How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view.
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| Title: | How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view. |
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| Authors: | Castelli M; Department of Chemistry, University of Pavia, via Taramelli 12, 27100 Pavia, Italy., Yan P; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA., Rodina A; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA., Digwal CS; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA., Panchal P; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA., Chiosis G; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA; Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA. Electronic address: chiosisg@mskcc.org., Moroni E; SCITEC-CNR, via Mario Bianco 9, 20131 Milano, Italy. Electronic address: elisabetta.moroni@scitec.cnr.it., Colombo G; Department of Chemistry, University of Pavia, via Taramelli 12, 27100 Pavia, Italy. Electronic address: g.colombo@unipv.it. |
| Source: | Structure (London, England : 1993) [Structure] 2023 Aug 03; Vol. 31 (8), pp. 987-1004.e8. Date of Electronic Publication: 2023 Jun 20. |
| Publication Type: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural |
| Journal Info: | Publisher: Cell Press Country of Publication: United States NLM ID: 101087697 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1878-4186 (Electronic) Linking ISSN: 09692126 NLM ISO Abbreviation: Structure Subsets: MEDLINE |
| Database: | MEDLINE Ultimate |
| FullText | Text: Availability: 0 |
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| Header | DbId: mdl DbLabel: MEDLINE Ultimate An: 37343552 AccessLevel: 2 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AU" term="%22Castelli+M%22">Castelli M</searchLink>; Department of Chemistry, University of Pavia, via Taramelli 12, 27100 Pavia, Italy.<br /><searchLink fieldCode="AU" term="%22Yan+P%22">Yan P</searchLink>; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.<br /><searchLink fieldCode="AU" term="%22Rodina+A%22">Rodina A</searchLink>; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.<br /><searchLink fieldCode="AU" term="%22Digwal+CS%22">Digwal CS</searchLink>; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.<br /><searchLink fieldCode="AU" term="%22Panchal+P%22">Panchal P</searchLink>; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.<br /><searchLink fieldCode="AU" term="%22Chiosis+G%22">Chiosis G</searchLink>; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA; Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA. Electronic address: chiosisg@mskcc.org.<br /><searchLink fieldCode="AU" term="%22Moroni+E%22">Moroni E</searchLink>; SCITEC-CNR, via Mario Bianco 9, 20131 Milano, Italy. Electronic address: elisabetta.moroni@scitec.cnr.it.<br /><searchLink fieldCode="AU" term="%22Colombo+G%22">Colombo G</searchLink>; Department of Chemistry, University of Pavia, via Taramelli 12, 27100 Pavia, Italy. Electronic address: g.colombo@unipv.it. – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22101087697%22">Structure (London, England : 1993)</searchLink> [Structure] 2023 Aug 03; Vol. 31 (8), pp. 987-1004.e8. <i>Date of Electronic Publication: </i>2023 Jun 20. – Name: TypePub Label: Publication Type Group: TypPub Data: Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural – Name: TitleSource Label: Journal Info Group: Src Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Cell+Press%22">Cell Press </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>101087697 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1878-4186 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2209692126%22">09692126 </searchLink><i>NLM ISO Abbreviation: </i>Structure <i>Subsets: </i>MEDLINE |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=mdl&AN=37343552 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.str.2023.05.017 Languages: – Code: eng Text: English PhysicalDescription: Pagination: StartPage: 987 Titles: – TitleFull: How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Castelli M – PersonEntity: Name: NameFull: Yan P – PersonEntity: Name: NameFull: Rodina A – PersonEntity: Name: NameFull: Digwal CS – PersonEntity: Name: NameFull: Panchal P – PersonEntity: Name: NameFull: Chiosis G – PersonEntity: Name: NameFull: Moroni E – PersonEntity: Name: NameFull: Colombo G IsPartOfRelationships: – BibEntity: Dates: – D: 03 M: 08 Text: 2023 Aug 03 Type: published Y: 2023 Identifiers: – Type: issn-electronic Value: 1878-4186 Numbering: – Type: volume Value: 31 – Type: issue Value: 8 Titles: – TitleFull: Structure (London, England : 1993) Type: main |
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