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  1. Book: Golgi

    Wang, Yanzhuang / Lupashin, Vladimir V. / Graham, Todd R.

    methods and protocols

    (Methods in molecular biology ; 2557 ; Springer protocols)

    2023  

    Author's details edited by Yanzhuang Wang, Vladimir V. Lupashin, Todd R. Graham
    Series title Methods in molecular biology ; 2557
    Springer protocols
    Collection
    Keywords Golgi apparatus
    Subject code 571.656
    Language English
    Size xvii, 816 Seiten, Illustrationen, 26 cm
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT021690760
    ISBN 978-1-0716-2638-2 ; 9781071626399 ; 1-0716-2638-8 ; 1071626396
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -2557- not available for loan Lesesaal EG

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  2. Book ; Online: Golgi Dynamics in Physiological and Pathological Conditions

    Saraste, Jaakko / Lupashin, Vladimir / Wang, Yanzhuang / Prydz, Kristian

    2020  

    Keywords Science: general issues ; Biology, life sciences ; Golgi apparatus ; Golgi dynamics ; Golgi structure ; Golgi function ; membrane trafficking
    Size 1 electronic resource (359 pages)
    Publisher Frontiers Media SA
    Document type Book ; Online
    Note English ; Open Access
    HBZ-ID HT021231292
    ISBN 9782889635399 ; 2889635392
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  3. Article ; Online: Emerging roles of O-GlcNAcylation in protein trafficking and secretion.

    Zhang, Jianchao / Wang, Yanzhuang

    The Journal of biological chemistry

    2024  Volume 300, Issue 3, Page(s) 105677

    Abstract: The emerging roles of O-GlcNAcylation, a distinctive post-translational modification, are increasingly recognized for their involvement in the intricate processes of protein trafficking and secretion. This modification exerts its influence on both ... ...

    Abstract The emerging roles of O-GlcNAcylation, a distinctive post-translational modification, are increasingly recognized for their involvement in the intricate processes of protein trafficking and secretion. This modification exerts its influence on both conventional and unconventional secretory pathways. Under healthy and stress conditions, such as during diseases, it orchestrates the transport of proteins within cells, ensuring timely delivery to their intended destinations. O-GlcNAcylation occurs on key factors, like coat protein complexes (COPI and COPII), clathrin, SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors), and GRASP55 (Golgi reassembly stacking protein of 55 kDa) that control vesicle budding and fusion in anterograde and retrograde trafficking and unconventional secretion. The understanding of O-GlcNAcylation offers valuable insights into its critical functions in cellular physiology and the progression of diseases, including neurodegeneration, cancer, and metabolic disorders. In this review, we summarize and discuss the latest findings elucidating the involvement of O-GlcNAc in protein trafficking and its significance in various human disorders.
    MeSH term(s) Humans ; Acetylglucosamine/metabolism ; Clathrin/metabolism ; Protein Processing, Post-Translational ; Protein Transport/physiology ; SNARE Proteins/metabolism ; Animals ; Acetylation ; Glucose/metabolism
    Chemical Substances Acetylglucosamine (V956696549) ; Clathrin ; SNARE Proteins ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2024-01-23
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2024.105677
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Quantitative Proteomics Analysis of Purified Rat Liver Golgi.

    Chen, Xuequn / Wang, Yanzhuang

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2557, Page(s) 417–430

    Abstract: The Golgi is the central organelle in the secretory pathway, essential for post-translational modifications, sorting and trafficking of secretory and membrane proteins and lipids in all eukaryotic cells. During mitosis, the mammalian Golgi membranes ... ...

    Abstract The Golgi is the central organelle in the secretory pathway, essential for post-translational modifications, sorting and trafficking of secretory and membrane proteins and lipids in all eukaryotic cells. During mitosis, the mammalian Golgi membranes undergo continuous disassembly and reassembly processes which are critical for Golgi biogenesis during the cell division. To better understand the underlying molecular mechanism of this highly dynamic process, we analyzed the proteins that are in or associated with interphase and mitotic Golgi membranes using an in vitro Golgi assembly assay and quantitative proteomics. In this study, by combining an isobaric mass tag labeling strategy with OFFGEL peptide fractionation, LC-MS/MS analyses identified and quantified a total of 1193 Golgi-resident or -associated proteins. These proteins included Golgi structural proteins, Golgi-resident enzymes, Rab GTPases, and SNARE proteins. This systematic quantitative proteomic study revealed the comprehensive molecular machinery of the Golgi and the dynamic protein changes in its disassembly and reassembly processes. Here we describe the detailed procedures and protocols for this analysis.
    MeSH term(s) Rats ; Animals ; Proteomics/methods ; Chromatography, Liquid ; Tandem Mass Spectrometry ; Golgi Apparatus/metabolism ; Mitosis ; SNARE Proteins/metabolism ; Liver/metabolism ; Mammals
    Chemical Substances SNARE Proteins
    Language English
    Publishing date 2022-12-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2639-9_25
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Golgi Metal Ion Homeostasis in Human Health and Diseases.

    Li, Jie / Wang, Yanzhuang

    Cells

    2022  Volume 11, Issue 2

    Abstract: The Golgi apparatus is a membrane organelle located in the center of the protein processing and trafficking pathway. It consists of sub-compartments with distinct biochemical compositions and functions. Main functions of the Golgi, including membrane ... ...

    Abstract The Golgi apparatus is a membrane organelle located in the center of the protein processing and trafficking pathway. It consists of sub-compartments with distinct biochemical compositions and functions. Main functions of the Golgi, including membrane trafficking, protein glycosylation, and sorting, require a well-maintained stable microenvironment in the sub-compartments of the Golgi, along with metal ion homeostasis. Metal ions, such as Ca
    MeSH term(s) Animals ; Disease ; Golgi Apparatus/metabolism ; Health ; Homeostasis ; Humans ; Ions ; Metals/metabolism
    Chemical Substances Ions ; Metals
    Language English
    Publishing date 2022-01-15
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells11020289
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The Golgi apparatus: Site for convergence of COVID-19 brain fog and Alzheimer's disease?

    Wang, Yanzhuang / Gandy, Sam

    Molecular neurodegeneration

    2022  Volume 17, Issue 1, Page(s) 67

    MeSH term(s) Humans ; Alzheimer Disease/metabolism ; COVID-19 ; Golgi Apparatus ; Protein Transport ; Brain
    Language English
    Publishing date 2022-10-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2244557-2
    ISSN 1750-1326 ; 1750-1326
    ISSN (online) 1750-1326
    ISSN 1750-1326
    DOI 10.1186/s13024-022-00568-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Correction to: Golgi.

    Wang, Yanzhuang / Lupashin, Vladimir V / Graham, Todd R

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2557, Page(s) C1

    Language English
    Publishing date 2023-02-10
    Publishing country United States
    Document type Published Erratum
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2639-9_48
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Analysis of mannosidase I activity in interphase and mitotic cells by lectin staining and endoglycosidase H treatment.

    Li, Jie / Zhang, Jianchao / Wang, Yanzhuang

    STAR protocols

    2023  Volume 4, Issue 2, Page(s) 102283

    Abstract: N-Glycosylation is a common protein modification catalyzed by a series of glycosylation enzymes in the endoplasmic reticulum and Golgi apparatus. Here, based on a previously established Golgi α-mannosidase-I-deficient cell line, we present a protocol to ... ...

    Abstract N-Glycosylation is a common protein modification catalyzed by a series of glycosylation enzymes in the endoplasmic reticulum and Golgi apparatus. Here, based on a previously established Golgi α-mannosidase-I-deficient cell line, we present a protocol to investigate the enzymatic activity of exogenously expressed Golgi α-mannosidase IA in interphase and mitotic cells. We describe steps for cell surface lectin staining and subsequent live cell imaging. We also detail PNGase F and Endo H cleavage assays to analyze protein glycosylation. For complete details on the use and execution of this protocol, please refer to Huang et al.
    Language English
    Publishing date 2023-05-05
    Publishing country United States
    Document type Journal Article
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2023.102283
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: HACE1 (HECT domain and ankyrin repeat containing E3 ubiquitin protein ligase 1).

    Cui, Feng / Wang, Yanzhuang

    Atlas of genetics and cytogenetics in oncology and haematology

    2021  Volume 2013, Issue 5, Page(s) 333–336

    Language English
    Publishing date 2021-10-22
    Publishing country France
    Document type Journal Article
    ISSN 1768-3262
    ISSN 1768-3262
    DOI 10.4267/2042/49701
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Generation of Stable Cell Lines Expressing Golgi Reassembly Stacking Proteins (GRASPs) by Viral Transduction.

    Bui, Sarah / Li, Jie / Stark, Drew / Houmani, Ali / Wang, Yanzhuang

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2557, Page(s) 391–416

    Abstract: Stable cell lines that express a gene of specific interest provide an advantage over transient gene expression by reducing variations in transfection efficiency between experiments, sustaining expression for long-term studies, and controlling expression ... ...

    Abstract Stable cell lines that express a gene of specific interest provide an advantage over transient gene expression by reducing variations in transfection efficiency between experiments, sustaining expression for long-term studies, and controlling expression levels in particular if a clonal population is selected. Transient transfection requires introduction of an exogenous gene into host cells via typically harsh chemicals or conditions that permeabilize the cell membrane, which does not normally integrate into the target cell genome. Here, we describe the method of using retroviral transduction to stably express Golgi proteins fused to a promiscuous biotin ligase (TurboID) in HeLa cells, thus creating cell lines that can be leveraged in studies of the proximome/interactome. We also demonstrate a similar protocol for stable expression of a Golgi protein fused to a fluorescent tag via lentiviral transduction. These methods can be further adapted to establish other cell lines with different sub-cellular markers or fusion tags. Viral transduction is a convenient method to create stable cell lines in cell-based studies.
    MeSH term(s) Humans ; Golgi Matrix Proteins/metabolism ; HeLa Cells ; Transfection ; Retroviridae ; Transduction, Genetic ; Golgi Apparatus/metabolism
    Chemical Substances Golgi Matrix Proteins
    Language English
    Publishing date 2023-05-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2639-9_24
    Database MEDical Literature Analysis and Retrieval System OnLINE

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