, Ueno, K., additional, Wake, M., additional, and Yamaoka, H., additional
- Published
- 2007
- Full Text
- View/download PDF
18. Revision of accelerating and damping structures for kek STF 45 MV/m accelerator modules
- Author
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Morozumi, Y., primary, Furuta, F., additional, Higo, T., additional, Saeki, T., additional, and Saito, K., additional
- Published
- 2007
- Full Text
- View/download PDF
19. Optimization of the low loss SRF cavity for the ILC
- Author
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Li, Z., primary, Ge, L., additional, Lee, L., additional, Ng, C., additional, Schussman, G., additional, Xiao, L., additional, Ko, K., additional, Sekutowicz, J., additional, Kneisel, P., additional, Higo, T., additional, Morozumi, Y., additional, and Saito, K., additional
- Published
- 2007
- Full Text
- View/download PDF
20. Modeling of gasification and fragmentation behavior of char particles having complicated structures
- Author
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YAMASHITA, T, primary, FUJII, Y, additional, MOROZUMI, Y, additional, AOKI, H, additional, and MIURA, T, additional
- Published
- 2006
- Full Text
- View/download PDF
21. NUMERICAL ANALYSIS OF 2 T/DAY ENTRAINED FLOW COAL GASIFIER- Effect of the Shape of the Gasifier -
- Author
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Matsushita, Y., primary, Goto, A., additional, Morozumi, Y., additional, Aoki, H., additional, and Miura, T., additional
- Published
- 2006
- Full Text
- View/download PDF
22. High-Performance MIM Capacitors based on TiO2/ZrO2/TiO2 and AlO-doped TiO2/ZrO2/TiO2 Dielectric Stacks for DRAM Applications.
- Author
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Padmanabhan, Revathy, Bhat, Navakanta, Mohan, S., Morozumi, Y., and Kaushal, Sanjeev
- Published
- 2013
- Full Text
- View/download PDF
23. Multi-cavity bridge coupler
- Author
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Morozumi, Y, Kageyama, T, and Yamazaki, Y
- Subjects
Engineering - Published
- 1990
24. Observation of multibunch phenomena in TRISTAN accumulation ring
- Author
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Funakoshi, Y, Hayano, H, Hanaoka, K, Urakawa, J, Kawamoto, T, Ogata, A, Morozumi, Y, Higo, T, and Satoh, K
- Subjects
Accelerators and Storage Rings - Published
- 1990
25. Conformable formation of high quality ultra-thin amorphous Ta2 O5 gate dielectrics utilizing water assisted deposition (WAD) for sub 50 nm damascene metal gate MOSFETs.
- Author
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Inumiya, S., Morozumi, Y., Yagishita, A., Saito, T., Gao, D., Choi, D., Hasebe, K., Suguro, K., Tsunashima, Y., and Arikado, T.
- Published
- 2000
- Full Text
- View/download PDF
26. Effect of external tensile stress on the growth of interstitial loops
- Author
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Saka, H., primary, Kawamura, K., additional, Morozumi, Y., additional, and Teshima, H., additional
- Published
- 1991
- Full Text
- View/download PDF
27. Design of a Low Loss SRF Cavity for the ILC.
- Author
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Sekutowicz, J., Ko, K., Ge, L., Lee, L., Li, Z., Ng, C., Schussman, G., Xiao, L., Gonin, I., Khabibouline, T., Solyak, N., Morozumi, Y., Saito, K., and Kneisel, P.
- Published
- 2005
- Full Text
- View/download PDF
28. μ+SR studies on cis- and transpolyacetylene
- Author
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Nagamine, K., Ishida, K., Matsuzaki, T., Nishiyama, K., Kuno, Y., Morozumi, Y., Suzuki, T., Yamazaki, T., and Shirakawa, H.
- Abstract
Electronic states and depolarization phenomena are studied for theμ
+ in cis- and transpolyacetylene (CH)x . Formation of weakly bound muonium-like paramagnetic state is found in cis-(CH)x at room temperature, while diamagneticμ+ state is formed in trans-(CH)x . The origin of this clear difference might reflect properties of excitation modes in these two-isomers.- Published
- 1984
- Full Text
- View/download PDF
29. Muon spin relaxation for Ar+NO2 systems in transverse and longitudinal magnetic fields
- Author
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Kondow, T., Matsushita, A., Kuchitsu, K., Nishiyama, K., Morozumi, Y., and Nagamine, K.
- Abstract
Abstract: Surface muons produced in UT-MSL were introduced into argon gas of 4.00.2 atm with NO
2 (0–30 ppm), and muonium signals were detected in the presence of a transverse (1.7–3.4 G) and a longitudinal magnetic field (0–3.5 kG) at 2951 K. The cross section for the transverse relaxation was (11.01.0)10−16 cm2 . The relaxation rates in different longitudinal magnetic fields show that the rate does not follow the conventional equation which assumes that the relaxation occurs mainly by spin-exchange interaction. Similar measurements were performed for the Mu+O2 system. These findings indicate that chemical reactions contribute to these relaxation rates.- Published
- 1986
- Full Text
- View/download PDF
30. The first measurement of low-loss 9-cell cavity in a cryomodule at stf
- Author
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Saeki, T., Akemoto, M., Fukuda, S., Furuta, F., Hara, K., Higashi, Y., Higo, T., Hosoyama, K., Inoue, H., Kabe, A., Katagiri, H., Kazakov, S., Kojima, Y., Matsumoto, H., Matsumoto, T., Michizono, S., Miura, T., Morozumi, Y., Hirotaka NAKAI, Nakanishi, K., Ohuchi, N., Saito, K., Takenaka, T., Tsuchiya, K., Satoh, M., Yamaoka, H., Yano, Y., Kenekiyo, T., and Zhai, J.
31. Turbulent combustion simulation in a jet burner
- Author
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Hirotatsu Watanabe, Suwa, Y., Morozumi, Y., Aoki, H., and Miura, T.
32. Detector concepts
- Author
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Aarons, G., Abe, T., Abernathy, J., Ablikim, M., Abramowicz, H., Adey, D., Adloff, C., Adolphsen, C., Afanaciev, K., Agapov, I., Ahn, J. -K, Aihara, H., Akemoto, M., Del Carmenalabau, M., Albert, J., Albrecht, H., Albrecht, M., Alesini, D., Alexander, G., Alexander, J., Allison, W., Amann, J., Amirikas, R., An, Q., Anami, S., Ananthanarayan, B., Anderson, T., Andricek, L., Anduze, M., Anerella, M., Anfimov, N., Angal-Kalinin, D., Antipov, S., Antoine, C., Aoki, M., Aoza, A., Aplin, S., Appleby, R., Arai, Y., Araki, S., Arkan, T., Arnold, N., Arnold, R., Arnowitt, R., Artru, X., Arya, K., Aryshev, A., Asakawa, E., Asiri, F., Asner, D., Atac, M., Atoian, G., Attié, D., Augustin, J. -E, Augustine, D. B., Ayres, B., Aziz, T., Baars, D., Badaud, F., Baddams, N., Bagger, J., Bai, S., Bailey, D., Bailey, I. R., Baker, D., Balalykin, N. I., Balbuena, J. P., Baldy, J. -L, Ball, M., Ballestrero, A., Ballin, J., Baltay, C., Bambade, P., Ban, S., Band, H., Bane, K., Banerjee, B., Barbanotti, S., Barbareschi, D., Barbaro-Galtieri, A., Barber, D. P., Barbi, M., Bardin, D. Y., Barish, B., Barklow, T. L., Barlow, R., Barnes, V. E., Barone, M., Bartels, C., Bartsch, V., Basu, R., Battaglia, M., Batygin, Y., Baudot, J., Baur, U., Baynham, D. E., Beard, C., Bebek, C., Bechtle, P., Becker, U. J., Bedeschi, F., Bedjidian, M., Behera, P., Behnke, T., Bellantoni, L., Bellerive, A., Bellomo, P., Bentson, L. D., Benyamna, M., Bergauer, T., Berger, E., Bergholz, M., Beri, S., Berndt, M., Bernreuther, W., Bertolini, A., Besancon, M., Besson, A., Beteille, A., Bettoni, S., Beyer, M., Bhandari, R. K., Bharadwaj, V., Bhatnagar, V., Bhattacharya, S., Bhattacharyya, G., Bhattacherjee, B., Bhuyan, R., Bi, X. -J, Biagini, M., Bialowons, W., Biebel, O., Bieler, T., Bierwagen, J., Birch, A., Bisset, M., Biswal, S. S., Blackmore, V., Blair, G., Blanchard, G., Blazey, G., Blue, A., Blümlein, J., Boffo, C., Bohn, C., Boiko, V. I., Boisvert, V., Bondarchuk, E. N., Boni, R., Bonvicini, G., Boogert, S., Boonekamp, M., Boorman, G., Borras, K., Bortoletto, D., Bosco, A., Bosio, C., Bosland, P., Bosotti, A., Boudry, V., Boumediene, D. -E, Bouquet, B., Bourov, S., Bowden, G., Bower, G., Boyarski, A., Bozovic-Jelisavcic, I., Bozzi, C., Brachmann, A., Bradshaw, T. W., Brandt, A., Brasser, H. P., Brau, B., Brau, J. E., Breidenbach, M., Bricker, S., Brient, J. -C, Brock, I., Brodsky, S., Brooksby, C., Broome, T. A., Brown, D., Brownell, J. H., Bruchon, M., Brueck, H., Brummitt, A. J., Brun, N., Buchholz, P., Budagov, Y. A., Bulgheroni, A., Bulyak, E., Bungau, A., Bürger, J., Burke, D., Burkhart, C., Burrows, P., Burt, G., Burton, D., Büsser, K., Butler, J., Butterworth, J., Buzulutskov, A., Cabruja, E., Caccia, M., Cai, Y., Calcaterra, A., Caliier, S., Camporesi, T., Cao, J. -J, Cao, J. S., Capatina, O., Cappellini, C., Carcagno, R., Carena, M., Carloganu, C., Carosi, R., Carr, F. S., Carrion, F., Carter, H. F., Carter, J., Carwardine, J., Cassel, R., Cassell, R., Cavallari, G., Cavallo, E., Cembranos, J. A. R., Chakraborty, D., Chandez, F., Charles, M., Chase, B., Chattopadhyay, S., Chauveau, J., Chefdeville, M., Chehab, R., Chel, S., Chelkov, G., Chen, C., Chen, H. S., Chen, H. B., Chen, J. E., Chen, S. Y., Chen, S., Chen, X., Chen, Y. B., Cheng, J., Chevallier, M., Chi, Y. L., Chickering, W., Cho, G. -C, Cho, M. -H, Choi, J. -H, Choi, J. B., Choi, S. Y., Choi, Y. -I, Choudhary, B., Choudhury, D., Choudhury, S. R., Christian, D., Christian, G., Christophe, G., Chung, J. -H, Church, M., Ciborowski, J., Cihangir, S., Ciovati, G., Clarke, C., Clarke, D. G., Clarke, J. A., Clements, E., Coca, C., Coe, P., Cogan, J., Colas, P., Collard, C., Colledani, C., Combaret, C., Comerma, A., Compton, C., Constance, B., Conway, J., Cook, E., Cooke, P., Cooper, W., Corcoran, S., Cornat, R., Corner, L., Gil, E. C., Corvin, W. C., Ramusino, A. C., Cowan, R., Crawford, C., Cremaldi, L. M., Crittenden, J. A., Cussans, D., Cvach, J., Da Silva, W., Khah, H. D., Dabrowski, A., Dabrowski, W., Dadoun, O., Dai, J. P., Dainton, J., Daly, C., Damerell, C., Danilov, M., Daniluk, W., Daram, S., Datta, A., Dauncey, P., David, J., Davier, M., Davies, K. P., Dawson, S., Boer, W., Curtis, S., Groot, N., La Taille, C., Lira, A., Roeck, A., Sangro, R., Santis, S., Deacon, L., Deandrea, A., Klaus Dehmelt, Delagnes, E., Delahaye, J. -P, Delebecque, P., Delerue, N., Delferriere, O., Demarteau, M., Deng, Z., Denisov, Yu N., Densham, C. J., Desch, K., Deshpande, N., Devanz, G., Devetak, E., Dexter, A., Di Benedetto, V., Diéguez, Á, Diener, R., Dinh, N. D., Dixit, M., Dixit, S., Djouadi, A., Dolezal, Z., Dollan, R., Dong, D., Dong, H. Y., Dorfan, J., Dorokhov, A., Doucas, G., Downing, R., Doyle, E., Doziere, G., Drago, A., Dragt, A., Drake, G., Drásal, Z., Dreiner, H., Drell, P., Driouichi, C., Drozhdin, A., Drugakov, V., Du, S., Dugan, G., Duginov, V., Dulinski, W., Dulucq, F., Dutta, S., Dwivedi, J., Dychkant, A., Dzahini, D., Eckerlin, G., Edwards, H., Ehrenfeld, W., Ehrlichman, M., Ehrlichmann, H., Eigen, G., Elagin, A., Elementi, L., Eliasson, P., Ellis, J., Ellwood, G., Elsen, E., Emery, L., Enami, K., Endo, K., Enomoto, A., Eozénou, F., Erbacher, R., Erickson, R., Eyser, K. O., Fadeyev, V., Fang, S. X., Fant, K., Fasso, A., Giannelli, M. F., Fehlberg, J., Feld, L., Feng, J. L., Ferguson, J., Fernandez-Garcia, M., Fernandez-Hernando, J. L., Fiala, P., Fieguth, T., Finch, A., Finocchiaro, G., Fischer, P., Fisher, P., Fisk, H. E., Fitton, M. D., Fleck, I., Fleischer, M., Fleury, J., Flood, K., Foley, M., Ford, R., Fortin, D., Foster, B., Fourches, N., Francis, K., Frey, A., Frey, R., Friedsam, H., Frisch, J., Frishman, A., Fuerst, J., Fujii, K., Fujimoto, J., Fukuda, M., Fukuda, S., Funahashi, Y., Funk, W., Furletova, J., Furukawa, K., Furuta, F., Fusayasu, T., Fuster, J., Gadow, K., Gaede, F., Gaglione, R., Gai, W., Gajewski, J., Galik, R., Galkin, A., Galkin, V., Gallin-Martel, L., Gannaway, F., Gao, J. S., Gao, J., Gao, Y., Garbincius, P., Garcia-Tabares, L., Garren, L., Garrido, L., Garutti, E., Garvey, T., Garwin, E., Gascón, D., Gastal, M., Gatto, C., Gatto, R., Gay, P., Ge, L., Ge, M. Q., Ge, R., Geiser, A., Gellrich, A., Genat, J. -F, Geng, Z. Q., Gentile, S., Gerbick, S., Gerig, R., Ghosh, D. K., Ghosh, K., Gibbons, L., Giganon, A., Gillespie, A., Gillman, T., Ginzburg, I., Giomataris, I., Giunta, M., Gladkikh, P., Gluza, J., Godbole, R., Godfrey, S., Goldhaber, G., Goldstein, J., Gollin, G. D., Gonzalez-Sanchez, F. J., Goodrick, M., Gornushkin, Y., Gostkin, M., Gottschalk, E., Goudket, P., Eschrich, I. G., Gournaris, F., Graciani, R., Graf, N., Grah, C., Grancagnolo, F., Grandjean, D., Grannis, P., Grassellino, A., Graugés, E., Gray, S., Green, M., Greenhalgh, J., Greenshaw, T., Grefe, C., Gregor, I. -M, Grenier, G., Grimes, M., Grimm, T., Gris, P., Grivaz, J. -F, Groll, M., Gronberg, J., Grondin, D., Groom, D., Gross, E., Grunewald, M., Grupen, C., Grzelak, G., Gu, J., Gu, Y. -T, Guchait, M., Guiducci, S., Guler, A. M., Guler, H., Gulmez, E., Gunion, J., Guo, Z. Y., Gurtu, A., Ha, H. B., Haas, T., Haase, A., Haba, N., Haber, H., Haensel, S., Hagge, L., Hagura, H., Hajdu, C., Haller, G., Haller, J., Hallermann, L., Halyo, V., Hamaguchi, K., Hammond, L., Han, L., Han, T., Hand, L., Handu, V. K., Hano, H., Hansen, C., Hansen, J. D., Hansen, J. B., Hara, K., Harder, K., Hartin, A., Hartung, W., Hast, C., Hauptman, J., Hauschild, M., Hauviller, C., Havranek, M., Hawkes, C., Hawkings, R., Hayano, H., Hazumi, M., He, A., He, H. J., Hearty, C., Heath, H., Hebbeker, T., Hedberg, V., Hedin, D., Heifets, S., Heinemeyer, S., Heini, S., Helebrant, C., Helms, R., Heltsley, B., Henrot-Versille, S., Henschel, H., Hensel, C., Hermel, R., Herms, A., Herten, G., Hesselbach, S., Heuer, R. -D, Heusch, C. A., Hewett, J., Higashi, N., Higashi, T., Higashi, Y., Higo, T., Hildreth, M. D., Hiller, K., Hillert, S., Hillier, S. J., Himel, T., Himmi, A., Hinchliffe, I., Hioki, Z., Hirano, K., Hirose, T., Hisamatsu, H., Hisano, J., Hlaing, C. T., Hock, K. M., Hoeferkamp, M., Hohlfeld, M., Honda, Y., Hong, J., Hong, T. M., Honma, H., Horii, Y., Horvath, D., Hosoyama, K., Hostachy, J. -Y, Hou, M., Hou, W. -S, Howell, D., Hronek, M., Hsiung, Y. B., Hu, B., Hu, T., Huang, J. -Y, Huang, T. M., Huang, W. H., Huedem, E., Huggard, P., Hugonie, C., Hu-Guo, C., Huitu, K., Hwang, Y., Idzik, M., Ignatenko, A., Ignatov, F., Ikeda, H., Ikematsu, K., Ilicheva, T., Imbault, D., Imhof, A., Incagli, M., Ingbir, R., Inoue, H., Inoue, Y., Introzzi, G., Ioakeimidi, K., Ishihara, S., Ishikawa, A., Ishikawa, T., Issakov, V., Ito, K., Ivanov, V. V., Ivanov, V., Ivanyushenkov, Y., Iwasaki, M., Iwashita, Y., Jackson, D., Jackson, F., Jacobsen, B., Jaganathan, R., Jamison, S., Janssen, M. E., Jaramillo-Echeverria, R., Jaros, J., Jauffret, C., Jawale, S. B., Jeans, D., Jedziniak, R., Jeffery, B., Jehanno, D., Jenner, L. J., Jensen, C., Jensen, D. R., Jiang, H., Jiang, X. M., Jimbo, M., Jin, S., Jobe, R. K., Johnson, A., Johnson, E., Johnson, M., Johnston, M., Joireman, P., Jokic, S., Jones, J., Jones, R. M., Jongewaard, E., Jönsson, L., Joshi, G., Joshi, S. C., Jung, J. -Y, Junk, T., Juste, A., Kado, M., Kadyk, J., Käfer, D., Kako, E., Kalavase, P., Kalinin, A., Kalinowski, J., Kamitani, T., Kamiya, Y., Kamoshita, J. -I, Kananov, S., Kanaya, K., Kanazawa, K. -I, Kanemura, S., Kang, H. -S, Kang, W., Kanjial, D., Kapusta, F., Karataev, P., Karchin, P. E., Karlen, D., Karyotakis, Y., Kashikhin, V., Kashiwagi, S., Kasley, P., Katagiri, H., Kato, T., Kato, Y., Katzy, J., Kaukher, A., Kaur, M., Kawagoe, K., Kawamura, H., Kazakov, S., Kekelidze, V. D., Keller, L., Kelley, M., Kelly, M., Kennedy, K., Kephart, R., Keung, J., Khainovski, O., Khan, S. A., Khare, P., Khovansky, N., Kiesling, C., Kikuchi, M., Kilian, W., Killenberg, M., Kim, D., Kim, E. S., Kim, E. -J, Kim, G., Kim, H., Kim, H. -C, Kim, J., Kim, K. -J, Kim, K. S., Kim, P., Kim, S., Kim, S. -H, Kim, S. K., Kim, T. J., Kim, Y., Kim, Y. -K, Kimmitt, M., Kirby, R., Kircher, F., Kisielewska, D., Kittel, O., Klanner, R., Klebaner, A. L., Kleinwort, C., Klimkovich, T., Klinkby, E., Kluth, S., Knecht, M., Kneisel, P., Ko, I. S., Ko, K., Kobayashi, M., Kobayashi, N., Kobel, M., Koch, M., Kodys, P., Koetz, U., Kohrs, R., Kojima, Y., Kolanoski, H., Kolodziej, K., Kolomensky, Y. G., Komamiya, S., Kong, X. C., Konigsberg, J., Korbel, V., Koscielniak, S., Kostromin, S., Kowalewski, R., Kraml, S., Krammer, M., Krasnykh, A., Krautscheid, T., Krawczyk, M., Krebs, H. J., Krempetz, K., Kribs, G., Krishnagopal, S., Kriske, R., Kronfeld, A., Kroseberg, J., Kruchonak, U., Kruecker, D., Krüger, H., Krumpa, N. A., Krumshtein, Z., Kuang, Y. P., Kubo, K., Kuchler, V., Kudoh, N., Kulis, S., Kumada, M., Kumar, A., Kume, T., Kundu, A., Kurevlev, G., Kurihara, Y., Kuriki, M., Kuroda, S., Kuroiwa, H., Kurokawa, S. -I, Kusano, T., Kush, P. K., Kutschke, R., Kuznetsova, E., Kvasnicka, P., Kwon, Y., Labarga, L., Lacasta, C., Lackey, S., Lackowski, T. W., Lafaye, R., Lafferty, G., Lagorio, E., Laktineh, I., Lal, S., Laloum, M., Lam, B., Lancaster, M., Lander, R., Lange, W., Langenfeld, U., Langeveld, W., Larbalestier, D., Larsen, R., Lastovicka, T., Lastovicka-Medin, G., Latina, A., Latour, E., Laurent, L., Le, B. N., Le, D. N., Le Diberder, F., Le Dû, P., Lebbolo, H., Lebrun, P., Lecoq, J., Lee, S. -W, Lehner, F., Leibfritz, J., Lenkszus, F., Lesiak, T., Levy, A., Lewandowski, J., Leyh, G., Li, C., Li, C. S., Li, C. H., Li, D. Z., Li, G., Li, J., Li, S. P., Li, W. M., Li, W., Li, X. P., Li, X. -Q, Li, Y., Li, Z., Li, Z. Q., Liang, J. T., Liao, Y., Lilje, L., Lima, J. G., Lintern, A. J., Lipton, R., List, B., List, J., Liu, C., Liu, J. F., Liu, K. X., Liu, L. Q., Liu, S. Z., Liu, S. G., Liu, S., Liu, W., Liu, W. B., Liu, Y. P., Liu, Y. D., Lockyer, N., Logan, H. E., Logatchev, P. V., Lohmann, W., Lohse, T., Lola, S., Lopez-Virto, A., Loveridge, P., Lozano, M., Lu, C. -D, Lu, C., Lu, G. -L, Lu, W. H., Lubatti, H., Lucotte, A., Lundberg, B., Lundin, T., Luo, M., Luong, M., Luth, V., Lutz, B., Lutz, P., Lux, T., Luzniak, P., Lyapin, A., Lykken, J., Lynch, C., Ma, L., Ma, Q., Ma, W. -G, Macfarlane, D., Maciel, A., Macleod, A., Macnair, D., Mader, W., Magill, S., Magnan, A. -M, Maiheu, B., Maity, M., Majchrzak, M., Majumder, G., Makarov, R., Makowski, D., Malaescu, B., Mallik, C., Mallik, U., Malton, S., Malyshev, O. B., Malysheva, L. I., Mammosser, J., Mamta, Mamuzic, J., Manen, S., Manghisoni, M., Manly, S., Marcellini, F., Marcisovsky, M., Markiewicz, T. W., Marks, S., Marone, A., Marti, F., Martin, J. -P, Martin, V., Martin-Chassard, G., Martinez, M., Martinez-Rivero, C., Martsch, D., Martyn, H. -U, Maruyama, T., Masuzawa, M., Mathez, H., Matsuda, T., Matsumoto, H., Matsumoto, S., Matsumoto, T., Matsunaga, H., Mättig, P., Mattison, T., Mavromanolakis, G., Mawatari, K., Mazzacane, A., Mcbride, P., Mccormick, D., Mccormick, J., Mcdonald, K. T., Mcgee, M., Mcintosh, P., Mckee, B., Mcpherson, R. A., Meidlinger, M., Meier, K., Mele, B., Meller, B., Melzer-Pellmann, I. -A, Mendez, H., Mercer, A., Merkin, M., Meshkov, I. N., Messner, R., Metcalfe, J., Meyer, C., Meyer, H., Meyer, J., Meyer, N., Meyners, N., Michelato, P., Michizono, S., Mihalcea, D., Mihara, S., Mihara, T., Mikami, Y., Mikhailichenko, A. A., Milardi, C., Miller, D. J., Miller, O., Miller, R. J., Milstene, C., Mimashi, T., Minashvili, I., Miquel, R., Mishra, S., Mitaroff, W., Mitchell, C., Miura, T., Miyamoto, A., Miyata, H., Mjörnmark, U., Mnich, J., Moenig, K., Moffeit, K., Mokhov, N., Molloy, S., Monaco, L., Monasterio, P. R., Montanari, A., Moon, S. I., Moortgat-Pick, G. A., Freitas, P. M., Morel, F., Moretti, S., Morgunov, V., Mori, T., Morin, L., Morisseau, F., Morita, Y., Morozov, N., Morozumi, Y., Morse, W., Moser, H. -G, Moultaka, G., Mtingwa, S., Mudrinic, M., Mueller, A., Mueller, W., Muennich, A., Muhlleitner, M. M., Mukherjee, B., Mukhopadhyaya, B., Müller, T., Munro, M., Murayama, H., Muto, T., Myneni, G. R., Nabhiraj, P. Y., Nagaitsev, S., Nagamine, T., Nagano, A., Naito, T., Nakai, H., Nakajima, H., Nakamura, I., Nakamura, T., Nakanishi, T., Nakao, K., Nakao, N., Nakayoshi, K., Nam, S., Namito, Y., Namkung, W., Nantista, C., Napoly, O., Narain, M., Naroska, B., Nauenberg, U., Nayyar, R., Neal, H., Nelson, C., Nelson, J., Nelson, T., Nemecek, S., Neubauer, M., Neuffer, D., Newman, M. Q., Nezhevenko, O., Ng, C. -K, Nguyen, A. K., Nguyen, M., Thi, H. V. N., Niebuhr, C., Niehoff, J., Niezurawski, P., Nishitani, T., Nitoh, O., Noguchi, S., Nomerotski, A., Noonan, J., Norbeck, E., Nosochkov, Y., Notz, D., Nowak, G., Nowak, H., Noy, M., Nozaki, M., Nyffeler, A., Nygren, D., Oddone, P., O, J., Oh, J. -S, Oh, S. K., Ohkuma, K., Ohlerich, M., Ohmi, K., Ohnishi, Y., Ohsawa, S., Ohuchi, N., Oide, K., Okada, N., Okada, Y., Okamura, T., Okugi, T., Okumi, S., Okumura, K. -I, Olchevski, A., Oliver, W., Olivier, B., Olsen, J., Olsen, S., Olshevsky, A. G., Olsson, J., Omori, T., Onel, Y., Onengut, G., Ono, H., Onoprienko, D., Oreglia, M., Oren, W., Orimoto, T. J., Oriunno, M., Orlandea, M. C., Oroku, M., Orr, L. H., Orr, R. S., Oshea, V., Oskarsson, A., Osland, P., Ossetski, D., Österman, L., Ostiguy, F., Otono, H., Ottewell, B., Ouyang, Q., Padamsee, H., Padilla, C., Pagani, C., Palmer, M. A., Pam, W. M., Pande, M., Pande, R., Pandit, V. S., Pandita, P. N., Pandurovic, M., Pankov, A., Panzeri, N., Papandreou, Z., Paparella, R., Para, A., Park, H., Parker, B., Parkes, C., Parma, V., Parsa, Z., Parsons, J., Partridge, R., Pasquinelli, R., Pásztor, G., Paterson, E., Patrick, J., Patteri, P., Patterson, J. R., Pauletta, G., Paver, N., Pavlicek, V., Pawlik, B., Payet, J., Pchalek, N., Pedersen, J., Pei, G. X., Pei, S. L., Pelka, J., Pellegrini, G., Pellett, D., Peng, G. X., Penn, G., Penzo, A., Perry, C., Peskin, M., Peters, F., Petersen, T. C., Peterson, D., Peterson, T., Petterson, M., Pfeffer, H., Pfund, P., Phelps, A., Phi, Q., Phillips, J., Phinney, N., Piccolo, M., Piemontese, L., Pierini, P., Piggott, W. T., Pike, G., Pillet, N., Jayawardena, T. P., Piot, P., Pitts, K., Pivi, M., Plate, D., Pleier, M. -A, Poblaguev, A., Poehler, M., Poelker, M., Poffenberger, P., Pogorelsky, I., Poirier, F., Poling, R., Poole, M., Popescu, S., Popielarski, J., Pöschl, R., Postranecky, M., Potukochi, P. N., Prast, J., Prat, S., Preger, M., Prepost, R., Price, M., Proch, D., Puntambekar, A., Qin, Q., Qu, H. M., Quadt, A., Quesnel, J. -P, Radeka, V., Rahmat, R., Rai, S. K., Raimondi, P., Ramberg, E., Ranjan, K., Rao, S. V. L. S., Raspereza, A., Ratti, A., Ratti, L., Raubenheimer, T., Raux, L., Ravindran, V., Raychaudhuri, S., Re, V., Rease, B., Reece, C. E., Regler, M., Rehlich, K., Reichel, I., Reichold, A., Reid, J., Reid, R., Reidy, J., Reinhard, M., Renz, U., Repond, J., Resta-Lopez, J., Reuen, L., Ribnik, J., Rice, T., Richard, F., Riemann, S., Riemann, T., Riles, K., Riley, D., Rimbault, C., Rindani, S., Rinolfi, L., Risigo, F., Riu, I., Rizhikov, D., Rizzo, T., Rochford, J. H., Rodriguez, P., Roeben, M., Rolandi, G., Roodman, A., Rosenberg, E., Roser, R., Ross, M., Rossel, F., Rossmanith, R., Roth, S., Rougé, A., Rowe, A., Roy, A., Roy, S. B., Roy, S., Royer, L., Royole-Degieux, P., Royon, C., Ruan, M., Rubin, D., Ruehl, I., Jimeno, A. R., Ruland, R., Rusnak, B., Ryu, S. -Y, Sabbi, G. L., Sadeh, I., Sadygov, Z. Y., Saeki, T., Sagan, D., Sahni, V. C., Saini, A., Saito, K., Sajot, G., Sakanaka, S., Sakaue, K., Salata, Z., Salih, S., Salvatore, F., Samson, J., Sanami, T., Sanchez, A. L., Sands, W., Santic, J., Sanuki, T., Sapronov, A., Sarkar, U., Sasao, N., Satoh, K., Sauli, F., Saunders, C., Saveliev, V., Savoy-Navarro, A., Sawyer, L., Saxton, L., Schäfer, O., Schälicke, A., Schade, P., Schaetzel, S., Scheitrum, G., Schibler, É, Schindler, R., Schlösser, M., Schlueter, R. D., Schmid, P., Schmidt, R. S., Schneekloth, U., Schreiber, H. J., Schreiber, S., Schroeder, H., Schüler, K. P., Schulte, D., Schultz-Coulon, H. -C, Schumacher, M., Schumann, S., Schumm, B. A., Schwienhorst, R., Schwierz, R., Scott, D. J., Scuri, F., Sefkow, F., Sefri, R., Seguin-Moreau, N., Seidel, S., Seidman, D., Sekmen, S., Seletskiy, S., Senaha, E., Senanayake, R., Sendai, H., Sertore, D., Seryi, A., Settles, R., Sever, R., Shales, N., Shao, M., Shelkov, G. A., Shepard, K., Shepherd-Themistocleous, C., Sheppard, J. C., Shi, C. T., Shidara, T., Shim, Y. -J, Shimizu, H., Shimizu, Y., Shimogawa, T., Shin, S., Shioden, M., Shipsey, I., Shirkov, G., Shishido, T., Shivpuri, R. K., Shrivastava, P., Shulga, S., Shumeiko, N., Shuvalov, S., Si, Z., Siddiqui, A. M., Siegrist, J., Simon, C., Simrock, S., Sinev, N., Singh, B. K., Singh, J., Singh, P., Singh, R. K., Singh, S. K., Singini, M., Sinha, A. K., Sinha, N., Sinha, R., Sinram, K., Sissakian, A. N., Skachkov, N. B., Skrinsky, A., Slater, M., Slominski, W., Smiljanic, I., Smith, A. J. S., Smith, A., Smith, B. J., Smith, J., Smith, S., Smith, T., Snodgrass, W. N., Sobloher, B., Sohn, Y. -U, Solidum, R., Solyak, N., Son, D., Sonmez, N., Sopczak, A., Soskov, V., Spencer, C. M., Spentzouris, P., Speziali, V., Spira, M., Sprehn, D., Sridhar, K., Srivastava, A., St Lorant, S., Stahl, A., Stanek, R. P., Stanitzki, M., Stanley, J., Stefanov, K., Stein, W., Steiner, H., Stenlund, E., Stern, A., Sternberg, M., Stockinger, D., Stockton, M., Stoeck, H., Strachan, J., Strakhovenko, V., Strauss, M., Striganov, S. I., Strologas, J., Strom, D., Strube, J., Stupakov, G., Su, D., Sudo, Y., Suehara, T., Suehiro, T., Suetsugu, Y., Sugahara, R., Sugimoto, Y., Sugiyama, A., Suh, J. S., Sukovic, G., Sun, H., Sun, S., Sun, W., Sun, Y., Suszycki, L., Sutcliffe, P., Suthar, R. L., Suwada, T., Suzuki, A., Suzuki, C., Suzuki, S., Suzuki, T., Swent, R., Swientek, K., Swinson, C., Syresin, E., Szleper, M., Tadday, A., Takahashi, R., Takahashi, T., Takano, M., Takasaki, F., Takeda, S., Takenaka, T., Takeshita, T., Takubo, Y., Tanaka, M., Tang, C. X., Taniguchi, T., Tantawi, S., Tapprogge, S., Tartaglia, M. A., Tassielli, G. F., Tauchi, T., Tavian, L., Tawara, H., Taylor, G., Telnov, A. V., Telnov, V., Tenenbaum, P., Teodorescu, E., Terashima, A., Terracciano, G., Terunuma, N., Teubner, T., Teuscher, R., Theilacker, J., Thomson, M., Tice, J., Tigner, M., Timmermans, J., Titov, M., Toge, N., Tokareva, N. A., Tollefson, K., Tomasek, L., Tomovic, S., Tompkins, J., Tonutti, M., Topkar, A., Toprek, D., Toral, F., Torrence, E., Traversi, G., Trimpl, M., Tripathi, S. M., Trischuk, W., Trodden, M., Trubnikov, G. V., Tschirhart, R., Tskhadadze, E., Tsuchiya, K., Tsukamoto, T., Tsunemi, A., Tucker, R., Turchetta, R., Tyndel, M., Uekusa, N., Ueno, K., Umemori, K., Ummenhofer, M., Underwood, D., Uozumi, S., Urakawa, J., Urban, J., Uriot, D., Urner, D., Ushakov, A., Usher, T., Uzunyan, S., Vachon, B., Valerio, L., Valin, I., Valishev, A., Vamra, R., Graaf, H., Kooten, R., Zandbergen, G., Vanel, J. -C, Variola, A., Varner, G., Velasco, M., Velte, U., Velthuis, J., Vempati, S. K., Venturini, M., Vescovi, C., Videau, H., Vila, I., Vincent, P., Virey, J. -M, Visentin, B., Viti, M., Vo, T. C., Vogel, A., Vogt, H., Toerne, E., Vorozhtsov, S. B., Vos, M., Votava, M., Vrba, V., Wackeroth, D., Wagner, A., Wagner, C. E. M., Wagner, S., Wake, M., Walczak, R., Walker, N. J., Walkowiak, W., Wallon, S., Walsh, R., Walston, S., Waltenberger, W., Walz, D., Wang, C. E., Wang, C. H., Wang, D., Wang, F., Wang, G. W., Wang, H., Wang, J., Wang, J. Q., Wang, L., Wang, M. -Z, Wang, Q., Wang, S. H., Wang, X., Wang, X. -L, Wang, Y. F., Wang, Z., Wanzenberg, R., Ward, B., Ward, D., Warmbein, B., Warner, D. W., Warren, M., Washio, M., Watanabe, I., Watanabe, K., Watanabe, T., Watanabe, Y., Watson, N., Wattimena, N., Wayne, M., Weber, M., Weerts, H., Weiglein, G., Weiland, T., Weinzierl, S., Weise, H., Weisend, J., Wendt, M., Wendt, O., Wenzel, H., Wenzel, W. A., Wermes, N., Werthenbach, U., Wesseln, S., Wester, W., White, A., White, G. R., Wichmann, K., Wienemann, P., Wierba, W., Wilksen, T., Willis, W., Wilson, G. W., Wilson, J. A., Wilson, R., Wing, M., Winter, M., Wirth, B. D., Wolbers, S. A., Wolff, D., Wolski, A., Woodley, M. D., Woods, M., Woodward, M. L., Woolliscroft, T., Worm, S., Wormser, G., Wright, D., Wu, A., Wu, T., Wu, Y. L., Xella, S., Xia, G., Xia, L., Xiao, A., Xiao, L., Xie, J. L., Xing, Z. -Z, Xiong, L. Y., Xu, G., Xu, Q. J., Yajnik, U. A., Yakimenko, V., Yamada, R., Yamaguchi, H., Yamamoto, A., Yamamoto, H., Yamamoto, M., Yamamoto, N., Yamamoto, R., Yamamoto, Y., Yamanaka, T., Yamaoka, H., Yamashita, S., Yamazaki, H., Yan, W., Yang, H. -J, Yang, J. M., Yang, J., Yang, Z., Yano, Y., Yazgan, E., Yeh, G. P., Yilmaz, H., Yock, P., Yoda, H., Yoh, J., Yokoya, K., Yokoyama, H., York, R. C., Yoshida, M., Yoshida, T., Yoshioka, T., Young, A., Yu, C. H., Yu, J., Yu, X. M., Yuan, C., Yue, C. -X, Yue, J. H., Zacek, J., Zagorodnov, I., Zalesak, J., Zalikhanov, B., Zarnecki, A. F., Zawiejski, L., Zeitnitz, C., Zeller, M., Zerwas, D., Zerwas, P., Zeyrek, M., Zhai, J. Y., Zhang, B. C., Zhang, B., Zhang, C., Zhang, H., Zhang, J., Zhang, J. R., Zhang, L., Zhang, X., Zhang, Y., Zhang, Z., Zhao, H., Zhao, J. J., Zhao, J. X., Zhao, M. H., Zhao, S. C., Zhao, T., Zhao, T. X., Zhao, Z. T., Zhao, Z., Zhou, D. M., Zhou, F., Zhou, S., Zhu, S. H., Zhu, X. W., Zhukov, V., Zimmermann, F., Ziolkowski, M., Zisman, M. S., Zomer, F., Zong, Z. G., Zorba, O., and Zutshi, V.
33. Muonium to diamagnetic muon conversion in KCl and NaCl revealed by time-differential muon spin resonance
- Author
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Morozumi, Y., primary, Nishiyama, K., additional, and Nagamine, K., additional
- Published
- 1986
- Full Text
- View/download PDF
34. Observation of “decoupled” diamagnetic muon states in Alkali halides by muon spin resonance
- Author
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Nishiyama, K, primary, Morozumi, Y, additional, Suzuki, T, additional, and Nagamine, K, additional
- Published
- 1985
- Full Text
- View/download PDF
35. X-band PPM klystron development for JLC
- Author
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Chin, Y.H., primary, Matsumoto, S., additional, Mizuno, H., additional, Morozumi, Y., additional, Ohkawa, T., additional, Ohya, K., additional, Takata, K., additional, Toge, N., additional, Tokumoto, S., additional, Kazakov, S., additional, Larionov, A., additional, and Teryaev, V., additional
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- View/download PDF
36. Conformable formation of high quality ultra-thin amorphous Ta/sub 2/O/sub 5/ gate dielectrics utilizing water assisted deposition (WAD) for sub 50 nm damascene metal gate MOSFETs
- Author
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Inumiya, S., primary, Morozumi, Y., additional, Yagishita, A., additional, Saito, T., additional, Gao, D., additional, Choi, D., additional, Hasebe, K., additional, Suguro, K., additional, Tsunashima, Y., additional, and Arikado, T., additional
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37. High Gradient Performance of NLC/GLC X-Band Accelerating Structures
- Author
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Dobert, S., primary, Adolphsen, C., additional, Bowden, G., additional, Burke, D., additional, Chan, J., additional, Dolgashev, V., additional, Frisch, J., additional, Jobe, K., additional, Jones, R., additional, Lewandowski, J., additional, Kirby, R., additional, Li, Z., additional, McCormick, D., additional, Miller, R., additional, Nantista, C., additional, Nelson, J., additional, Pearson, C., additional, Ross, M., additional, Schultz, D., additional, Smith, T., additional, Tantawi, S., additional, Wang, J., additional, Arkan, T., additional, Boffo, C., additional, Carter, H., additional, Gonin, I., additional, Khabiboulline, T., additional, Mishra, S., additional, Romanov, G., additional, Solyak, N., additional, Funahashi, Y., additional, Hayano, H., additional, Higashi, N., additional, Higashi, Y., additional, Higo, T., additional, Kawamata, H., additional, Kume, T., additional, Morozumi, Y., additional, Takata, K., additional, Takatomi, T., additional, Toge, N., additional, Ueno, K., additional, and Watanabe, Y., additional
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38. Development of X-band PPM klystron for JLC project.
- Author
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Yong Ho Chin, Matsumoto, S., Morozumi, Y., Ohya, K., Takata, K., Tokumoto, S., Kanno, M., Miyake, S., and Urakata, H.
- Published
- 2002
- Full Text
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39. X-band PPM klystron development for JLC.
- Author
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Chin, Y.H., Matsumoto, S., Mizuno, H., Morozumi, Y., Ohkawa, T., Ohya, K., Takata, K., Toge, N., Tokumoto, S., Kazakov, S., Larionov, A., and Teryaev, V.
- Published
- 2001
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- View/download PDF
40. Development of the 1 GeV proton linac for the Japanese Hadron Facility.
- Author
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Yamazaki, Y., Anami, S., Arai, S., Baba, H., Kageyama, T., Kato, T., Kihara, M., Kubo, T., Mori, Y., Morozumi, Y., Naito, F., Ono, M., Takasaki, E., Tokuda, N., and Ueno, A.
- Published
- 1989
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41. Fission yeast Pib2 localizes to vacuolar membranes and regulates TOR complex 1 through evolutionarily conserved domains.
- Author
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Morozumi Y, Hayashi Y, Chu CM, Sofyantoro F, Akikusa Y, Fukuda T, and Shiozaki K
- Abstract
TOR complex 1 (TORC1) is a multi-protein kinase complex that coordinates cellular growth with environmental cues. Recent studies have identified Pib2 as a critical activator of TORC1 in budding yeast. Here, we show that loss of Pib2 causes severe growth defects in fission yeast cells, particularly when basal TORC1 activity is diminished by hypomorphic mutations in tor2, the gene encoding the catalytic subunit of TORC1. Consistently, TORC1 activity is significantly compromised in the tor2 hypomorphic mutants lacking Pib2. Moreover, as in budding yeast, fission yeast Pib2 localizes to vacuolar membranes via its FYVE domain, with its tail motif indispensable for TORC1 activation. These results strongly suggest that Pib2-mediated positive regulation of TORC1 is evolutionarily conserved between the two yeast species., (© 2024 Federation of European Biochemical Societies.)
- Published
- 2024
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42. Rapamycin-sensitive mechanisms confine the growth of fission yeast below the temperatures detrimental to cell physiology.
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Morozumi Y, Mahayot F, Nakase Y, Soong JX, Yamawaki S, Sofyantoro F, Imabata Y, Oda AH, Tamura M, Kofuji S, Akikusa Y, Shibatani A, Ohta K, and Shiozaki K
- Abstract
Cells cease to proliferate above their growth-permissible temperatures, a ubiquitous phenomenon generally attributed to heat damage to cellular macromolecules. We here report that, in the presence of rapamycin, a potent inhibitor of Target of Rapamycin Complex 1 (TORC1), the fission yeast Schizosaccharomyces pombe can proliferate at high temperatures that usually arrest its growth. Consistently, mutations to the TORC1 subunit RAPTOR/Mip1 and the TORC1 substrate Sck1 significantly improve cellular heat resistance, suggesting that TORC1 restricts fission yeast growth at high temperatures. Aiming for a more comprehensive understanding of the negative regulation of high-temperature growth, we conducted genome-wide screens, which identified additional factors that suppress cell proliferation at high temperatures. Among them is Mks1, which is phosphorylated in a TORC1-dependent manner, forms a complex with the 14-3-3 protein Rad24, and suppresses the high-temperature growth independently of Sck1. Our study has uncovered unexpected mechanisms of growth restraint even below the temperatures deleterious to cell physiology., Competing Interests: The authors declare no competing interests., (© 2023 The Author(s).)
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- 2023
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43. Role of trisaccharides in larval secretion of Lycaeides argyrognomon butterfly on ant attendance.
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Mizuta H, Morozumi Y, Watanabe M, Ohta S, and Ômura H
- Abstract
Several myrmecophilous insects participate in symbiotic relationships with ants that receive sugar-rich food rewards. For instance, certain aphid species secrete honeydew containing high concentration of melezitose, which acts as a potent feeding-stimulant and attractant for ants. Lycaenid butterfly larvae possess dorsal nectary glands that secrete sugar-rich droplets for tending ants. However, the roles of sugar components in ant foraging and larva-tending activities are unknown. Lycaeides (Plebejus) argyrognomon are larvae that are frequently and facultatively attended by various ant species, including Formica japonica, on the host plant Indigofera pseudotinctoria. The larval secretions of this insect contained small amounts of trisaccharides, melezitose and maltotriose, which were not detected in the host plant's flower nectar, and larval secretions of two sympatric and myrmecophilous lycaenids, Zizeeria maha and Everes argiades. Melezitose and maltotriose, along with sucrose, were preferred by the worker ants. Of the four sugar mixture samples that mimicked I. pseudotinctoria floral nectar and the larval secretions of three lycaenids, respectively, the L. argyrognomon mimic was the most preferred by F. japonica ants. Moreover, the removal of trisaccharides from this mimic significantly reduced its stimulatory activity to ant feedings. These results indicated that the sugar composition of L. argyrognomon larval secretions is suited to the feeding preference of F. japonica ants, and that the trisaccharide components play a key role in increasing their preference. However, only half of the ants responded to the L. argyrognomon mimic even at the concentration corresponding to the maximum total sugar concentration in the collected larval secretions. The fact that the secretions of all L. argyrognomon larvae did not have sufficient sugar levels to stimulate ant feedings suggests that the production of sugar-rich secretions and trisaccharide components is metabolically costly for the larvae and that components other than sugars may be involved in ant attendance., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)
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- 2023
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44. Fission Yeast TORC1 Promotes Cell Proliferation through Sfp1, a Transcription Factor Involved in Ribosome Biogenesis.
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Tai YT, Fukuda T, Morozumi Y, Hirai H, Oda AH, Kamada Y, Akikusa Y, Kanki T, Ohta K, and Shiozaki K
- Subjects
- Transcription Factors genetics, Transcription Factors metabolism, Saccharomyces cerevisiae metabolism, Mechanistic Target of Rapamycin Complex 1 metabolism, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Ribosomes metabolism, Cell Proliferation, Gene Expression Regulation, Fungal, Saccharomyces cerevisiae Proteins genetics, Saccharomyces cerevisiae Proteins metabolism, Schizosaccharomyces genetics, Schizosaccharomyces metabolism
- Abstract
Target of rapamycin complex 1 (TORC1) is activated in response to nutrient availability and growth factors, promoting cellular anabolism and proliferation. To explore the mechanism of TORC1-mediated proliferation control, we performed a genetic screen in fission yeast and identified Sfp1, a zinc-finger transcription factor, as a multicopy suppressor of temperature-sensitive TORC1 mutants. Our observations suggest that TORC1 phosphorylates Sfp1 and protects Sfp1 from proteasomal degradation. Transcription analysis revealed that Sfp1 positively regulates genes involved in ribosome production together with two additional transcription factors, Ifh1/Crf1 and Fhl1. Ifh1 physically interacts with Fhl1, and the nuclear localization of Ifh1 is regulated in response to nutrient levels in a manner dependent on TORC1 and Sfp1. Taken together, our data suggest that the transcriptional regulation of the genes involved in ribosome biosynthesis by Sfp1, Ifh1, and Fhl1 is one of the key pathways through which nutrient-activated TORC1 promotes cell proliferation.
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- 2023
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45. Spectrophotometric microplate assay for titration and neutralization of avian nephritis virus based on the virus cytopathicity.
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Kodama T, Ueno K, Kondo T, Morozumi Y, Kato A, Nagai S, Shibuya K, and Sasakawa C
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- Animals, Antibodies, Viral, Chickens, Neutralization Tests methods, Reproducibility of Results, Avastrovirus
- Abstract
Introduction: Plaque assay (PA) is a gold standard for virus titration and neutralization of various cytopathic viruses, including avian nephritis virus (ANV), the etiological agent associated with kidney disorders in chickens. In this study, as an alternative to the labor-intensive PA, we developed a spectrophotometric microplate assay (MA) for ANV titration and neutralization based on the virus cytopathicity to primary chicken kidney (CK) cells., Methods: CK cells were infected with ANV in the presence or absence of chicken serum in a 96-well microplate, and the virus-induced cytolysis was quantified by measurement of neutral red uptake using a spectrophotometer. The absorbance values obtained were subjected to a sigmoidal four-parameter logistic regression analysis for the virus titer determination and serum neutralization assessment. Accuracy and reliability of the serum neutralization MA in comparison to the standard PA was statistically evaluated., Results: The ANV-MA was capable of quantifying infectious virus titers based on a virus dose-dependent cytolysis of CK cells, and serum neutralization could be assessed as an inhibition of the virus-induced cytolysis accordingly. Statistical evaluation using a 2 × 2 contingency table and receiver-operating characteristic analyses showed 82 % sensitivity, 99 % specificity and 0.97 area under the curve, supporting an overall diagnostic accuracy of the neutralization MA., Conclusion: The newly developed MA using simplified experimental procedures in the microplate format and direct spectophotometric data readout is readily applicable to general laboratories for high-throughput screening of serum neutralization of ANV., (Copyright © 2021 Elsevier B.V. All rights reserved.)
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- 2022
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46. Fission yeast TOR complex 1 phosphorylates Psk1 through an evolutionarily conserved interaction mediated by the TOS motif.
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Morozumi Y, Hishinuma A, Furusawa S, Sofyantoro F, Tatebe H, and Shiozaki K
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- Animals, Mechanistic Target of Rapamycin Complex 1 genetics, Mechanistic Target of Rapamycin Complex 1 metabolism, Phosphorylation, Regulatory-Associated Protein of mTOR, Schizosaccharomyces genetics, Schizosaccharomyces metabolism, Schizosaccharomyces pombe Proteins genetics, Schizosaccharomyces pombe Proteins metabolism
- Abstract
TOR complex 1 (TORC1) is a multi-subunit protein kinase complex that controls cellular growth in response to environmental cues. The regulatory subunits of mammalian TORC1 (mTORC1) include RAPTOR (also known as RPTOR), which recruits mTORC1 substrates, such as S6K1 (also known as RPS6KB1) and 4EBP1 (EIF4EBP1), by interacting with their TOR signaling (TOS) motif. Despite the evolutionary conservation of TORC1, no TOS motif has been described in lower eukaryotes. In the present study, we show that the fission yeast S6 kinase Psk1 contains a TOS motif that interacts with Mip1, a RAPTOR ortholog. The TOS motif in Psk1 resembles those in mammals, including the conserved phenylalanine and aspartic acid residues essential for the Mip1 interaction and TORC1-dependent phosphorylation of Psk1. The binding of the TOS motif to Mip1 is dependent on Mip1 Tyr-533, whose equivalent in RAPTOR is known to interact with the TOS motif in their co-crystals. Furthermore, we utilized the mip1-Y533A mutation to screen the known TORC1 substrates in fission yeast and successfully identified Atg13 as a novel TOS-motif-containing substrate. These results strongly suggest that the TOS motif represents an evolutionarily conserved mechanism of the substrate recognition by TORC1., Competing Interests: Competing interests The authors declare no competing or financial interests., (© 2021. Published by The Company of Biologists Ltd.)
- Published
- 2021
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47. ATAD2 controls chromatin-bound HIRA turnover.
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Wang T, Perazza D, Boussouar F, Cattaneo M, Bougdour A, Chuffart F, Barral S, Vargas A, Liakopoulou A, Puthier D, Bargier L, Morozumi Y, Jamshidikia M, Garcia-Saez I, Petosa C, Rousseaux S, Verdel A, and Khochbin S
- Subjects
- ATPases Associated with Diverse Cellular Activities genetics, Animals, Cell Proliferation genetics, DNA-Binding Proteins genetics, Gene Deletion, Gene Knockout Techniques, Genotype, HeLa Cells, Hep G2 Cells, Humans, Mice, Microorganisms, Genetically-Modified, Schizosaccharomyces genetics, Schizosaccharomyces pombe Proteins genetics, Transfection, ATPases Associated with Diverse Cellular Activities metabolism, Cell Cycle Proteins metabolism, DNA-Binding Proteins metabolism, Histone Chaperones metabolism, Mouse Embryonic Stem Cells metabolism, Nucleosomes metabolism, Schizosaccharomyces metabolism, Schizosaccharomyces pombe Proteins metabolism, Signal Transduction genetics, Transcription Factors metabolism
- Abstract
Taking advantage of the evolutionary conserved nature of ATAD2, we report here a series of parallel functional studies in human, mouse, and Schizosaccharomyces pombe to investigate ATAD2's conserved functions. In S. pombe , the deletion of ATAD2 ortholog, abo1 , leads to a dramatic decrease in cell growth, with the appearance of suppressor clones recovering normal growth. The identification of the corresponding suppressor mutations revealed a strong genetic interaction between Abo1 and the histone chaperone HIRA. In human cancer cell lines and in mouse embryonic stem cells, we observed that the KO of ATAD2 leads to an accumulation of HIRA. A ChIP-seq mapping of nucleosome-bound HIRA and FACT in Atad2 KO mouse ES cells demonstrated that both chaperones are trapped on nucleosomes at the transcription start sites of active genes, resulting in the abnormal presence of a chaperone-bound nucleosome on the TSS-associated nucleosome-free regions. Overall, these data highlight an important layer of regulation of chromatin dynamics ensuring the turnover of histone-bound chaperones., (© 2021 Wang et al.)
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- 2021
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48. Tripartite suppression of fission yeast TORC1 signaling by the GATOR1-Sea3 complex, the TSC complex, and Gcn2 kinase.
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Fukuda T, Sofyantoro F, Tai YT, Chia KH, Matsuda T, Murase T, Morozumi Y, Tatebe H, Kanki T, and Shiozaki K
- Subjects
- Mechanistic Target of Rapamycin Complex 1 metabolism, Schizosaccharomyces metabolism, Schizosaccharomyces pombe Proteins metabolism, Mechanistic Target of Rapamycin Complex 1 genetics, Schizosaccharomyces genetics, Schizosaccharomyces pombe Proteins genetics, Signal Transduction
- Abstract
Mammalian target of rapamycin complex 1 (TORC1) is controlled by the GATOR complex composed of the GATOR1 subcomplex and its inhibitor, the GATOR2 subcomplex, sensitive to amino acid starvation. Previously, we identified fission yeast GATOR1 that prevents deregulated activation of TORC1 (Chia et al., 2017). Here, we report identification and characterization of GATOR2 in fission yeast. Unexpectedly, the GATOR2 subunit Sea3, an ortholog of mammalian WDR59, is physically and functionally proximal to GATOR1, rather than GATOR2, attenuating TORC1 activity. The fission yeast GATOR complex is dispensable for TORC1 regulation in response to amino acid starvation, which instead activates the Gcn2 pathway to inhibit TORC1 and induce autophagy. On the other hand, nitrogen starvation suppresses TORC1 through the combined actions of the GATOR1-Sea3 complex, the Gcn2 pathway, and the TSC complex, another conserved TORC1 inhibitor. Thus, multiple, parallel signaling pathways implement negative regulation of TORC1 to ensure proper cellular starvation responses., Competing Interests: TF, FS, YT, KC, TM, TM, YM, HT, TK, KS No competing interests declared, (© 2021, Fukuda et al.)
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- 2021
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49. Conserved and Divergent Mechanisms That Control TORC1 in Yeasts and Mammals.
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Morozumi Y and Shiozaki K
- Subjects
- Animals, Humans, Lysosomes genetics, Mechanistic Target of Rapamycin Complex 1 genetics, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, Transcription Factors genetics, Vacuoles genetics, Intracellular Membranes metabolism, Lysosomes metabolism, Mechanistic Target of Rapamycin Complex 1 metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins metabolism, Transcription Factors metabolism, Vacuoles metabolism
- Abstract
Target of rapamycin complex 1 (TORC1), a serine/threonine-protein kinase complex highly conserved among eukaryotes, coordinates cellular growth and metabolism with environmental cues, including nutrients and growth factors. Aberrant TORC1 signaling is associated with cancers and various human diseases, and TORC1 also plays a key role in ageing and lifespan, urging current active research on the mechanisms of TORC1 regulation in a variety of model organisms. Identification and characterization of the RAG small GTPases as well as their regulators, many of which are highly conserved from yeast to humans, led to a series of breakthroughs in understanding the molecular bases of TORC1 regulation. Recruitment of mammalian TORC1 (mTORC1) by RAGs to lysosomal membranes is a key step for mTORC1 activation. Interestingly, the RAG GTPases in fission yeast are primarily responsible for attenuation of TORC1 activity on vacuoles, the yeast equivalent of lysosomes. In this review, we summarize our current knowledge about the functions of TORC1 regulators on yeast vacuoles, and illustrate the conserved and divergent mechanisms of TORC1 regulation between yeasts and mammals.
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- 2021
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50. Non-invasive intravital observation of lingual surface features using sliding oral mucoscopy techniques in clinically healthy subjects.
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Tsuchida S, Yoshimura K, Nakamura N, Asanuma N, Iwasaki SI, Miyagawa Y, Yamagiwa S, Ebihara T, Morozumi Y, Asami T, and Kosuge N
- Subjects
- Adult, Female, Healthy Volunteers, Humans, Microscopy, Electron, Scanning, Mouth Mucosa, Tongue, Young Adult, Taste Buds
- Abstract
To investigate intravital morphological features of the broader area of the lingual mucosa in clinically healthy subjects, and to attempt to evaluate subclinical conditions, we evaluated detailed intravital morphological features of the lingual mucosa using our newly developed oral contact mucoscopy techniques. Clinically healthy subjects (female: 19-22 years, average age: 20.27 years, and n = 28) were enrolled. A position indicator stain was placed on the lingual mucosal surface, and sliding images were captured and then reconstructed. In addition, the lingual mucosa was divided into six areas, and morphometry of the fungiform and filiform papillae was performed. The results were statistically analyzed. There were two morphological features among clinically healthy subjects involving the filiform papillae: the length of the papillae and the degree of biofilm (tongue coat) deposition. We defined a modified tongue coat index (mTCI) with scores ranging from 0 (tongue coating not visible) to 0.5, 1, 1.5, and 2 (thick tongue coating) for six sections of the tongue dorsum. No subjects received a score of 2. Significant differences were found in the mTCI between the six sections of the tongue dorsum, especially between the posterior areas and the lingual apex. The fungiform papillae of some subjects exhibited elongated morphological changes. Our findings suggest that magnified lingual dorsum examination of a broader area is especially important in accurate screening for subclinical or transient conditions of potential lingual mucosal diseases. For this purpose, our new oral mucoscopy and non-invasive intravital observational techniques were especially effective.
- Published
- 2020
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