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  1. Article ; Online: Lambda Red-Mediated Recombination in Shiga Toxin-Producing Escherichia coli.

    Campellone, Kenneth G / Coulter, Alyssa M

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

    2021  Volume 2291, Page(s) 145–162

    Abstract: The bacteriophage Lambda (λ) "Red" recombination system has enabled the development of efficient methods for engineering bacterial chromosomes. This system has been particularly important to the field of bacterial pathogenesis, where it has advanced the ... ...

    Abstract The bacteriophage Lambda (λ) "Red" recombination system has enabled the development of efficient methods for engineering bacterial chromosomes. This system has been particularly important to the field of bacterial pathogenesis, where it has advanced the study of virulence factors from Shiga toxin-producing and enteropathogenic Escherichia coli (STEC and EPEC). Transient plasmid-driven expression of Lambda Red allows homologous recombination between PCR-derived linear DNA substrates and target loci in the STEC/EPEC chromosomes. Red-associated techniques can be used to create individual gene knockouts, generate deletions of large pathogenicity islands, and make markerless allelic exchanges. This chapter describes specific strategies and procedures for performing Lambda Red-mediated genome engineering in STEC.
    MeSH term(s) Bacteriophage lambda/genetics ; Bacteriophage lambda/metabolism ; Enteropathogenic Escherichia coli/genetics ; Enteropathogenic Escherichia coli/metabolism ; Escherichia coli Infections/genetics ; Escherichia coli Infections/metabolism ; Recombination, Genetic ; Shiga-Toxigenic Escherichia coli/genetics ; Shiga-Toxigenic Escherichia coli/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances Viral Proteins
    Language English
    Publishing date 2021-03-11
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1339-9_6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: WHAMM functions in kidney reabsorption and polymerizes actin to promote autophagosomal membrane closure and cargo sequestration.

    Coulter, Alyssa M / Cortés, Valerie / Theodore, Corey J / Cianciolo, Rachel E / Korstanje, Ron / Campellone, Kenneth G

    Molecular biology of the cell

    2024  Volume 35, Issue 6, Page(s) ar80

    Abstract: The actin cytoskeleton is essential for many functions of eukaryotic cells, but the factors that nucleate actin assembly are not well understood at the organismal level or in the context of disease. To explore the function of the actin nucleation factor ... ...

    Abstract The actin cytoskeleton is essential for many functions of eukaryotic cells, but the factors that nucleate actin assembly are not well understood at the organismal level or in the context of disease. To explore the function of the actin nucleation factor WHAMM in mice, we examined how
    MeSH term(s) Animals ; Mice ; Actins/metabolism ; Autophagy/physiology ; Mice, Knockout ; Humans ; Autophagosomes/metabolism ; Kidney/metabolism ; Male ; Kidney Tubules, Proximal/metabolism ; Actin Cytoskeleton/metabolism ; Actin-Related Protein 2-3 Complex/metabolism ; Membrane Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Polymerization ; Fibroblasts/metabolism
    Chemical Substances Actins ; Actin-Related Protein 2-3 Complex ; Membrane Proteins ; Microtubule-Associated Proteins ; WHAMM protein, human
    Language English
    Publishing date 2024-04-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E24-01-0025
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 410: Show issues

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  3. Article: WHAMM functions in kidney reabsorption and polymerizes actin to promote autophagosomal membrane closure and cargo sequestration.

    Coulter, Alyssa M / Cortés, Valerie / Theodore, Corey J / Cianciolo, Rachel E / Korstanje, Ron / Campellone, Kenneth G

    bioRxiv : the preprint server for biology

    2024  

    Abstract: The actin cytoskeleton is essential for many functions of eukaryotic cells, but the factors that nucleate actin assembly are not well understood at the organismal level or in the context of disease. To explore the function of the actin nucleation factor ... ...

    Abstract The actin cytoskeleton is essential for many functions of eukaryotic cells, but the factors that nucleate actin assembly are not well understood at the organismal level or in the context of disease. To explore the function of the actin nucleation factor WHAMM in mice, we examined how
    Language English
    Publishing date 2024-01-23
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.01.22.576497
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: The actin nucleation factors JMY and WHAMM enable a rapid Arp2/3 complex-mediated intrinsic pathway of apoptosis.

    King, Virginia L / Leclair, Nathan K / Coulter, Alyssa M / Campellone, Kenneth G

    PLoS genetics

    2021  Volume 17, Issue 4, Page(s) e1009512

    Abstract: The actin cytoskeleton is a well-known player in most vital cellular processes, but comparably little is understood about how the actin assembly machinery impacts programmed cell death pathways. In the current study, we explored roles for the human ... ...

    Abstract The actin cytoskeleton is a well-known player in most vital cellular processes, but comparably little is understood about how the actin assembly machinery impacts programmed cell death pathways. In the current study, we explored roles for the human Wiskott-Aldrich Syndrome Protein (WASP) family of actin nucleation factors in DNA damage-induced apoptosis. Inactivation of each WASP-family gene revealed that two of them, JMY and WHAMM, are necessary for rapid apoptotic responses. JMY and WHAMM participate in a p53-dependent cell death pathway by enhancing mitochondrial permeabilization, initiator caspase cleavage, and executioner caspase activation. JMY-mediated apoptosis requires actin nucleation via the Arp2/3 complex, and actin filaments are assembled in cytoplasmic territories containing clusters of cytochrome c and active caspase-3. The loss of JMY additionally results in significant changes in gene expression, including upregulation of the WHAMM-interacting G-protein RhoD. Depletion or deletion of RHOD increases cell death, suggesting that RhoD normally contributes to cell survival. These results give rise to a model in which JMY and WHAMM promote intrinsic cell death responses that can be opposed by RhoD.
    MeSH term(s) Actin Cytoskeleton/genetics ; Actin-Related Protein 2/genetics ; Actin-Related Protein 2-3 Complex/genetics ; Actin-Related Protein 3/genetics ; Apoptosis/genetics ; Cytochromes c/genetics ; DNA Damage/genetics ; Humans ; Membrane Proteins/genetics ; Microtubule-Associated Proteins/genetics ; Mitochondria/genetics ; Mitochondria/metabolism ; Nuclear Proteins/genetics ; RNA, Small Interfering/genetics ; Trans-Activators/genetics ; Tumor Suppressor Protein p53/genetics ; Wiskott-Aldrich Syndrome/genetics ; Wiskott-Aldrich Syndrome Protein/genetics ; rho GTP-Binding Proteins/genetics
    Chemical Substances ACTR3 protein, human ; Actin-Related Protein 2 ; Actin-Related Protein 2-3 Complex ; Actin-Related Protein 3 ; JMY protein, human ; Membrane Proteins ; Microtubule-Associated Proteins ; Nuclear Proteins ; RNA, Small Interfering ; TP53 protein, human ; Trans-Activators ; Tumor Suppressor Protein p53 ; WAS protein, human ; WHAMM protein, human ; Wiskott-Aldrich Syndrome Protein ; Cytochromes c (9007-43-6) ; RHOD protein, human (EC 3.6.1-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2021-04-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2186725-2
    ISSN 1553-7404 ; 1553-7390
    ISSN (online) 1553-7404
    ISSN 1553-7390
    DOI 10.1371/journal.pgen.1009512
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: An Amish founder mutation disrupts a PI(3)P-WHAMM-Arp2/3 complex-driven autophagosomal remodeling pathway.

    Mathiowetz, Alyssa J / Baple, Emma / Russo, Ashley J / Coulter, Alyssa M / Carrano, Eric / Brown, Judith D / Jinks, Robert N / Crosby, Andrew H / Campellone, Kenneth G

    Molecular biology of the cell

    2017  Volume 28, Issue 19, Page(s) 2492–2507

    Abstract: Actin nucleation factors function to organize, shape, and move membrane-bound organelles, yet they remain poorly defined in relation to disease. Galloway-Mowat syndrome (GMS) is an inherited disorder characterized by microcephaly and nephrosis resulting ... ...

    Abstract Actin nucleation factors function to organize, shape, and move membrane-bound organelles, yet they remain poorly defined in relation to disease. Galloway-Mowat syndrome (GMS) is an inherited disorder characterized by microcephaly and nephrosis resulting from mutations in the
    MeSH term(s) Actin-Related Protein 2-3 Complex/genetics ; Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Amish/genetics ; Autophagosomes/metabolism ; Autophagosomes/physiology ; Cells, Cultured ; Cytoskeleton/metabolism ; Founder Effect ; Frameshift Mutation ; Hernia, Hiatal/genetics ; Homozygote ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Microcephaly/genetics ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Models, Molecular ; Nephrosis/genetics ; Phosphatidylinositol Phosphates/genetics ; Phosphatidylinositol Phosphates/metabolism ; Proteins/genetics ; Proteins/metabolism
    Chemical Substances Actin-Related Protein 2-3 Complex ; Actins ; Membrane Proteins ; Microtubule-Associated Proteins ; Phosphatidylinositol Phosphates ; Proteins ; WDR73 protein, human ; WHAMM protein, human ; phosphatidylinositol 3-phosphate
    Language English
    Publishing date 2017-07-18
    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.E17-01-0022
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 410: Show issues

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