The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing.
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| Title: | The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing. |
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| Authors: | Pfoh R; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Subramanian AS; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Huang J; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Little DJ; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Forman A; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada., DiFrancesco BR; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada., Balouchestani-Asli N; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Kitova EN; Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada., Klassen JS; Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada., Pomès R; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada., Nitz M; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada., Howell PL; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. |
| Source: | PLoS pathogens [PLoS Pathog] 2022 Aug 05; Vol. 18 (8), pp. e1010750. Date of Electronic Publication: 2022 Aug 05 (Print Publication: 2022). |
| Publication Type: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. |
| Journal Info: | Publisher: Public Library of Science Country of Publication: United States NLM ID: 101238921 Publication Model: eCollection Cited Medium: Internet ISSN: 1553-7374 (Electronic) Linking ISSN: 15537366 NLM ISO Abbreviation: PLoS Pathog Subsets: MEDLINE |
| Database: | MEDLINE Ultimate |
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| FullText | Links: – Type: pdflink Text: Availability: 1 |
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| Header | DbId: mdl DbLabel: MEDLINE Ultimate An: 35930610 AccessLevel: 2 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AU" term="%22Pfoh+R%22">Pfoh R</searchLink>; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Subramanian+AS%22">Subramanian AS</searchLink>; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Huang+J%22">Huang J</searchLink>; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Little+DJ%22">Little DJ</searchLink>; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Forman+A%22">Forman A</searchLink>; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22DiFrancesco+BR%22">DiFrancesco BR</searchLink>; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Balouchestani-Asli+N%22">Balouchestani-Asli N</searchLink>; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Kitova+EN%22">Kitova EN</searchLink>; Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada.<br /><searchLink fieldCode="AU" term="%22Klassen+JS%22">Klassen JS</searchLink>; Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada.<br /><searchLink fieldCode="AU" term="%22Pomès+R%22">Pomès R</searchLink>; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Nitz+M%22">Nitz M</searchLink>; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Howell+PL%22">Howell PL</searchLink>; Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22101238921%22">PLoS pathogens</searchLink> [PLoS Pathog] 2022 Aug 05; Vol. 18 (8), pp. e1010750. <i>Date of Electronic Publication: </i>2022 Aug 05 (<i>Print Publication: </i>2022). – Name: TypePub Label: Publication Type Group: TypPub Data: Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. – Name: TitleSource Label: Journal Info Group: Src Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Public+Library+of+Science%22">Public Library of Science </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>101238921 <i>Publication Model: </i>eCollection <i>Cited Medium: </i>Internet <i>ISSN: </i>1553-7374 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2215537366%22">15537366 </searchLink><i>NLM ISO Abbreviation: </i>PLoS Pathog <i>Subsets: </i>MEDLINE |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=mdl&AN=35930610 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1371/journal.ppat.1010750 Languages: – Code: eng Text: English PhysicalDescription: Pagination: StartPage: e1010750 Titles: – TitleFull: The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Pfoh R – PersonEntity: Name: NameFull: Subramanian AS – PersonEntity: Name: NameFull: Huang J – PersonEntity: Name: NameFull: Little DJ – PersonEntity: Name: NameFull: Forman A – PersonEntity: Name: NameFull: DiFrancesco BR – PersonEntity: Name: NameFull: Balouchestani-Asli N – PersonEntity: Name: NameFull: Kitova EN – PersonEntity: Name: NameFull: Klassen JS – PersonEntity: Name: NameFull: Pomès R – PersonEntity: Name: NameFull: Nitz M – PersonEntity: Name: NameFull: Howell PL IsPartOfRelationships: – BibEntity: Dates: – D: 05 M: 08 Text: 2022 Aug 05 Type: published Y: 2022 Identifiers: – Type: issn-electronic Value: 1553-7374 Numbering: – Type: volume Value: 18 – Type: issue Value: 8 Titles: – TitleFull: PLoS pathogens Type: main |
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