109 research outputs found

    Estimation of nitrogen in cotton leaves using different hyperspectral region data

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    As an important index of a plant’s N nutrition, leaf nitrogen content (LNC) can be quickly monitored in real time with hyperspectral information, which is helpful to guide the precise application of N in cotton leaves. In this study, taking cotton dripping in Xinjiang, China, as the object of study, five N application treatments (0, 120, 240, 360, 480 kg·ha-1) were set up, and the hyperspectral data and the N content of main stem functional leaves at the cotton flower and boll stage were collected. The results showed that (1) comparing the correlations of the three types of spectral data from the original spectra, first derivative spectra, and second derivative spectra with the LNC of cotton, the first derivative spectra increased the correlation between the reflectance in the peak and valley ranges of the spectral curves and the LNC of cotton; (2) in the three hyperspectral regions of VIS, NIR, and SWIR, all R2 values of the estimation model for the LNC of cotton established based on the characteristic wavelengths of the original and the first derivative spectra were greater than 0.8, and the model accuracy was better than that of the second derivative spectra; and (3) the normalized root mean square error (n-RMSE) values of the validated model using MLR, PCR, and PLSR regression methods were all in the range of 10–20%, indicating that the established model could well estimate the nitrogen content of cotton leaves. The results of this study demonstrate the potential of the three hyperspectral domains of VIR, NIR, and SWIR to estimate the LNC of cotton and provide a new basis for hyperspectral data application in crop nutrient monitoring

    Structural analysis of metalloform-selective inhibition of methionine aminopeptidase

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    One of the challenges in the development of methionine aminopeptidase (MetAP) inhibitors as antibacterial and anticancer agents is to define the metal ion actually used by MetAP in vivo and to discover MetAP inhibitors that can inhibit the metalloform that is relevant in vivo. Two distinct classes of novel nonpeptidic MetAP inhibitors that are not only potent but also highly selective for either the MnII or CoII form have been identified. Three crystal structures of Escherichia coli MetAP complexed with the metalloform-selective inhibitors 5-(2,5-dichlorophenyl)furan-2-carboxylic acid (2), 5-[2-(trifluoromethyl)phenyl]furan-2-carboxylic acid (3) and N-cyclopentyl-N-(thiazol-2-yl)oxalamide (4) have been solved and analysis of these structures has revealed the structural basis for their metalloform-selective inhibition. The MnII-form selective inhibitors (2) and (3) both use their carboxylate group to coordinate with the two MnII ions at the dinuclear metal site and both adopt a non-coplanar conformation for the two aromatic rings. The unique coordination geometry of these inhibitors may determine their MnII-form selectivity. In contrast, the CoII-form selective inhibitor (4) recruits an unexpected third metal ion, forming a trimetallic enzyme–metal–inhibitor complex. Thus, an important factor in the selectivity of (4) for the CoII form may be a consequence of a greater preference for a softer N,O-donor ligand for the softer CoII

    Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes

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    Background: Methionine aminopeptidase is a potential target of future antibacterial and anticancer drugs. Structural analysis of complexes of the enzyme with its inhibitors provides valuable information for structure-based drug design efforts. Results: Five new X-ray structures of such enzyme-inhibitor complexes were obtained. Analysis of these and other three similar structures reveals the adaptability of a surface-exposed loop bearing Y62, H63, G64 and Y65 (the YHGY loop) that is an integral part of the substrate and inhibitor binding pocket. This adaptability is important for accommodating inhibitors with variations in size. When compared with the human isozymes, this loop either becomes buried in the human type I enzyme due to an N-terminal extension that covers its position or is replaced by a unique insert in the human type II enzyme. Conclusion: The adaptability of the YHGY loop in E. coli methionine aminopeptidase, and likely in other bacterial methionine aminopeptidases, enables the enzyme active pocket to accommodate inhibitors of differing size. The differences in this adaptable loop between the bacterial and human methionine aminopeptidases is a structural feature that can be exploited to design inhibitors of bacterial methionine aminopeptidases as therapeutic agents with minimal inhibition of the corresponding human enzymes

    Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes

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    <p>Abstract</p> <p>Background</p> <p>Methionine aminopeptidase is a potential target of future antibacterial and anticancer drugs. Structural analysis of complexes of the enzyme with its inhibitors provides valuable information for structure-based drug design efforts.</p> <p>Results</p> <p>Five new X-ray structures of such enzyme-inhibitor complexes were obtained. Analysis of these and other three similar structures reveals the adaptability of a surface-exposed loop bearing Y62, H63, G64 and Y65 (the YHGY loop) that is an integral part of the substrate and inhibitor binding pocket. This adaptability is important for accommodating inhibitors with variations in size. When compared with the human isozymes, this loop either becomes buried in the human type I enzyme due to an N-terminal extension that covers its position or is replaced by a unique insert in the human type II enzyme.</p> <p>Conclusion</p> <p>The adaptability of the YHGY loop in <it>E. coli </it>methionine aminopeptidase, and likely in other bacterial methionine aminopeptidases, enables the enzyme active pocket to accommodate inhibitors of differing size. The differences in this adaptable loop between the bacterial and human methionine aminopeptidases is a structural feature that can be exploited to design inhibitors of bacterial methionine aminopeptidases as therapeutic agents with minimal inhibition of the corresponding human enzymes.</p

    Protective Effects of a Rhodiola Crenulata Extract and Salidroside on Hippocampal Neurogenesis against Streptozotocin-Induced Neural Injury in the Rat

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    Previously we have demonstrated that a Rhodiola crenulata extract (RCE), containing a potent antioxidant salidroside, promotes neurogenesis in the hippocampus of depressive rats. The current study was designed to further investigate the protective effect of the RCE on neurogenesis in a rat model of Alzheimer's disease (AD) induced by an intracerebroventricular injection of streptozotocin (STZ), and to determine whether this neuroprotective effect is induced by the antioxidative activity of salidroside. Our results showed that pretreatment with the RCE significantly improved the impaired neurogenesis and simultaneously reduced the oxidative stress in the hippocampus of AD rats. In vitro studies revealed that (1) exposure of neural stem cells (NSCs) from the hippocampus to STZ strikingly increased intracellular reactive oxygen species (ROS) levels, induced cell death and perturbed cell proliferation and differentiation, (2) hydrogen peroxide induced similar cellular activities as STZ, (3) pre-incubation of STZ-treated NSCs with catalase, an antioxidant, suppressed all these cellular activities induced by STZ, and (4) likewise, pre-incubation of STZ-treated NSCs with salidroside, also an antioxidant, suppressed all these activities as catalase: reduction of ROS levels and NSC death with simultaneous increases in proliferation and differentiation. Our findings indicated that the RCE improved the impaired hippocampal neurogenesis in the rat model of AD through protecting NSCs by its main ingredient salidroside which scavenged intracellular ROS

    Finishing the euchromatic sequence of the human genome

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    The sequence of the human genome encodes the genetic instructions for human physiology, as well as rich information about human evolution. In 2001, the International Human Genome Sequencing Consortium reported a draft sequence of the euchromatic portion of the human genome. Since then, the international collaboration has worked to convert this draft into a genome sequence with high accuracy and nearly complete coverage. Here, we report the result of this finishing process. The current genome sequence (Build 35) contains 2.85 billion nucleotides interrupted by only 341 gaps. It covers ∼99% of the euchromatic genome and is accurate to an error rate of ∼1 event per 100,000 bases. Many of the remaining euchromatic gaps are associated with segmental duplications and will require focused work with new methods. The near-complete sequence, the first for a vertebrate, greatly improves the precision of biological analyses of the human genome including studies of gene number, birth and death. Notably, the human enome seems to encode only 20,000-25,000 protein-coding genes. The genome sequence reported here should serve as a firm foundation for biomedical research in the decades ahead

    Relationship between choroidal thickness and idiopathic macular epiretinal membrane

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    AIM: To investigate the relationship between the thickness of choroid and the development of idiopathic macular epiretinal membrane(IMEM). METHODS: A retrospective analysis on 48 cases(48 eyes)of idiopathic macular epiretinal membrane patients(the IMEM group)was taken in our hospital from January 2014 to December 2016, and 50 right eyes in 50 healthy persons with physical examination were selected the control group, comparison on subfoveal choroidal thickness(SFCT)levels of sicked eyes, normal eyes in IMEM group and the control group were made, postoperative SFCT level change of sicked eyes in IMEM patients and normal eyes were investigated via follow-up, and analysis on correlation between postoperative choroidal thickness and the best corrected visual acuity was taken. RESULTS: The SFCT of sicked eyes in IMEM group 362.22±40.75μm was significantly lower than that of the contralateral eyes(410.56±38.45μm)and the right eyes of the control group(420.73±39.63μm), and data of the contralateral eyes was lower than right eyes of the control group, distinct difference was shown between groups(PP>0.05), and at postoperative 1mo, SFCT of sicked eyes and normal eyes evidently increased, showing sharp difference compared with that before operation(PP>0.05). The numbers of patients whose postoperative BCVA ≥0.5 with different preoperative SFCT values had statistically significant differences(P 380μm were significantly higher than those with r=0.629, PCONCLUSION: Choroidal thinning may be an important cause of IMEM, and preoperative choroidal thickness also has an influential effect on postoperative visual recovery
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