1 Ocak 2019 Dergi makalesi Açık Erişim

Kalfa, Aylin; Demir, Elif Ayazoglu; Colak, Ahmet; Yasar, Ahmet; Bekircan, Olcay

DataCite XML

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/69459</identifier>
  <creators>
    <creator>
      <creatorName>Kalfa, Aylin</creatorName>
      <givenName>Aylin</givenName>
      <familyName>Kalfa</familyName>
      <affiliation>Karadeniz Tech Univ, Fac Sci, Dept Chem, TR-61080 Trabzon, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Demir, Elif Ayazoglu</creatorName>
      <givenName>Elif Ayazoglu</givenName>
      <familyName>Demir</familyName>
      <affiliation>Karadeniz Tech Univ, Fac Sci, Dept Chem, TR-61080 Trabzon, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Colak, Ahmet</creatorName>
      <givenName>Ahmet</givenName>
      <familyName>Colak</familyName>
      <affiliation>Karadeniz Tech Univ, Fac Sci, Dept Chem, TR-61080 Trabzon, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Yasar, Ahmet</creatorName>
      <givenName>Ahmet</givenName>
      <familyName>Yasar</familyName>
      <affiliation>Karadeniz Tech Univ, Fac Pharm, Dept Analyt Chem, TR-61080 Trabzon, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Bekircan, Olcay</creatorName>
      <givenName>Olcay</givenName>
      <familyName>Bekircan</familyName>
      <affiliation>Karadeniz Tech Univ, Fac Sci, Dept Chem, TR-61080 Trabzon, Turkey</affiliation>
    </creator>
  </creators>
  <titles>
    <title>Inhibition Of Urease By Some New Synthesized 1,2,4-Triazol Derivatives: Inhibition Mechanism And Molecular Docking</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2019</publicationYear>
  <dates>
    <date dateType="Issued">2019-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/69459</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsVersionOf">10.81043/aperta.69458</relatedIdentifier>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.81043/aperta.69459</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">Urease is a metalloenzyme that catalyzes the hydrolysis of urea to ammonia and carbon dioxide. This ammonia secretion may cause significant increase in pH and is responsible for negative effects of urease activity in human health and agriculture. So, jack bean urease inhibition potentials of a newly synthesized of 243-(4-chloropheny1)-5-(4-methoxybenzy1)4H-1,2,4-triazol-4-1]acetohydrazide derivative compounds have been investigated in this study. Initially, IC50 values of six molecules (B16-B21) have been determined. According to this, it is seen that the B20 molecule is the most effective inhibitor. Docking studies also supported this end result. Urease inhibition type and K-i value are found to be noncompetitive and 32.01 mu 0.25 mu M, respectively, in the presence of compound B20. These results suggest that the B20 compound is a potential urease inhibitor.</description>
  </descriptions>
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