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  1. Artikel: Multimodal identification of rare potent effector CD8 T cells in solid tumors.

    Ray, Arja / Bassette, Molly / Hu, Kenneth H / Pass, Lomax F / Samad, Bushra / Combes, Alexis / Johri, Vrinda / Davidson, Brittany / Hernandez, Grace / Zaleta-Linares, Itzia / Krummel, Matthew F

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Antitumor immunity is driven by CD8 T cells, yet we lack signatures for the exceptional effectors in tumors, amongst the vast majority of CD8 T cells undergoing exhaustion. By leveraging the measurement of a canonical T cell activation protein (CD69) ... ...

    Abstract Antitumor immunity is driven by CD8 T cells, yet we lack signatures for the exceptional effectors in tumors, amongst the vast majority of CD8 T cells undergoing exhaustion. By leveraging the measurement of a canonical T cell activation protein (CD69) together with its RNA (
    Sprache Englisch
    Erscheinungsdatum 2023-09-28
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.09.26.559470
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Quantitative Effects of O-Linked Glycans on Protein Folding

    Chaffey, Patrick K / Guan Xiaoyang / Wang Xinfeng / Ruan Yuan / Li Yaohao / Miller Suzannah G / Tran Amy H / Koelsch Theo N / Pass Lomax F / Tan Zhongping

    Biochemistry. 2017 Aug. 29, v. 56, no. 34

    2017  

    Abstract: Protein O-glycosylation is a diverse, common, and important post-translational modification of both proteins inside the cell and those that are secreted or membrane-bound. Much work has shown that O-glycosylation can alter the structure, function, and ... ...

    Abstract Protein O-glycosylation is a diverse, common, and important post-translational modification of both proteins inside the cell and those that are secreted or membrane-bound. Much work has shown that O-glycosylation can alter the structure, function, and physical properties of the proteins to which it is attached. One gap remaining in our understanding of O-glycoproteins is how O-glycans might affect the folding of proteins. Here, we took advantage of synthetic, homogeneous O-glycopeptides to show that certain glycosylation patterns have an intrinsic effect, independent of any cellular folding machinery, on the folding pathway of a model O-glycoprotein, a carbohydrate binding module (CBM) derived from the Trichoderma reesei cellulase TrCel7A. The strongest effect, a 6-fold increase in overall folding rate, was observed when a single O-mannose was the glycan, and the glycosylation site was near the N-terminus of the peptide sequence. We were also able to show that glycosylation patterns affected the kinetics of each step in unique ways, which may help to explain the observations made here. This work is a first step toward quantitative understanding of how O-glycosylation might control, through intrinsic means, the folding of O-glycoproteins. Such an understanding is expected to facilitate future investigations into the effects of glycosylation on more biological processes related to protein folding.
    Schlagwörter Trichoderma reesei ; carbohydrate binding ; endo-1,4-beta-glucanase ; glycosylation ; models ; physical properties ; polysaccharides ; protein folding ; proteins
    Sprache Englisch
    Erscheinungsverlauf 2017-0829
    Umfang p. 4539-4548.
    Erscheinungsort American Chemical Society
    Dokumenttyp Artikel
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021%2Facs.biochem.7b00483
    Datenquelle NAL Katalog (AGRICOLA)

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  3. Artikel ; Online: Quantitative Effects of O-Linked Glycans on Protein Folding.

    Chaffey, Patrick K / Guan, Xiaoyang / Wang, Xinfeng / Ruan, Yuan / Li, Yaohao / Miller, Suzannah G / Tran, Amy H / Koelsch, Theo N / Pass, Lomax F / Tan, Zhongping

    Biochemistry

    2017  Band 56, Heft 34, Seite(n) 4539–4548

    Abstract: Protein O-glycosylation is a diverse, common, and important post-translational modification of both proteins inside the cell and those that are secreted or membrane-bound. Much work has shown that O-glycosylation can alter the structure, function, and ... ...

    Abstract Protein O-glycosylation is a diverse, common, and important post-translational modification of both proteins inside the cell and those that are secreted or membrane-bound. Much work has shown that O-glycosylation can alter the structure, function, and physical properties of the proteins to which it is attached. One gap remaining in our understanding of O-glycoproteins is how O-glycans might affect the folding of proteins. Here, we took advantage of synthetic, homogeneous O-glycopeptides to show that certain glycosylation patterns have an intrinsic effect, independent of any cellular folding machinery, on the folding pathway of a model O-glycoprotein, a carbohydrate binding module (CBM) derived from the Trichoderma reesei cellulase TrCel7A. The strongest effect, a 6-fold increase in overall folding rate, was observed when a single O-mannose was the glycan, and the glycosylation site was near the N-terminus of the peptide sequence. We were also able to show that glycosylation patterns affected the kinetics of each step in unique ways, which may help to explain the observations made here. This work is a first step toward quantitative understanding of how O-glycosylation might control, through intrinsic means, the folding of O-glycoproteins. Such an understanding is expected to facilitate future investigations into the effects of glycosylation on more biological processes related to protein folding.
    Mesh-Begriff(e) Cellulase/chemistry ; Cellulase/genetics ; Cellulase/metabolism ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Glycoproteins/chemistry ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Polysaccharides/chemistry ; Polysaccharides/genetics ; Polysaccharides/metabolism ; Protein Folding ; Trichoderma/enzymology ; Trichoderma/genetics
    Chemische Substanzen Fungal Proteins ; Glycoproteins ; Polysaccharides ; Cellulase (EC 3.2.1.4)
    Sprache Englisch
    Erscheinungsdatum 2017-08-29
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.7b00483
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

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