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9 results on '"S. M. Duff"'

1. A microwave SQUID multiplexer optimized for bolometric applications

Author

B. Dober, Z. Ahmed, K. Arnold, D. T. Becker, D. A. Bennett, J. A. Connors, A. Cukierman, J. M. D'Ewart, S. M. Duff, J. E. Dusatko, J. C. Frisch, J. D. Gard, S. W. Henderson, R. Herbst, G. C. Hilton, J. Hubmayr, Y. Li, J. A. B. Mates, H. McCarrick, C. D. Reintsema, M. Silva-Feaver, L. Ruckman, J. N. Ullom, L. R. Vale, D. D. Van Winkle, J. Vasquez, Y. Wang, E. Young, C. Yu, and K. Zheng

Published
2021
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4. Optical Characterization of OMT-Coupled TES Bolometers for LiteBIRD

Author

J. Hubmayr, P. A. R. Ade, A. Adler, E. Allys, D. Alonso, K. Arnold, D. Auguste, J. Aumont, R. Aurlien, J. E. Austermann, S. Azzoni, C. Baccigalupi, A. J. Banday, R. Banerji, R. B. Barreiro, N. Bartolo, S. Basak, E. Battistelli, L. Bautista, J. A. Beall, D. Beck, S. Beckman, K. Benabed, J. Bermejo-Ballesteros, M. Bersanelli, J. Bonis, J. Borrill, F. Bouchet, F. Boulanger, S. Bounissou, M. Brilenkov, M. L. Brown, M. Bucher, E. Calabrese, M. Calvo, P. Campeti, A. Carones, F. J. Casas, A. Catalano, A. Challinor, V. Chan, K. Cheung, Y. Chinone, C. Chiocchetta, S. E. Clark, L. Clermont, S. Clesse, J. Cliche, F. Columbro, J. A. Connors, A. Coppolecchia, W. Coulton, J. Cubas, A. Cukierman, D. Curtis, F. Cuttaia, G. D’Alessandro, K. Dachlythra, P. de Bernardis, T. de Haan, E. de la Hoz, M. De Petris, S. Della Torre, J. J. Daz Garca, C. Dickinson, P. Diego-Palazuelos, M. Dobbs, T. Dotani, D. Douillet, E. Doumayrou, L. Duband, A. Ducout, S. M. Duff, J. M. Duval, K. Ebisawa, T. Elleflot, H. K. Eriksen, J. Errard, T. Essinger-Hileman, S. Farrens, F. Finelli, R. Flauger, K. Fleury-Frenette, C. Franceschet, U. Fuskeland, L. Galli, S. Galli, M. Galloway, K. Ganga, J. R. Gao, R. T. Genova-Santos, M. Georges, M. Gerbino, M. Gervasi, T. Ghigna, S. Giardiello, E. Gjerlw, R. Gonzlez Gonzles, M. L. Gradziel, J. Grain, L. Grandsire, F. Grupp, A. Gruppuso, J. E. Gudmundsson, N. W. Halverson, J. Hamilton, P. Hargrave, T. Hasebe, M. Hasegawa, M. Hattori, M. Hazumi, S. Henrot-Versill, B. Hensley, D. Herman, D. Herranz, G. C. Hilton, E. Hivon, R. A. Hlozek, D. Hoang, A. L. Hornsby, Y. Hoshino, K. Ichiki, T. Iida, T. Ikemoto, H. Imada, K. Ishimura, H. Ishino, G. Jaehnig, M. Jones, T. Kaga, S. Kashima, N. Katayama, A. Kato, T. Kawasaki, R. Keskitalo, C. Kintziger, T. Kisner, Y. Kobayashi, N. Kogiso, A. Kogut, K. Kohri, E. Komatsu, K. Komatsu, K. Konishi, N. Krachmalnicoff, I. Kreykenbohm, C. L. Kuo, A. Kushino, L. Lamagna, J. V. Lanen, G. Laquaniello, M. Lattanzi, A. T. Lee, C. Leloup, F. Levrier, E. Linder, M. J. Link, A. I. Lonappan, T. Louis, G. Luzzi, J. Macias-Perez, T. Maciaszek, B. Maffei, D. Maino, M. Maki, S. Mandelli, M. Maris, B. Marquet, E. Martnez-Gonzlez, F. A. Martire, S. Masi, M. Massa, M. Masuzawa, S. Matarrese, F. T. Matsuda, T. Matsumura, L. Mele, A. Mennella, M. Migliaccio, Y. Minami, K. Mitsuda, A. Moggi, M. Monelli, A. Monfardini, J. Montgomery, L. Montier, G. Morgante, B. Mot, Y. Murata, J. A. Murphy, M. Nagai, Y. Nagano, T. Nagasaki, R. Nagata, S. Nakamura, R. Nakano, T. Namikawa, F. Nati, P. Natoli, S. Nerval, N. Neto Godry Farias, T. Nishibori, H. Nishino, F. Noviello, G. C. O’Neil, C. O’Sullivan, K. Odagiri, H. Ochi, H. Ogawa, S. Oguri, H. Ohsaki, I. S. Ohta, N. Okada, L. Pagano, A. Paiella, D. Paoletti, G. Pascual Cisneros, A. Passerini, G. Patanchon, V. Pelgrim, J. Peloton, V. Pettorino, F. Piacentini, M. Piat, G. Piccirilli, F. Pinsard, G. Pisano, J. Plesseria, G. Polenta, D. Poletti, T. Prouv, G. Puglisi, D. Rambaud, C. Raum, S. Realini, M. Reinecke, C. D. Reintsema, M. Remazeilles, A. Ritacco, P. Rosier, G. Roudil, J. Rubino-Martin, M. Russell, H. Sakurai, Y. Sakurai, M. Sandri, M. Sasaki, G. Savini, D. Scott, J. Seibert, Y. Sekimoto, B. Sherwin, K. Shinozaki, M. Shiraishi, P. Shirron, A. Shitvov, G. Signorelli, G. Smecher, F. Spinella, J. Starck, S. Stever, R. Stompor, R. Sudiwala, S. Sugiyama, R. Sullivan, A. Suzuki, J. Suzuki, T. Suzuki, T. L. Svalheim, E. Switzer, R. Takaku, H. Takakura, S. Takakura, Y. Takase, Y. Takeda, A. Tartari, D. Tavagnacco, A. Taylor, E. Taylor, Y. Terao, L. Terenzi, J. Thermeau, H. Thommesen, K. L. Thompson, B. Thorne, T. Toda, M. Tomasi, M. Tominaga, N. Trappe, M. Tristram, M. Tsuji, M. Tsujimoto, C. Tucker, R. Ueki, J. N. Ullom, K. Umemori, L. Vacher, J. Van Lanen, G. Vermeulen, P. Vielva, F. Villa, M. R. Vissers, N. Vittorio, B. Wandelt, W. Wang, I. K. Wehus, J. Weller, B. Westbrook, G. Weymann-Despres, J. Wilms, B. Winter, E. J. Wollack, N. Y. Yamasaki, T. Yoshida, J. Yumoto, K. Watanuki, A. Zacchei, M. Zannoni, A. Zonca, Hubmayr, J, Ade, P, Adler, A, Allys, E, Alonso, D, Arnold, K, Auguste, D, Aumont, J, Aurlien, R, Austermann, J, Azzoni, S, Baccigalupi, C, Banday, A, Banerji, R, Barreiro, R, Bartolo, N, Basak, S, Battistelli, E, Bautista, L, Beall, J, Beck, D, Beckman, S, Benabed, K, Bermejo-Ballesteros, J, Bersanelli, M, Bonis, J, Borrill, J, Bouchet, F, Boulanger, F, Bounissou, S, Brilenkov, M, Brown, M, Bucher, M, Calabrese, E, Calvo, M, Campeti, P, Carones, A, Casas, F, Catalano, A, Challinor, A, Chan, V, Cheung, K, Chinone, Y, Chiocchetta, C, Clark, S, Clermont, L, Clesse, S, Cliche, J, Columbro, F, Connors, J, Coppolecchia, A, Coulton, W, Cubas, J, Cukierman, A, Curtis, D, Cuttaia, F, D’Alessandro, G, Dachlythra, K, de Bernardis, P, de Haan, T, de la Hoz, E, De Petris, M, Della Torre, S, Daz Garca, J, Dickinson, C, Diego-Palazuelos, P, Dobbs, M, Dotani, T, Douillet, D, Doumayrou, E, Duband, L, Ducout, A, Duff, S, Duval, J, Ebisawa, K, Elleflot, T, Eriksen, H, Errard, J, Essinger-Hileman, T, Farrens, S, Finelli, F, Flauger, R, Fleury-Frenette, K, Franceschet, C, Fuskeland, U, Galli, L, Galli, S, Galloway, M, Ganga, K, Gao, J, Genova-Santos, R, Georges, M, Gerbino, M, Gervasi, M, Ghigna, T, Giardiello, S, Gjerlw, E, Gonzles, R, Gradziel, M, Grain, J, Grandsire, L, Grupp, F, Gruppuso, A, Gudmundsson, J, Halverson, N, Hamilton, J, Hargrave, P, Hasebe, T, Hasegawa, M, Hattori, M, Hazumi, M, Henrot-Versill, S, Hensley, B, Herman, D, Herranz, D, Hilton, G, Hivon, E, Hlozek, R, Hoang, D, Hornsby, A, Hoshino, Y, Ichiki, K, Iida, T, Ikemoto, T, Imada, H, Ishimura, K, Ishino, H, Jaehnig, G, Jones, M, Kaga, T, Kashima, S, Katayama, N, Kato, A, Kawasaki, T, Keskitalo, R, Kintziger, C, Kisner, T, Kobayashi, Y, Kogiso, N, Kogut, A, Kohri, K, Komatsu, E, Komatsu, K, Konishi, K, Krachmalnicoff, N, Kreykenbohm, I, Kuo, C, Kushino, A, Lamagna, L, Lanen, J, Laquaniello, G, Lattanzi, M, Lee, A, Leloup, C, Levrier, F, Linder, E, Link, M, Lonappan, A, Louis, T, Luzzi, G, Macias-Perez, J, Maciaszek, T, Maffei, B, Maino, D, Maki, M, Mandelli, S, Maris, M, Marquet, B, Martnez-Gonzlez, E, Martire, F, Masi, S, Massa, M, Masuzawa, M, Matarrese, S, Matsuda, F, Matsumura, T, Mele, L, Mennella, A, Migliaccio, M, Minami, Y, Mitsuda, K, Moggi, A, Monelli, M, Monfardini, A, Montgomery, J, Montier, L, Morgante, G, Mot, B, Murata, Y, Murphy, J, Nagai, M, Nagano, Y, Nagasaki, T, Nagata, R, Nakamura, S, Nakano, R, Namikawa, T, Nati, F, Natoli, P, Nerval, S, Neto Godry Farias, N, Nishibori, T, Nishino, H, Noviello, F, O’Neil, G, O’Sullivan, C, Odagiri, K, Ochi, H, Ogawa, H, Oguri, S, Ohsaki, H, Ohta, I, Okada, N, Pagano, L, Paiella, A, Paoletti, D, Pascual Cisneros, G, Passerini, A, Patanchon, G, Pelgrim, V, Peloton, J, Pettorino, V, Piacentini, F, Piat, M, Piccirilli, G, Pinsard, F, Pisano, G, Plesseria, J, Polenta, G, Poletti, D, Prouv, T, Puglisi, G, Rambaud, D, Raum, C, Realini, S, Reinecke, M, Reintsema, C, Remazeilles, M, Ritacco, A, Rosier, P, Roudil, G, Rubino-Martin, J, Russell, M, Sakurai, H, Sakurai, Y, Sandri, M, Sasaki, M, Savini, G, Scott, D, Seibert, J, Sekimoto, Y, Sherwin, B, Shinozaki, K, Shiraishi, M, Shirron, P, Shitvov, A, Signorelli, G, Smecher, G, Spinella, F, Starck, J, Stever, S, Stompor, R, Sudiwala, R, Sugiyama, S, Sullivan, R, Suzuki, A, Suzuki, J, Suzuki, T, Svalheim, T, Switzer, E, Takaku, R, Takakura, H, Takakura, S, Takase, Y, Takeda, Y, Tartari, A, Tavagnacco, D, Taylor, A, Taylor, E, Terao, Y, Terenzi, L, Thermeau, J, Thommesen, H, Thompson, K, Thorne, B, Toda, T, Tomasi, M, Tominaga, M, Trappe, N, Tristram, M, Tsuji, M, Tsujimoto, M, Tucker, C, Ueki, R, Ullom, J, Umemori, K, Vacher, L, Van Lanen, J, Vermeulen, G, Vielva, P, Villa, F, Vissers, M, Vittorio, N, Wandelt, B, Wang, W, Wehus, I, Weller, J, Westbrook, B, Weymann-Despres, G, Wilms, J, Winter, B, Wollack, E, Yamasaki, N, Yoshida, T, Yumoto, J, Watanuki, K, Zacchei, A, Zannoni, M, Zonca, A, and National Aeronautics and Space Administration (US)

Subjects
CMB, TES, OMT, Low temperature detector, Bolometer, FIS/05 - ASTRONOMIA E ASTROFISICA, Settore FIS/05 - Astronomia e Astrofisica, General Materials Science, Condensed Matter Physics, CMB, TES, OMT, Low temperature detector, Bolometer, Atomic and Molecular Physics, and Optics
Abstract

et al., Feedhorn- and orthomode transducer- (OMT) coupled transition edge sensor (TES) bolometers have been designed and micro-fabricated to meet the optical specifications of the LiteBIRD high frequency telescope (HFT) focal plane. We discuss the design and optical characterization of two LiteBIRD HFT detector types: dual-polarization, dual-frequency-band pixels with 195/280 GHz and 235/337 GHz band centers. Results show well-matched passbands between orthogonal polarization channels and frequency centers within 3% of the design values. The optical efficiency of each frequency channel is conservatively reported to be within the range 0.64−0.72, determined from the response to a cryogenic, temperature-controlled thermal source. These values are in good agreement with expectations and either exceed or are within 10% of the values used in the LiteBIRD sensitivity forecast. Lastly, we report a measurement of loss in Nb/SiNx/Nb microstrip at 100 mK and over the frequency range 200–350 GHz, which is comparable to values previously reported in the literature., This work is supported by NASA under grant no. 80NSSC18K0132.

Published
2022

5. Serum albumin binds beta- and alpha-monoolein in vitro

Author

S M, Duff, S, Kalambur, and E, Boyle-Roden

Subjects
Carbon Isotopes, Magnetic Resonance Spectroscopy, Nephelometry and Turbidimetry, Spectrophotometry, Animals, Cattle, Serum Albumin, Bovine, Glycerides
Abstract

We investigated the interaction of bovine serum albumin (BSA) and monoolein (MO) and estimated the number of BSA binding sites for the alpha- and beta-isomers of MO. The turbidity of increasing concentrations of aqueous dispersions of alpha-MO and beta-MO in the presence and absence of BSA was measured in triplicate by absorption spectrophotometry. Aqueous dispersions of [13C(1)]MO and [13C(1)]MO/BSA mixtures at molar ratios of 1:1, 3:1 and 5:1 were analyzed in duplicate by [13C]nuclear magnetic resonance (NMR) at pH 7.4 and 36 degrees C. BSA bound significantly more beta-MO than alpha-MO at 15 min: 5.4 +/- 0.42 and 3.3 +/- 0.60 mol MO/mol BSA, respectively (P:0.05). [13C]NMR spectra of the 1:1 molar ratio of [13C(1)]MO /BSA exhibited a single carbonyl peak at 175.19 ppm, whereas spectra of 3:1 and 5:1 molar ratios exhibited three peaks between 172 and 174 (ppm), each distinct from carbonyl resonances of either [13C(1)]MO dispersed in water, 176.72 (ppm) or BSA alone. The intensities of individual peaks, but not their chemical shift values, varied between 3:1 and 5:1 molar ratios, indicating that BSA has at least three MO binding sites and may bind up to five molecules of MO per molecule. This study confirms that serum albumin binds MO in vitro and supports the theory that albumin transports monoglycerides produced by lipoprotein lipase hydrolysis of triglyceride.

Published
2001

6. Expression, purification, and properties of recombinant barley (Hordeum sp.) hemoglobin. Optical spectra and reactions with gaseous ligands

Author

S M, Duff, J B, Wittenberg, and R D, Hill

Subjects
Hemeproteins, Carbon Monoxide, Recombinant Fusion Proteins, Molecular Sequence Data, Hordeum, Ligands, Electron Transport, Molecular Weight, Oxygen, Hemoglobins, Kinetics, Spectrophotometry, Seeds, Escherichia coli, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Dimerization, Plant Proteins
Abstract

A cDNA encoding barley hemoglobin (Hb) has been cloned into pUC 19 and expressed in Escherichia coli. The resulting fusion protein has five extra amino acids at the N terminus compared with the native protein, resulting in a protein of 168 amino acids (18.5 kDa). The recombinant Hb is expressed constitutively. Extracts made from the bacteria containing the recombinant fusion construct contain a protein with a subunit molecular mass of approximately 18.5 kDa comprising approximately 5% total soluble protein. Recombinant Hb was purified to homogeneity according to SDS-polyacrylamide gel electrophoresis by sequential polyethylene glycol precipitation and fast protein liquid chromatography. Its native molecular mass as assessed by fast protein liquid chromatography-size exclusion was 40 kDa suggesting that it is a dimer. Ligand binding experiments demonstrate that 1) barley Hb has a very slow oxygen dissociation rate constant (0.0272 s-1) relative to other Hbs, and 2) the heme of ferrous and ferric forms of the barley Hb is low spin six-coordinate. The subunit structure, optical spectrum, and oxygen dissociation rate of native barley hemoglobin are indistinguishable from those obtained for the recombinant protein. The implications of these kinetic data on the in vivo function of barley Hb are discussed.

Published
1997

7. Phosphate starvation-inducible synthesis of the alpha-subunit of the pyrophosphate-dependent phosphofructokinase in black mustard suspension cells

Author

M E, Theodorou, F A, Cornel, S M, Duff, and W C, Plaxton

Subjects
Enzyme Activation, Kinetics, Enzyme Induction, Blotting, Western, Phosphotransferases, Fructosediphosphates, Brassica, Precipitin Tests, Cells, Cultured, Phosphates
Abstract

PP(i)-dependent phosphofructokinase (PFP) activity, measured in the forward direction, increased approximately 19-fold when suspension cell cultures of black mustard (Brassica nigra) were subjected to 18 days of P(i) deprivation. Fructose 2,6-bisphosphate (2 microM) elicited a 10-fold activation of PFP from P(i)-deficient cells, compared to only a 2-fold activation of the enzyme from nutrient-sufficient cells. Also, PFP from P(i)-starved cells exhibited a greater affinity for the activator (Ka = 0.09 microM) than the enzyme from nutrient-sufficient cells (Ka = 0.32 microM). Western blots of extracts from P(i)-deficient cells were probed with rabbit anti-(potato tuber PFP) immune serum and revealed equal intensity staining immunoreactive polypeptides of M(r) 66,000 (alpha-subunit) and 60,000 (beta-subunit) that co-migrated with the alpha- and beta-subunits of homogeneous potato tuber PFP. By contrast, only the M(r) 60,000 beta-subunit was observed on immunoblots of extracts prepared from nutrient-sufficient cells. Quantification of immunoblots indicated that in black mustard cells experiencing transition from P(i) sufficiency to deficiency or vice versa, the relative amount of immunoreactive alpha-subunit correlated with the degree of activation of PFP by fructose 2,6-bisphosphate. These observations provide additional evidence that (i) plant PFP is an adaptive enzyme that may function in glycolysis during P(i) deprivation, and (ii) the alpha-subunit acts as a regulatory protein in controlling the catalytic activity of the beta-subunit and its regulation by fructose 2,6-bisphosphate.

Published
1992

8. Site-directed mutagenesis of the phosphorylatable serine (Ser8) in C4 phosphoenolpyruvate carboxylase from sorghum. The effect of negative charge at position 8

Author

Y H, Wang, S M, Duff, L, Lepiniec, C, Crétin, G, Sarath, S A, Condon, J, Vidal, P, Gadal, and R, Chollet

Subjects
Kinetics, Base Sequence, Light, Oligodeoxyribonucleotides, Molecular Sequence Data, Mutagenesis, Site-Directed, Serine, Amino Acid Sequence, Cloning, Molecular, Darkness, Plants, Phosphoenolpyruvate Carboxylase, Recombinant Proteins
Abstract

The properties of the dephospho and in vitro phosphorylated forms of recombinant sorghum phosphoenolpyruvate carboxylase have been compared with those of the authentic dark (dephospho) and light (phospho) leaf enzyme forms and two mutant enzymes in which the phosphorylatable serine residue (Ser8) has been changed by site-directed mutagenesis to Cys (S8C) or Asp (S8D). Kinetic analysis of the purified recombinant, mutant, and leaf enzyme forms at pH 8.0 indicated virtually identical Vmax, apparent Km (phosphoenolpyruvate), and half-maximal activation (glucose 6-P) values of about 44 units/mg, 1.1 mM, and 0.23 mM, respectively. In contrast, the Ser8, S8C, and dark leaf enzymes were about 3-fold more sensitive to inhibition by L-malate at pH 7.3 than the Ser8-P, S8D, and light leaf enzyme forms. These comparative results indicate that: (i) Ser8 is an important determinant in the regulation of sorghum phosphoenolpyruvate carboxylase activity by negative (L-malate), but not positive (glucose 6-phosphate) metabolite effectors, (ii) phosphorylation of this target residue can be functionally mimicked by Asp, but not Cys, and (iii) negative charge contributes to the effect of regulatory phosphorylation on this C4-photosynthesis enzyme.

Published
1992

9. A clinical and virological study of acute mouth ulcers

Author

C P, Anyon, S M, Duff, and W, Hamilton

Subjects
Male, Herpangina, Child, Preschool, Acute Disease, Viruses, Coxsackievirus Infections, Humans, Female, Stomatitis, Aphthous, Child, Mouth Diseases, Ulcer
Published
1967

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