Search Results - "Milisav, I."

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  1. 1

    The Role of Antioxidants in Cancer, Friends or Foes? by Poljsak, B, Milisav, I

    Published in Current pharmaceutical design (01-01-2018)
    “…Consumption of dietary supplements by millions of people is increasing [1]. Between 64 to 81% of cancer patients and survivors use multivitamin supplements…”
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  2. 2

    Vitamin B3 forms as precursors to NAD+: Are they safe? by Poljsak, B., Milisav, I.

    Published in Trends in food science & technology (01-09-2018)
    “…The oxidized form of cellular nicotinamide adenine dinucleotide (NAD+) is implicated in longevity, health improvement and even attenuation of some…”
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  3. 3

    The Neglected Significance of “Antioxidative Stress” by Poljsak, Borut, Milisav, Irina

    Published in Oxidative medicine and cellular longevity (01-01-2012)
    “…Oxidative stress arises when there is a marked imbalance between the production and removal of reactive oxygen species (ROS) in favor of the prooxidant…”
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  4. 4

    Yin and Yang: Why did evolution implement and preserve the circadian rhythmicity? by Poljsak, B., Ribarič, S., Milisav, I.

    Published in Medical hypotheses (01-10-2019)
    “…Yin and Yang concept emphasizes the reciprocal and interrelated nature; neither is sufficient, both are needed to sustain the overall balance of the living…”
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  5. 5

    Reproductive Benefit of Oxidative Damage : An Oxidative Stress “Malevolence”? by Poljsak, Borut, Milisav, Irina, Lampe, T., Ostan, I.

    Published in Oxidative medicine and cellular longevity (01-01-2011)
    “…High levels of reactive oxygen species (ROS) compared to antioxidant defenses are considered to play a major role in diverse chronic age-related diseases and…”
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  6. 6

    Apoptosis triggered redistribution of caspase-9 from cytoplasm to mitochondria by Potokar, M, Milisav, I, Kreft, M, Stenovec, M, Zorec, R

    Published in FEBS letters (05-06-2003)
    “…Caspase-9 is an apoptosis initiator protease activated as a response to the mitochondrial damage in the cytoplasmic complex apoptosome. By fluorescence…”
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  7. 7

    Automated high through-put colocalization analysis of multichannel confocal images by Kreft, M., Milisav, I., Potokar, M., Zorec, R.

    “…The laser scanning confocal microscope (LSCM) generates images of multiple labelled fluorescent samples. Colocalization of fluorescent labels is frequently…”
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  8. 8

    Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells by Kreft, M, Kuster, V, Grilc, S, Rupnik, M, Milisav, I, Zorec, R

    “…Synaptotagmin I (Syt I), a low-affinity Ca(2+)-binding protein, is thought to serve as the Ca(2+) sensor in the release of neurotransmitter. However,…”
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  9. 9
  10. 10

    Characterization of a novel human dynein-related gene that is specifically expressed in testis by Milisav, I, Jones, M H, Affara, N A

    Published in Mammalian genome (01-09-1996)
    “…A novel dynein-related transcript (designated DNEL1) from human adult testis has been identified that can encode a protein with a size of 91087 Da. The…”
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  11. 11

    Corrigendum to âEuropean contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)â [Redox Biol. 13 (2017) 94â162] by J. Egea, I. Fabregat, Y.M. Frapart, P. Ghezzi, A. Görlach, T. Kietzmann, K. Kubaichuk, U.G. Knaus, M.G. Lopez, G. Olaso-Gonzalez, A. Petry, R. Schulz, J. Vina, P. Winyard, K. Abbas, O.S. Ademowo, C.B. Afonso, I. Andreadou, H. Antelmann, F. Antunes, M. Aslan, M.M. Bachschmid, R.M. Barbosa, V. Belousov, C. Berndt, D. Bernlohr, E. Bertrán, A. Bindoli, S.P. Bottari, P.M. Brito, G. Carrara, A.I. Casas, A. Chatzi, N. Chondrogianni, M. Conrad, M.S. Cooke, J.G. Costa, A. Cuadrado, P. My-Chan Dang, B. De Smet, B. Debelec-Butuner, I.H.K. Dias, J.D. Dunn, A.J. Edson, M. El Assar, J. El-Benna, P. Ferdinandy, A.S. Fernandes, K.E. Fladmark, U. Förstermann, R. Giniatullin, Z. Giricz, A. Görbe, H. Griffiths, V. Hampl, A. Hanf, J. Herget, P. Hernansanz-Agustín, M. Hillion, J. Huang, S. Ilikay, P. Jansen-Dürr, V. Jaquet, J.A. Joles, B. Kalyanaraman, D. Kaminskyy, M. Karbaschi, M. Kleanthous, L.O. Klotz, B. Korac, K.S. Korkmaz, R. Koziel, D. KraÄun, K.H. Krause, V. KÅen, T. Krieg, J. Laranjinha, A. Lazou, H. Li, A. Martínez-Ruiz, R. Matsui, G.J. McBean, S.P. Meredith, J. Messens, V. Miguel, Y. Mikhed, I. Milisav, L. MilkoviÄ, A. Miranda-Vizuete, M. MojoviÄ, M. Monsalve, P.A. Mouthuy, J. Mulvey, T. Münzel, V. Muzykantov, I.T.N. Nguyen, M. Oelze, N.G. Oliveira, C.M. Palmeira, N. Papaevgeniou

    Published in Redox biology (01-04-2018)
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  12. 12

    Corrigendum to “European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)” [Redox Biol. 13 (2017) 94–162] by Egea, J., Fabregat, I., Kietzmann, T., Olaso-Gonzalez, G., Petry, A., Schulz, R., Vina, J., Winyard, P., Afonso, C.B., Andreadou, I., Antelmann, H., Antunes, F., Aslan, M., Bachschmid, M.M., Barbosa, R.M., Bernlohr, D., Bertrán, E., Bottari, S.P., Brito, P.M., Carrara, G., Casas, A.I., Chatzi, A., Conrad, M., Cooke, M.S., My-Chan Dang, P., De Smet, B., Dunn, J.D., Edson, A.J., El-Benna, J., Ferdinandy, P., Fladmark, K.E., Förstermann, U., Giniatullin, R., Giricz, Z., Griffiths, H., Hanf, A., Hernansanz-Agustín, P., Huang, J., Ilikay, S., Jansen-Dürr, P., Kalyanaraman, B., Kaminskyy, D., Kleanthous, M., Klotz, L.O., Korac, B., Koziel, R., Krieg, T., Laranjinha, J., Li, H., Matsui, R., Meredith, S.P., Messens, J., Miguel, V., Mikhed, Y., Milisav, I., Miranda-Vizuete, A., Mojović, M., Mouthuy, P.A., Münzel, T., Muzykantov, V., Nguyen, I.T.N., Oliveira, N.G., Palmeira, C.M., Papaevgeniou, N., Pavićević, A., Pedre, B., Pircalabioru, G.G., Pitt, A.R., Poulsen, H.E., Prieto, I., Robledinos-Antón, N., Rousset, F., Ruskovska, T., Saraiva, N., Schröder, K., Semen, K., Seredenina, T., Shakirzyanova, A., Smith, G.L., Soldati, T., Sousa, B.C., Spickett, C.M., Stancic, A., Stasia, M.J., Steinbrenner, H., Tuncay, E., Turan, B., Ursini, F., Vacek, J., Valentová, K., Van Breusegem, F., Yalçın, A.S., Yelisyeyeva, O., Žarković, N., Touyz, R.M., Grune, T., Lamas, S., Schmidt, H.H.H.W., Di Lisa, F., Daiber, A.

    Published in Redox biology (01-04-2018)
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  13. 13

    Modular Structure of the TIM23 Preprotein Translocase of Mitochondria by Milisav, Irina, Moro, Fernando, Neupert, Walter, Brunner, Michael

    Published in The Journal of biological chemistry (13-07-2001)
    “…The TIM23 complex mediates import into mitochondria of nuclear encoded preproteins with a matrix-targeting signal. It is composed of the integral membrane…”
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  14. 14

    Ecm10, a novel Hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae by Baumann, Frank, Milisav, Irina, Neupert, Walter, Herrmann, Johannes M

    Published in FEBS letters (29-12-2000)
    “…Members of the heat shock protein 70 (Hsp70) family are found in most of the compartments of eukaryotic cells where they play essential roles in protein…”
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  15. 15

    Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB by Koronakis, E, Hughes, C, Milisav, I, Koronakis, V

    Published in Molecular microbiology (01-04-1995)
    “…The Escherichia coli toxin exporter HlyB comprises an integral membrane domain fused to a cytoplasmic domain of the ATP-binding cassette (ABC) super-family,…”
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  16. 16

    Simulation of some short-term control mechanisms in cardiovascular physiology by Podnar, T., Runovc, F., Milisav, Irina, Kordaš, M.

    Published in Computers in biology and medicine (2004)
    “…The equivalent electronic circuit, developed to simulate cardiovascular physiology, is upgraded to incorporate negative feedback loops. In this way homeostasis…”
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  17. 17
  18. 18

    A potential human axonemal dynein heavy-chain gene maps to 17q25 by Milisav, I, Affara, N A

    Published in Mammalian genome (01-05-1998)
    “…This paper reports the partial sequence, expression analysis, and mapping of the human dynein-related gene DNEL2…”
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  19. 19

    Dynein and dynein-related genes by Milisav, Irina

    “…Dyneins are large, multisubunit ATPases that interact with microtubules to generate force. Dyneins move eukaryotic cilia and flagella and are in the cytoplasm,…”
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