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  1. Article: Novel functions of TIMPs in cell signaling.

    Chirco, Rosemarie / Liu, Xu-Wen / Jung, Ki-Kyung / Kim, Hyeong-Reh Choi

    Cancer metastasis reviews

    2006  Volume 25, Issue 1, Page(s) 99–113

    Abstract: Tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors of matrix metalloproteinases (MMPs) and the balance between MMPs/TIMPs regulates the extracellular matrix (ECM) turnover and remodeling during normal development and pathogenesis. ... ...

    Abstract Tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors of matrix metalloproteinases (MMPs) and the balance between MMPs/TIMPs regulates the extracellular matrix (ECM) turnover and remodeling during normal development and pathogenesis. Increasing evidence indicates a much more complex role for TIMPs during tumor progression and angiogenesis, in addition to their regulation of MMP-mediated ECM degradation. In this article, we review both the MMP-dependent and -independent actions of TIMPs for the regulation of cell death, cell proliferation, and angiogenesis, with a particular emphasis on TIMP-1 in the regulation of tetraspanin/integrin-mediated cell survival signal transduction pathways.
    MeSH term(s) Animals ; Antigens, CD/metabolism ; Apoptosis ; Cell Proliferation ; Cell Survival ; Disease Progression ; Humans ; Integrin beta1/metabolism ; Matrix Metalloproteinase Inhibitors ; Mice ; Models, Biological ; Neoplasms/enzymology ; Neoplasms/pathology ; Neovascularization, Pathologic/metabolism ; Platelet Membrane Glycoproteins/metabolism ; Prognosis ; Signal Transduction ; Tetraspanin 30 ; Tissue Inhibitor of Metalloproteinase-1/physiology ; Tissue Inhibitor of Metalloproteinases/physiology
    Chemical Substances Antigens, CD ; CD63 protein, human ; Cd63 protein, mouse ; Integrin beta1 ; Matrix Metalloproteinase Inhibitors ; Platelet Membrane Glycoproteins ; Tetraspanin 30 ; Tissue Inhibitor of Metalloproteinase-1 ; Tissue Inhibitor of Metalloproteinases
    Language English
    Publishing date 2006-03
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 604857-2
    ISSN 1573-7233 ; 0167-7659
    ISSN (online) 1573-7233
    ISSN 0167-7659
    DOI 10.1007/s10555-006-7893-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: TIMP-1 induces an EMT-like phenotypic conversion in MDCK cells independent of its MMP-inhibitory domain.

    Jung, Young Suk / Liu, Xu-Wen / Chirco, Rosemarie / Warner, Richard B / Fridman, Rafael / Kim, Hyeong-Reh Choi

    PloS one

    2012  Volume 7, Issue 6, Page(s) e38773

    Abstract: Matrix metalloproteinases (MMPs) and their endogenous inhibitors (TIMPs) regulate epithelial-mesenchymal transition (EMT) critical for the development of epithelial organs as well as cancer cell invasion. TIMP-1 is frequently overexpressed in several ... ...

    Abstract Matrix metalloproteinases (MMPs) and their endogenous inhibitors (TIMPs) regulate epithelial-mesenchymal transition (EMT) critical for the development of epithelial organs as well as cancer cell invasion. TIMP-1 is frequently overexpressed in several types of human cancers and serves as a prognostic marker. The present study investigates the roles of TIMP-1 on the EMT process and formation of the lumen-like structure in a 3D Matrigel culture of MDCK cells. We show that TIMP-1 overexpression effectively prevents cell polarization and acinar-like structure formation. TIMP-1 induces expression of the developmental EMT transcription factors such as SLUG, TWIST, ZEB1 and ZEB2, leading to downregulation of epithelial marker and upregulation of mesenchymal markers. Importantly, TIMP-1's ability to induce the EMT-like process is independent of its MMP-inhibitory domain. To our surprise, TIMP-1 induces migratory and invasive properties in MDCK cells. Here, we present a novel finding that TIMP-1 signaling upregulates MT1-MMP and MMP-2 expression, and potentiates MT1-MMP activation of pro-MMP-2, contributing to tumor cell invasion. In spite of the fact that TIMP-1, as opposed to TIMP-2, does not interact with and inhibit MT1-MMP, TIMP-1 may act as a key regulator of MT1-MMP/MMP-2 axis. Collectively, our findings suggest a model in which TIMP-1 functions as a signaling molecule and also as an endogenous inhibitor of MMPs. This concept represents a paradigm shift in the current view of TIMP-1/MT1-MMP interactions and functions during cancer development/progression.
    MeSH term(s) Animals ; Cell Line ; Cell Movement/physiology ; Cell Polarity/physiology ; Cell Proliferation ; DNA Primers/genetics ; Dogs ; Epithelial-Mesenchymal Transition/physiology ; Flow Cytometry ; Gene Expression Regulation/physiology ; Gene Knockdown Techniques ; Immunoblotting ; Matrix Metalloproteinase 14/metabolism ; Matrix Metalloproteinase 2/metabolism ; Phenotype ; Reverse Transcriptase Polymerase Chain Reaction ; Tetrazolium Salts ; Thiazoles ; Tissue Inhibitor of Metalloproteinase-1/metabolism ; Transcription Factors/metabolism
    Chemical Substances DNA Primers ; Tetrazolium Salts ; Thiazoles ; Tissue Inhibitor of Metalloproteinase-1 ; Transcription Factors ; Matrix Metalloproteinase 2 (EC 3.4.24.24) ; Matrix Metalloproteinase 14 (EC 3.4.24.80) ; thiazolyl blue (EUY85H477I)
    Language English
    Publishing date 2012-06-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0038773
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein.

    Jung, Ki-Kyung / Liu, Xu-Wen / Chirco, Rosemarie / Fridman, Rafael / Kim, Hyeong-Reh Choi

    The EMBO journal

    2006  Volume 25, Issue 17, Page(s) 3934–3942

    Abstract: This study identified CD63, a member of the tetraspanin family, as a TIMP-1 interacting protein by yeast two-hybrid screening. Immunoprecipitation and confocal microscopic analysis confirmed CD63 interactions with TIMP-1, integrin beta1, and their co- ... ...

    Abstract This study identified CD63, a member of the tetraspanin family, as a TIMP-1 interacting protein by yeast two-hybrid screening. Immunoprecipitation and confocal microscopic analysis confirmed CD63 interactions with TIMP-1, integrin beta1, and their co-localizations on the cell surface of human breast epithelial MCF10A cells. TIMP-1 expression correlated with the level of active integrin beta1 on the cell surface independent of cell adhesion. While MCF10A cells within a three-dimensional (3D) matrigel matrix form polarized acinar-like structures, TIMP-1 overexpression disrupted breast epithelial cell polarization and inhibited caspase-mediated apoptosis in centrally located cells, necessary for the formation and maintenance of the hollow acinar-like structures. Small hairpin RNA (shRNA)-mediated CD63 downregulation effectively reduced TIMP-1 binding to the cell surface, TIMP-1 co-localization with integrin beta1, and consequently reversed TIMP-1-mediated integrin beta1 activation, cell survival signaling and apoptosis inhibition. CD63 downregulation also restored polarization and apoptosis of TIMP-1 overexpressing MCF10A cells within a 3D-matrigel matrix. Taken together, the present study identified CD63 as a cell surface binding partner for TIMP-1, regulating cell survival and polarization via TIMP-1 modulation of tetraspanin/integrin signaling complex.
    MeSH term(s) Antigens, CD/metabolism ; Antigens, CD/physiology ; Apoptosis ; Cell Adhesion ; Cell Line ; Cell Membrane/metabolism ; Cell Polarity ; Cell Survival ; Down-Regulation ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Gene Library ; Humans ; Integrin beta1/metabolism ; Mammary Glands, Human/cytology ; Membrane Proteins/metabolism ; Platelet Membrane Glycoproteins/metabolism ; Platelet Membrane Glycoproteins/physiology ; Protein Binding ; Signal Transduction ; Tetraspanin 30 ; Tissue Inhibitor of Metalloproteinase-1/metabolism ; Two-Hybrid System Techniques
    Chemical Substances Antigens, CD ; CD63 protein, human ; Integrin beta1 ; Membrane Proteins ; Platelet Membrane Glycoproteins ; Tetraspanin 30 ; Tissue Inhibitor of Metalloproteinase-1
    Language English
    Publishing date 2006-09-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/sj.emboj.7601281
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Measurement of the ν_{e}-Nucleus Charged-Current Double-Differential Cross Section at ⟨E_{ν}⟩=2.4  GeV Using NOvA.

    Acero, M A / Adamson, P / Aliaga, L / Anfimov, N / Antoshkin, A / Arrieta-Diaz, E / Asquith, L / Aurisano, A / Back, A / Baird, M / Balashov, N / Baldi, P / Bambah, B A / Bashar, S / Bays, K / Bernstein, R / Bhatnagar, V / Bhattarai, D / Bhuyan, B /
    Bian, J / Booth, A C / Bowles, R / Brahma, B / Bromberg, C / Buchanan, N / Butkevich, A / Calvez, S / Carroll, T J / Catano-Mur, E / Childress, S / Chatla, A / Chirco, R / Choudhary, B C / Christensen, A / Coan, T E / Colo, M / Cremonesi, L / Davies, G S / Derwent, P F / Ding, P / Djurcic, Z / Dolce, M / Doyle, D / Dueñas Tonguino, D / Dukes, E C / Ehrlich, R / Elkins, M / Ewart, E / Feldman, G J / Filip, P / Franc, J / Frank, M J / Gallagher, H R / Gandrajula, R / Gao, F / Giri, A / Gomes, R A / Goodman, M C / Grichine, V / Groh, M / Group, R / Guo, B / Habig, A / Hakl, F / Hall, A / Hartnell, J / Hatcher, R / Hausner, H / He, M / Heller, K / Hewes, V / Himmel, A / Jargowsky, B / Jarosz, J / Jediny, F / Johnson, C / Judah, M / Kakorin, I / Kaplan, D M / Kalitkina, A / Keloth, R / Klimov, O / Koerner, L W / Kolupaeva, L / Kotelnikov, S / Kralik, R / Kullenberg, Ch / Kubu, M / Kumar, A / Kuruppu, C D / Kus, V / Lackey, T / Lang, K / Lasorak, P / Lesmeister, J / Lin, S / Lister, A / Liu, J / Lokajicek, M / Lopez, J M C / Mahji, R / Magill, S / Manrique Plata, M / Mann, W A / Manoharan, M T / Marshak, M L / Martinez-Casales, M / Matveev, V / Mayes, B / Messier, M D / Meyer, H / Miao, T / Mikola, V / Miller, W H / Mishra, S / Mishra, S R / Mislivec, A / Mohanta, R / Moren, A / Morozova, A / Mu, W / Mualem, L / Muether, M / Mulder, K / Naples, D / Nath, A / Nayak, N / Nelleri, S / Nelson, J K / Nichol, R / Niner, E / Norman, A / Norrick, A / Nosek, T / Oh, H / Olshevskiy, A / Olson, T / Ott, J / Pal, A / Paley, J / Panda, L / Patterson, R B / Pawloski, G / Petrova, O / Petti, R / Phan, D D / Plunkett, R K / Pobedimov, A / Porter, J C C / Rafique, A / Prais, L R / Raj, V / Rajaoalisoa, M / Ramson, B / Rebel, B / Rojas, P / Roy, P / Ryabov, V / Samoylov, O / Sanchez, M C / Sánchez Falero, S / Shanahan, P / Shukla, S / Sheshukov, A / Singh, I / Singh, P / Singh, V / Smith, E / Smolik, J / Snopok, P / Solomey, N / Sousa, A / Soustruznik, K / Strait, M / Suter, L / Sutton, A / Swain, S / Sweeney, C / Sztuc, A / Talaga, R L / Tapia Oregui, B / Tas, P / Temizel, B N / Thakore, T / Thayyullathil, R B / Thomas, J / Tiras, E / Tripathi, J / Trokan-Tenorio, J / Torun, Y / Urheim, J / Vahle, P / Vallari, Z / Vasel, J / Vrba, T / Wallbank, M / Warburton, T K / Wetstein, M / Whittington, D / Wickremasinghe, D A / Wieber, T / Wolcott, J / Wu, W / Xiao, Y / Yaeggy, B / Yallappa Dombara, A / Yankelevich, A / Yonehara, K / Yu, S / Yu, Y / Zadorozhnyy, S / Zalesak, J / Zhang, Y / Zwaska, R

    Physical review letters

    2023  Volume 130, Issue 5, Page(s) 51802

    Abstract: The inclusive electron neutrino charged-current cross section is measured in the NOvA near detector using 8.02×10^{20} protons-on-target in the NuMI beam. The sample of GeV electron neutrino interactions is the largest analyzed to date and is limited by ≃ ...

    Abstract The inclusive electron neutrino charged-current cross section is measured in the NOvA near detector using 8.02×10^{20} protons-on-target in the NuMI beam. The sample of GeV electron neutrino interactions is the largest analyzed to date and is limited by ≃17% systematic rather than the ≃7.4% statistical uncertainties. The double-differential cross section in final-state electron energy and angle is presented for the first time, together with the single-differential dependence on Q^{2} (squared four-momentum transfer) and energy, in the range 1  GeV≤E_{ν}<6  GeV. Detailed comparisons are made to the predictions of the GENIE, GiBUU, NEUT, and NuWro neutrino event generators. The data do not strongly favor a model over the others consistently across all three cross sections measured, though some models have especially good or poor agreement in the single differential cross section vs Q^{2}.
    Language English
    Publishing date 2023-02-17
    Publishing country United States
    Document type Journal Article
    ZDB-ID 208853-8
    ISSN 1079-7114 ; 0031-9007
    ISSN (online) 1079-7114
    ISSN 0031-9007
    DOI 10.1103/PhysRevLett.130.051802
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  5. Article: Synthesis, biochemical, and cellular evaluation of farnesyl monophosphate prodrugs as farnesyltransferase inhibitors.

    Clark, Michelle K / Scott, Sarah A / Wojtkowiak, Jonathan / Chirco, Rosemarie / Mathieu, Patricia / Reiners, John J / Mattingly, Raymond R / Borch, Richard F / Gibbs, Richard A

    Journal of medicinal chemistry

    2007  Volume 50, Issue 14, Page(s) 3274–3282

    Abstract: Certain farnesyl diphosphate (FPP) analogs are potent inhibitors of the potential anticancer drug target protein farnesyltransferase (FTase), but these compounds are not suitable as drug candidates. Thus, phosphoramidate prodrug derivatives of the ... ...

    Abstract Certain farnesyl diphosphate (FPP) analogs are potent inhibitors of the potential anticancer drug target protein farnesyltransferase (FTase), but these compounds are not suitable as drug candidates. Thus, phosphoramidate prodrug derivatives of the monophosphate precursors of FPP-based FTase inhibitors have been synthesized. The monophosphates themselves were significantly more potent inhibitors of FTase than the corresponding FPP analogs. The effects of the prodrug 5b (a derivative of 3-allylfarnesyl monophosphate) have been evaluated on prenylation of RhoB and on the cell cycle in a human malignant schwannoma cell line (STS-26T). In combination treatments, 1-3 microM 5b plus 1 microM lovastatin induced a significant inhibition of RhoB prenylation, and a combination of these drugs at 1 microM each also resulted in significant cell cycle arrest in G1. Indeed, combinations as low as 50 nM lovastatin + 1 microM 5c or 250 nM lovastatin + 50 nM 5c were highly cytostatic in STS-26T cell culture.
    MeSH term(s) Cell Line ; Cell Proliferation/drug effects ; Chromatography, High Pressure Liquid ; Enzyme Inhibitors/chemical synthesis ; Enzyme Inhibitors/pharmacology ; Farnesyltranstransferase/antagonists & inhibitors ; Magnetic Resonance Spectroscopy ; Polyisoprenyl Phosphates/chemical synthesis ; Polyisoprenyl Phosphates/pharmacology ; Prodrugs/chemical synthesis ; Prodrugs/pharmacology ; Spectrometry, Mass, Electrospray Ionization
    Chemical Substances Enzyme Inhibitors ; Polyisoprenyl Phosphates ; Prodrugs ; farnesyl monophosphate (15416-91-8) ; Farnesyltranstransferase (EC 2.5.1.29)
    Language English
    Publishing date 2007-07-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/jm0701829
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Scintillation light detection in the 6-m drift-length ProtoDUNE Dual Phase liquid argon TPC.

    Abud, A Abed / Abi, B / Acciarri, R / Acero, M A / Adames, M R / Adamov, G / Adamowski, M / Adams, D / Adinolfi, M / Aduszkiewicz, A / Aguilar, J / Ahmad, Z / Ahmed, J / Aimard, B / Ali-Mohammadzadeh, B / Alion, T / Allison, K / Monsalve, S Alonso / AlRashed, M /
    Alt, C / Alton, A / Alvarez, R / Amedo, P / Anderson, J / Andreopoulos, C / Andreotti, M / Andrews, M / Andrianala, F / Andringa, S / Anfimov, N / Ankowski, A / Antoniassi, M / Antonova, M / Antoshkin, A / Antusch, S / Aranda-Fernandez, A / Arellano, L / Arnold, L O / Arroyave, M A / Asaadi, J / Asquith, L / Aurisano, A / Aushev, V / Autiero, D / Lara, V Ayala / Ayala-Torres, M / Azfar, F / Back, A / Back, H / Back, J J / Backhouse, C / Bagaturia, I / Bagby, L / Balashov, N / Balasubramanian, S / Baldi, P / Baller, B / Bambah, B / Barao, F / Barenboim, G / Alzas, P Barham / Barker, G / Barkhouse, W / Barnes, C / Barr, G / Monarca, J Barranco / Barros, A / Barros, N / Barrow, J L / Basharina-Freshville, A / Bashyal, A / Basque, V / Batchelor, C / Chagas, E Batista das / Battat, J B R / Battisti, F / Bay, F / Bazetto, M C Q / Alba, J L L Bazo / Beacom, J F / Bechetoille, E / Behera, B / Beigbeder, C / Bellantoni, L / Bellettini, G / Bellini, V / Beltramello, O / Benekos, N / Montiel, C Benitez / Neves, F Bento / Berger, J / Berkman, S / Bernardini, P / Berner, R M / Bersani, A / Bertolucci, S / Betancourt, M / Rodríguez, A Betancur / Bevan, A / Bezawada, Y / Bezerra, T J C / Bhardwaj, A / Bhatnagar, V / Bhattacharjee, M / Bhattarai, D / Bhuller, S / Bhuyan, B / Biagi, S / Bian, J / Biassoni, M / Biery, K / Bilki, B / Bishai, M / Bitadze, A / Blake, A / Blaszczyk, F / Blazey, G C / Blucher, E / Boissevain, J / Bolognesi, S / Bolton, T / Bomben, L / Bonesini, M / Bongrand, M / Bonilla-Diaz, C / Bonini, F / Booth, A / Boran, F / Bordoni, S / Borkum, A / Bostan, N / Bour, P / Bourgeois, C / Boyden, D / Bracinik, J / Braga, D / Brailsford, D / Branca, A / Brandt, A / Bremer, J / Breton, D / Brew, C / Brice, S J / Brizzolari, C / Bromberg, C / Brooke, J / Bross, A / Brunetti, G / Brunetti, M / Buchanan, N / Budd, H / Butorov, I / Cagnoli, I / Cai, T / Caiulo, D / Calabrese, R / Calafiura, P / Calcutt, J / Calin, M / Calvez, S / Calvo, E / Caminata, A / Campanelli, M / Caratelli, D / Carber, D / Carceller, J C / Carini, G / Carlus, B / Carneiro, M F / Carniti, P / Terrazas, I Caro / Carranza, H / Carroll, T / Forero, J F Castaño / Castillo, A / Castromonte, C / Catano-Mur, E / Cattadori, C / Cavalier, F / Cavallaro, G / Cavanna, F / Centro, S / Cerati, G / Cervelli, A / Villanueva, A Cervera / Chalifour, M / Chappell, A / Chardonnet, E / Charitonidis, N / Chatterjee, A / Chattopadhyay, S / Neyra, M S S Chavarry / Chen, H / Chen, M / Chen, Y / Chen, Z / Chen-Wishart, Z / Cheon, Y / Cherdack, D / Chi, C / Childress, S / Chirco, R / Chiriacescu, A / Chisnall, G / Cho, K / Choate, S / Chokheli, D / Chong, P S / Christensen, A / Christian, D / Christodoulou, G / Chukanov, A / Chung, M / Church, E / Cicero, V / Clarke, P / Cline, G / Coan, T E / Cocco, A G / Coelho, J A B / Colton, N / Conley, E / Conley, R / Conrad, J / Convery, M / Copello, S / Cova, P / Cremaldi, L / Cremonesi, L / Crespo-Anadón, J I / Crisler, M / Cristaldo, E / Crnkovic, J / Cross, R / Cudd, A / Cuesta, C / Cui, Y / Cussans, D / Dalager, O / da Motta, H / Da Silva Peres, L / David, C / David, Q / Davies, G S / Davini, S / Dawson, J / De, K / De, S / Debbins, P / De Bonis, I / Decowski, M P / De Gouvêa, A / De Holanda, P C / De Icaza Astiz, I L / Deisting, A / De Jong, P / Delbart, A / Delepine, D / Delgado, M / Dell'Acqua, A / Delmonte, N / De Lurgio, P / de Mello Neto, J R T / DeMuth, D M / Dennis, S / Densham, C / Deptuch, G W / De Roeck, A / De Romeri, V / De Souza, G / Devi, R / Dharmapalan, R / Dias, M / Diaz, F / Díaz, J S / Domizio, S Di / Giulio, L Di / Ding, P / Noto, L Di / Dirkx, G / Distefano, C / Diurba, R / Diwan, M / Djurcic, Z / Doering, D / Dolan, S / Dolek, F / Dolinski, M / Domine, L / Donon, Y / Douglas, D / Douillet, D / Dragone, A / Drake, G / Drielsma, F / Duarte, L / Duchesneau, D / Duffy, K / Dunne, P / Dutta, B / Duyang, H / Dvornikov, O / Dwyer, D / Dyshkant, A / Eads, M / Earle, A / Edmunds, D / Eisch, J / Emberger, L / Emery, S / Englezos, P / Ereditato, A / Erjavec, T / Escobar, C / Eurin, G / Evans, J J / Ewart, E / Ezeribe, A C / Fahey, K / Falcone, A / Fani', M / Farnese, C / Farzan, Y / Fedoseev, D / Felix, J / Feng, Y / Fernandez-Martinez, E / Menendez, P Fernandez / Morales, M Fernandez / Ferraro, F / Fields, L / Filip, P / Filthaut, F / Fiorini, M / Fischer, V / Fitzpatrick, R S / Flanagan, W / Fleming, B / Flight, R / Fogarty, S / Foreman, W / Fowler, J / Fox, W / Franc, J / Francis, K / Franco, D / Freeman, J / Freestone, J / Fried, J / Friedland, A / Robayo, F Fuentes / Fuess, S / Furic, I K / Furman, K / Furmanski, A P / Gabrielli, A / Gago, A / Gallagher, H / Gallas, A / Gallego-Ros, A / Gallice, N / Galymov, V / Gamberini, E / Gamble, T / Ganacim, F / Gandhi, R / Gandrajula, R / Gao, F / Gao, S / Garcia-Gamez, D / García-Peris, M Á / Gardiner, S / Gastler, D / Gauvreau, J / Ge, G / Geffroy, N / Gelli, B / Gendotti, A / Gent, S / Ghorbani-Moghaddam, Z / Giammaria, P / Giammaria, T / Giangiacomi, N / Gibin, D / Gil-Botella, I / Gilligan, S / Girerd, C / Giri, A K / Gnani, D / Gogota, O / Gold, M / Gollapinni, S / Gollwitzer, K / Gomes, R A / Bermeo, L V Gomez / Fajardo, L S Gomez / Gonnella, F / Gonzalez-Diaz, D / Gonzalez-Lopez, M / Goodman, M C / Goodwin, O / Goswami, S / Gotti, C / Goudzovski, E / Grace, C / Gran, R / Granados, E / Granger, P / Grant, A / Grant, C / Gratieri, D / Green, P / Greenler, L / Greer, J / Grenard, J / Griffith, W C / Groh, M / Grudzinski, J / Grzelak, K / Gu, W / Guardincerri, E / Guarino, V / Guarise, M / Guenette, R / Guerard, E / Guerzoni, M / Guffanti, D / Guglielmi, A / Guo, B / Gupta, A / Gupta, V / Guthikonda, K K / Gutierrez, R / Guzowski, P / Guzzo, M M / Gwon, S / Ha, C / Haaf, K / Habig, A / Hadavand, H / Haenni, R / Hahn, A / Haiston, J / Hamacher-Baumann, P / Hamernik, T / Hamilton, P / Han, J / Harris, D A / Hartnell, J / Hartnett, T / Harton, J / Hasegawa, T / Hasnip, C / Hatcher, R / Hatfield, K W / Hatzikoutelis, A / Hayes, C / Hayrapetyan, K / Hays, J / Hazen, E / He, M / Heavey, A / Heeger, K M / Heise, J / Henry, S / Morquecho, M A Hernandez / Herner, K / Hewes, J / Hilgenberg, C / Hill, T / Hillier, S J / Himmel, A / Hinkle, E / Hirsch, L R / Ho, J / Hoff, J / Holin, A / Hoppe, E / Horton-Smith, G A / Hostert, M / Hourlier, A / Howard, B / Howell, R / Hoyos, J / Hristova, I / Hronek, M S / Huang, J / Hulcher, Z / Iles, G / Ilic, N / Iliescu, A M / Illingworth, R / Ingratta, G / Ioannisian, A / Irwin, B / Isenhower, L / Itay, R / Jackson, C M / Jain, V / James, E / Jang, W / Jargowsky, B / Jediny, F / Jena, D / Jeong, Y S / Jesús-Valls, C / Ji, X / Jiang, L / Jiménez, S / Jipa, A / Johnson, R / Johnson, W / Johnston, N / Jones, B / Jones, S / Judah, M / Jung, C K / Junk, T / Jwa, Y / Kabirnezhad, M / Kaboth, A / Kadenko, I / Kakorin, I / Kalitkina, A / Kalra, D / Kamiya, F / Kaneshige, N / Kaplan, D M / Karagiorgi, G / Karaman, G / Karcher, A / Karolak, M / Karyotakis, Y / Kasai, S / Kasetti, S P / Kashur, 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Zennamo, J / Zeug, K / Zhang, C / Zhang, S / Zhang, Y / Zhao, M / Zhivun, E / Zhu, G / Zimmerman, E D / Zucchelli, S / Zuklin, J / Zutshi, V / Zwaska, R

    The European physical journal. C, Particles and fields

    2022  Volume 82, Issue 7, Page(s) 618

    Abstract: DUNE is a dual-site experiment for long-baseline neutrino oscillation studies, neutrino astrophysics and nucleon decay searches. ProtoDUNE Dual Phase (DP) is a ... ...

    Abstract DUNE is a dual-site experiment for long-baseline neutrino oscillation studies, neutrino astrophysics and nucleon decay searches. ProtoDUNE Dual Phase (DP) is a 6
    Language English
    Publishing date 2022-07-16
    Publishing country France
    Document type Journal Article
    ZDB-ID 1459069-4
    ISSN 1434-6052 ; 1434-6044
    ISSN (online) 1434-6052
    ISSN 1434-6044
    DOI 10.1140/epjc/s10052-022-10549-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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