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  1. Article ; Online: Constraining the p-Mode-g-Mode Tidal Instability with GW170817.

    Abbott, B P / Abbott, R / Abbott, T D / Acernese, F / Ackley, K / Adams, C / Adams, T / Addesso, P / Adhikari, R X / Adya, V B / Affeldt, C / Agarwal, B / Agathos, M / Agatsuma, K / Aggarwal, N / Aguiar, O D / Aiello, L / Ain, A / Ajith, P /
    Allen, B / Allen, G / Allocca, A / Aloy, M A / Altin, P A / Amato, A / Ananyeva, A / Anderson, S B / Anderson, W G / Angelova, S V / Antier, S / Appert, S / Arai, K / Araya, M C / Areeda, J S / Arène, M / Arnaud, N / Arun, K G / Ascenzi, S / Ashton, G / Ast, M / Aston, S M / Astone, P / Atallah, D V / Aubin, F / Aufmuth, P / Aulbert, C / AultONeal, K / Austin, C / Avila-Alvarez, A / Babak, S / Bacon, P / Badaracco, F / Bader, M K M / Bae, S / Baker, P T / Baldaccini, F / Ballardin, G / Ballmer, S W / Banagiri, S / Barayoga, J C / Barclay, S E / Barish, B C / Barker, D / Barkett, K / Barnum, S / Barone, F / Barr, B / Barsotti, L / Barsuglia, M / Barta, D / Bartlett, J / Bartos, I / Bassiri, R / Basti, A / Batch, J C / Bawaj, M / Bayley, J C / Bazzan, M / Bécsy, B / Beer, C / Bejger, M / Belahcene, I / Bell, A S / Beniwal, D / Bensch, M / Berger, B K / Bergmann, G / Bernuzzi, S / Bero, J J / Berry, C P L / Bersanetti, D / Bertolini, A / Betzwieser, J / Bhandare, R / Bilenko, I A / Bilgili, S A / Billingsley, G / Billman, C R / Birch, J / Birney, R / Birnholtz, O / Biscans, S / Biscoveanu, S / Bisht, A / Bitossi, M / Bizouard, M A / Blackburn, J K / Blackman, J / Blair, C D / Blair, D G / Blair, R M / Bloemen, S / Bock, O / Bode, N / Boer, M / Boetzel, Y / Bogaert, G / Bohe, A / Bondu, F / Bonilla, E / Bonnand, R / Booker, P / Boom, B A / Booth, C D / Bork, R / Boschi, V / Bose, S / Bossie, K / Bossilkov, V / Bosveld, J / Bouffanais, Y / Bozzi, A / Bradaschia, C / Brady, P R / Bramley, A / Branchesi, M / Brau, J E / Briant, T / Brighenti, F / Brillet, A / Brinkmann, M / Brisson, V / Brockill, P / Brooks, A F / Brown, D D / Brunett, S / Buchanan, C C / Buikema, A / Bulik, T / Bulten, H J / Buonanno, A / Buskulic, D / Buy, C / Byer, R L / Cabero, M / Cadonati, L / Cagnoli, G / Cahillane, C / Calderón Bustillo, J / Callister, T A / Calloni, E / Camp, J B / Canepa, M / Canizares, P / Cannon, K C / Cao, H / Cao, J / Capano, C D / Capocasa, E / Carbognani, F / Caride, S / Carney, M F / Casanueva Diaz, J / Casentini, C / Caudill, S / Cavaglià, M / Cavalier, F / Cavalieri, R / Cella, G / Cepeda, C B / Cerdá-Durán, P / Cerretani, G / Cesarini, E / Chaibi, O / Chamberlin, S J / Chan, M / Chao, S / Charlton, P / Chase, E / Chassande-Mottin, E / Chatterjee, D / Chatziioannou, Katerina / Cheeseboro, B D / Chen, H Y / Chen, X / Chen, Y / Cheng, H-P / Chia, H Y / Chincarini, A / Chiummo, A / Chmiel, T / Cho, H S / Cho, M / Chow, J H / Christensen, N / Chu, Q / Chua, A J K / Chua, S / Chung, K W / Chung, S / Ciani, G / Ciobanu, A A / Ciolfi, R / Cipriano, F / Cirelli, C E / Cirone, A / Clara, F / Clark, J A / Clearwater, P / Cleva, F / Cocchieri, C / Coccia, E / Cohadon, P-F / Cohen, D / Colla, A / Collette, C G / Collins, C / Cominsky, L R / Constancio, M / Conti, L / Cooper, S J / Corban, P / Corbitt, T R / Cordero-Carrión, I / Corley, K R / Cornish, N / Corsi, A / Cortese, S / Costa, C A / Cotesta, R / Coughlin, M W / Coughlin, S B / Coulon, J-P / Countryman, S T / Couvares, P / Covas, P B / Cowan, E E / Coward, D M / Cowart, M J / Coyne, D C / Coyne, R / Creighton, J D E / Creighton, T D / Cripe, J / Crowder, S G / Cullen, T J / Cumming, A / Cunningham, L / Cuoco, E / Canton, T Dal / Dálya, G / Danilishin, S L / D'Antonio, S / Danzmann, K / Dasgupta, A / Costa, C F Da Silva / Dattilo, V / Dave, I / Davier, M / Davis, D / Daw, E J / Day, B / DeBra, D / Deenadayalan, M / Degallaix, J / De Laurentis, M / Deléglise, S / Del Pozzo, W / Demos, N / Denker, T / Dent, T / De Pietri, R / Derby, J / Dergachev, V / De Rosa, R / De Rossi, C / DeSalvo, R / de Varona, O / Dhurandhar, S / Díaz, M C / Di Fiore, L / Di Giovanni, M / Di Girolamo, T / Di Lieto, A / Ding, B / Di Pace, S / Di Palma, I / Di Renzo, F / Dmitriev, A / Doctor, Z / Dolique, V / Donovan, F / Dooley, K L / Doravari, S / Dorrington, I / Dovale Álvarez, M / Downes, T P / Drago, M / Dreissigacker, C / Driggers, J C / Du, Z / Dupej, P / Dwyer, S E / Easter, P J / Edo, T B / Edwards, M C / Effler, A / Eggenstein, H-B / Ehrens, P / Eichholz, J / Eikenberry, S S / Eisenmann, M / Eisenstein, R A / Essick, R C / Estelles, H / Estevez, D / Etienne, Z B / Etzel, T / Evans, M / Evans, T M / Fafone, V / Fair, H / Fairhurst, S / Fan, X / Farinon, S / Farr, B / Farr, W M / Fauchon-Jones, E J / Favata, M / Fays, M / Fee, C / Fehrmann, H / Feicht, J / Fejer, M M / Feng, F / Fernandez-Galiana, A / Ferrante, I / Ferreira, E C / Ferrini, F / Fidecaro, F / Fiori, I / Fiorucci, D / Fishbach, M / Fisher, R P / Fishner, J M / Fitz-Axen, M / Flaminio, R / Fletcher, M / Fong, H / Font, J A / Forsyth, P W F / Forsyth, S S / Fournier, J-D / Frasca, S / Frasconi, F / Frei, Z / Freise, A / Frey, R / Frey, V / Fritschel, P / Frolov, V V / Fulda, P / Fyffe, M / Gabbard, H A / Gadre, B U / Gaebel, S M / Gair, J R / Gammaitoni, L / Ganija, M R / Gaonkar, S G / Garcia, A / García-Quirós, C / Garufi, F / Gateley, B / Gaudio, S / Gaur, G / Gayathri, V / Gemme, G / Genin, E / Gennai, A / George, D / George, J / Gergely, L / Germain, V / Ghonge, S / Ghosh, Abhirup / Ghosh, Archisman / Ghosh, S / Giacomazzo, B / Giaime, J A / Giardina, K D / Giazotto, A / Gill, K / Giordano, G / Glover, L / Goetz, E / Goetz, R / Goncharov, B / González, G / Gonzalez Castro, J M / Gopakumar, A / Gorodetsky, M L / Gossan, S E / Gosselin, M / Gouaty, R / Grado, A / Graef, C / Granata, M / Grant, A / Gras, S / Gray, C / Greco, G / Green, A C / Green, R / Gretarsson, E M / Groot, P / Grote, H / Grunewald, S / Gruning, P / Guidi, G M / Gulati, H K / Guo, X / Gupta, A / Gupta, M K / Gushwa, K E / Gustafson, E K / Gustafson, R / Halim, O / Hall, B R / Hall, E D / Hamilton, E Z / Hamilton, H F / Hammond, G / Haney, M / Hanke, M M / Hanks, J / Hanna, C / Hannam, M D / Hannuksela, O A / Hanson, J / Hardwick, T / Harms, J / Harry, G M / Harry, I W / Hart, M J / Haster, C-J / Haughian, K / Healy, J / Heidmann, A / Heintze, M C / Heitmann, H / Hello, P / Hemming, G / Hendry, M / Heng, I S / Hennig, J / Heptonstall, A W / Hernandez, F J / Heurs, M / Hild, S / Hinderer, T / Hoak, D / Hochheim, S / Hofman, D / Holland, N A / Holt, K / Holz, D E / Hopkins, P / Horst, C / Hough, J / Houston, E A / Howell, E J / Hreibi, A / Huerta, E A / Huet, D / Hughey, B / Hulko, M / Husa, S / Huttner, S H / Huynh-Dinh, T / Iess, A / Indik, N / Ingram, C / Inta, R / Intini, G / Isa, H N / Isac, J-M / Isi, M / Iyer, B R / Izumi, K / Jacqmin, T / Jani, K / Jaranowski, P / Johnson, D S / Johnson, W W / Jones, D I / Jones, R / Jonker, R J G / Ju, L / Junker, J / Kalaghatgi, C V / Kalogera, V / Kamai, B / Kandhasamy, S / Kang, G / Kanner, J B / Kapadia, S J / Karki, S / Karvinen, K S / Kasprzack, M / Katolik, M / Katsanevas, S / Katsavounidis, E / Katzman, W / Kaufer, S / Kawabe, K / Keerthana, N V / Kéfélian, F / Keitel, D / Kemball, A J / Kennedy, R / Key, J S / Khalili, F Y / Khamesra, B / Khan, H / Khan, I / Khan, S / Khan, Z / Khazanov, E A / Kijbunchoo, N / Kim, Chunglee / Kim, J C / Kim, K / Kim, W / Kim, W S / Kim, Y-M / King, E J / King, P J / Kinley-Hanlon, M / Kirchhoff, R / Kissel, J S / Kleybolte, L / Klimenko, S / Knowles, T D / Koch, P / Koehlenbeck, S M / Koley, S / Kondrashov, V / Kontos, A / Korobko, M / Korth, W Z / Kowalska, I / Kozak, D B / Krämer, C / Kringel, V / Krishnan, B / Królak, A / Kuehn, G / Kumar, P / Kumar, R / Kumar, S / Kuo, L / Kutynia, A / Kwang, S / Lackey, B D / Lai, K H / Landry, M / Lang, R N / Lange, J / Lantz, B / Lanza, R K / Lartaux-Vollard, A / Lasky, P D / Laxen, M / Lazzarini, A / Lazzaro, C / Leaci, P / Leavey, S / Lee, C H / Lee, H K / Lee, H M / Lee, H W / Lee, K / Lehmann, J / Lenon, A / Leonardi, M / Leroy, N / Letendre, N / Levin, Y / Li, J / Li, T G F / Li, X / Linker, S D / Littenberg, T B / Liu, J / Liu, X / Lo, R K L / Lockerbie, N A / London, L T / Longo, A / Lorenzini, M / Loriette, V / Lormand, M / Losurdo, G / Lough, J D / Lovelace, G / Lück, H / Lumaca, D / Lundgren, A P / Lynch, R / Ma, Y / Macas, R / Macfoy, S / Machenschalk, B / MacInnis, M / Macleod, D M / Magaña Hernandez, I / Magaña-Sandoval, F / Magaña Zertuche, L / Magee, R M / Majorana, E / Maksimovic, I / Man, N / Mandic, V / Mangano, V / Mansell, G L / Manske, M / Mantovani, M / Marchesoni, F / Marion, F / Márka, S / Márka, Z / Markakis, C / Markosyan, A S / Markowitz, A / Maros, E / Marquina, A / Martelli, F / Martellini, L / Martin, I W / Martin, R M / Martynov, D V / Mason, K / Massera, E / Masserot, A / Massinger, T J / Masso-Reid, M / Mastrogiovanni, S / Matas, A / Matichard, F / Matone, L / Mavalvala, N / Mazumder, N / McCann, J J / McCarthy, R / McClelland, D E / McCormick, S / McCuller, L / McGuire, S C / McIver, J / McManus, D J / McRae, T / McWilliams, S T / Meacher, D / Meadors, G D / Mehmet, M / Meidam, J / Mejuto-Villa, E / Melatos, A / Mendell, G / Mendoza-Gandara, D / Mercer, R A / Mereni, L / Merilh, E L / Merzougui, M / Meshkov, S / Messenger, C / Messick, C / Metzdorff, R / Meyers, P M / Miao, H / Michel, C / Middleton, H / Mikhailov, E E / Milano, L / Miller, A L / Miller, A / Miller, B B / Miller, J / Millhouse, M / Mills, J / Milovich-Goff, M C / Minazzoli, O / Minenkov, Y / Ming, J / Mishra, C / Mitra, S / Mitrofanov, V P / Mitselmakher, G / Mittleman, R / Moffa, D / Mogushi, K / Mohan, M / Mohapatra, S R P / Montani, M / Moore, C J / Moraru, D / Moreno, G / Morisaki, S / Mours, B / Mow-Lowry, C M / Mueller, G / Muir, A W / Mukherjee, Arunava / Mukherjee, D / Mukherjee, S / Mukund, N / Mullavey, A / Munch, J / Muñiz, E A / Muratore, M / Murray, P G / Nagar, A / Napier, K / Nardecchia, I / Naticchioni, L / Nayak, R K / Neilson, J / Nelemans, G / Nelson, T J N / Nery, M / Neunzert, A / Nevin, L / Newport, J M / Ng, K Y / Ng, S / Nguyen, P / Nguyen, T T / Nichols, D / Nielsen, A B / Nissanke, S / Nitz, A / Nocera, F / Nolting, D / North, C / Nuttall, L K / Obergaulinger, M / Oberling, J / O'Brien, B D / O'Dea, G D / Ogin, G H / Oh, J J / Oh, S H / Ohme, F / Ohta, H / Okada, M A / Oliver, M / Oppermann, P / Oram, Richard J / O'Reilly, B / Ormiston, R / Ortega, L F / O'Shaughnessy, R / Ossokine, S / Ottaway, D J / Overmier, H / Owen, B J / Pace, A E / Pagano, G / Page, J / Page, M A / Pai, A / Pai, S A / Palamos, J R / Palashov, O / Palomba, C / Pal-Singh, A / Pan, Howard / Pan, Huang-Wei / Pang, B / Pang, P T H / Pankow, C / Pannarale, F / Pant, B C / Paoletti, F / Paoli, A / Papa, M A / Parida, A / Parker, W / Pascucci, D / Pasqualetti, A / Passaquieti, R / Passuello, D / Patil, M / Patricelli, B / Pearlstone, B L / Pedersen, C / Pedraza, M / Pedurand, R / Pekowsky, L / Pele, A / Penn, S / Perez, C J / Perreca, A / Perri, L M / Pfeiffer, H P / Phelps, M / Phukon, K S / Piccinni, O J / Pichot, M / Piergiovanni, F / Pierro, V / Pillant, G / Pinard, L / Pinto, I M / Pirello, M / Pitkin, M / Poggiani, R / Popolizio, P / Porter, E K / Possenti, L / Post, A / Powell, J / Prasad, J / Pratt, J W W / Pratten, G / Predoi, V / Prestegard, T / Principe, M / Privitera, S / Prodi, G A / Prokhorov, L G / Puncken, O / Punturo, M / Puppo, P / Pürrer, M / Qi, H / Quetschke, V / Quintero, E A / Quitzow-James, R / Rabeling, D S / Radkins, H / Raffai, P / Raja, S / Rajan, C / Rajbhandari, B / Rakhmanov, M / Ramirez, K E / Ramos-Buades, A / Rana, Javed / Rapagnani, P / Raymond, V / Razzano, M / Read, J / Regimbau, T / Rei, L / Reid, S / Reitze, D H / Ren, W / Ricci, F / Ricker, P M / Riles, K / Rizzo, M / Robertson, N A / Robie, R / Robinet, F / Robson, T / Rocchi, A / Rolland, L / Rollins, J G / Roma, V J / Romano, R / Romel, C L / Romie, J H / Rosińska, D / Ross, M P / Rowan, S / Rüdiger, A / Ruggi, P / Rutins, G / Ryan, K / Sachdev, S / Sadecki, T / Sakellariadou, M / Salconi, L / Saleem, M / Salemi, F / Samajdar, A / Sammut, L / Sampson, L M / Sanchez, E J / Sanchez, L E / Sanchis-Gual, N / Sandberg, V / Sanders, J R / Sarin, N / Sassolas, B / Saulson, P R / Sauter, O / Savage, R L / Sawadsky, A / Schale, P / Scheel, M / Scheuer, J / Schmidt, P / Schnabel, R / Schofield, R M S / Schönbeck, A / Schreiber, E / Schuette, D / Schulte, B W / Schutz, B F / Schwalbe, S G / Scott, J / Scott, S M / Seidel, E / Sellers, D / Sengupta, A S / Sentenac, D / Sequino, V / Sergeev, A / Setyawati, Y / Shaddock, D A / Shaffer, T J / Shah, A A / Shahriar, M S / Shaner, M B / Shao, L / Shapiro, B / Shawhan, P / Shen, H / Shoemaker, D H / Shoemaker, D M / Siellez, K / Siemens, X / Sieniawska, M / Sigg, D / Silva, A D / Singer, L P / Singh, A / Singhal, A / Sintes, A M / Slagmolen, B J J / Slaven-Blair, T J / Smith, B / Smith, J R / Smith, R J E / Somala, S / Son, E J / Sorazu, B / Sorrentino, F / Souradeep, T / Spencer, A P / Srivastava, A K / Staats, K / Steinke, M / Steinlechner, J / Steinlechner, S / Steinmeyer, D / Steltner, B / Stevenson, S P / Stocks, D / Stone, R / Stops, D J / Strain, K A / Stratta, G / Strigin, S E / Strunk, A / Sturani, R / Stuver, A L / Summerscales, T Z / Sun, L / Sunil, S / Suresh, J / Sutton, P J / Swinkels, B L / Szczepańczyk, M J / Tacca, M / Tait, S C / Talbot, C / Talukder, D / Tanner, D B / Tápai, M / Taracchini, A / Tasson, J D / Taylor, J A / Taylor, R / Tewari, S V / Theeg, T / Thies, F / Thomas, E G / Thomas, M / Thomas, P / Thorne, K A / Thrane, E / Tiwari, S / Tiwari, V / Tokmakov, K V / Toland, K / Tonelli, M / Tornasi, Z / Torres-Forné, A / Torrie, C I / Töyrä, D / Travasso, F / Traylor, G / Trinastic, J / Tringali, M C / Trozzo, L / Tsang, K W / Tse, M / Tso, R / Tsuna, D / Tsukada, L / Tuyenbayev, D / Ueno, K / Ugolini, D / Urban, A L / Usman, S A / Vahlbruch, H / Vajente, G / Valdes, G / van Bakel, N / van Beuzekom, M / van den Brand, J F J / Van Den Broeck, C / Vander-Hyde, D C / van der Schaaf, L / van Heijningen, J V / van Veggel, A A / Vardaro, M / Varma, V / Vass, S / Vasúth, M / Vecchio, A / Vedovato, G / Veitch, J / Veitch, P J / Venkateswara, K / Venugopalan, G / Verkindt, D / Vetrano, F / Viceré, A / Viets, A D / Vinciguerra, S / Vine, D J / Vinet, J-Y / Vitale, S / Vo, T / Vocca, H / Vorvick, C / Vyatchanin, S P / Wade, A R / Wade, L E / Wade, M / Walet, R / Walker, M / Wallace, L / Walsh, S / Wang, G / Wang, H / Wang, J Z / Wang, W H / Wang, Y F / Ward, R L / Warner, J / Was, M / Watchi, J / Weaver, B / Wei, L-W / Weinert, M / Weinstein, A J / Weiss, R / Wellmann, F / Wen, L / Wessel, E K / Weßels, P / Westerweck, J / Wette, K / Whelan, J T / Whiting, B F / Whittle, C / Wilken, D / Williams, D / Williams, R D / Williamson, A R / Willis, J L / Willke, B / Wimmer, M H / Winkler, W / Wipf, C C / Wittel, H / Woan, G / Woehler, J / Wofford, J K / Wong, W K / Worden, J / Wright, J L / Wu, D S / Wysocki, D M / Xiao, S / Yam, W / Yamamoto, H / Yancey, C C / Yang, L / Yap, M J / Yazback, M / Yu, Hang / Yu, Haocun / Yvert, M / Zadrożny, A / Zanolin, M / Zelenova, T / Zendri, J-P / Zevin, M / Zhang, J / Zhang, L / Zhang, M / Zhang, T / Zhang, Y-H / Zhao, C / Zhou, M / Zhou, Z / Zhu, S J / Zhu, X J / Zimmerman, A B / Zucker, M E / Zweizig, J / Weinberg, N N

    Physical review letters

    2019  Volume 122, Issue 6, Page(s) 61104

    Abstract: We analyze the impact of a proposed tidal instability coupling p modes and g modes within neutron ... we compute the Bayes factor (lnB_{!pg}^{pg}) comparing our p-g model to a standard one. We find ... that the observed signal is consistent with waveform models that neglect p-g effects, with lnB_{!pg}^{pg}=0.03_{-0 ...

    Abstract We analyze the impact of a proposed tidal instability coupling p modes and g modes within neutron stars on GW170817. This nonresonant instability transfers energy from the orbit of the binary to internal modes of the stars, accelerating the gravitational-wave driven inspiral. We model the impact of this instability on the phasing of the gravitational wave signal using three parameters per star: an overall amplitude, a saturation frequency, and a spectral index. Incorporating these additional parameters, we compute the Bayes factor (lnB_{!pg}^{pg}) comparing our p-g model to a standard one. We find that the observed signal is consistent with waveform models that neglect p-g effects, with lnB_{!pg}^{pg}=0.03_{-0.58}^{+0.70} (maximum a posteriori and 90% credible region). By injecting simulated signals that do not include p-g effects and recovering them with the p-g model, we show that there is a ≃50% probability of obtaining similar lnB_{!pg}^{pg} even when p-g effects are absent. We find that the p-g amplitude for 1.4  M_{⊙} neutron stars is constrained to less than a few tenths of the theoretical maximum, with maxima a posteriori near one-tenth this maximum and p-g saturation frequency ∼70  Hz. This suggests that there are less than a few hundred excited modes, assuming they all saturate by wave breaking. For comparison, theoretical upper bounds suggest ≲10^{3} modes saturate by wave breaking. Thus, the measured constraints only rule out extreme values of the p-g parameters. They also imply that the instability dissipates ≲10^{51}  erg over the entire inspiral, i.e., less than a few percent of the energy radiated as gravitational waves.
    Language English
    Publishing date 2019-03-01
    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.122.061104
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The Elovl4 Spinocerebellar Ataxia-34 Mutation 736T>G (p.W246G) Impairs Retinal Function in the Absence of Photoreceptor Degeneration.

    Agbaga, Martin-Paul / Stiles, Megan A / Brush, Richard S / Sullivan, Michael T / Machalinski, Adeline / Jones, Kenneth L / Anderson, Robert E / Sherry, David M

    Molecular neurobiology

    2020  Volume 57, Issue 11, Page(s) 4735–4753

    Abstract: ... remains unclear. We generated a knock-in rat line (SCA34-KI) that expresses the 736T>G (p.W246G) form ...

    Abstract Elongation of very long chain fatty acids-4 (ELOVL4) is essential for synthesis of very long chain polyunsaturated and saturated fatty acids (VLC-PUFA and VLC-SFA, respectively) of chain length greater than 26 carbons. Mutations in the ELOVL4 gene cause several distinct neurodegenerative diseases including Stargardt-like macular dystrophy (STGD3), spinocerebellar ataxia 34 (SCA34), and a neuro-ichthyotic syndrome with severe seizures and spasticity, as well as erythrokeratitis variabilis (EKV), a skin disorder. However, the relationship between ELOVL4 mutations, its VLC-PUFA and VLC-SFA products, and specific neurological symptoms remains unclear. We generated a knock-in rat line (SCA34-KI) that expresses the 736T>G (p.W246G) form of ELOVL4 that causes human SCA34. Lipids were analyzed by gas chromatography and mass spectrometry. Retinal function was assessed using electroretinography. Retinal integrity was assessed by histology, optical coherence tomography, and immunolabeling. Analysis of retina and skin lipids showed that the W246G mutation selectively impaired synthesis of VLC-SFA, but not VLC-PUFA. Homozygous SCA34-KI rats showed reduced ERG a- and b-wave amplitudes by 90 days of age, particularly for scotopic responses. Anatomical analyses revealed no indication of neurodegeneration in heterozygote or homozygote SCA34-KI rats out to 6-7 months of age. These studies reveal a previously unrecognized role for VLC-SFA in regulating retinal function, particularly transmission from photoreceptors to the inner retina, in the absence of neurodegeneration. Furthermore, these findings suggest that the tissue specificity and symptoms associated with disease-causing ELOVL4 mutations likely arise from selective differences in the ability of the mutant ELOVL4 enzymes to support synthesis of VLC-PUFA and/or VLC-SFA.
    MeSH term(s) Animals ; Disease Models, Animal ; Electroretinography ; Eye Proteins/genetics ; Fatty Acids/metabolism ; Humans ; Membrane Proteins/genetics ; Mutation/genetics ; Night Vision ; Phenotype ; Photoreceptor Cells, Vertebrate/pathology ; Rats ; Rats, Transgenic ; Retina/physiopathology ; Retinal Degeneration/genetics ; Retinal Degeneration/physiopathology ; Spinocerebellar Ataxias/genetics ; Spinocerebellar Ataxias/physiopathology
    Chemical Substances ELOVL4 protein, human ; Eye Proteins ; Fatty Acids ; Membrane Proteins
    Language English
    Publishing date 2020-08-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 645020-9
    ISSN 1559-1182 ; 0893-7648
    ISSN (online) 1559-1182
    ISSN 0893-7648
    DOI 10.1007/s12035-020-02052-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Severe Cloverleaf Skull Deformity in c.1061C>G (p.Ser354Cys) Mutated Fibroblast Growth Factor Receptor 2 Gene in Crouzon Syndrome.

    Chaisrisawadisuk, Sarut / Hammam, Elie / Molloy, Cindy J / Barnett, Christopher / Anderson, Peter J / Moore, Mark H

    The Journal of craniofacial surgery

    2020  Volume 32, Issue 1, Page(s) 261–264

    Abstract: ... with CS and the pathogenic c.1061C>G (p.Ser354Cys) variant of the fibroblast growth factor receptor 2 ...

    Abstract Abstract: Cloverleaf skull deformity (CSD), or Kleeblattschädel, is a condition with severe and unpatterned multisuture craniosynostosis, resulting in a trilobar-shaped skull. This deformity mainly comprises a cranio-orbito-facial malformation that leads to a spectrum of multidisciplinary issues. Several syndromes are associated with CSD, such as Crouzon syndrome (CS). Here, we report the case of an infant with CS and the pathogenic c.1061C>G (p.Ser354Cys) variant of the fibroblast growth factor receptor 2 (FGFR2) gene. The child presented with the severe form of CSD despite having a normal, mid-trimester, sonographic scan.
    MeSH term(s) Child ; Craniofacial Dysostosis/diagnostic imaging ; Craniofacial Dysostosis/genetics ; Craniosynostoses/diagnostic imaging ; Craniosynostoses/genetics ; Humans ; Infant ; Mutation ; Receptor, Fibroblast Growth Factor, Type 2/genetics ; Skull/diagnostic imaging ; Ultrasonography
    Chemical Substances Receptor, Fibroblast Growth Factor, Type 2 (EC 2.7.10.1)
    Language English
    Publishing date 2020-09-21
    Publishing country United States
    Document type Case Reports ; Journal Article
    ZDB-ID 1159501-2
    ISSN 1536-3732 ; 1049-2275
    ISSN (online) 1536-3732
    ISSN 1049-2275
    DOI 10.1097/SCS.0000000000006999
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  4. Article: Membrane translocation of P-Rex1 is mediated by G protein betagamma subunits and phosphoinositide 3-kinase.

    Barber, Mark A / Donald, Sarah / Thelen, Sylvia / Anderson, Karen E / Thelen, Marcus / Welch, Heidi C E

    The Journal of biological chemistry

    2007  Volume 282, Issue 41, Page(s) 29967–29976

    Abstract: ... but 7% of the total was present in the 117,000 x g membrane fraction. Co-expression of P-Rex1 ... P-Rex1 is a guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that is directly ... activated by the betagamma subunits of heterotrimeric G proteins and by the lipid second messenger ...

    Abstract P-Rex1 is a guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that is directly activated by the betagamma subunits of heterotrimeric G proteins and by the lipid second messenger phosphatidylinositol (3,4,5)-trisphosphate (PIP(3)), which is generated by phosphoinositide 3-kinase (PI3K). Gbetagamma subunits and PIP(3) are membrane-bound, whereas the intracellular localization of P-Rex1 in basal cells is cytosolic. Activation of PI3K alone is not sufficient to promote significant membrane translocation of P-Rex1. Here we investigated the subcellular localization of P-Rex1 by fractionation of Sf9 cells co-expressing P-Rex1 with Gbetagamma and/or PI3K. In basal, serum-starved cells, P-Rex1 was mainly cytosolic, but 7% of the total was present in the 117,000 x g membrane fraction. Co-expression of P-Rex1 with either Gbetagamma or PI3K caused only an insignificant increase in P-Rex1 membrane localization, whereas Gbetagamma and PI3K together synergistically caused a robust increase in membrane-localized P-Rex1 to 23% of the total. PI3K-driven P-Rex1 membrane recruitment was wortmannin-sensitive. The use of P-Rex1 mutants showed that the isolated Dbl homology/pleckstrin homology domain tandem of P-Rex1 is sufficient for synergistic Gbetagamma- and PI3K-driven membrane localization; that the enzymatic GEF activity of P-Rex1 is not required for membrane translocation; and that the other domains of P-Rex1 (DEP, PDZ, and IP4P) contribute to keeping the enzyme localized in the cytosol of basal cells. In vitro Rac2-GEF activity assays showed that membrane-derived purified P-Rex1 has a higher basal activity than cytosol-derived P-Rex1, but both can be further activated by PIP(3) and Gbetagamma subunits.
    MeSH term(s) Androstadienes/pharmacology ; Animals ; Cell Membrane/metabolism ; Cytosol/metabolism ; Enzyme Inhibitors/pharmacology ; GTP-Binding Protein beta Subunits/metabolism ; GTP-Binding Protein gamma Subunits/metabolism ; Gene Expression Regulation ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Insecta ; Microscopy, Fluorescence/methods ; Models, Biological ; Phosphatidylinositol 3-Kinases/metabolism ; Wortmannin
    Chemical Substances Androstadienes ; Enzyme Inhibitors ; GTP-Binding Protein beta Subunits ; GTP-Binding Protein gamma Subunits ; Guanine Nucleotide Exchange Factors ; PREX1 protein, human ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Wortmannin (XVA4O219QW)
    Language English
    Publishing date 2007-08-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M701877200
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  5. Article: The G glycoprotein of respiratory syncytial virus depresses respiratory rates through the CX3C motif and substance P.

    Tripp, Ralph A / Dakhama, Azzeddine / Jones, Les P / Barskey, Albert / Gelfand, Erwin W / Anderson, Larry J

    Journal of virology

    2003  Volume 77, Issue 11, Page(s) 6580–6584

    Abstract: ... of substance P (SP) and G glycoprotein-CX3CR1 interaction, an effect that is inhibited by treatment with anti-G ... to episodes of apnea. We show that RSV G glycoprotein reduces respiratory rates associated with the induction ...

    Abstract Respiratory syncytial virus (RSV) infection in the neonate can alter respiratory rates, i.e., lead to episodes of apnea. We show that RSV G glycoprotein reduces respiratory rates associated with the induction of substance P (SP) and G glycoprotein-CX3CR1 interaction, an effect that is inhibited by treatment with anti-G glycoprotein, anti-SP, or anti-CX3CR1 monoclonal antibodies. These data suggest new approaches for treating some aspects of RSV disease.
    MeSH term(s) Animals ; Apnea/etiology ; CX3C Chemokine Receptor 1 ; Chemokines, CX3C/chemistry ; Female ; Humans ; Mice ; Mice, Inbred BALB C ; Receptors, Cytokine/metabolism ; Receptors, HIV/metabolism ; Respiration/drug effects ; Respiratory Syncytial Virus, Human/pathogenicity ; Substance P/metabolism ; Viral Proteins/chemistry ; Viral Proteins/pharmacology ; Viral Proteins/physiology
    Chemical Substances CX3C Chemokine Receptor 1 ; Chemokines, CX3C ; Receptors, Cytokine ; Receptors, HIV ; Viral Proteins ; Substance P (33507-63-0)
    Language English
    Publishing date 2003-05-07
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.77.11.6580-6584.2003
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  6. Article: Membrane Translocation of P-Rex1 Is Mediated by G Protein βγ Subunits and Phosphoinositide 3-Kinase

    Barber, Mark A / Donald, Sarah / Thelen, Sylvia / Anderson, Karen E / Thelen, Marcus / Welch, Heidi C.E

    Journal of biological chemistry. 2007 Oct. 12, v. 282, no. 41

    2007  

    Abstract: ... of the total was present in the 117,000 x g membrane fraction. Co-expression of P-Rex1 with either Gβγ or PI3K ... P-Rex1 is a guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that is directly ... activated by the βγ subunits of heterotrimeric G proteins and by the lipid second messenger ...

    Abstract P-Rex1 is a guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that is directly activated by the βγ subunits of heterotrimeric G proteins and by the lipid second messenger phosphatidylinositol (3,4,5)-trisphosphate (PIP₃), which is generated by phosphoinositide 3-kinase (PI3K). Gβγ subunits and PIP₃ are membrane-bound, whereas the intracellular localization of P-Rex1 in basal cells is cytosolic. Activation of PI3K alone is not sufficient to promote significant membrane translocation of P-Rex1. Here we investigated the subcellular localization of P-Rex1 by fractionation of Sf9 cells co-expressing P-Rex1 with Gβγ and/or PI3K. In basal, serum-starved cells, P-Rex1 was mainly cytosolic, but 7% of the total was present in the 117,000 x g membrane fraction. Co-expression of P-Rex1 with either Gβγ or PI3K caused only an insignificant increase in P-Rex1 membrane localization, whereas Gβγ and PI3K together synergistically caused a robust increase in membrane-localized P-Rex1 to 23% of the total. PI3K-driven P-Rex1 membrane recruitment was wortmannin-sensitive. The use of P-Rex1 mutants showed that the isolated Dbl homology/pleckstrin homology domain tandem of P-Rex1 is sufficient for synergistic Gβγ- and PI3K-driven membrane localization; that the enzymatic GEF activity of P-Rex1 is not required for membrane translocation; and that the other domains of P-Rex1 (DEP, PDZ, and IP4P) contribute to keeping the enzyme localized in the cytosol of basal cells. In vitro Rac2-GEF activity assays showed that membrane-derived purified P-Rex1 has a higher basal activity than cytosol-derived P-Rex1, but both can be further activated by PIP₃ and Gβγ subunits.
    Language English
    Dates of publication 2007-1012
    Size p. 29967-29976.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database NAL-Catalogue (AGRICOLA)

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  7. Article: Enhanced disease and pulmonary eosinophilia associated with formalin-inactivated respiratory syncytial virus vaccination are linked to G glycoprotein CX3C-CX3CR1 interaction and expression of substance P.

    Haynes, Lia M / Jones, Les P / Barskey, Albert / Anderson, Larry J / Tripp, Ralph A

    Journal of virology

    2003  Volume 77, Issue 18, Page(s) 9831–9844

    Abstract: Vaccination with formalin-inactivated respiratory syncytial virus (FI-RSV) vaccine or RSV G ... that the absence of the G glycoprotein or G glycoprotein CX3C motif during FI-RSV vaccination or RSV challenge ... of FI-RSV-vaccinated mice, or treatment with anti-substance P or anti-CX3CR1 antibodies, reduces or ...

    Abstract Vaccination with formalin-inactivated respiratory syncytial virus (FI-RSV) vaccine or RSV G glycoprotein results in enhanced pulmonary disease after live RSV infection. Enhanced pulmonary disease is characterized by pulmonary eosinophilia and is associated with a substantial inflammatory response. We show that the absence of the G glycoprotein or G glycoprotein CX3C motif during FI-RSV vaccination or RSV challenge of FI-RSV-vaccinated mice, or treatment with anti-substance P or anti-CX3CR1 antibodies, reduces or eliminates enhanced pulmonary disease, modifies T-cell receptor Vbeta usage, and alters CC and CXC chemokine expression. These data suggest that the G glycoprotein, and in particular the G glycoprotein CX3C motif, is key in the enhanced inflammatory response to FI-RSV vaccination, possibly through the induction of substance P.
    MeSH term(s) Amino Acid Motifs ; Animals ; CD4-Positive T-Lymphocytes/immunology ; CX3C Chemokine Receptor 1 ; Cell Movement ; Chemokines/genetics ; Chemokines, CX3C/metabolism ; Female ; Formaldehyde ; Membrane Proteins ; Mice ; Mice, Inbred BALB C ; Pulmonary Eosinophilia/etiology ; RNA, Messenger/analysis ; Receptors, Antigen, T-Cell, alpha-beta/physiology ; Receptors, Chemokine/metabolism ; Respiratory Syncytial Viruses/immunology ; Substance P/biosynthesis ; Vaccination/adverse effects ; Vaccines, Inactivated/toxicity ; Viral Proteins/chemistry ; Viral Proteins/physiology ; Viral Vaccines/toxicity
    Chemical Substances CX3C Chemokine Receptor 1 ; CX3CR1 protein, human ; Chemokines ; Chemokines, CX3C ; Membrane Proteins ; RNA, Messenger ; Receptors, Antigen, T-Cell, alpha-beta ; Receptors, Chemokine ; Vaccines, Inactivated ; Viral Proteins ; Viral Vaccines ; Formaldehyde (1HG84L3525) ; Substance P (33507-63-0)
    Language English
    Publishing date 2003-07-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.77.18.9831-9844.2003
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  8. Article: Respiratory syncytial virus infection and G and/or SH protein expression contribute to substance P, which mediates inflammation and enhanced pulmonary disease in BALB/c mice.

    Tripp, R A / Moore, D / Winter, J / Anderson, L J

    Journal of virology

    2000  Volume 74, Issue 4, Page(s) 1614–1622

    Abstract: ... bronchiolitis, which has clinical features similar to those of asthma. Substance P (SP), a tachykinin ... of RSV that lacks the G and SH genes, the SP response to RSV infection appears to be associated with G ...

    Abstract A distinct clinical presentation of respiratory syncytial virus (RSV) infection of humans is bronchiolitis, which has clinical features similar to those of asthma. Substance P (SP), a tachykinin neuropeptide, has been associated with neurogenic inflammation and asthma; therefore, we chose to examine SP-induced inflammation with RSV infection. In this study, we examined the production of pulmonary SP associated with RSV infection of BALB/c mice and the effect of anti-SP F(ab)(2) antibodies on the pulmonary inflammatory response. The peak production of pulmonary SP occurred between days 3 and 5 following primary RSV infection and day 1 after secondary infection. Treatment of RSV-infected mice with anti-SP F(ab)(2) antibodies suggested that SP may alter the natural killer cell response to primary and secondary infection. In mice challenged after formalin-inactivated RSV vaccination, SP appears to markedly enhance pulmonary eosinophilia as well as increase polymorphonuclear cell trafficking to the lung. Based on studies with a strain of RSV that lacks the G and SH genes, the SP response to RSV infection appears to be associated with G and/or SH protein expression. These data suggest that SP may be an important contributor to the inflammatory response to RSV infection and that anti-SP F(ab)(2) antibodies might be used to ameliorate RSV-associated disease.
    MeSH term(s) Animals ; Antigens, Viral/immunology ; Bronchiolitis/immunology ; Bronchiolitis/metabolism ; Bronchoalveolar Lavage ; CD3 Complex/immunology ; Cercopithecus aethiops ; Cytokines/biosynthesis ; Female ; HN Protein ; Humans ; Mice ; Mice, Inbred BALB C ; Respiratory Syncytial Virus Infections/immunology ; Respiratory Syncytial Virus Infections/metabolism ; Respiratory Syncytial Virus, Human/immunology ; Substance P/immunology ; Substance P/metabolism ; T-Lymphocytes/immunology ; Vero Cells ; Viral Envelope Proteins ; Viral Proteins/immunology
    Chemical Substances Antigens, Viral ; CD3 Complex ; Cytokines ; HN Protein ; Viral Envelope Proteins ; Viral Proteins ; attachment protein G ; Substance P (33507-63-0)
    Language English
    Publishing date 2000-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.74.4.1614-1622.2000
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  9. Article: G.-6-P.D. deficiency and cancer.

    Naik, S N / Anderson, D E

    Lancet (London, England)

    1970  Volume 1, Issue 7655, Page(s) 1060–1061

    MeSH term(s) African Americans ; Female ; Glucosephosphate Dehydrogenase Deficiency/epidemiology ; Humans ; Male ; Neoplasms/epidemiology ; Sex Factors ; Texas
    Language English
    Publishing date 1970-05-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 3306-6
    ISSN 1474-547X ; 0140-6736 ; 0023-7507
    ISSN (online) 1474-547X
    ISSN 0140-6736 ; 0023-7507
    DOI 10.1016/s0140-6736(70)91195-5
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  10. Article: Evaluation of the protective immunogenicity of the N, P, M, NV and G proteins of infectious hematopoietic necrosis virus in rainbow trout oncorhynchus mykiss using DNA vaccines.

    Corbeil, S / Lapatra, S E / Anderson, E D / Jones, J / Vincent, B / Hsu, Y L / Kurath, G

    Diseases of aquatic organisms

    1999  Volume 39, Issue 1, Page(s) 29–36

    Abstract: The protective immunogenicity of the nucleoprotein (N), phosphoprotein (P), matrix protein (M), non ... virion protein (NV) and glycoprotein (G) of the rhabdovirus infectious hematopoietic necrosis virus (IHNV ... titers were also determined in vaccinated rainbow trout Oncorhynchus mykiss fry (mean weight 2 g) and 150 ...

    Abstract The protective immunogenicity of the nucleoprotein (N), phosphoprotein (P), matrix protein (M), non-virion protein (NV) and glycoprotein (G) of the rhabdovirus infectious hematopoietic necrosis virus (IHNV) was assessed in rainbow trout using DNA vaccine technology. DNA vaccines were produced by amplifying and cloning the viral genes in the plasmid pCDNA 3.1. The protective immunity elicited by each vaccine was evaluated through survival of immunized fry after challenge with live virus. Neutralizing antibody titers were also determined in vaccinated rainbow trout Oncorhynchus mykiss fry (mean weight 2 g) and 150 g sockeye salmon Oncorhynchus nerka. The serum from the 150 g fish was also used in passive immunization studies with naive fry. Our results showed that neither the internal structural proteins (N, P and M) nor the NV protein of IHNV induced protective immunity in fry or neutralizing antibodies in fry and 150 g fish when expressed by a DNA vaccine construct. The G protein, however, did confer significant protection in fry up to 80 d post-immunization and induced protective neutralizing antibodies. We are currently investigating the role of different arms of the fish immune system that contribute to the high level of protection against IHNV seen in vaccinated fish.
    MeSH term(s) Animals ; Antibodies, Viral/blood ; Fish Diseases/immunology ; Fish Diseases/prevention & control ; Gene Amplification ; Genes, Viral ; Immunization, Passive/veterinary ; Neutralization Tests/veterinary ; Oncorhynchus mykiss ; Plasmids ; Rhabdoviridae/genetics ; Rhabdoviridae/immunology ; Rhabdoviridae Infections/immunology ; Rhabdoviridae Infections/prevention & control ; Rhabdoviridae Infections/veterinary ; Salmon ; Vaccines, DNA/genetics ; Viral Proteins/genetics ; Viral Proteins/immunology ; Viral Vaccines/genetics
    Chemical Substances Antibodies, Viral ; Vaccines, DNA ; Viral Proteins ; Viral Vaccines
    Language English
    Publishing date 1999-12-22
    Publishing country Germany
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 0177-5103
    ISSN 0177-5103
    DOI 10.3354/dao039029
    Database MEDical Literature Analysis and Retrieval System OnLINE

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