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  1. Article ; Online: MODIFICATION OF THE COBWEB MODEL INTO GENERALIZED LOGISTIC EQUATION FOR THE WHEAT PRICE ANALYSIS

    Jelena Stanojević / Nemanja Vuksanović / Katarina Kukić / Vesna Jablanović

    Ekonomika Poljoprivrede (1979), Vol 70, Iss

    2023  Volume 4

    Abstract: In the paper we constructed the new wheat growth model, based on the generalized logistic equation. Starting from the theoretical framework of the cobweb model, we adapted generalized logistic equation to better fit the real data of wheat prices, ... ...

    Abstract In the paper we constructed the new wheat growth model, based on the generalized logistic equation. Starting from the theoretical framework of the cobweb model, we adapted generalized logistic equation to better fit the real data of wheat prices, according to the presented wheat growth model. The aim of the paper is to present how logistic and generalized logistic equations can be used for both prediction of wheat prices and for the wheat price stability analysis. Data analysis showed better performances of the generalized logistic map in comparation with the conventional logistic map as a main result of this paper. For estimated parameters of the model the bifurcation diagrams also have been presented to show stability of wheat price over time. The conclusion is that the proposed model can be useful in predicting future wheat prices in the short-run period, as well as for the analysis of stability in conditions of uncertainty, which is also a recommendation for the application of the model in the future research.
    Keywords cobweb theorem ; wheat price ; growth model ; generalized logistic equation ; Agriculture ; S
    Subject code 330
    Language English
    Publishing date 2023-12-01T00:00:00Z
    Publisher Naučno društvo agrarnih ekonomista Balkana, Beograd; Institut za ekonomiku poljoprivrede, Beograd i Akademija ekonomskih nauka, Bukurešt
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose

    David N. Frick / Rajdeep S. Virdi / Nemanja Vuksanovic / Narayan Dahal / Nicholas R Silvaggi

    Abstract: ABSTRACTThe virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymers, helicase and main protease, are well ... ...

    Abstract ABSTRACTThe virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymers, helicase and main protease, are well conserved between SARS-CoV-2 and the original SARS virus, but several others are not. This study examines one of the most novel proteins encoded by SARS-CoV-2, a macrodomain of nonstructural protein 3 (nsp3). Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those seen in other corona-viruses, the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses, and potential therapeutic target.
    Keywords covid19
    Publisher biorxiv
    Document type Article ; Online
    DOI 10.1101/2020.03.31.014639
    Database COVID19

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  3. Article: Streptomyces wadayamensis MppP is a PLP-Dependent Oxidase, Not an Oxygenase

    Han, Lanlan / Alan W. Schwabacher / Nemanja Vuksanovic / Nicholas R. Silvaggi / Sarah A. Oehm / Tyler G. Fenske

    Biochemistry. 2018 Feb. 23, v. 57, no. 23

    2018  

    Abstract: The PLP-dependent l-arginine hydroxylase/deaminase MppP from Streptomyces wadayamensis (SwMppP) is involved in the biosynthesis of l-enduracididine, a nonproteinogenic amino acid found in several nonribosomally produced peptide antibiotics. SwMppP uses ... ...

    Abstract The PLP-dependent l-arginine hydroxylase/deaminase MppP from Streptomyces wadayamensis (SwMppP) is involved in the biosynthesis of l-enduracididine, a nonproteinogenic amino acid found in several nonribosomally produced peptide antibiotics. SwMppP uses only PLP and molecular oxygen to catalyze a 4-electron oxidation of l-arginine to form a mixture of 2-oxo-4(S)-hydroxy-5-guanidinovaleric acid and 2-oxo-5-guanidinovaleric acid. Steady-state kinetics analysis in the presence and absence of catalase shows that one molecule of peroxide is formed for every molecule of dioxygen consumed in the reaction. Moreover, for each molecule of 2-oxo-4(S)-hydroxy-5-guanidinovaleric acid produced, two molecules of dioxygen are consumed, suggesting that both the 4-hydroxy and 2-keto groups are derived from water. This was confirmed by running the reactions using either [18]O2 or H2[18]O and analyzing the products by ESI-MS. Incorporation of [18]O was only observed when the reaction was performed in H2[18]O. Crystal structures of SwMppP with l-arginine, 2-oxo-4(S)-hydroxy-5-guanidinovaleric acid, or 2-oxo-5-guanidinovaleric acid bound were determined at resolutions of 2.2, 1.9. and 1.8 Å, respectively. The structural data show that the N-terminal portion of the protein is disordered unless substrate or product is bound in the active site, in which case it forms a well-ordered helix that covers the catalytic center. This observation suggested that the N-terminal helix may have a role in substrate binding and/or catalysis. Our structural and kinetic characterizations of N-terminal variants show that the N-terminus is critical for catalysis. In light of this new information, we have refined our previously proposed mechanism of the SwMppP-catalyzed oxidation of l-arginine.
    Keywords active sites ; arginine ; biosynthesis ; catalase ; catalytic activity ; crystal structure ; electrospray ionization mass spectrometry ; hydrogen ; oxidation ; oxygen ; peptide antibiotics ; Streptomyces wadayamensis
    Language English
    Dates of publication 2018-0223
    Size p. 3252-3264.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.8b00130
    Database NAL-Catalogue (AGRICOLA)

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