<PubmedArticle>
    <MedlineCitation Status="Publisher" Owner="NLM">
        <PMID>19894211</PMID>
        <DateCreated>
            <Year>2009</Year>
            <Month>11</Month>
            <Day>6</Day>
        </DateCreated>
        <Article PubModel="Print-Electronic">
            <Journal>
                <ISSN IssnType="Electronic">1097-0061</ISSN>
                <JournalIssue CitedMedium="Internet">
                    <PubDate>
                        <Year>2009</Year>
                        <Month>Nov</Month>
                        <Day>4</Day>
                    </PubDate>
                </JournalIssue>
                <Title>Yeast (Chichester, England)</Title>
                <ISOAbbreviation>Yeast</ISOAbbreviation>
            </Journal>
            <ArticleTitle>Dual functions of Mdt1 in genome maintenance and cell integrity pathways in Saccharomyces cerevisiae.</ArticleTitle>
            <Pagination>
                <MedlinePgn/>
            </Pagination>
            <Abstract>
                <AbstractText>Recent evidence indicates considerable cross-talk between genome maintenance and cell integrity control pathways. The RNA recognition motif (RRM)- and SQ/TQ cluster domain (SCD)-containing protein Mdt1 is required for repair of 3'-blocked DNA double-strand breaks (DSBs) and efficient recombinational maintenance of telomeres in budding yeast. Here we show that deletion of MDT1 (PIN4/YBL051C) leads to severe synthetic sickness in the absence of the genes for the central cell integrity MAP kinases Bck1 and Slt2/Mpk1. Consistent with a cell integrity function, mdt1Delta cells are hypersensitive to the cell wall toxin calcofluor white and the Bck1-Slt2 pathway activator caffeine. An RRM-deficient mdt1-RRM0 allele shares the severe bleomycin hypersensitivity, inefficient recombinational telomere maintenance and slt2 synthetic sickness phenotypes, but not the cell wall toxin hypersensitivity with mdt1Delta. However, the mdt1-RRM(3A) allele, where only the RNA-binding site is mutated, behaves similarly to the wild-type, suggesting that the Mdt1 RRM functions as a protein-protein interaction rather than a nucleic acid-binding module. Surprisingly, in a strain background where double mutants are sick but still viable, bck1Deltamdt1Delta and slt2Deltamdt1Delta mutants differ in some of their phenotypes, consistent with the emerging concept of flexible signal entry and exit points in the Bck1-Mkk1/2-Slt2 pathway. Overall, the results indicate that Mdt1 has partially separable functions in both cell wall and genome integrity pathways. Copyright (c) 2009 John Wiley &amp; Sons, Ltd.</AbstractText>
            </Abstract>
            <Affiliation>St. Vincent's Institute of Medical Research and Department of Medicine SVH, University of Melbourne, Fitzroy, Victoria 3065, Australia.</Affiliation>
            <AuthorList>
                <Author>
                    <LastName>Traven</LastName>
                    <FirstName>Ana</FirstName>
                    <Initials>A</Initials>
                </Author>
                <Author>
                    <LastName>Lo</LastName>
                    <FirstName>Tricia L</FirstName>
                    <Initials>TL</Initials>
                </Author>
                <Author>
                    <LastName>Pike</LastName>
                    <FirstName>Brietta L</FirstName>
                    <Initials>BL</Initials>
                </Author>
                <Author>
                    <LastName>Friesen</LastName>
                    <FirstName>Helena</FirstName>
                    <Initials>H</Initials>
                </Author>
                <Author>
                    <LastName>Guzzo</LastName>
                    <FirstName>Julie</FirstName>
                    <Initials>J</Initials>
                </Author>
                <Author>
                    <LastName>Andrews</LastName>
                    <FirstName>Brenda</FirstName>
                    <Initials>B</Initials>
                </Author>
                <Author>
                    <LastName>Heierhorst</LastName>
                    <FirstName>Jrg</FirstName>
                    <Initials>J</Initials>
                </Author>
            </AuthorList>
            <Language>ENG</Language>
            <PublicationTypeList>
                <PublicationType>JOURNAL ARTICLE</PublicationType>
            </PublicationTypeList>
            <ArticleDate DateType="Electronic">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>4</Day>
            </ArticleDate>
        </Article>
        <MedlineJournalInfo>
            <MedlineTA>Yeast</MedlineTA>
            <NlmUniqueID>8607637</NlmUniqueID>
        </MedlineJournalInfo>
    </MedlineCitation>
    <PubmedData>
        <History>
            <PubMedPubDate PubStatus="entrez">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="pubmed">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
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                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
        </History>
        <PublicationStatus>aheadofprint</PublicationStatus>
        <ArticleIdList>
            <ArticleId IdType="doi">10.1002/yea.1730</ArticleId>
            <ArticleId IdType="pubmed">19894211</ArticleId>
        </ArticleIdList>
    </PubmedData>
</PubmedArticle>


<PubmedArticle>
    <MedlineCitation Owner="NLM" Status="In-Process">
        <PMID>19894176</PMID>
        <DateCreated>
            <Year>2009</Year>
            <Month>11</Month>
            <Day>06</Day>
        </DateCreated>
        <Article PubModel="Print">
            <Journal>
                <ISSN IssnType="Electronic">1545-9632</ISSN>
                <JournalIssue CitedMedium="Internet">
                    <Volume>6</Volume>
                    <Issue>12</Issue>
                    <PubDate>
                        <Year>2009</Year>
                        <Month>Dec</Month>
                    </PubDate>
                </JournalIssue>
                <Title>Journal of occupational and environmental hygiene</Title>
            </Journal>
            <ArticleTitle>Beryllium and strong hydrogen bonds.</ArticleTitle>
            <Pagination>
                <MedlinePgn>751-7</MedlinePgn>
            </Pagination>
            <Abstract>
                <AbstractText>We compare beryllium to H+ and show that beryllium can displace H+ in many &quot;strong hydrogen bonds&quot; where Be as a &quot;tetrahedral proton&quot; (O-Be-O angle is tetrahedral as opposed to the nearly linear O-H-O angle) is thermodynamically preferred. The strong hydrogen bond provides two advantages. First, the O-X distance in a strong hydrogen bond is in the range 2.4-2.8 A, which brings two oxygen atoms into a predefined chelating binding site for beryllium. Second, the strong hydrogen bond provides a low barrier pathway to displace the proton without breaking a strong covalent O-H bond by shifting the proton to the more acidic site as Be interacts with the basic oxygen. The low barrier to proton transfer associated with a strong hydrogen bond provides a kinetic pathway for Be binding, and the binding strength increases with the increasing basicity of the site as indicated by the pKa. The physiological importance of this type of interaction is demonstrated with the solubility of a variety of Be complexes at pH 7. Based on this concept, new ligands have been designed for Be binding that solubilize Be in phosphate media and can be used as fluorescent imaging agents. Finally, the binding of Be to the iron transport protein transferrin is discussed as it relates to the same type of binding.</AbstractText>
            </Abstract>
            <Affiliation>Los Alamos National Laboratory, Los Alamos, New Mexico 87545, USA. tmark@lanl.gov</Affiliation>
            <AuthorList CompleteYN="Y">
                <Author ValidYN="Y">
                    <LastName>McCleskey</LastName>
                    <ForeName>T Mark</ForeName>
                    <Initials>TM</Initials>
                </Author>
                <Author ValidYN="Y">
                    <LastName>Scott</LastName>
                    <ForeName>Brian L</ForeName>
                    <Initials>BL</Initials>
                </Author>
            </AuthorList>
            <Language>eng</Language>
            <PublicationTypeList>
                <PublicationType>Journal Article</PublicationType>
            </PublicationTypeList>
        </Article>
        <MedlineJournalInfo>
            <Country>United States</Country>
            <MedlineTA>J Occup Environ Hyg</MedlineTA>
            <NlmUniqueID>101189458</NlmUniqueID>
        </MedlineJournalInfo>
        <CitationSubset>IM</CitationSubset>
    </MedlineCitation>
    <PubmedData>
        <History>
            <PubMedPubDate PubStatus="entrez">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="pubmed">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="medline">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
        </History>
        <PublicationStatus>ppublish</PublicationStatus>
        <ArticleIdList>
            <ArticleId IdType="pii">916670962</ArticleId>
            <ArticleId IdType="doi">10.1080/15459620903025574</ArticleId>
            <ArticleId IdType="pubmed">19894176</ArticleId>
        </ArticleIdList>
    </PubmedData>
</PubmedArticle>


<PubmedArticle>
    <MedlineCitation Status="Publisher" Owner="NLM">
        <PMID>19894125</PMID>
        <DateCreated>
            <Year>2009</Year>
            <Month>11</Month>
            <Day>6</Day>
        </DateCreated>
        <Article PubModel="Print-Electronic">
            <Journal>
                <ISSN IssnType="Electronic">1572-8773</ISSN>
                <JournalIssue CitedMedium="Internet">
                    <PubDate>
                        <Year>2009</Year>
                        <Month>Nov</Month>
                        <Day>6</Day>
                    </PubDate>
                </JournalIssue>
                <Title>Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine</Title>
                <ISOAbbreviation>Biometals</ISOAbbreviation>
            </Journal>
            <ArticleTitle>Characterization of NikR-responsive promoters of urease and metal transport genes of Helicobacter mustelae.</ArticleTitle>
            <Pagination>
                <MedlinePgn/>
            </Pagination>
            <Abstract>
                <AbstractText>The NikR protein is a nickel-responsive regulator, which in the gastric pathogen Helicobacter pylori controls expression of nickel-transporters and the nickel-cofactored urease acid resistance determinant. Although NikR-DNA interaction has been well studied, the Helicobacter NikR operator site remains poorly defined. In this study we have identified the NikR operators in the promoters of two inversely nickel-regulated urease operons (ureAB and ureA2B2) in the ferret pathogen Helicobacter mustelae, and have used bioinformatic approaches for the prediction of putative NikR operators in the genomes of four urease-positive Helicobacter species. Helicobacter mustelae NikR bound to the ureA2 promoter to a sequence overlapping with the -35 promoter region, leading to repression. In contrast, NikR binding to a site far upstream of the canonical sigma(80) promoter in the H. mustelae ureA promoter resulted in transcriptional induction, similar to the situation in H. pylori. Using H. pylori NikR operators and the newly identified H. mustelae NikR operators a new consensus sequence was generated (TRWYA-N(15)-TRWYA), which was used to screen the genomes of four urease-positive Helicobacter species (H. mustelae, H. pylori, H. acinonychis and H. hepaticus) for putative NikR-regulated promoters. One of these novel putative NikR-regulated promoters in H. mustelae is located upstream of a putative TonB-dependent outer membrane protein designated NikH, which displayed nickel-responsive expression. Insertional inactivation of the nikH gene in H. mustelae resulted in a significant decrease in urease activity, and this phenotype was complemented by nickel-supplementation of the growth medium, suggesting a function for NikH in nickel transport accross the outer membrane. In conclusion, the H. mustelae NikR regulator directly controls nickel-responsive regulation of ureases and metal transporters. The improved consensus NikR operator sequence allows the prediction of additional NikR targets in Helicobacter genomes, as demonstrated by the identification of a new nickel-repressed outer membrane protein in H. mustelae.</AbstractText>
            </Abstract>
            <Affiliation>Department of Gastroenterology and Hepatology, Erasmus MC, University Medical Center, 's Gravendijkwal 230, 3015 CE, Rotterdam, The Netherlands.</Affiliation>
            <AuthorList>
                <Author>
                    <LastName>Stoof</LastName>
                    <FirstName>Jeroen</FirstName>
                    <Initials>J</Initials>
                </Author>
                <Author>
                    <LastName>Kuipers</LastName>
                    <FirstName>Ernst</FirstName>
                    <MiddleName>J</MiddleName>
                    <Initials>EJ</Initials>
                </Author>
                <Author>
                    <LastName>van Vliet</LastName>
                    <FirstName>Arnoud</FirstName>
                    <MiddleName>H M</MiddleName>
                    <Initials>AH</Initials>
                </Author>
            </AuthorList>
            <Language>ENG</Language>
            <PublicationTypeList>
                <PublicationType>JOURNAL ARTICLE</PublicationType>
            </PublicationTypeList>
            <ArticleDate DateType="Electronic">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>6</Day>
            </ArticleDate>
        </Article>
        <MedlineJournalInfo>
            <MedlineTA>Biometals</MedlineTA>
            <NlmUniqueID>9208478</NlmUniqueID>
        </MedlineJournalInfo>
    </MedlineCitation>
    <PubmedData>
        <History>
            <PubMedPubDate PubStatus="received">
                <Year>2009</Year>
                <Month>9</Month>
                <Day>22</Day>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="accepted">
                <Year>2009</Year>
                <Month>10</Month>
                <Day>23</Day>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="aheadofprint">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>6</Day>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="entrez">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="pubmed">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="medline">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
        </History>
        <PublicationStatus>aheadofprint</PublicationStatus>
        <ArticleIdList>
            <ArticleId IdType="doi">10.1007/s10534-009-9275-7</ArticleId>
            <ArticleId IdType="pubmed">19894125</ArticleId>
        </ArticleIdList>
    </PubmedData>
</PubmedArticle>


<PubmedArticle>
    <MedlineCitation Status="Publisher" Owner="NLM">
        <PMID>19894120</PMID>
        <DateCreated>
            <Year>2009</Year>
            <Month>11</Month>
            <Day>6</Day>
        </DateCreated>
        <Article PubModel="Print-Electronic">
            <Journal>
                <ISSN IssnType="Electronic">1557-1904</ISSN>
                <JournalIssue CitedMedium="Internet">
                    <PubDate>
                        <Year>2009</Year>
                        <Month>Nov</Month>
                        <Day>6</Day>
                    </PubDate>
                </JournalIssue>
                <Title>Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology</Title>
                <ISOAbbreviation>J Neuroimmune Pharmacol</ISOAbbreviation>
            </Journal>
            <ArticleTitle>Lipopolysaccharide Increases the Expression of Multidrug Resistance-Associated Protein 1 (MRP1) in RAW 264.7 Macrophages.</ArticleTitle>
            <Pagination>
                <MedlinePgn/>
            </Pagination>
            <Abstract>
                <AbstractText>Multidrug resistance-associated protein 1 (MRP-1) is a ubiquitously expressed member of the ATP-binding cassette transporter family. MRP-1 is one of the primary transporters of glutathione and glutathione conjugates. This protein also transports antiretroviral therapeutics, such as HIV-1 protease inhibitors (PI). We hypothesized that inflammatory mediators that activate macrophages would modify the expression and activity of MRP-1 in macrophages. Real-time PCR assays, western blots, and calcein efflux assays were used to show that exposure of macrophage cell line RAW 264.7 to lipopolysaccharide (LPS) increased expression of MRP-1 at the levels of mRNA, protein, and functional activity. Treatment of macrophages with LPS resulted in 2-fold increases of MRP-1 expression or functional activity. LPS-mediated increases in calcein efflux were repressed by the MRP-specific inhibitor MK-571. These results suggest that the effectiveness of HIV-1 PI therapy may be compromised by the presence of opportunistic infections.</AbstractText>
            </Abstract>
            <Affiliation>Division of Pharmacology and Toxicology, School of Pharmacy, University of Missouri-Kansas City, Kansas City, MO, 64108, USA, Silversteinp@umkc.edu.</Affiliation>
            <AuthorList>
                <Author>
                    <LastName>Silverstein</LastName>
                    <FirstName>Peter</FirstName>
                    <MiddleName>S</MiddleName>
                    <Initials>PS</Initials>
                </Author>
                <Author>
                    <LastName>Audus</LastName>
                    <FirstName>Kenneth</FirstName>
                    <MiddleName>L</MiddleName>
                    <Initials>KL</Initials>
                </Author>
                <Author>
                    <LastName>Qureshi</LastName>
                    <FirstName>Nilofer</FirstName>
                    <Initials>N</Initials>
                </Author>
                <Author>
                    <LastName>Kumar</LastName>
                    <FirstName>Anil</FirstName>
                    <Initials>A</Initials>
                </Author>
            </AuthorList>
            <Language>ENG</Language>
            <PublicationTypeList>
                <PublicationType>JOURNAL ARTICLE</PublicationType>
            </PublicationTypeList>
            <ArticleDate DateType="Electronic">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>6</Day>
            </ArticleDate>
        </Article>
        <MedlineJournalInfo>
            <MedlineTA>J Neuroimmune Pharmacol</MedlineTA>
            <NlmUniqueID>101256586</NlmUniqueID>
        </MedlineJournalInfo>
    </MedlineCitation>
    <PubmedData>
        <History>
            <PubMedPubDate PubStatus="received">
                <Year>2009</Year>
                <Month>8</Month>
                <Day>13</Day>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="accepted">
                <Year>2009</Year>
                <Month>10</Month>
                <Day>14</Day>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="aheadofprint">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>6</Day>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="entrez">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="pubmed">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
            <PubMedPubDate PubStatus="medline">
                <Year>2009</Year>
                <Month>11</Month>
                <Day>7</Day>
                <Hour>6</Hour>
                <Minute>0</Minute>
            </PubMedPubDate>
        </History>
        <PublicationStatus>aheadofprint</PublicationStatus>
        <ArticleIdList>
            <ArticleId IdType="doi">10.1007/s11481-009-9180-4</ArticleId>
            <ArticleId IdType="pubmed">19894120</ArticleId>
        </ArticleIdList>
    </PubmedData>
</PubmedArticle>

