View in EDS HTML Full Text PDF Full Text

The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.

Saved in:
Bibliographic Details
Title: The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.
Authors: Koy C; Proteome Center Rostock, Medical Faculty and Natural Science Faculty, University of Rostock, Schillingallee 69, 18057, Rostock, Germany., Zimmer T; Department of Chemistry, Philipps-University Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany., Opuni KFM; Department of Pharmaceutical Chemistry, School of Pharmacy, College of Health Science, University of Ghana, P.O. Box LG43, Legon, Ghana., Geyer A; Department of Chemistry, Philipps-University Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany., Glocker MO; Proteome Center Rostock, Medical Faculty and Natural Science Faculty, University of Rostock, Schillingallee 69, 18057, Rostock, Germany. michael.glocker@uni-rostock.de.
Source: Scientific reports [Sci Rep] 2025 Nov 22; Vol. 15 (1), pp. 41467. Date of Electronic Publication: 2025 Nov 22.
Publication Type: Journal Article
Journal Info: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE
Database: MEDLINE Ultimate
Full text is not displayed to guests.
FullText Links:
  – Type: pdflink
Text:
  Availability: 1
Header DbId: mdl
DbLabel: MEDLINE Ultimate
An: 41274901
AccessLevel: 2
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AU" term="%22Koy+C%22">Koy C</searchLink>; Proteome Center Rostock, Medical Faculty and Natural Science Faculty, University of Rostock, Schillingallee 69, 18057, Rostock, Germany.<br /><searchLink fieldCode="AU" term="%22Zimmer+T%22">Zimmer T</searchLink>; Department of Chemistry, Philipps-University Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany.<br /><searchLink fieldCode="AU" term="%22Opuni+KFM%22">Opuni KFM</searchLink>; Department of Pharmaceutical Chemistry, School of Pharmacy, College of Health Science, University of Ghana, P.O. Box LG43, Legon, Ghana.<br /><searchLink fieldCode="AU" term="%22Geyer+A%22">Geyer A</searchLink>; Department of Chemistry, Philipps-University Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany.<br /><searchLink fieldCode="AU" term="%22Glocker+MO%22">Glocker MO</searchLink>; Proteome Center Rostock, Medical Faculty and Natural Science Faculty, University of Rostock, Schillingallee 69, 18057, Rostock, Germany. michael.glocker@uni-rostock.de.
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22101563288%22">Scientific reports</searchLink> [Sci Rep] 2025 Nov 22; Vol. 15 (1), pp. 41467. <i>Date of Electronic Publication: </i>2025 Nov 22.
– Name: TypePub
  Label: Publication Type
  Group: TypPub
  Data: Journal Article
– Name: TitleSource
  Label: Journal Info
  Group: Src
  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Nature+Publishing+Group%22">Nature Publishing Group </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>101563288 <i>Publication Model: </i>Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>2045-2322 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2220452322%22">20452322 </searchLink><i>NLM ISO Abbreviation: </i>Sci Rep <i>Subsets: </i>MEDLINE
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=mdl&AN=41274901
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1038/s41598-025-28101-7
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 41467
    Titles:
      – TitleFull: The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Koy C
      – PersonEntity:
          Name:
            NameFull: Zimmer T
      – PersonEntity:
          Name:
            NameFull: Opuni KFM
      – PersonEntity:
          Name:
            NameFull: Geyer A
      – PersonEntity:
          Name:
            NameFull: Glocker MO
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 22
              M: 11
              Text: 2025 Nov 22
              Type: published
              Y: 2025
          Identifiers:
            – Type: issn-electronic
              Value: 2045-2322
          Numbering:
            – Type: volume
              Value: 15
            – Type: issue
              Value: 1
          Titles:
            – TitleFull: Scientific reports
              Type: main
ResultId 1