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1.
Rep Prog Phys ; 83(12): 124201, 2020 Nov 21.
Artigo em Inglês | MEDLINE | ID: mdl-33226008

RESUMO

The combination of the high intensity proton beam facilities and massive detectors for precision measurements of neutrino oscillation parameters including the charge-parity violating (CPV) phase will open the door to help make beyond the standard model (BSM) physics reachable even in low energy regimes in the accelerator-based experiments. Large-mass detectors with highly precise tracking and energy measurements, excellent timing resolution, and low energy thresholds will enable the searches for BSM phenomena from cosmogenic origin, as well. Therefore, it is also conceivable that BSM topics in the next-generation neutrino experiments could be the dominant physics topics in the foreseeable future, as the precision of the neutrino oscillation parameter and CPV measurements continue to improve.This paper provides a review of the current landscape of BSM theory in neutrino experiments in two selected areas of the BSM topics-dark matter and neutrino related BSM-and summarizes the current results from existing neutrino experiments to set benchmarks for both theory and experiment. This paper then provides a review of upcoming neutrino experiments throughout the next 10 to 15 year time scale and their capabilities to set the foundation for potential reach in BSM physics in the two aforementioned themes. An important outcome of this paper is to ensure theoretical and simulation tools exist to carry out studies of these new areas of physics, from the first day of the experiments, such as Deep Underground Neutrino Experiment in the U.S. and Hyper-Kamiokande Experiment in Japan.

2.
Eur Phys J C Part Fields ; 77(12): 837, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-31997936

RESUMO

We investigate the impact of displaced heavy-quark matching scales in a global fit. The heavy-quark matching scale µ m determines at which energy scale µ the QCD theory transitions from N F to N F + 1 in the variable flavor number scheme (VFNS) for the evolution of the parton distribution functions (PDFs) and strong coupling α S ( µ ) . We study the variation of the matching scales, and their impact on a global PDF fit of the combined HERA data. As the choice of the matching scale µ m effectively is a choice of scheme, this represents a theoretical uncertainty; ideally, we would like to see minimal dependence on this parameter. For the transition across the charm quark (from N F = 3 to 4), we find a large µ m = µ c dependence of the global fit χ 2 at NLO, but this is significantly reduced at NNLO. For the transition across the bottom quark (from N F = 4 to 5), we have a reduced µ m = µ b dependence of the χ 2 at both NLO and NNLO as compared to the charm. This feature is now implemented in xFitter 2.0.0, an open source QCD fit framework.

3.
Phys Rev Lett ; 106(12): 122301, 2011 Mar 25.
Artigo em Inglês | MEDLINE | ID: mdl-21517308

RESUMO

We perform a global χ² analysis of nuclear parton distribution functions using data from charged current neutrino-nucleus (νA) deep-inelastic scattering (DIS), charged-lepton-nucleus (ℓ(±)A) DIS, and the Drell-Yan (DY) process. We show that the nuclear corrections in νA DIS are not compatible with the predictions derived from ℓ(±)A DIS and DY data. We quantify this result using a hypothesis-testing criterion based on the χ² distribution which we apply to the total χ² as well as to the χ² of the individual data sets. We find that it is not possible to accommodate the data from νA and ℓ(±)A DIS by an acceptable combined fit. Our result has strong implications for the extraction of both nuclear and proton parton distribution functions using combined neutrino and charged-lepton data sets.

4.
J Biol Chem ; 272(49): 31022-8, 1997 Dec 05.
Artigo em Inglês | MEDLINE | ID: mdl-9388251

RESUMO

Organelle compartments are used by cells as reservoirs of exchangeable Ca2+ and as Ca2+ buffers. The following study uses recombinant aequorins (CYT-AEQ and MT-AEQ) to measure the dynamics of Ca2+ flux between organelles in procyclic forms of the pathogenic protozoan, Trypanosoma brucei. Emphasis is placed on the exchange between an acidic Ca2+ reservoir and the mitochondrion. The mammalian mitochondrial targeting sequence was functional in trypanosomes as determined by immunoblots, immunolocalizations, and the observation that MT-AEQ was in a compartment whose Ca2+ uptake was inhibited 82% with carbonyl cyanide p-trifluoromethoxyphenylhydrazone and KCN. The resting level of free calcium ion concentration in the mitochondrion ([Ca2+]mit) was slightly higher than that in the cytoplasm ([Ca2+]cyt) (400 +/- 50 nM and 290 +/- 40 nM, respectively). Melittin (125 nM) disrupted Ca2+ homeostasis by inducing Ca2+ influx across the plasma membrane. [Ca2+]cyt became slightly elevated to 410 +/- 100 nM, whereas [Ca2+]mit was selectively increased approximately 12-fold, with a broad peak at 4.8 +/- 1.9 microM. At the peak, the mitochondrion contained approximately three times more free Ca2+ than the cytosol. However, mitochondrial retention of the Ca2+ was transient. Similar selective transport into the mitochondrion was observed when Ca2+ efflux from an acidic compartment was induced with monensin (2 microg/ml) in the presence of 5 mM EGTA. [Ca2+]cyt was transiently elevated to 400 +/- 50 nM, whereas [Ca2+]mit was elevated to 3.3+/-1.3 microM. When cells were treated sequentially with monensin (2 microg/ml) and then melittin (200 nM), mitochondrial Ca2+ transport was normal. However, [Ca2+]cyt became elevated to a level that was 1.4-fold higher than with melittin alone. Overall, these data demonstrate that the trypanosome mitochondrion is not a reservoir of exchangeable Ca2+ in the resting cell. However, Ca2+ is selectively channeled to the mitochondrion from the plasma membrane or acidic Ca2+ storage compartment. Additionally, the acidic compartment contributes to maintenance of Ca2+ homeostasis in response to melittin.


Assuntos
Equorina/metabolismo , Cálcio/metabolismo , Compartimento Celular , Mitocôndrias/metabolismo , Trypanosoma brucei brucei/metabolismo , Animais , Transporte Biológico , Homeostase , Ionóforos/farmacologia , Medições Luminescentes , Meliteno/farmacologia , Monensin/farmacologia , Proteínas Recombinantes/metabolismo
5.
6.
Phys Rev D Part Fields ; 40(5): 1546-1561, 1989 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-10011975
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