PubMed

Example XML File

<!DOCTYPE ArticleSet PUBLIC "-//NLM//DTD PubMed 2.0//EN" "http://www.ncbi.nlm.nih.gov:80/entrez/query/static/PubMed.dtd"> 
<ArticleSet> 
     <Article> 
          <Journal> 
           <PublisherName>AAAS</PublisherName> 
            <JournalTitle>Science</JournalTitle> 
            <Issn>0036-8075</Issn> 
            <Volume>271 Suppl 3</Volume> 
            <Issue>5</Issue> 
            <PubDate> 
              <Year>1996</Year> 
              <Month>Mar</Month> 
              <Day>3</Day> 
            </PubDate> 
          </Journal> 
          <ArticleTitle>Fourteen-Member Macrolides Inhibit Interleukin-8 Release by Human Eosinophils from Atopic Donors</ArticleTitle> 
          <FirstPage>1835</FirstPage> 
          <LastPage>1837</LastPage> 
          <Language>EN</Language> 
          <AuthorList> 
            <Author> 
              <FirstName>Kenneth</FirstName> 
              <MiddleName>S.</MiddleName> 
              <LastName>F&uuml;tterer</LastName> 
              <Suffix>Jr.</Suffix> 
              <Affiliation> 
                Laboratoire de Biophysique de l' ADN, Institut Pasteur, Paris, 75015 France. kenneth@pasteur.fr 
              </Affiliation> 
            </Author> 
            <Author> 
            <FirstName>J.-F.</FirstName> 
            <LastName>Allemand</LastName> 
            </Author> 
          </AuthorList> 
          <ArticleIdList> 
            <ArticleId IdType="pii">040579197</ArticleId> 
            <ArticleId IdType="doi">10.1267/science.040579197</ArticleId> 
          </ArticleIdList> 
          <Abstract> 
           Only 14-member macrolides (erythromycin and clarithromycin) showed a 
           concentration-dependent suppressive effect on IL-8 release (control, 100&percnt; 
           erythromycin at 1 &mgr;g/ml, 67.82&percnt; &plusmn;3.45&percnt; [P &lt; 0.01]; 
           clarithromycin at 5 &mgr;g/ml, 56.81&percnt; &plusmn; 9.61&percnt; [P &lt; 0.01]). 
           The effect was found at therapeutic concentrations and appeared to occur at the  
           posttranscriprtional level. Upon mutation of Asp-L210 or Asp-M17 to Asn, k<inf>H</inf> 
           decreased from P<sup>n-1</sup> to P<sup>n+i</sup>. 
          </Abstract> 
        </Article> 
     <Article> 
          <Journal> 
           <PublisherName>AAAS</PublisherName> 
            <JournalTitle>Science</JournalTitle> 
            <Issn>0036-8075</Issn> 
            <Volume>271 Suppl 3</Volume> 
            <Issue>5</Issue> 
            <PubDate> 
              <Year>1996</Year> 
              <Month>Mar</Month> 
              <Day>3</Day> 
            </PubDate> 
          </Journal> 
          <ArticleTitle>Uncoupling of GTP binding from target stimulation by a single mutation in the
transducin &alpha; subunit.</ArticleTitle> 
          <FirstPage>1838</FirstPage> 
          <LastPage>1845</LastPage> 
          <Language>EN</Language> 
          <AuthorList> 
            <Author> 
              <FirstName>Robert</FirstName> 
              <MiddleName></MiddleName> 
              <LastName>Mittal</LastName> 
              <Suffix>Sr.</Suffix> 
              <Affiliation> 
               Department of Pharmacology, Cornell University, Ithaca, NY 14853-6401, USA.
              </Affiliation> 
            </Author> 
            <Author> 
            <FirstName>J.W.</FirstName> 
            <LastName>Erickson</LastName> 
            </Author> 
          </AuthorList> 
          <Abstract> 
Glutamic acid-203 of the &alpha; subunit of transducin (&alpha;T) resides within
a domain that undergoes a guanosine triphosphate (GTP)-induced conformational change that is essential
for effector recognition. Changing the glutamic acid to an alanine in bovine &alpha;(T) yielded an &alpha;
subunit (&alpha;(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange
and showed GTP hydrolytic activity similar to that measured for wild-type &alpha;(T). However, unlike the
wild-type protein, the GDP-bound form of &alpha;(T)E203A was constitutively active toward the effector
of transducin, the cyclic guanosine monophosphate phosphodiesterase. Thus, the &alpha;(T)E203A mutant represents
a short-circuited protein switch that no longer requires GTP for the activation of the effector target
phosphodiesterase. 
          </Abstract> 
        </Article> 
      </ArticleSet>