Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts.
Identifieur interne : 000507 ( Main/Exploration ); précédent : 000506; suivant : 000508Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts.
Auteurs : Michele Scian [États-Unis] ; William M. Atkins [États-Unis]Source :
- Data in brief [ 2352-3409 ] ; 2015.
Abstract
This article describes data related to a research article titled "The Busulfan Metabolite EdAG Irreversibly Glutathionylates Glutaredoxins" [1]. EdAG is an electrophilic GSH analog formed in vivo from busulfan, which is used in hematopoietic stem cell transplants. EdAG glutathionylates Glutaredoxins (Grx's) but not glutathione transferase A1-1 (GSTA1-1) in vitro. This article includes a complete NMR characterization of synthetic EdAG including homonuclear and heteronuclear correlation spectra. Also included are mass spectra of peptides from Grx's or GSTA1-1 that have cys residues that do not react with EdAG.
DOI: 10.1016/j.dib.2015.09.002
PubMed: 26501085
PubMed Central: PMC4588412
Affiliations:
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Atkins</name><affiliation wicri:level="4"><nlm:affiliation>Department of Medicinal Chemistry, University of Washington, United States.</nlm:affiliation><orgName type="university">Université de Washington</orgName><country>États-Unis</country><placeName><settlement type="city">Seattle</settlement><region type="state">Washington (État)</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26501085</idno><idno type="pmid">26501085</idno><idno type="doi">10.1016/j.dib.2015.09.002</idno><idno type="pmc">PMC4588412</idno><idno type="wicri:Area/Main/Corpus">000492</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000492</idno><idno type="wicri:Area/Main/Curation">000492</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000492</idno><idno type="wicri:Area/Main/Exploration">000492</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts.</title><author><name sortKey="Scian, Michele" sort="Scian, Michele" uniqKey="Scian M" first="Michele" last="Scian">Michele Scian</name><affiliation wicri:level="4"><nlm:affiliation>Department of Medicinal Chemistry, University of Washington, United States.</nlm:affiliation><orgName type="university">Université de Washington</orgName><country>États-Unis</country><placeName><settlement type="city">Seattle</settlement><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Atkins, William M" sort="Atkins, William M" uniqKey="Atkins W" first="William M" last="Atkins">William M. Atkins</name><affiliation wicri:level="4"><nlm:affiliation>Department of Medicinal Chemistry, University of Washington, United States.</nlm:affiliation><orgName type="university">Université de Washington</orgName><country>États-Unis</country><placeName><settlement type="city">Seattle</settlement><region type="state">Washington (État)</region></placeName></affiliation></author></analytic><series><title level="j">Data in brief</title><idno type="ISSN">2352-3409</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">This article describes data related to a research article titled "The Busulfan Metabolite EdAG Irreversibly Glutathionylates Glutaredoxins" [1]. EdAG is an electrophilic GSH analog formed in vivo from busulfan, which is used in hematopoietic stem cell transplants. EdAG glutathionylates Glutaredoxins (Grx's) but not glutathione transferase A1-1 (GSTA1-1) in vitro. This article includes a complete NMR characterization of synthetic EdAG including homonuclear and heteronuclear correlation spectra. Also included are mass spectra of peptides from Grx's or GSTA1-1 that have cys residues that do not react with EdAG. </div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">26501085</PMID><DateCompleted><Year>2015</Year><Month>10</Month><Day>27</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2352-3409</ISSN><JournalIssue CitedMedium="Print"><Volume>5</Volume><PubDate><Year>2015</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Data in brief</Title><ISOAbbreviation>Data Brief</ISOAbbreviation></Journal><ArticleTitle>Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts.</ArticleTitle><Pagination><MedlinePgn>161-70</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.dib.2015.09.002</ELocationID><Abstract><AbstractText>This article describes data related to a research article titled "The Busulfan Metabolite EdAG Irreversibly Glutathionylates Glutaredoxins" [1]. EdAG is an electrophilic GSH analog formed in vivo from busulfan, which is used in hematopoietic stem cell transplants. EdAG glutathionylates Glutaredoxins (Grx's) but not glutathione transferase A1-1 (GSTA1-1) in vitro. This article includes a complete NMR characterization of synthetic EdAG including homonuclear and heteronuclear correlation spectra. Also included are mass spectra of peptides from Grx's or GSTA1-1 that have cys residues that do not react with EdAG. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Scian</LastName><ForeName>Michele</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, University of Washington, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Atkins</LastName><ForeName>William M</ForeName><Initials>WM</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, University of Washington, United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 CA182963</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>09</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Data Brief</MedlineTA><NlmUniqueID>101654995</NlmUniqueID><ISSNLinking>2352-3409</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>08</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>08</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>09</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>10</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>10</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>10</Month><Day>27</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26501085</ArticleId><ArticleId IdType="doi">10.1016/j.dib.2015.09.002</ArticleId><ArticleId IdType="pii">S2352-3409(15)00196-1</ArticleId><ArticleId IdType="pmc">PMC4588412</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biomol NMR. 1992 Nov;2(6):661-5</Citation><ArticleIdList><ArticleId IdType="pubmed">1490109</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 2015 Oct 1;583:96-104</Citation><ArticleIdList><ArticleId IdType="pubmed">26278353</ArticleId></ArticleIdList></Reference><Reference><Citation>J Magn Reson B. 1994 May;104(1):1-10</Citation><ArticleIdList><ArticleId IdType="pubmed">8025810</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Washington (État)</li></region><settlement><li>Seattle</li></settlement><orgName><li>Université de Washington</li></orgName></list><tree><country name="États-Unis"><region name="Washington (État)"><name sortKey="Scian, Michele" sort="Scian, Michele" uniqKey="Scian M" first="Michele" last="Scian">Michele Scian</name></region><name sortKey="Atkins, William M" sort="Atkins, William M" uniqKey="Atkins W" first="William M" last="Atkins">William M. 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