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  1. Article: 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 (
    Language English
    Publishing date 2023-09-28
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.09.26.559470
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: 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.
    Keywords Trichoderma reesei ; carbohydrate binding ; endo-1,4-beta-glucanase ; glycosylation ; models ; physical properties ; polysaccharides ; protein folding ; proteins
    Language English
    Dates of publication 2017-0829
    Size p. 4539-4548.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021%2Facs.biochem.7b00483
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

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  3. Article ; 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  Volume 56, Issue 34, Page(s) 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 term(s) 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
    Chemical Substances Fungal Proteins ; Glycoproteins ; Polysaccharides ; Cellulase (EC 3.2.1.4)
    Language English
    Publishing date 2017-08-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.7b00483
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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