263 research outputs found
Carmina Catulli, quibus accessere Tibulli. Sulpiciae Elegiae. Propertii Carmina. et Statii Sylvae
No full textComprend : Sulpiciae elegiae ; Propertii carmina ; Statii sylva
Oeuvres complètes d'Horace, de Juvénal, de Perse, de Sulpicia, de Turnus, de Catulle, de Properce, de Gallus et Maximien, de Tibulle, de Phèdre et de Syrus : avec la traduction en français / publiées sous la direction de M. Nisard,...
No full textCollection : Collection des auteurs latins, avec la traduction en françaisCollection : Collection des auteurs latins, avec la traduction en françaisComprend : Sentences ; Satir
D. Junii Juvenalis sexdecim Satirae. Volumen 2 / , ad codices parisinos recensitae, cum interpretatione latina, lectionum varietate, notis rupertianis, excursibus et indice absoluto, quibus plurima subjunxit additamenta N.-E. Lemaire
No full text[Satires (latin). 1823]Collection : Bibliotheca classica latinaCollection : Bibliotheca classica latinaComprend : A. Persii Flacci sex satirae ; Caii Lucilii Suessani Auruncani unius e quatuor latinis satiricis satirarum quae supersunt fragmenta ; Sulpiciae satiricon carmen ; D. Junii Juvenalis vita ; Auli Persii Flacci vit
D. Junii Juvenalis sexdecim Satirae. Volumen 1 / , ad codices parisinos recensitae, cum interpretatione latina, lectionum varietate, notis rupertianis, excursibus et indice absoluto, quibus plurima subjunxit additamenta N.-E. Lemaire
No full text[Satires (latin). 1823]Collection : Bibliotheca classica latinaCollection : Bibliotheca classica latinaComprend : A. Persii Flacci sex satirae ; Caii Lucilii Suessani Auruncani unius e quatuor latinis satiricis satirarum quae supersunt fragmenta ; Sulpiciae satiricon carmen ; D. Junii Juvenalis vita ; Auli Persii Flacci vitaContient une table des matière
Tax ubiquitylation and sumoylation control critical cytoplasmic and nuclear steps of NF-κB activation
No full textThe Tax oncoprotein plays a crucial role in the proliferation and transformation of human T-cell leukemia virus type I (HTLV-I)-infected T lymphocytes through various mechanisms, including activation of the nuclear factor (NF)-κB pathway. We found that cytoplasmic ubiquitylation of Tax C-terminal lysines is critical for Tax binding to the IkappaB kinase complex and subsequent nuclear translocation of RelA. Conversely, we demonstrate that the same lysines are sumoylated in the nucleus, an event required for the formation of RelA-p300-enriched Tax nuclear bodies and full NF-κB transcriptional activation. In contrast, Tax ubiquitylation and sumoylation are dispensable for its activation of cyclic adenosine monophosphate response element binding protein (CREB)-dependent genes. Thus, ubiquitylation and sumoylation of the same residues of Tax regulate 2 essential steps controlling NF-κB activation, demonstrating how these post-translational modifications can cooperate to promote Tax-induced transformation. © 2006 by The American Society of Hematology.Bex F, 1998, MOL CELL BIOL, V18, P2392; Bres V, 2003, NAT CELL BIOL, V5, P754, DOI 10.1038-ncb1023; Carter RS, 2003, J BIOL CHEM, V278, P48903, DOI 10.1074-jbc.M310686200; Chiari E, 2004, J VIROL, V78, P11823, DOI 10.1128-JVI.78.21.11823-11832.2004; Conaway RC, 2002, SCIENCE, V296, P1254, DOI 10.1126-science.1067466; Desterro JMP, 1998, MOL CELL, V2, P233, DOI 10.1016-S1097-2765(00)80133-1; Ghosh S, 2002, CELL, V109, pS81, DOI 10.1016-S0092-8674(02)00703-1; Grassmann R, 2005, ONCOGENE, V24, P5976, DOI 10.1038-sj.onc.1208978; Harhaj EW, 1999, J BIOL CHEM, V274, P22911, DOI 10.1074-jbc.274.33.22911; Harrod R, 1998, MOL CELL BIOL, V18, P5052; Hilgarth RS, 2004, J BIOL CHEM, V279, P53899, DOI 10.1074-jbc.R400021200; Hoege C, 2002, NATURE, V419, P135, DOI 10.1038-nature00991; Huang TT, 2003, CELL, V115, P565, DOI 10.1016-S0092-8674(03)00895-X; Li XH, 2000, AIDS RES HUM RETROV, V16, P1583, DOI 10.1089-08892220050192994; Meertens L, 2004, ONCOGENE, V23, P5447, DOI 10.1038-sj.onc.1207719; Nasr R, 2003, BLOOD, V101, P4576, DOI 10.1182-blood-2002-09-2986; NASR R, 2005, ONCOGENE, V13, P419; Peloponese JM, 2004, J VIROL, V78, P11686, DOI 10.1128-JVI.78.21.11686-11695.2004; PICKART CM, 1994, J BIOL CHEM, V269, P7115; Robek MD, 1999, J VIROL, V73, P4856; SMITH MR, 1991, J CLIN INVEST, V88, P1038, DOI 10.1172-JCI115364; Sun SC, 2005, ONCOGENE, V24, P5952, DOI 10.1038-sj.onc.1208969; Takahashi Y, 2004, ONCOGENE, V23, P2819, DOI 10.1038-sj.onc.1207533; Yamaoka S, 1998, CELL, V93, P1231, DOI 10.1016-S0092-8674(00)81466-X58595
Modification of Loop 1 Affects the Nucleotide Binding Properties of Myo1c, the Adaptation Motor in the Inner Ear
Get PDFMyo1c is one of eight members of the mammalian myosin I family of actin-associated molecular motors. In stereocilia of the hair cells in the inner ear, Myo1c presumably serves as the adaptation motor, which regulates the opening and closing of transduction channels. Although there is conservation of sequence and structure among all myosins in the N-terminal motor domain, which contains the nucleotide- and actin-binding sites, some differences include the length and composition of surface loops, including loop 1, which lies near the nucleotide-binding domain. To investigate the role of loop 1, we expressed in insect cells mutants of a truncated form of Myo1c, Myo1c1IQ, as well as chimeras of Myo1c1IQ with the analogous loop from other myosins. We found that replacement of the charged residues in loop 1 with alanines or the whole loop with a series of alanines did not alter the ATPase activity, transient kinetics properties, or Ca2+ sensitivity of Myo1c1IQ. Substitution of loop 1 with that of the corresponding region from tonic smooth muscle myosin II (Myo1c1IQ-tonic) or replacement with a single glycine (Myo1c1IQ-G) accelerated the release of ADP from A.M 2?3-fold in Ca2+, whereas substitution with loop 1 from phasic muscle myosin II (Myo1c1IQ-phasic) accelerated the release of ADP 35-fold. Motility assays with chimeras containing a single ?-helix, or SAH, domain showed that Myo1cSAH-tonic translocated actin in vitro twice as fast as Myo1cSAH-WT and 3-fold faster than Myo1cSAH-G. The studies show that changes induced in Myo1c via modification of loop 1 showed no resemblance to the behavior of the loop donor myosins or to the changes previously observed with similar Myo1b chimeras
High-precision photometry by telescope defocussing - VI. WASP-24, WASP-25 and WASP-26
Get PDFThe research leading to these results has received funding from the European Community's Seventh Framework Programme (FP7/2007-2013/) under grant agreement nos. 229517 and 268421. This publication was supported by grants NPRP 09-476-1-078 and NPRP X-019-1-006 from Qatar National Research Fund (a member of Qatar Foundation). TCH acknowledges financial support from the Korea Research Council for Fundamental Science and Technology (KRCF) through the Young Research Scientist Fellowship Programme and is supported by the KASI (Korea Astronomy and Space Science Institute) grant 2012-1-410-02/2013-9-400-00. SG, XW and XF acknowledge the support from NSFC under the grant no. 10873031. The research is supported by the ASTERISK project (ASTERoseismic Investigations with SONG and Kepler) funded by the European Research Council (grant agreement no. 267864). DR, YD, AE, FF (ARC), OW (FNRS research fellow) and J Surdej acknowledge support from the Communauté française de Belgique – Actions de recherche concertées – Académie Wallonie-Europe.We present time series photometric observations of 13 transits in the planetary systems WASP-24, WASP-25 and WASP-26. All three systems have orbital obliquity measurements, WASP-24 and WASP-26 have been observed with Spitzer, and WASP-25 was previously comparatively neglected. Our light curves were obtained using the telescope-defocussing method and have scatters of 0.5–1.2 mmag relative to their best-fitting geometric models. We use these data to measure the physical properties and orbital ephemerides of the systems to high precision, finding that our improved measurements are in good agreement with previous studies. High-resolution Lucky Imaging observations of all three targets show no evidence for faint stars close enough to contaminate our photometry. We confirm the eclipsing nature of the star closest to WASP-24 and present the detection of a detached eclipsing binary within 4.25 arcmin of WASP-26.Peer reviewe
Eradication of acute promyelocytic leukemia-initiating cells by PML-RARA-targeting
No full textAcute promyelocytic leukemia (APL) is characterized by a t(15;17) translocation that yields a PML-RARA fusion protein. Expression of PML-RARA, a potent transcriptional repressor, induces APL in mice. Both retinoic acid (RA) and arsenic trioxide directly target PML-RARA-mediated transcriptional repression and protein stability, inducing rapid differentiation of the promyelocytes and clinical remission in most APL patients. RA also triggers growth arrest and progressive clearance of leukemia initiating cells (LIC), both ex vivo and in vivo. Suboptimal RA concentrations or expression of the PLZF-RARA variant allows complete RA-induced differentiation, but neither LIC clearance nor disease remission. Thus, RA-induced differentiation and LIC clearance may be uncoupled. The RA-arsenic trioxide association, which dramatically synergizes for PML-RARA degradation but not for differentiation, rapidly clears LIC in a proteasome-dependent manner, resulting in APL eradication in murine models and patients. Collectively, these results demonstrate that LIC clearance, which mirrors PML-RARA degradation, is the primary basis for APL cure by the RA-arsenic trioxide association, rather than differentiation. Oncogene degradation could be a generally applicable therapeutic strategy to clear LICs in several types of tumors. © 2010 The Japanese Society of Hematology.Altucci L, 2005, CANCER RES, V65, P8754, DOI 10.1158-0008-5472; Bernardi R, 2002, ONCOGENE, V21, P3445, DOI 10.1038-sj-onc-1205313; Bernardi R, 2007, NAT REV MOL CELL BIO, V8, P1006, DOI 10.1038-nrm2277; Boukarabila H, 2009, GENE DEV, V23, P1195, DOI 10.1101-gad.512009; Bour G, 2005, P NATL ACAD SCI USA, V102, P16608, DOI 10.1073-pnas.0505556102; Bruck N, 2009, EMBO J, V28, P34, DOI 10.1038-emboj.2008.256; Cassinat Bruno, 2006, Haematologica, V91, pECR58; Chen GQ, 1996, BLOOD, V88, P1052; Chen GQ, 1997, BLOOD, V89, P3345; CHEN Z, 1993, EMBO J, V12, P1161; Degos L, 2001, ONCOGENE, V20, P7140, DOI 10.1038-sj.onc.1204763; DEGOS L, 1995, BLOOD, V85, P2643; Douer D, 2001, BLOOD, V97, P73, DOI 10.1182-blood.V97.1.73; Du CC, 1999, BLOOD, V94, P793; Duprez E, 1996, ONCOGENE, V12, P2451; DYCK JA, 1994, CELL, V76, P333, DOI 10.1016-0092-8674(94)90340-9; Estey E, 2006, BLOOD, V107, P3469, DOI 10.1182-blood-2005-10-4006; Gaillard E, 2006, P NATL ACAD SCI USA, V103, P9548, DOI 10.1073-pnas.0509717103; Ghavamzadeh A, 2006, ANN ONCOL, V17, P131, DOI 10.1093-annonc-mdj019; Grignani F, 1998, NATURE, V391, P815; Guibal FC, 2009, BLOOD, V114, P5415, DOI 10.1182-blood-2008-10-182071; Guillemin MC, 2002, J EXP MED, V196, P1373, DOI 10.1084-jem.20021129; He LZ, 1998, NAT GENET, V18, P126, DOI 10.1038-ng0298-126; Hu J, 2009, P NATL ACAD SCI USA, V106, P3342, DOI 10.1073-pnas.0813280106; HUANG ME, 1988, BLOOD, V72, P567; Ito K, 2008, NATURE, V453, P1072, DOI 10.1038-nature07016; Jing YK, 2001, BLOOD, V97, P264, DOI 10.1182-blood.V97.1.264; Kamashev D.E., 2004, J EXP MED, V199, P1; Kogan SC, 2009, CANCER CELL, V15, P7, DOI 10.1016-j.ccr.2008.12.012; KOKEN MHM, 1994, EMBO J, V13, P1073; Lallemand-Breitenbach V, 2008, NAT CELL BIOL, V10, P547, DOI 10.1038-ncb1717; Lallemand-Breitenbach V, 1999, J EXP MED, V189, P1043, DOI 10.1084-jem.189.7.1043; Lallemand-Breitenbach V, 2005, NAT REV CANCER, V5, P821, DOI 10.1038-nrc1719; Lallemand-Breitenbach V, 2001, J EXP MED, V193, P1361, DOI 10.1084-jem.193.12.1361; LALLEMANDBREITE.V, 2010, CSH PERSPEC IN PRESS; Licht JD, 2006, CANCER CELL, V9, P73, DOI 10.1016-j.ccr.2006.01.024; Licht JD, 2009, NEW ENGL J MED, V360, P928, DOI 10.1056-NEJMcibr0810371; LICHT JD, 1995, BLOOD, V85, P1083; Lin RJ, 2000, MOL CELL, V5, P821, DOI 10.1016-S1097-2765(00)80322-6; Lin RJ, 1998, NATURE, V391, P811; Martens JHA, 2010, CANCER CELL, V17, P173, DOI 10.1016-j.ccr.2009.12.042; Mathews V, 2006, BLOOD, V107, P2627, DOI 10.1182-blood2005-08-3532; Melnick A, 1999, BLOOD, V93, P3167; Minucci S, 2000, MOL CELL, V5, P811, DOI 10.1016-S1097-2765(00)80321-4; Nasr R, 2009, CLIN CANCER RES, V15, P6321, DOI 10.1158-1078-0432.CCR-09-0209; Nasr R, 2008, NAT MED, V14, P1333, DOI 10.1038-nm.1891; Nervi C, 1998, BLOOD, V92, P2244; Quenech'Du N, 1998, LEUKEMIA, V12, P1829, DOI 10.1038-sj.leu.2401171; Quignon F, 1997, BBA-REV CANCER, V1333, pM53, DOI 10.1016-S0304-419X(97)00025-5; Rego EM, 2000, P NATL ACAD SCI USA, V97, P10173, DOI 10.1073-pnas.180290497; Rice KL, 2009, BLOOD, V114, P5499, DOI 10.1182-blood-2009-03-206524; RochetteEgly C, 1997, CELL, V90, P97, DOI 10.1016-S0092-8674(00)80317-7; Shao WL, 1998, J NATL CANCER I, V90, P124, DOI 10.1093-jnci-90.2.124; Shen ZX, 2004, P NATL ACAD SCI USA, V101, P5328, DOI 10.1073-pnas.0400053101; Tatham MH, 2008, NAT CELL BIOL, V10, P538, DOI 10.1038-ncb1716; Tsimberidou AM, 2006, LEUKEMIA LYMPHOMA, V47, P1062, DOI 10.1080-10428190500463932; Villa R, 2007, CANCER CELL, V11, P513, DOI 10.1016-j.ccr.2007.04.009; Wang JCY, 2005, TRENDS CELL BIOL, V15, P494, DOI 10.1016-j.tcb.2005.07.004; Wang ZY, 2008, BLOOD, V111, P2505, DOI 10.1182-blood-2007-07-102798; WARRELL RP, 1993, NEW ENGL J MED, V329, P177, DOI 10.1056-NEJM199307153290307; Wojiski S, 2009, LEUKEMIA, V23, P1462, DOI 10.1038-leu.2009.63; Zeisig BB, 2007, CANCER CELL, V12, P36, DOI 10.1016-j.ccr.2007.06.006; Zheng XM, 2007, HAEMATOL-HEMATOL J, V92, P323, DOI 10.3324-haematol.10541; Zhu J, 2005, CANCER CELL, V7, P143, DOI 10.1016-j.ccr.2005.01.005; Zhu J, 2001, ONCOGENE, V20, P7257, DOI 10.1038-sj.onc.1204852; Zhu J, 1997, P NATL ACAD SCI USA, V94, P3978, DOI 10.1073-pnas.94.8.3978; Zhu J, 2007, CANCER CELL, V12, P23, DOI 10.1016-j.ccr.2007.06.004; Zhu J, 1999, P NATL ACAD SCI USA, V96, P14807, DOI 10.1073-pnas.96.26.14807; Zhu Q, 2002, BLOOD, V99, P101418181
Proapoptotic regimes for HTLV-I-transformed cells: targeting Tax and the NF-κB pathway
No full text[No abstract available]Adams J, 2003, CANCER TREAT REV, V29, P3, DOI 10.1016-S0305-7372(03)00081-1; Arnulf B, 2002, BLOOD, V100, P4129, DOI 10.1182-blood-2001-12-0372; BAEUERLE PA, 1994, ANNU REV IMMUNOL, V12, P141, DOI 10.1146-annurev.immunol.12.1.141; Baldwin AS, 1996, ANNU REV IMMUNOL, V14, P649, DOI 10.1146-annurev.immunol.14.1.649; BALLARD DW, 1988, SCIENCE, V241, P1652, DOI 10.1126-science.2843985; Bangham CRM, 2000, CURR OPIN IMMUNOL, V12, P397, DOI 10.1016-S0952-7915(00)00107-2; Bazarbachi A, 1999, BLOOD, V93, P278; Bazarbachi A, 2001, VIRUS RES, V78, P79, DOI 10.1016-S0168-1702(01)00286-6; Bazarbachi A, 2004, CANCER RES, V64, P2039, DOI 10.1158-0008-5472.CAN-03-2390; Bazarbachi A, 2004, LANCET ONCOL, V5, P664, DOI 10.1016-S1470-2045(04)01608-0; BERAUD C, 1996, J ACQ IMMUN DEF SYND, V13, P76; Bex F, 1998, MOL CELL BIOL, V18, P2392; Bex F, 1997, J VIROL, V71, P3484; BOES B, 1994, J EXP MED, V179, P901, DOI 10.1084-jem.179.3.901; Brauweiler A, 1997, VIROLOGY, V231, P135, DOI 10.1006-viro.1997.8509; Burton M, 2000, J VIROL, V74, P2351, DOI 10.1128-JVI.74.5.2351-2364.2000; Caamano JH, 1996, MOL CELL BIOL, V16, P1342; Cascio P, 2002, EMBO J, V21, P2636, DOI 10.1093-emboj-21.11.2636; Chen GQ, 1996, BLOOD, V88, P1052; Chen ZJ, 1996, CELL, V84, P853, DOI 10.1016-S0092-8674(00)81064-8; Chiari E, 2004, J VIROL, V78, P11823, DOI 10.1128-JVI.78.21.11823-11832.2004; Chu ZL, 1998, J BIOL CHEM, V273, P15891, DOI 10.1074-jbc.273.26.15891; Ciechanover A, 2004, TRENDS CELL BIOL, V14, P103, DOI 10.1016-j.tcb.2004.01.004; Dewan MZ, 2003, J VIROL, V77, P5286, DOI 10.1128-JVI.77.9.5286-5294.2003; El-Sabban ME, 2002, BLOOD, V99, P3383, DOI 10.1182-blood.V99.9.3383; El-Sabban ME, 2000, BLOOD, V96, P2849; Fu DX, 2003, J BIOL CHEM, V278, P1487, DOI 10.1074-jbc.M210631200; Gabet AS, 2003, ONCOGENE, V22, P3734, DOI 10.1038-sj.onc.1206468; GESSAIN A, 1985, LANCET, V2, P407; Gessain A, 1996, ADV VIRUS RES, V47, P377, DOI 10.1016-S0065-3527(08)60740-X; Good LF, 1996, J VIROL, V70, P2730; GRASSMANN R, 1989, P NATL ACAD SCI USA, V86, P3351, DOI 10.1073-pnas.86.9.3351; Harhaj EW, 1998, J BIOL CHEM, V273, P25185, DOI 10.1074-jbc.273.39.25185; Hemelaar J, 2001, J VIROL, V75, P11106, DOI 10.1128-JVI.75.22.11106-11115.2001; HENKEL T, 1992, CELL, V68, P1121, DOI 10.1016-0092-8674(92)90083-O; Hermine O, 2004, HEMATOL J, V5, P130, DOI 10.1038-sj.thj.6200374; Hershko A, 1998, ANNU REV BIOCHEM, V67, P425, DOI 10.1146-annurev.biochem.67.1.425; HINUMA Y, 1982, GAN TO KAGAKU RYOHO, V8, P1313; HIRAI H, 1994, P NATL ACAD SCI USA, V91, P3584, DOI 10.1073-pnas.91.9.3584; HIRAI H, 1992, ONCOGENE, V7, P1737; Huang GJ, 2002, FEBS LETT, V531, P494, DOI 10.1016-S0014-5793(02)03590-1; Ikeda K, 1999, INT J CANCER, V82, P599, DOI 10.1002-(SICI)1097-0215(19990812)82:4599::AID-IJC213.0.CO;2-R; INOUE J, 1992, CELL, V68, P1109, DOI 10.1016-0092-8674(92)90082-N; Jeang KT, 2004, J BIOL CHEM, V279, P31991, DOI 10.1074-jbc.R400009200; JEANG KT, 1990, SCIENCE, V247, P1082, DOI 10.1126-science.2309119; JENTSCH S, 1995, CELL, V82, P881, DOI 10.1016-0092-8674(95)90021-7; Kawakami A, 1999, BLOOD, V94, P3847; Lallemand-Breitenbach V, 2001, J EXP MED, V193, P1361, DOI 10.1084-jem.193.12.1361; LANOIX J, 1994, ONCOGENE, V9, P841; Lau A, 1998, BLOOD, V91, P2467; LEBAIL O, 1993, EMBO J, V12, P5043; Lomas M, 2002, J GEN VIROL, V83, P641; Lonard DM, 2000, MOL CELL, V5, P939, DOI 10.1016-S1097-2765(00)80259-2; Mahieux R, 2000, AIDS RES HUM RETROV, V16, P1677, DOI 10.1089-08892220050193137; MERCURIO F, 1993, GENE DEV, V7, P705, DOI 10.1101-gad.7.4.705; Mesnard JM, 1999, VIROLOGY, V257, P277, DOI 10.1006-viro.1999.9685; Mitra-Kaushik S, 2004, BLOOD, V104, P802, DOI 10.1182-blood-2003-11-3967; Mori N, 2002, BLOOD, V100, P1828, DOI 10.1182-blood-2002-01-0151; Mori N, 2001, VIRUS GENES, V22, P279, DOI 10.1023-A:1011158021749; Mortreux F, 2003, LEUKEMIA, V17, P26, DOI 10.1038-sj.leu.2402777; Nakano H, 1998, P NATL ACAD SCI USA, V95, P3537, DOI 10.1073-pnas.95.7.3537; Nasr R, 2003, BLOOD, V101, P4576, DOI 10.1182-blood-2002-09-2986; Nasr R, 2005, ONCOGENE, V24, P419, DOI 10.1038-sj.onc.1208212; NERENBERG M, 1987, SCIENCE, V237, P1324, DOI 10.1126-science.2888190; Neuveut C, 1998, MOL CELL BIOL, V18, P3620; NOLAN GP, 1993, MOL CELL BIOL, V13, P3557; Pahl HL, 1999, ONCOGENE, V18, P6853, DOI 10.1038-sj.onc.1203239; PALOMBELLA VJ, 1994, CELL, V78, P773, DOI 10.1016-S0092-8674(94)90482-0; PEPIN N, 1994, VIROLOGY, V204, P706, DOI 10.1006-viro.1994.1586; Pise-Masison CA, 2000, AIDS RES HUM RETROV, V16, P1669, DOI 10.1089-08892220050193128; Portis T, 2001, BLOOD, V98, P1200, DOI 10.1182-blood.V98.4.1200; Prajapati S, 2002, J BIOL CHEM, V277, P24331, DOI 10.1074-jbc.M201393200; Robek MD, 1999, J VIROL, V73, P4856; Rothwarf DM, 1998, NATURE, V395, P297; Rousset R, 1996, NATURE, V381, P328, DOI 10.1038-381328a0; RYSECK RP, 1992, MOL CELL BIOL, V12, P674; Satou Y, 2004, LEUKEMIA, V18, P1357, DOI 10.1038-sj.leu.2403400; Sun SC, 1999, ONCOGENE, V18, P6948, DOI 10.1038-sj.onc.1203220; SUN SC, 1994, MOL CELL BIOL, V14, P7377; Sun SC, 2003, CANCER METAST REV, V22, P405, DOI 10.1023-A:1023733231406; Suzuki T, 1999, VIROLOGY, V259, P384, DOI 10.1006-viro.1999.9760; SUZUKI T, 1995, ONCOGENE, V10, P1199; SUZUKI T, 1994, ONCOGENE, V9, P3099; Tamiya S, 1998, BLOOD, V91, P3935; Tan C, 2002, CANCER RES, V62, P1083; TANAKA A, 1990, P NATL ACAD SCI USA, V87, P1071, DOI 10.1073-pnas.87.3.1071; Thrower JS, 2000, EMBO J, V19, P94, DOI 10.1093-emboj-19.1.94; Tojima Y, 2000, NATURE, V404, P778; Uhlik M, 1998, J BIOL CHEM, V273, P21132, DOI 10.1074-jbc.273.33.21132; VERMA IM, 1995, GENE DEV, V9, P2723, DOI 10.1101-gad.9.22.2723; WALDMANN TA, 1993, BLOOD, V82, P1701; Whiteside ST, 1997, EMBO J, V16, P1413, DOI 10.1093-emboj-16.6.1413; Xiao GT, 2000, ONCOGENE, V19, P5198, DOI 10.1038-sj.onc.1203894; Xiao GT, 2001, EMBO J, V20, P6805, DOI 10.1093-emboj-20.23.6805; Yamaoka S, 1998, CELL, V93, P1231, DOI 10.1016-S0092-8674(00)81466-X; Yin MJ, 1998, CELL, V93, P875, DOI 10.1016-S0092-8674(00)81447-6; Yoshida M, 2001, ANNU REV IMMUNOL, V19, P475, DOI 10.1146-annurev.immunol.19.1.475; ZABEL U, 1990, CELL, V61, P255, DOI 10.1016-0092-8674(90)90806-P; Zhu J, 2001, ONCOGENE, V20, P7257, DOI 10.1038-sj.onc.120485223222
Effect of partial sodium replacement on physicochemical parameters of smoked sea bass during storage
No full textThe objective of this work was to study the effect of partial sodium replacement by potassium and packaging conditions on the physicochemical properties of smoked sea bass during cold storage. Sea bass fillets were salted with 100% NaCl (Na samples) or with 50% NaCl-50% KCl (Na:K samples), smoked, packaged under three different conditions (air, vacuum and modified atmosphere) and stored at 4 °C for 42 days. Physicochemical parameters, color and texture were periodically determined in the raw material and in smoked samples during cold storage. The smoking process led to a reduction in moisture, pH and aw values, and an increase in water holding capacity, ash and mineral contents. Smoked fish exhibited significant differences in color and texture as compared to fresh fish. The type of packaging had an effect on the pH, water holding capacity and texture. Samples in air exhibited the highest pH values and water holding capacity in these samples gradually decreased during storage. Textural parameters decreased during storage in samples packaged in vacuum and modified atmosphere. The pH of Na samples was initially higher than in Na:K samples, and this difference remained over the rest of the study. The type of salt did not affect the texture or other physicochemical parameters. © 2012 The Author(s).The revision of this paper was funded by the Universidad Politecnica de Valencia, Spain.Fuentes López, A.; Fernández Segovia, I.; Serra Belenguer, JA.; Barat Baviera, JM. (2012). Effect of partial sodium replacement on physicochemical parameters of smoked sea bass during storage. Food Science and Technology International. 18(3):207-217. doi:10.1177/1082013211415156S207217183Alasalvar, C., Taylor, K. D. ., Zubcov, E., Shahidi, F., & Alexis, M. (2002). Differentiation of cultured and wild sea bass (Dicentrarchus labrax): total lipid content, fatty acid and trace mineral composition. Food Chemistry, 79(2), 145-150. doi:10.1016/s0308-8146(02)00122-xAkse L, Gundersen B, Lauritzen K, Ofstad R, Solberg T. (1993). Saltfisk: saltmonding, utproving av analysemetoder, misfarget saltfisk. Tromsö: Fiskeriforskning, pp. 1–61.Birkeland, S., Bencze Rørå, A. M., Skåra, T., & Bjerkeng, B. (2004). Effects of cold smoking procedures and raw material characteristics on product yield and quality parameters of cold smoked Atlantic salmon (Salmo salar L.) fillets. Food Research International, 37(3), 273-286. doi:10.1016/j.foodres.2003.12.004Boskou, G., & Debevere, J. (2000). Shelf-life extension of cod fillets with an acetate buffer spray prior to packaging under modified atmospheres. Food Additives and Contaminants, 17(1), 17-25. doi:10.1080/026520300283559Cardinal, M., Knockaert, C., Torrissen, O., Sigurgisladottir, S., Mørkøre, T., Thomassen, M., & Luc Vallet, J. (2001). Relation of smoking parameters to the yield, colour and sensory quality of smoked Atlantic salmon (Salmo salar). Food Research International, 34(6), 537-550. doi:10.1016/s0963-9969(01)00069-2Chobanian, A. V., Bakris, G. L., Black, H. R., Cushman, W. C., Green, L. A., … Izzo, J. L. (2003). Seventh Report of the Joint National Committee on Prevention, Detection, Evaluation, and Treatment of High Blood Pressure. Hypertension, 42(6), 1206-1252. doi:10.1161/01.hyp.0000107251.49515.c2ERKAN, N., & OZDEN, O. (2007). Proximate composition and mineral contents in aqua cultured sea bass (Dicentrarchus labrax), sea bream (Sparus aurata) analyzed by ICP-MS. Food Chemistry, 102(3), 721-725. doi:10.1016/j.foodchem.2006.06.004FNB (Food and Nutrition Board-Institute of medicine of the national academies). (2005). Dietary Reference Intakes for Water, Potassium, Sodium, Chloride, and Sulfate. Washington: The National Academies Press, Inc, pp. 187–188.Fuentes, A., Fernández-Segovia, I., Serra, J. A., & Barat, J. M. (2010). Development of a smoked sea bass product with partial sodium replacement. LWT - Food Science and Technology, 43(9), 1426-1433. doi:10.1016/j.lwt.2010.04.013Fuentes, A., Fernández-Segovia, I., Barat, J. M., & Serra, J. A. (2011). Influence of sodium replacement and packaging on quality and shelf life of smoked sea bass (Dicentrarchus labrax L.). LWT - Food Science and Technology, 44(4), 917-923. doi:10.1016/j.lwt.2010.11.030Gelabert, J., Gou, P., Guerrero, L., & Arnau, J. (2003). Effect of sodium chloride replacement on some characteristics of fermented sausages. Meat Science, 65(2), 833-839. doi:10.1016/s0309-1740(02)00288-7Geleijnse, J. M., Witteman, J. C. M., Stijnen, T., Kloos, M. W., Hofman, A., & Grobbee, D. E. (2007). Sodium and potassium intake and risk of cardiovascular events and all-cause mortality: the Rotterdam Study. European Journal of Epidemiology, 22(11), 763-770. doi:10.1007/s10654-007-9186-2Gimeno, O., Astiasarán, I., & Bello, J. (2001). Influence of partial replacement of NaCl with KCl and CaCl2on microbiological evolution of dry fermented sausages. Food Microbiology, 18(3), 329-334. doi:10.1006/fmic.2001.0405GOMEZ-GUILLEN, M. C., MONTERO, P., HURTADO, O., & BORDERIAS, A. J. (2000). Biological Characteristics Affect the Quality of Farmed Atlantic Salmon and Smoked Muscle. Journal of Food Science, 65(1), 53-60. doi:10.1111/j.1365-2621.2000.tb15955.xGoulas, A. E., & Kontominas, M. G. (2007). Combined effect of light salting, modified atmosphere packaging and oregano essential oil on the shelf-life of sea bream (Sparus aurata): Biochemical and sensory attributes. Food Chemistry, 100(1), 287-296. doi:10.1016/j.foodchem.2005.09.045HAND, L. W., TERRELL, R. N., & SMITH, G. C. (1982). Effects of Chloride Salts on Physical, Chemical and Sensory Properties of Frankfurters. Journal of Food Science, 47(6), 1800-1802. doi:10.1111/j.1365-2621.1982.tb12886.xHASSAN, I. (1988). Processing of smoked common carp fish and its relation to some chemical, physical and organoleptic properties. Food Chemistry, 27(2), 95-106. doi:10.1016/0308-8146(88)90081-7He, F. J., & MacGregor, G. A. (2002). Effect of modest salt reduction on blood pressure: a meta-analysis of randomized trials. Implications for public health. Journal of Human Hypertension, 16(11), 761-770. doi:10.1038/sj.jhh.1001459Hultmann, L., Bencze Rørå, A. M., Steinsland, I., Skåra, T., & Rustad, T. (2004). Proteolytic activity and properties of proteins in smoked salmon (Salmo salar)—effects of smoking temperature. Food Chemistry, 85(3), 377-387. doi:10.1016/j.foodchem.2003.07.014Katsiari, M. ., Alichanidis, E., Voutsinas, L. ., & Roussis, I. . (2001). Proteolysis in reduced sodium Kefalograviera cheese made by partial replacement of NaCl with KCl. Food Chemistry, 73(1), 31-43. doi:10.1016/s0308-8146(00)00275-2Kyrana, V. R., & Lougovois, V. P. (2002). Sensory, chemical and microbiological assessment of farm-raised European sea bass (Dicentrarchus labrax) stored in melting ice. International Journal of Food Science and Technology, 37(3), 319-328. doi:10.1046/j.1365-2621.2002.00572.xLakshmanan, R., Piggott, J. R., & Paterson, A. (2003). Potential applications of high pressure for improvement in salmon quality. Trends in Food Science & Technology, 14(9), 354-363. doi:10.1016/s0924-2244(03)00121-3LEROI, F., & JOFFRAUD, J. J. (2000). Salt and Smoke Simultaneously Affect Chemical and Sensory Quality of Cold-Smoked Salmon during 5°C Storage Predicted Using Factorial Design. Journal of Food Protection, 63(9), 1222-1227. doi:10.4315/0362-028x-63.9.1222Masniyom, P., Benjakul, S., & Visessanguan, W. (2002). Shelf-life extension of refrigerated seabass slices under modified atmosphere packaging. Journal of the Science of Food and Agriculture, 82(8), 873-880. doi:10.1002/jsfa.1108Muguerza, E., Gimeno, O., Ansorena, D., & Astiasarán, I. (2004). New formulations for healthier dry fermented sausages: a review. Trends in Food Science & Technology, 15(9), 452-457. doi:10.1016/j.tifs.2003.12.010Periago, M. J., Ayala, M. D., López-Albors, O., Abdel, I., Martínez, C., García-Alcázar, A., … Gil, F. (2005). Muscle cellularity and flesh quality of wild and farmed sea bass, Dicentrarchus labrax L. Aquaculture, 249(1-4), 175-188. doi:10.1016/j.aquaculture.2005.02.047REDDY, K. A., & MARTH, E. H. (1991). Reducing the Sodium Content of Foods: A Review. Journal of Food Protection, 54(2), 138-150. doi:10.4315/0362-028x-54.2.138Regost, C., Jakobsen, J. V., & Rørå, A. M. B. (2004). Flesh quality of raw and smoked fillets of Atlantic salmon as influenced by dietary oil sources and frozen storage. Food Research International, 37(3), 259-271. doi:10.1016/j.foodres.2003.12.003Rodrigues, M. J., Ho, P., López-Caballero, M. E., Bandarra, N. M., & Nunes, M. L. (2005). Chemical, Microbiological, and Sensory Quality of Cod Products Salted in Different Brines. Journal of Food Science, 70(1), M1-M6. doi:10.1111/j.1365-2621.2005.tb09039.xRuusunen, M., & Puolanne, E. (2005). Reducing sodium intake from meat products. Meat Science, 70(3), 531-541. doi:10.1016/j.meatsci.2004.07.016Sanceda, N., Suzuki, E., & Kurata, T. (2003). Quality and sensory acceptance of fish sauce partially substituting sodium chloride or natural salt with potassium chloride during the fermentation process. International Journal of Food Science and Technology, 38(4), 435-443. doi:10.1046/j.1365-2621.2003.00710.xSigurgisladottir, S., Sigurdardottir, M. S., Torrissen, O., Vallet, J. L., & Hafsteinsson, H. (2000). Effects of different salting and smoking processes on the microstructure, the texture and yield of Atlantic salmon (Salmo salar) fillets. Food Research International, 33(10), 847-855. doi:10.1016/s0963-9969(00)00104-6Sivertsvik, M., Jeksrud, W. K., & Rosnes, J. T. (2002). A review of modified atmosphere packaging of fish and fishery products - significance of microbial growth, activities and safety. International Journal of Food Science and Technology, 37(2), 107-127. doi:10.1046/j.1365-2621.2002.00548.xTorrieri, E., Cavella, S., Villani, F., & Masi, P. (2006). Influence of modified atmosphere packaging on the chilled shelf life of gutted farmed bass (Dicentrarchus labrax). Journal of Food Engineering, 77(4), 1078-1086. doi:10.1016/j.jfoodeng.2005.08.03
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