2,459 research outputs found
Hole concentration in a diluted ferromagnetic semiconductor
We consider a mean-field approach to the hole-mediated ferromagnetism in
III-V Mn-based semiconductor compounds to discuss the dependence of the hole
density on that of Mn sites in Ga_{1-x}Mn_xAs. The hole concentration, p, as a
function of the fraction of Mn sites, x, is parametrized in terms of the
product m*J_{pd}^2 (where m* is the hole effective mass and J_{pd} is the
Kondo-like hole/local-moment coupling), and the critical temperature Tc. By
using experimental data for these quantities, we have established the
dependence of the hole concentration with x, which can be associated with the
occurrence of a reentrant metal-insulator transition taking place in the hole
gas. We also calculate the dependence of the Mn magnetization with x, for
different temperatures (T), and found that as T increases, the width of the
composition-dependent magnetization decreases drammatically, and that the
magnetization maxima also decreases, indicating the need for quality-control of
Mn-doping composition in diluted magnetic semiconductor devices.Comment: 4 pages, 3 figures, RevTeX 3; Fig. 1 changed, new references adde
A combined approach for comparative exoproteome analysis of Corynebacterium pseudotuberculosis
Background: Bacterial exported proteins represent key components of the host-pathogen interplay. Hence, we
sought to implement a combined approach for characterizing the entire exoproteome of the pathogenic
bacterium Corynebacterium pseudotuberculosis, the etiological agent of caseous lymphadenitis (CLA) in sheep and
goats.
Results: An optimized protocol of three-phase partitioning (TPP) was used to obtain the C. pseudotuberculosis
exoproteins, and a newly introduced method of data-independent MS acquisition (LC-MSE) was employed for
protein identification and label-free quantification. Additionally, the recently developed tool SurfG+ was used for in
silico prediction of sub-cellular localization of the identified proteins. In total, 93 different extracellular proteins of
C. pseudotuberculosis were identified with high confidence by this strategy; 44 proteins were commonly identified
in two different strains, isolated from distinct hosts, then composing a core C. pseudotuberculosis exoproteome.
Analysis with the SurfG+ tool showed that more than 75% (70/93) of the identified proteins could be predicted as
containing signals for active exportation. Moreover, evidence could be found for probable non-classical export of
most of the remaining proteins.
Conclusions: Comparative analyses of the exoproteomes of two C. pseudotuberculosis strains, in addition to
comparison with other experimentally determined corynebacterial exoproteomes, were helpful to gain novel
insights into the contribution of the exported proteins in the virulence of this bacterium. The results presented
here compose the most comprehensive coverage of the exoproteome of a corynebacterial species so far
Genetic diversity of the E Protein of Dengue Type 3 Virus
<p>Abstract</p> <p>Background</p> <p>Dengue is the most important arbovirus disease in tropical and subtropical countries. The viral envelope (E) protein is responsible for cell receptor binding and is the main target of neutralizing antibodies. The aim of this study was to analyze the diversity of the E protein gene of DENV-3. E protein gene sequences of 20 new viruses isolated in Ribeirao Preto, Brazil, and 427 sequences retrieved from GenBank were aligned for diversity and phylogenetic analysis.</p> <p>Results</p> <p>Comparison of the E protein gene sequences revealed the presence of 47 variable sites distributed in the protein; most of those amino acids changes are located on the viral surface. The phylogenetic analysis showed the distribution of DENV-3 in four genotypes. Genotypes I, II and III revealed internal groups that we have called lineages and sub-lineages. All amino acids that characterize a group (genotype, lineage, or sub-lineage) are located in the 47 variable sites of the E protein.</p> <p>Conclusion</p> <p>Our results provide information about the most frequent amino acid changes and diversity of the E protein of DENV-3.</p
Virus Replication as a Phenotypic Version of Polynucleotide Evolution
In this paper we revisit and adapt to viral evolution an approach based on
the theory of branching process advanced by Demetrius, Schuster and Sigmund
("Polynucleotide evolution and branching processes", Bull. Math. Biol. 46
(1985) 239-262), in their study of polynucleotide evolution. By taking into
account beneficial effects we obtain a non-trivial multivariate generalization
of their single-type branching process model. Perturbative techniques allows us
to obtain analytical asymptotic expressions for the main global parameters of
the model which lead to the following rigorous results: (i) a new criterion for
"no sure extinction", (ii) a generalization and proof, for this particular
class of models, of the lethal mutagenesis criterion proposed by Bull,
Sanju\'an and Wilke ("Theory of lethal mutagenesis for viruses", J. Virology 18
(2007) 2930-2939), (iii) a new proposal for the notion of relaxation time with
a quantitative prescription for its evaluation, (iv) the quantitative
description of the evolution of the expected values in in four distinct
"stages": extinction threshold, lethal mutagenesis, stationary "equilibrium"
and transient. Finally, based on these quantitative results we are able to draw
some qualitative conclusions.Comment: 23 pages, 1 figure, 2 tables. arXiv admin note: substantial text
overlap with arXiv:1110.336
Efferent Pathways in Sodium Overload-Induced Renal Vasodilation in Rats
Hypernatremia stimulates the secretion of oxytocin (OT), but the physiological role of OT remains unclear. the present study sought to determine the involvement of OT and renal nerves in the renal responses to an intravenous infusion of hypertonic saline. Male Wistar rats (280-350 g) were anesthetized with sodium thiopental (40 mg. kg(-1), i.v.). A bladder cannula was implanted for collection of urine. Animals were also instrumented for measurement of mean arterial pressure (MAP) and renal blood flow (RBF). Renal vascular conductance (RVC) was calculated as the ratio of RBF by MAP. in anesthetized rats (n = 6), OT infusion (0.03 mu g . kg(-1), i.v.) induced renal vasodilation. Consistent with this result, ex vivo experiments demonstrated that OT caused renal artery relaxation. Blockade of OT receptors (OXTR) reduced these responses to OT, indicating a direct effect of this peptide on OXTR on this artery. Hypertonic saline (3 M NaCl, 1.8 ml . kg(-1) b.wt., i.v.) was infused over 60 s. in sham rats (n = 6), hypertonic saline induced renal vasodilation. the OXTR antagonist (AT; atosiban, 40 mu g . kg(-1) . h(-1), i.v.; n = 7) and renal denervation (RX) reduced the renal vasodilation induced by hypernatremia. the combination of atosiban and renal denervation (RX+AT; n = 7) completely abolished the renal vasodilation induced by sodium overload. Intact rats excreted 51% of the injected sodium within 90 min. Natriuresis was slightly blunted by atosiban and renal denervation (42% and 39% of load, respectively), whereas atosiban with renal denervation reduced sodium excretion to 16% of the load. These results suggest that OT and renal nerves are involved in renal vasodilation and natriuresis induced by acute plasma hypernatremia.Fundacao de Amparo a Pesquisa do Estado de Goias (FAPEG)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Univ Fed Goias, Ctr Neurosci & Cardiovasc Physiol, Inst Biol Sci, Dept Physiol Sci, Goiania, Go, BrazilUniv Fed Uberlandia, Fac Phys Educ, Inst Biol Sci, BR-38400 Uberlandia, MG, BrazilUniversidade Federal de São Paulo, Dept Physiol, São Paulo, BrazilUniv Fed Goias, Inst Biol Sci, Mol Biol Lab, Goiania, Go, BrazilUniv Fed Goias, Inst Biol Sci, Dept Biochem & Mol Biol, Goiania, Go, BrazilUniversidade Federal de São Paulo, Dept Physiol, São Paulo, BrazilFundacao de Amparo a Pesquisa do Estado de Goias (FAPEG): 2012/0055431086Fundacao de Amparo a Pesquisa do Estado de Goias (FAPEG): 2009/10267000352CNPq: 477832/2010-5CNPq: 483411/2012-4Web of Scienc
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