<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>0034-7418</journal-id>
<journal-title><![CDATA[Revista Colombiana de Ciencias Químico - Farmacéuticas]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. colomb. cienc. quim. farm.]]></abbrev-journal-title>
<issn>0034-7418</issn>
<publisher>
<publisher-name><![CDATA[Departamento de Farmácia, Facultad de Ciencias, Universidade Nacional da Colombia]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0034-74182023000100311</article-id>
<article-id pub-id-type="doi">10.15446/rcciquifa.v52n1.109381</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Molecular insights into the binding mechanisms of human and mouse Glutamate-cysteine ligases]]></article-title>
<article-title xml:lang="es"><![CDATA[Información molecular sobre los mecanismos de unión de las ligasas de glutamato-cisteína humana y de ratón]]></article-title>
<article-title xml:lang="pt"><![CDATA[Insights moleculares sobre os mecanismos de ligação de ligases de glutamato-cisteína humanas e de camundongos]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Olaoye]]></surname>
<given-names><![CDATA[Ige]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Oso]]></surname>
<given-names><![CDATA[Babatunde]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Aberuagba]]></surname>
<given-names><![CDATA[Adepeju]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,McPherson University  ]]></institution>
<addr-line><![CDATA[Seriki Sotayo ]]></addr-line>
<country>Nigeria</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,University of Ilorin  ]]></institution>
<addr-line><![CDATA[Ilorin ]]></addr-line>
<country>Nigeria</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>04</month>
<year>2023</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>04</month>
<year>2023</year>
</pub-date>
<volume>52</volume>
<numero>1</numero>
<fpage>311</fpage>
<lpage>336</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_arttext&amp;pid=S0034-74182023000100311&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_abstract&amp;pid=S0034-74182023000100311&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_pdf&amp;pid=S0034-74182023000100311&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[ Background the significant role of glutamate-cysteine ligase (GCL) towards the synthesis of glutathione for the sequestration of reactive species as a regulatory point is second to none. However, much still need to be known about the enzyme molecular characterization. Thus, the homology modeling of GCL was carried out using different modeling webserver tools. The quality of the predicted crystal structures of human and mouse GCLs with inhibition were further assessed on molecular interaction with naphthalene and its metabolites.  Results the predicted human GCL and mouse GCL model structures have respective 89.8% and 89.6% residues in the most favored region of the Ramachandran plot. However, the molecular docking interaction study with the assessed ligands revealed two different binding pockets with pi-interactions as major non-covalent bond and better binding scores than glutathione.  Conclusion the predicted model could provide better mechanism of GCL catalysis to preserve its essential residues for reasonable GSH synthesis.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[ Antecedentes el importante papel de la glutamato-cisteína ligasa (GCL) en la síntesis de glutatión para el secuestro de especies reactivas como punto regulador es insuperable. Sin embargo, aún queda mucho por conocer acerca de la caracterización molecular de enzimas. Por lo tanto, el modelado de homología de GCL se llevó a cabo utilizando diferentes herramientas de servidor web de modelado. La calidad de las estructuras cristalinas predichas de los GCL humanos y de ratón con inhibición se evaluó más a fondo en la interacción molecular con el naftaleno y sus metabolitos.  Resultados las estructuras del modelo de GCL humano y GCL de ratón predichas tienen residuos respectivos del 89,8 % y el 89,6 % en la región más favorecida del diagrama de Ramachandran. Sin embargo, el estudio de interacción de acoplamiento molecular con los ligandos evaluados reveló dos bolsillos de unión diferentes con interacciones pi como enlace no covalente principal y mejores puntajes de unión que el glutatión.  Conclusión el modelo predicho podría proporcionar un mejor mecanismo de catálisis de GCL para preservar sus residuos esenciales para una síntesis razonable de GSH.]]></p></abstract>
<abstract abstract-type="short" xml:lang="pt"><p><![CDATA[ Antecedentes o papel significativo da glutamato-cisteína ligase (GCL) para a síntese de glutationa para o sequestro de espécies reativas como um ponto regulador é inigualável. No entanto, muito ainda precisa ser conhecido sobre a caracterização molecular da enzima. Assim, a modelagem de homologia do GCL foi realizada usando diferentes ferramentas de modelagem do servidor web. A qualidade das estruturas cristalinas previstas de GCLs humanos e de camundongos com inibição foi ainda avaliada na interação molecular com naftaleno e seus metabólitos.  Resultados as estruturas do modelo de GCL humano e GCL de camundongo têm resíduos respectivos de 89,8% e 89,6% na região mais favorecida do gráfico de Ramachandran. No entanto, o estudo da interação de docking molecular com os ligantes avaliados revelou dois bolsos de ligação diferentes com interações pi como principal ligação não covalente e melhores pontuações de ligação do que a glutationa.  Conclusão o modelo previsto pode fornecer um melhor mecanismo de catálise de GCL para preservar seus resíduos essenciais para síntese razoável de GSH.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[GSH]]></kwd>
<kwd lng="en"><![CDATA[GCL]]></kwd>
<kwd lng="en"><![CDATA[homology modeling]]></kwd>
<kwd lng="en"><![CDATA[naphthalene]]></kwd>
<kwd lng="en"><![CDATA[molecular docking]]></kwd>
<kwd lng="es"><![CDATA[GSH]]></kwd>
<kwd lng="es"><![CDATA[GCL]]></kwd>
<kwd lng="es"><![CDATA[modelado por homología]]></kwd>
<kwd lng="es"><![CDATA[naftalina]]></kwd>
<kwd lng="es"><![CDATA[acoplamiento molecular]]></kwd>
<kwd lng="pt"><![CDATA[GSH]]></kwd>
<kwd lng="pt"><![CDATA[GCL]]></kwd>
<kwd lng="pt"><![CDATA[modelagem de homologia]]></kwd>
<kwd lng="pt"><![CDATA[naftaleno]]></kwd>
<kwd lng="pt"><![CDATA[docking molecular]]></kwd>
</kwd-group>
</article-meta>
</front><back>
<ref-list>
<ref id="B1">
<label>[1]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Espinosa-Diez]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Miguel]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Mennerich]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Kietzmann]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Sanchez-Perez]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
<name>
<surname><![CDATA[Cadenas]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Lamas]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Antioxidant responses and cellular adjustments to oxidative stress]]></article-title>
<source><![CDATA[Redox Biol.]]></source>
<year>2015</year>
<volume>6</volume>
<page-range>183-97</page-range></nlm-citation>
</ref>
<ref id="B2">
<label>[2]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Dalton]]></surname>
<given-names><![CDATA[T.P.]]></given-names>
</name>
<name>
<surname><![CDATA[Chen]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Schneider]]></surname>
<given-names><![CDATA[S.N.]]></given-names>
</name>
<name>
<surname><![CDATA[Nebert]]></surname>
<given-names><![CDATA[D.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Shertzer]]></surname>
<given-names><![CDATA[H.G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Genetically altered mice to evaluate glutathione homeostasis in health and disease]]></article-title>
<source><![CDATA[Free Radic. Biol. Med.]]></source>
<year>2004</year>
<volume>37</volume>
<page-range>1511-26</page-range></nlm-citation>
</ref>
<ref id="B3">
<label>[3]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Morris]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Ly]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Chi]]></surname>
<given-names><![CDATA[P.-T.]]></given-names>
</name>
<name>
<surname><![CDATA[Daliva]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Nguyen]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Soofer]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Chen]]></surname>
<given-names><![CDATA[Y.C.]]></given-names>
</name>
<name>
<surname><![CDATA[Lagman]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Venketaraman]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Glutathione synthesis is compromised in erythrocytes from individuals with HIV]]></article-title>
<source><![CDATA[Front. Pharmacol.]]></source>
<year>2014</year>
<volume>5</volume>
</nlm-citation>
</ref>
<ref id="B4">
<label>[4]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Yang]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Dieter]]></surname>
<given-names><![CDATA[M.Z.]]></given-names>
</name>
<name>
<surname><![CDATA[Chen]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Shertzer]]></surname>
<given-names><![CDATA[H.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Nebert]]></surname>
<given-names><![CDATA[D.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Dalton]]></surname>
<given-names><![CDATA[T.P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm(-/-) knockout mouse. Novel model system for a severely compromised oxidative stress response]]></article-title>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2002</year>
<volume>277</volume>
<page-range>49446-52</page-range></nlm-citation>
</ref>
<ref id="B5">
<label>[5]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Franklin]]></surname>
<given-names><![CDATA[C.C.]]></given-names>
</name>
<name>
<surname><![CDATA[Backos]]></surname>
<given-names><![CDATA[D.S.]]></given-names>
</name>
<name>
<surname><![CDATA[Mohar]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
<name>
<surname><![CDATA[White]]></surname>
<given-names><![CDATA[C.C.]]></given-names>
</name>
<name>
<surname><![CDATA[Forman]]></surname>
<given-names><![CDATA[H.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Kavanagh]]></surname>
<given-names><![CDATA[T.J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate cysteine ligase]]></article-title>
<source><![CDATA[Mol. Aspects Med.]]></source>
<year>2009</year>
<volume>30</volume>
<page-range>86-98</page-range></nlm-citation>
</ref>
<ref id="B6">
<label>[6]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Fu]]></surname>
<given-names><![CDATA[N.]]></given-names>
</name>
<name>
<surname><![CDATA[Li]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Li]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhao]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Liu]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhao]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Du]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Kong]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<name>
<surname><![CDATA[Wang]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Nan]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Glutamate-cysteine ligase catalytic subunit attenuated hepatitis C virus-related liver fibrosis and suppressed endoplasmic reticulum stress]]></article-title>
<source><![CDATA[Front. Mol. Biosci.]]></source>
<year>2020</year>
<volume>7</volume>
</nlm-citation>
</ref>
<ref id="B7">
<label>[7]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Xiong]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Xiong]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Wang]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Wang]]></surname>
<given-names><![CDATA[Z.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhao]]></surname>
<given-names><![CDATA[N.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhao]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Yu]]></surname>
<given-names><![CDATA[Z.]]></given-names>
</name>
<name>
<surname><![CDATA[Wang]]></surname>
<given-names><![CDATA[Z.]]></given-names>
</name>
<name>
<surname><![CDATA[Yi]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Luan]]></surname>
<given-names><![CDATA[X.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Inhibition of glutathione synthesis via decreased glucose metabolism in stored RBCs]]></article-title>
<source><![CDATA[Cell. Physiol. Biochem.]]></source>
<year>2018</year>
<volume>51</volume>
<page-range>2172-84</page-range></nlm-citation>
</ref>
<ref id="B8">
<label>[8]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kumagai]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Abiko]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Environmental electrophiles: Protein adducts, modulation of redox signaling, and interaction with persulfides/polysulfides]]></article-title>
<source><![CDATA[Chem. Res. Toxicol.]]></source>
<year>2017</year>
<volume>30</volume>
<page-range>203-19</page-range></nlm-citation>
</ref>
<ref id="B9">
<label>[9]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Baldwin]]></surname>
<given-names><![CDATA[R.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Jewell]]></surname>
<given-names><![CDATA[W.T.]]></given-names>
</name>
<name>
<surname><![CDATA[Fanucchi]]></surname>
<given-names><![CDATA[M.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Plopper]]></surname>
<given-names><![CDATA[C.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Buckpitt]]></surname>
<given-names><![CDATA[A.R.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Comparison of pulmonary/nasal CYP2F expression levels in rodents and rhesus macaque]]></article-title>
<source><![CDATA[J. Pharmacol. Exp. Therapy]]></source>
<year>2004</year>
<volume>309</volume>
<page-range>127-36</page-range></nlm-citation>
</ref>
<ref id="B10">
<label>[10]</label><nlm-citation citation-type="journal">
<collab>The UniProt Consortium</collab>
<article-title xml:lang=""><![CDATA[UniProt: the universal protein knowledgebase in 2021]]></article-title>
<source><![CDATA[Nucleic Acids Research]]></source>
<year>2021</year>
<volume>49</volume>
<numero>D1</numero>
<issue>D1</issue>
<page-range>D480-9</page-range></nlm-citation>
</ref>
<ref id="B11">
<label>[11]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Combet]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Blanchet]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Geourjon]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Deleage]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[NPS@: Network protein sequence analysis]]></article-title>
<source><![CDATA[Trends Biochem. Sci.]]></source>
<year>2000</year>
<volume>25</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>147-50</page-range></nlm-citation>
</ref>
<ref id="B12">
<label>[12]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Waterhouse]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Bertoni]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Bienert]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Studer]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Tauriello]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Gumienny]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Heer]]></surname>
<given-names><![CDATA[FT.]]></given-names>
</name>
<name>
<surname><![CDATA[de Beer]]></surname>
<given-names><![CDATA[TAP.]]></given-names>
</name>
<name>
<surname><![CDATA[Rempfer]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Bordoli]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<name>
<surname><![CDATA[Lepore]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Schwede]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[SWISS-MODEL: homology modelling of protein structures and complexes]]></article-title>
<source><![CDATA[Nucleic Acids Res.]]></source>
<year>2018</year>
<volume>46</volume>
<numero>W1</numero>
<issue>W1</issue>
<page-range>W296-303</page-range></nlm-citation>
</ref>
<ref id="B13">
<label>[13]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Bhattacharya]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Cheng]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[3Drefine: Consistent protein structure refinement by optimizing hydrogen bonding network and atomic level energy minimization]]></article-title>
<source><![CDATA[Proteins: Structure, Function, and Bioinformatics]]></source>
<year>2012</year>
<volume>81</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>119-31</page-range></nlm-citation>
</ref>
<ref id="B14">
<label>[14]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Bhattacharya]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Cheng]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[i3Drefine software for protein 3D structure refinement and its assessment in CASP10]]></article-title>
<source><![CDATA[PLoS One]]></source>
<year>2013</year>
<volume>8</volume>
<numero>7</numero>
<issue>7</issue>
</nlm-citation>
</ref>
<ref id="B15">
<label>[15]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Bhattacharya]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Nowotny]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Cao]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Cheng]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[3Drefine: an interactive web server for efficient protein structure refinement]]></article-title>
<source><![CDATA[Nucleic Acids Res.]]></source>
<year>2016</year>
<volume>44</volume>
<numero>W1</numero>
<issue>W1</issue>
<page-range>W406-9</page-range></nlm-citation>
</ref>
<ref id="B16">
<label>[16]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Laskowski]]></surname>
<given-names><![CDATA[R.A.]]></given-names>
</name>
<name>
<surname><![CDATA[MacArthur]]></surname>
<given-names><![CDATA[M.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Moss]]></surname>
<given-names><![CDATA[D.S.]]></given-names>
</name>
<name>
<surname><![CDATA[Thornton]]></surname>
<given-names><![CDATA[J.M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[PROCHECK: a program to check the stereochemical quality of protein structures]]></article-title>
<source><![CDATA[J. Appl. Crystal.]]></source>
<year>1993</year>
<volume>26</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>283-91</page-range></nlm-citation>
</ref>
<ref id="B17">
<label>[17]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Laskowski]]></surname>
<given-names><![CDATA[R.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Rullmann]]></surname>
<given-names><![CDATA[J.A.]]></given-names>
</name>
<name>
<surname><![CDATA[MacArthur]]></surname>
<given-names><![CDATA[M.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Kaptein]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Thornton]]></surname>
<given-names><![CDATA[J.M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR]]></article-title>
<source><![CDATA[J. Biomol. NMR]]></source>
<year>1996</year>
<volume>8</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>477-86</page-range></nlm-citation>
</ref>
<ref id="B18">
<label>[18]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Benkert]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
<name>
<surname><![CDATA[Biasini]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Schwede]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Toward the estimation of the absolute quality of individual protein structure models]]></article-title>
<source><![CDATA[Bioinformatics]]></source>
<year>2011</year>
<volume>27</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>343-50</page-range></nlm-citation>
</ref>
<ref id="B19">
<label>[19]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Roy]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Yang]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[COFACTOR: an accurate comparative algorithm for structure-based protein function annotation]]></article-title>
<source><![CDATA[Nucleic Acids Res.]]></source>
<year>2012</year>
<volume>40</volume>
<numero>W1</numero>
<issue>W1</issue>
<page-range>W471-7</page-range></nlm-citation>
</ref>
<ref id="B20">
<label>[20]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kim]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Chen]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Cheng]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Gindulyte]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[He]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[He]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Li]]></surname>
<given-names><![CDATA[Q.]]></given-names>
</name>
<name>
<surname><![CDATA[Shoemaker]]></surname>
<given-names><![CDATA[B.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Thiessen]]></surname>
<given-names><![CDATA[P.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Yu]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Zaslavsky]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Bolton]]></surname>
<given-names><![CDATA[E.E.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[PubChem 2019 update: improved access to chemical data]]></article-title>
<source><![CDATA[Nucleic Acids Res.]]></source>
<year>2019</year>
<volume>47</volume>
<numero>D1</numero>
<issue>D1</issue>
<page-range>D1102-9</page-range></nlm-citation>
</ref>
<ref id="B21">
<label>[21]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[O'Boyle]]></surname>
<given-names><![CDATA[N.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Banck]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[James]]></surname>
<given-names><![CDATA[C.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Morley]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Vandermeersch]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Hutchison]]></surname>
<given-names><![CDATA[GR.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Open Babel: An Open chemical toolbox]]></article-title>
<source><![CDATA[J. Cheminformatics]]></source>
<year>2011</year>
<volume>3</volume>
<numero>10</numero>
<issue>10</issue>
</nlm-citation>
</ref>
<ref id="B22">
<label>[22]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Trott]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
<name>
<surname><![CDATA[Olson]]></surname>
<given-names><![CDATA[AJ.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading]]></article-title>
<source><![CDATA[J. Comput. Chem.]]></source>
<year>2010</year>
<volume>31</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>455-61</page-range></nlm-citation>
</ref>
<ref id="B23">
<label>[23]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Meister]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Glutathione metabolism and its selective modification]]></article-title>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>1988</year>
<volume>263</volume>
<numero>33</numero>
<issue>33</issue>
<page-range>17205-8</page-range></nlm-citation>
</ref>
<ref id="B24">
<label>[24]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Seelig]]></surname>
<given-names><![CDATA[G.F.]]></given-names>
</name>
<name>
<surname><![CDATA[Simondsen]]></surname>
<given-names><![CDATA[R.P.]]></given-names>
</name>
<name>
<surname><![CDATA[Meister]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits]]></article-title>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>1984</year>
<volume>259</volume>
<page-range>9345-7</page-range></nlm-citation>
</ref>
<ref id="B25">
<label>[25]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Chen]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Shertzer]]></surname>
<given-names><![CDATA[H.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Schneider]]></surname>
<given-names><![CDATA[S.N.]]></given-names>
</name>
<name>
<surname><![CDATA[Nebert]]></surname>
<given-names><![CDATA[D.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Dalton]]></surname>
<given-names><![CDATA[T.P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Glutamate cysteine ligase catalysis: Dependence on ATP and modifier subunit for regulation of tissue glutathione levels]]></article-title>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2005</year>
<volume>280</volume>
<page-range>33766-74</page-range></nlm-citation>
</ref>
<ref id="B26">
<label>[26]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Huang]]></surname>
<given-names><![CDATA[CS.]]></given-names>
</name>
<name>
<surname><![CDATA[Anderson]]></surname>
<given-names><![CDATA[ME.]]></given-names>
</name>
<name>
<surname><![CDATA[Meister]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase]]></article-title>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>1993</year>
<volume>268</volume>
<page-range>20578-83</page-range></nlm-citation>
</ref>
<ref id="B27">
<label>[27]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Mason]]></surname>
<given-names><![CDATA[JM.]]></given-names>
</name>
<name>
<surname><![CDATA[Arndt]]></surname>
<given-names><![CDATA[KM.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Coiled coil domains: stability, specificity and biological implications]]></article-title>
<source><![CDATA[ChemBioChem]]></source>
<year>2004</year>
<volume>5</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>170-6</page-range></nlm-citation>
</ref>
<ref id="B28">
<label>[28]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Geourjon]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Deleage]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments]]></article-title>
<source><![CDATA[Bioinformatics]]></source>
<year>1995</year>
<volume>11</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>681-4</page-range></nlm-citation>
</ref>
<ref id="B29">
<label>[29]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Cardoso]]></surname>
<given-names><![CDATA[JM.]]></given-names>
</name>
<name>
<surname><![CDATA[Fonseca]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<name>
<surname><![CDATA[Egas]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Abrantes]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Cysteine proteases secreted by the pinewood nematode, Bursaphelenchus xylophilus: in silico analysis]]></article-title>
<source><![CDATA[Comput. Biol. Chem.]]></source>
<year>2018</year>
<volume>77</volume>
<page-range>291-6</page-range></nlm-citation>
</ref>
<ref id="B30">
<label>[30]</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Patel]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Singh]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Patel]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structural bioinformatics]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Shaik]]></surname>
<given-names><![CDATA[N.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Hakeem]]></surname>
<given-names><![CDATA[K.R.]]></given-names>
</name>
<name>
<surname><![CDATA[Banaganapalli]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Elango]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
</person-group>
<source><![CDATA[Essentials of Bioinformatics]]></source>
<year>2019</year>
<volume>I.</volume>
<page-range>169-99</page-range><publisher-loc><![CDATA[Cham, Switzerland ]]></publisher-loc>
<publisher-name><![CDATA[Springer]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B31">
<label>[31]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Oduselu]]></surname>
<given-names><![CDATA[O.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Ajani]]></surname>
<given-names><![CDATA[O.O.]]></given-names>
</name>
<name>
<surname><![CDATA[Ajamma1]]></surname>
<given-names><![CDATA[UY.]]></given-names>
</name>
<name>
<surname><![CDATA[Brors]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Adebiyi]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Homology modelling and molecular docking studies of selected substituted benzo[d]imidazol-1-yl)methyl) benzimidamide scaffolds on Plasmodium falciparum adenylosuccinate lyase receptor]]></article-title>
<source><![CDATA[Bioinform. Biol. Insights]]></source>
<year>2019</year>
<volume>13</volume>
</nlm-citation>
</ref>
<ref id="B32">
<label>[32]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Roland]]></surname>
<given-names><![CDATA[A.O.]]></given-names>
</name>
<name>
<surname><![CDATA[Morayo]]></surname>
<given-names><![CDATA[A.E.]]></given-names>
</name>
<name>
<surname><![CDATA[Joan]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
<name>
<surname><![CDATA[Gbadamosi]]></surname>
<given-names><![CDATA[F.I.]]></given-names>
</name>
<name>
<surname><![CDATA[Kayode]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Adelabu]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Modelling profile of onchocerca volvulus glutamate-cysteine ligase (ONCVOGCL)]]></article-title>
<source><![CDATA[J. Anal. Pharm. Res.]]></source>
<year>2021</year>
<volume>10</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>118-22</page-range></nlm-citation>
</ref>
<ref id="B33">
<label>[33]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Yamaguchi]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Akitaya]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Kidachi]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Kamie]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Umetsu]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Homology modeling and structural analysis of human &#947;-glutamylcysteine ligase catalytic subunit for antitumor drug development]]></article-title>
<source><![CDATA[J. Biophys. Chem.]]></source>
<year>2012</year>
<volume>3</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>238-48</page-range></nlm-citation>
</ref>
<ref id="B34">
<label>[34]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Morris]]></surname>
<given-names><![CDATA[A.L.]]></given-names>
</name>
<name>
<surname><![CDATA[MacArthur]]></surname>
<given-names><![CDATA[M.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Hutchinson]]></surname>
<given-names><![CDATA[E.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Thornton]]></surname>
<given-names><![CDATA[J.M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Stereochemical quality of protein structure coordinates]]></article-title>
<source><![CDATA[Proteins]]></source>
<year>1992</year>
<volume>12</volume>
<page-range>345-64</page-range></nlm-citation>
</ref>
<ref id="B35">
<label>[35]</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Laskowski]]></surname>
<given-names><![CDATA[RA.]]></given-names>
</name>
<name>
<surname><![CDATA[MacArthur]]></surname>
<given-names><![CDATA[M.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Thornton]]></surname>
<given-names><![CDATA[JM.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[PROCHECK: validation of protein structure coordinates]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Rossmann]]></surname>
<given-names><![CDATA[M.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Arnold]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
</person-group>
<source><![CDATA[International Tables of Crystallography, Volume F. Crystallography of Biological Macromolecules]]></source>
<year>2001</year>
<page-range>722-5</page-range><publisher-loc><![CDATA[The Netherlands ]]></publisher-loc>
<publisher-name><![CDATA[Kluwer Academic Publishers]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B36">
<label>[36]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Luthy]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Bowie]]></surname>
<given-names><![CDATA[J.U.]]></given-names>
</name>
<name>
<surname><![CDATA[Eisenberg]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[A method to identify protein sequences that fold into a known three-dimensional structure]]></article-title>
<source><![CDATA[Science]]></source>
<year>1991</year>
<volume>253</volume>
<numero>5016</numero>
<issue>5016</issue>
<page-range>164-70</page-range></nlm-citation>
</ref>
<ref id="B37">
<label>[37]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Luthy]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Bowie]]></surname>
<given-names><![CDATA[J.U.]]></given-names>
</name>
<name>
<surname><![CDATA[Eisenberg]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Assessment of protein models with three-dimensional profiles]]></article-title>
<source><![CDATA[Nature]]></source>
<year>1992</year>
<volume>356</volume>
<numero>6364</numero>
<issue>6364</issue>
<page-range>83-5</page-range></nlm-citation>
</ref>
<ref id="B38">
<label>[38]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Freddolino]]></surname>
<given-names><![CDATA[P.L.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[COFACTOR: improved protein function prediction by combining structure, sequence and protein-protein interaction information]]></article-title>
<source><![CDATA[Nucleic Acids Res.]]></source>
<year>2017</year>
<volume>45</volume>
<numero>Web Server issue</numero>
<issue>Web Server issue</issue>
<page-range>W291-9</page-range></nlm-citation>
</ref>
<ref id="B39">
<label>[39]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Elokely]]></surname>
<given-names><![CDATA[K.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Doerkse]]></surname>
<given-names><![CDATA[R.J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Docking challenge: protein sampling and molecular docking performance]]></article-title>
<source><![CDATA[J. Chem. Inform. Model.]]></source>
<year>2013</year>
<volume>53</volume>
<numero>8</numero>
<issue>8</issue>
<page-range>1934-45</page-range></nlm-citation>
</ref>
<ref id="B40">
<label>[40]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Bernaldez]]></surname>
<given-names><![CDATA[M.J.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Billones]]></surname>
<given-names><![CDATA[J.B.]]></given-names>
</name>
<name>
<surname><![CDATA[Magpantay]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[In silico analysis of binding interactions between GSK983 and Human DHODH through docking and molecular dynamics]]></article-title>
<source><![CDATA[AIP Conference Proceedings]]></source>
<year>2018</year>
<volume>2045</volume>
</nlm-citation>
</ref>
<ref id="B41">
<label>[41]</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Olaoye]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
<name>
<surname><![CDATA[Oso]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Aberuagba]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Molecular mechanisms of anti-inflammatory activities of the extracts of Ocimum gratissimum and Thymus vulgaris]]></article-title>
<source><![CDATA[Avicenna Journal of Medical Biotechnology]]></source>
<year>2021</year>
<volume>13</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>207-16</page-range></nlm-citation>
</ref>
</ref-list>
</back>
</article>
