Institution
Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto
Education•
About: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto is a based out in . It is known for research contribution in the topics: Population & Genus. The organization has 2143 authors who have published 3674 publications receiving 71071 citations. The organization is also known as: FFCLRP & FFCLRP-USP.
Topics: Population, Genus, Catalysis, Ruthenium, Elevated plus maze
Papers published on a yearly basis
Papers
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TL;DR: The results suggested that the essential oil extracted from the leaves of Plectranthus neochilus displays promising activity against most of the evaluated cariogenic bacteria, especially S. mutans.
Abstract: This work used the broth microdilution method to investigate the antimicrobial activity of the essential oil obtained from the leaves of Plectranthus neochilus (PN-EO) against a representative panel of oral pathogens. We assessed the antimicrobial activity of this oil in terms of the minimum inhibitory concentration (MIC). PN-EO displayed moderate activity against Enterococcus faecalis (MIC = 250 μg/mL) and Streptococcus salivarus (MIC = 250 μg/mL), significant activity against Streptococcus sobrinus (MIC = 62.5 μg/mL), Streptococcus sanguinis (MIC = 62.5 μg/mL), Streptococcus mitis (MIC = 31.25 μg/mL), and Lactobacillus casei (MIC = 31.25 μg/mL), and interesting activity against Streptococcus mutans (MIC = 3.9 μg/mL). GC-FID and GC-MS helped to identify thirty-one compounds in PN-EO; α-pinene (1, 14.1%), β-pinene (2, 7.1%), trans-caryophyllene (3, 29.8%), and caryophyllene oxide (4, 12.8%) were the major chemical constituents of this essential oil. When tested alone, compounds 1, 2, 3, and 4 were inactive (MIC > 4000 μg/mL) against all the microorganisms. These results suggested that the essential oil extracted from the leaves of Plectranthus neochilus displays promising activity against most of the evaluated cariogenic bacteria, especially S. mutans.
42 citations
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TL;DR: Two xylanases belong to family 11, and they are the most structurally similar mesophilic–thermophilic pair, which indicates that this domain must be the target for the site-directed mutagenesis responsible for improving the temperature tolerance of this family of enzymes.
Abstract: Xylanases are enzymes that are very tolerant to temperature. Their potential use in several biotechnological applications, such as animal food manufacture and pulp bleaching, is due to their intrinsic thermostability. The present report deals with two xylanases, the mesophilic xylanase from Bacillus circulans, BCX, and the thermophilic xylanase from Thermomyces lanuginosus,TLX. These enzymes belong to family 11, and they are the most structurally similar mesophilic–thermophilic pair. Molecular dynamics simulations were employed to investigate the factors responsible for the different thermostabilities exhibited by these structurally similar enzymes. Their active site is their most rigid region, and it is equally rigid at all temperatures. Inter and intramolecular interactions, hydrogen bonds in particular, are the key to the main differences between BCX and TLX. The intramolecular hydrogen bonds and salt bridges are important for maintenance of the backbone rigidity even at high temperature, and the highl...
42 citations
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TL;DR: In this paper, a borohydride reduction of aqueous metal salts on carbon paper, and screened by fluorescence assay for activity as ethanol electrooxidation catalysts.
42 citations
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TL;DR: Assays employing various inhibitors suggest the presence of mitochondrial F0F1-, and K+- and V-ATPase activities in the gill microsomes, suggesting that altered membrane composition results from salinity acclimation.
Abstract: We evaluate hemolymph osmotic and ionic regulatory abilities and characterize a posterior gill microsomal (Na+, K+)-ATPase from the marine swimming crab, Callinectes ornatus, acclimated to 21 per thousand or 33 per thousand salinity. C. ornatus is isosmotic after acclimation to 21 per thousand but is hyposmotic at 33 per thousand salinity; hemolymph ions do not recover initial levels on acclimation to 21 per thousand salinity but are anisoionic compared to ambient concentrations, revealing modest regulatory ability. NH4+ modulates enzyme affinity for K+, which increases 187-fold in crabs acclimated to 33 per thousand salinity. The (Na+, K+)-ATPase redistributes into membrane fractions of different densities, suggesting that altered membrane composition results from salinity acclimation. ATP was hydrolyzed at maximum rates of 182.6 +/- 7.1 nmol Pi min(-1) mg(-1) (21 per thousand) and 76.2 +/- 3.5 nmol Pi min(-1) mg(-1) (33 per thousand), with little change in KM values (approximately 50 micromol L(-1)). K+ together with NH4+ synergistically stimulated activity to maximum rates of approximately 240 nmol Pi min(-1) mg(-1). KI values for ouabain inhibition (approximately 110 micromol L(-1)) decreased to 44.9 +/- 1.0 micromol L(-1) (21 per thousand) and 28.8 +/- 1.3 micromol L(-1) (33 per thousand) in the presence of both K+ and NH4+. Assays employing various inhibitors suggest the presence of mitochondrial F0F1-, and K+- and V-ATPase activities in the gill microsomes.
42 citations
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TL;DR: The mean EU age of the shells is 224−±24.6 as mentioned in this paper, but this value is considered younger than the real age because of excessive Uranium uptake observed among the younger shells.
41 citations
Authors
Showing all 2195 results
Name | H-index | Papers | Citations |
---|---|---|---|
Jon Lloyd | 80 | 230 | 30995 |
Peter C. Ford | 74 | 495 | 20821 |
Frederico Guilherme Graeff | 60 | 183 | 12209 |
Marcus Lira Brandão | 54 | 243 | 9248 |
David W. Roubik | 54 | 177 | 10070 |
Richard J. Ward | 53 | 242 | 9502 |
Juan Cornejo | 49 | 147 | 6478 |
Norberto Peporine Lopes | 47 | 457 | 12031 |
Carlos Alemán | 47 | 634 | 11349 |
Klaus Hartfelder | 45 | 150 | 7708 |
Valtencir Zucolotto | 45 | 212 | 6253 |
Rosane Marina Peralta | 44 | 212 | 5701 |
Antonio Claudio Tedesco | 44 | 307 | 6778 |
Roberto M. Torresi | 44 | 213 | 5822 |
Zilá Luz Paulino Simões | 43 | 113 | 8020 |