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  1. Article ; Online: Folding the Mitochondrial UPR into the Integrated Stress Response.

    Anderson, Nadine S / Haynes, Cole M

    Trends in cell biology

    2020  Volume 30, Issue 6, Page(s) 428–439

    Abstract: Eukaryotic cells must accurately monitor the integrity of the mitochondrial network to overcome environmental insults and respond to physiological cues. The mitochondrial unfolded protein response ( ... ...

    Abstract Eukaryotic cells must accurately monitor the integrity of the mitochondrial network to overcome environmental insults and respond to physiological cues. The mitochondrial unfolded protein response (UPR
    MeSH term(s) Animals ; Humans ; Mitochondria/metabolism ; Protein Biosynthesis ; Signal Transduction ; Stress, Physiological ; Unfolded Protein Response
    Language English
    Publishing date 2020-04-02
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2020.03.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 25: Show issues
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    Zs.A 3410: Show issues Location:
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  2. Article ; Online: Conserved juxtamembrane domains in the yeast golgin Coy1 drive assembly of a megadalton-sized complex and mediate binding to tethering and SNARE proteins.

    Anderson, Nadine S / Barlowe, Charles

    The Journal of biological chemistry

    2019  Volume 294, Issue 25, Page(s) 9690–9705

    Abstract: The architecture and organization of the Golgi complex depend on a family of coiled-coil proteins called golgins. Golgins are thought to form extended homodimers that are C-terminally anchored to Golgi membranes, whereas their N termini extend into the ... ...

    Abstract The architecture and organization of the Golgi complex depend on a family of coiled-coil proteins called golgins. Golgins are thought to form extended homodimers that are C-terminally anchored to Golgi membranes, whereas their N termini extend into the cytoplasm to initiate vesicle capture. Previously, we reported that the
    MeSH term(s) Biological Transport ; Cell Membrane/metabolism ; Golgi Apparatus ; Golgi Matrix Proteins/genetics ; Golgi Matrix Proteins/metabolism ; Macromolecular Substances/metabolism ; Protein Binding ; SNARE Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Coy1 protein, S cerevisiae ; Golgi Matrix Proteins ; Macromolecular Substances ; SNARE Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2019-05-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA119.008107
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Antibody charge variant modulation by in vitro enzymatic treatment in different Chinese hamster ovary cell cultures.

    Xu, Jianlin / Santos, Johanna / Anderson, Nadine S / Borys, Michael C / Pendse, Girish / Li, Zheng Jian

    Biotechnology progress

    2022  Volume 38, Issue 5, Page(s) e3268

    Abstract: Charge variants represent a critical quality attribute that must be controlled during the development and manufacturing of monoclonal antibodies (mAb). Previously, we reported the development of a cost-effective enzymatic treatment capable of removing ... ...

    Abstract Charge variants represent a critical quality attribute that must be controlled during the development and manufacturing of monoclonal antibodies (mAb). Previously, we reported the development of a cost-effective enzymatic treatment capable of removing the C-terminal lysine from a mAb produced by a Chinese hamster ovary (CHO) GS cell line. This treatment resulted in a significant decrease in basic charge variants and a corresponding improvement in the main peak, enabling a longer cell culture production duration for titer improvement. Here, we describe this enzymatic treatment protocol in detail and demonstrate its applicability to two additional mAbs produced by distinct industrial cell lines. The simple addition of carboxypeptidase B (CpB) at a ratio of 1:10,000 (w/w) to whole cell cultures significantly improved the main peaks for both mAbs without affecting other critical quality attributes, including size exclusion chromatography impurities and N-glycans. Our results demonstrate that this in vitro CpB treatment protocol can be used as a platform strategy to improve main peak for mAbs that exhibit high levels of basic variants attributable to C-terminal lysines. An in vitro enzymatic treatment in general may be another good addition to existing in vivo CHO cell culture strategies for titer improvement and control of critical quality attributes.
    MeSH term(s) Animals ; Antibodies, Monoclonal/chemistry ; CHO Cells ; Carboxypeptidase B ; Cell Culture Techniques ; Cricetinae ; Cricetulus ; Lysine/metabolism ; Polysaccharides
    Chemical Substances Antibodies, Monoclonal ; Polysaccharides ; Carboxypeptidase B (EC 3.4.17.2) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2022-05-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 165657-0
    ISSN 1520-6033 ; 8756-7938
    ISSN (online) 1520-6033
    ISSN 8756-7938
    DOI 10.1002/btpr.3268
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4253: Show issues Location:
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  4. Article ; Online: The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs.

    Anderson, Nadine S / Mukherjee, Indrani / Bentivoglio, Christine M / Barlowe, Charles

    Molecular biology of the cell

    2017  

    Abstract: Extended coiled-coil proteins of the Golgin family play prominent roles in maintaining the structure and function of the Golgi complex. Here we further investigate the Golgin protein Coy1 and document its function in retrograde transport between early ... ...

    Abstract Extended coiled-coil proteins of the Golgin family play prominent roles in maintaining the structure and function of the Golgi complex. Here we further investigate the Golgin protein Coy1 and document its function in retrograde transport between early Golgi compartments. Cells that lack Coy1 displayed a reduced half-life of the Och1 mannosyltransferase, an established cargo of intra-Golgi retrograde transport. Combining the
    Language English
    Publishing date 2017-08-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E17-03-0137
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 410: Show issues

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  5. Article ; Online: LONP-1 and ATFS-1 sustain deleterious heteroplasmy by promoting mtDNA replication in dysfunctional mitochondria.

    Yang, Qiyuan / Liu, Pengpeng / Anderson, Nadine S / Shpilka, Tomer / Du, YunGuang / Naresh, Nandhitha Uma / Li, Rui / Zhu, Lihua Julie / Luk, Kevin / Lavelle, Josh / Zeinert, Rilee D / Chien, Peter / Wolfe, Scot A / Haynes, Cole M

    Nature cell biology

    2022  Volume 24, Issue 2, Page(s) 181–193

    Abstract: The accumulation of deleterious mitochondrial DNA (∆mtDNA) causes inherited mitochondrial diseases and ageing-associated decline in mitochondrial functions such as oxidative phosphorylation. Following mitochondrial perturbations, the bZIP protein ATFS-1 ... ...

    Abstract The accumulation of deleterious mitochondrial DNA (∆mtDNA) causes inherited mitochondrial diseases and ageing-associated decline in mitochondrial functions such as oxidative phosphorylation. Following mitochondrial perturbations, the bZIP protein ATFS-1 induces a transcriptional programme to restore mitochondrial function. Paradoxically, ATFS-1 is also required to maintain ∆mtDNAs in heteroplasmic worms. The mechanism by which ATFS-1 promotes ∆mtDNA accumulation relative to wild-type mtDNAs is unclear. Here we show that ATFS-1 accumulates in dysfunctional mitochondria. ATFS-1 is absent in healthy mitochondria owing to degradation by the mtDNA-bound protease LONP-1, which results in the nearly exclusive association between ATFS-1 and ∆mtDNAs in heteroplasmic worms. Moreover, we demonstrate that mitochondrial ATFS-1 promotes the binding of the mtDNA replicative polymerase (POLG) to ∆mtDNAs. Interestingly, inhibition of the mtDNA-bound protease LONP-1 increased ATFS-1 and POLG binding to wild-type mtDNAs. LONP-1 inhibition in Caenorhabditis elegans and human cybrid cells improved the heteroplasmy ratio and restored oxidative phosphorylation. Our findings suggest that ATFS-1 promotes mtDNA replication in dysfunctional mitochondria by promoting POLG-mtDNA binding, which is antagonized by LONP-1.
    MeSH term(s) Animals ; Humans ; Animals, Genetically Modified ; ATP-Dependent Proteases/genetics ; ATP-Dependent Proteases/metabolism ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Line ; DNA Polymerase gamma/genetics ; DNA Polymerase gamma/metabolism ; DNA Replication ; DNA, Mitochondrial/biosynthesis ; DNA, Mitochondrial/genetics ; Heteroplasmy ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondria/pathology ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Oxidative Phosphorylation ; Proteolysis ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances ATFS-1 protein, C elegans ; ATP-Dependent Proteases (EC 3.4.21.-) ; Caenorhabditis elegans Proteins ; DNA Polymerase gamma (EC 2.7.7.7) ; DNA, Mitochondrial ; LONP1 protein, human (EC 3.4.21.-) ; Mitochondrial Proteins ; Polg-1 protein, C elegans (EC 2.7.7.7) ; Transcription Factors ; LONP-1 protein, C elegans
    Language English
    Publishing date 2022-02-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/s41556-021-00840-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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