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  1. Article ; Online: Spindle checkpoint activation by fungal orthologs of the S. cerevisiae Mps1 kinase.

    Fabritius, Amy / Alonso, Anabel / Wood, Andrew / Sulthana, Shaheen / Winey, Mark

    PloS one

    2024  Volume 19, Issue 3, Page(s) e0301084

    Abstract: There is an ongoing need for antifungal agents to treat humans. Identification of new antifungal agents can be based on screening compounds using whole cell assays. Screening compounds that target a particular molecule is possible in budding yeast ... ...

    Abstract There is an ongoing need for antifungal agents to treat humans. Identification of new antifungal agents can be based on screening compounds using whole cell assays. Screening compounds that target a particular molecule is possible in budding yeast wherein sophisticated strain engineering allows for controlled expression of endogenous or heterologous genes. We have considered the yeast Mps1 protein kinase as a reasonable target for antifungal agents because mutant or druggable forms of the protein, upon inactivation, cause rapid loss of cell viability. Furthermore, extensive analysis of the Mps1 in budding yeast has offered potential tactics for identifying inhibitors of its enzymatic activity. One such tactic is based on the finding that overexpression of Mps1 leads to cell cycle arrest via activation of the spindle assembly checkpoint. We have endeavored to adapt this assay to be based on the overexpression of Mps1 orthologs from pathogenic yeast in hopes of having a whole-cell assay system to test the activity of these orthologs. Mps1 orthologous genes from seven pathogenic yeast or other pathogenic fungal species were isolated and expressed in budding yeast. Two orthologs clearly produced phenotypes similar to those produced by the overexpression of budding yeast Mps1, indicating that this system for heterologous Mps1 expression has potential as a platform for identifying prospective antifungal agents.
    MeSH term(s) Humans ; Antifungal Agents/metabolism ; Cell Cycle Proteins/metabolism ; M Phase Cell Cycle Checkpoints ; Prospective Studies ; Protein Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Spindle Apparatus/metabolism
    Chemical Substances Antifungal Agents ; Cell Cycle Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Saccharomyces cerevisiae Proteins ; MPS1 protein, S cerevisiae (EC 2.7.12.2)
    Language English
    Publishing date 2024-03-26
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0301084
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  2. Article ; Online: Recent Advances in Ciliate Biology.

    Howard-Till, Rachel A / Kar, Usha Pallabi / Fabritius, Amy S / Winey, Mark

    Annual review of cell and developmental biology

    2022  Volume 38, Page(s) 75–102

    Abstract: Ciliates are a diverse group of unicellular eukaryotes that vary widely in size, shape, body plan, and ecological niche. Here, we review recent research advances achieved with ciliate models. Studies on patterning and regeneration have been revived in ... ...

    Abstract Ciliates are a diverse group of unicellular eukaryotes that vary widely in size, shape, body plan, and ecological niche. Here, we review recent research advances achieved with ciliate models. Studies on patterning and regeneration have been revived in the giant ciliate
    MeSH term(s) Biology ; Ciliophora/genetics ; Cryoelectron Microscopy ; RNA, Catalytic ; Telomerase
    Chemical Substances RNA, Catalytic ; Telomerase (EC 2.7.7.49)
    Language English
    Publishing date 2022-07-28
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 1293750-2
    ISSN 1530-8995 ; 1081-0706
    ISSN (online) 1530-8995
    ISSN 1081-0706
    DOI 10.1146/annurev-cellbio-120420-020656
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  3. Article: Motile Cilia: Innovation and Insight From Ciliate Model Organisms.

    Bayless, Brian A / Navarro, Francesca M / Winey, Mark

    Frontiers in cell and developmental biology

    2019  Volume 7, Page(s) 265

    Abstract: Ciliates are a powerful model organism for the study of basal bodies and motile cilia. These single-celled protists contain hundreds of cilia organized in an array making them an ideal system for both light and electron microscopy studies. Isolation and ... ...

    Abstract Ciliates are a powerful model organism for the study of basal bodies and motile cilia. These single-celled protists contain hundreds of cilia organized in an array making them an ideal system for both light and electron microscopy studies. Isolation and subsequent proteomic analysis of both cilia and basal bodies have been carried out to great success in ciliates. These studies reveal that ciliates share remarkable protein conservation with metazoans and have identified a number of essential basal body/ciliary proteins. Ciliates also boast a genetic and molecular toolbox that allows for facile manipulation of ciliary genes. Reverse genetics studies in ciliates have expanded our understanding of how cilia are positioned within an array, assembled, stabilized, and function at a molecular level. The advantages of cilia number coupled with a robust genetic and molecular toolbox have established ciliates as an ideal system for motile cilia and basal body research and prove a promising system for future research.
    Language English
    Publishing date 2019-11-01
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2019.00265
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  4. Article ; Online: Electron cryo-tomography structure of axonemal doublet microtubule from

    Li, Sam / Fernandez, Jose-Jesus / Fabritius, Amy S / Agard, David A / Winey, Mark

    Life science alliance

    2021  Volume 5, Issue 3

    Abstract: Doublet microtubules (DMTs) provide a scaffold for axoneme assembly in motile cilia. Aside from α/β tubulins, the DMT comprises a large number of non-tubulin proteins in the luminal wall of DMTs, collectively named the microtubule inner proteins (MIPs). ... ...

    Abstract Doublet microtubules (DMTs) provide a scaffold for axoneme assembly in motile cilia. Aside from α/β tubulins, the DMT comprises a large number of non-tubulin proteins in the luminal wall of DMTs, collectively named the microtubule inner proteins (MIPs). We used cryoET to study axoneme DMT isolated from
    MeSH term(s) Axoneme/metabolism ; Binding Sites ; Microtubule Proteins/chemistry ; Microtubule Proteins/genetics ; Microtubule Proteins/metabolism ; Microtubules/metabolism ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Structure-Activity Relationship ; Tetrahymena thermophila
    Chemical Substances Microtubule Proteins ; Protozoan Proteins
    Language English
    Publishing date 2021-12-30
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 2575-1077
    ISSN (online) 2575-1077
    DOI 10.26508/lsa.202101225
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Hydronium ion diffusion in model proton exchange membranes at low hydration: insights from ab initio molecular dynamics

    Zelovich, Tamar / Winey, Karen I / Tuckerman, Mark E

    Journal of materials chemistry A. 2021 Feb. 2, v. 9, no. 4

    2021  

    Abstract: Fuel-cell deployable proton exchange membranes (PEMs) are considered to be a promising technology for clean and efficient power generation. However, a fundamental atomistic understanding of the hydronium diffusion process in the PEM environment is an ... ...

    Abstract Fuel-cell deployable proton exchange membranes (PEMs) are considered to be a promising technology for clean and efficient power generation. However, a fundamental atomistic understanding of the hydronium diffusion process in the PEM environment is an ongoing challenge. In this work, we employ fully atomistic ab initio molecular dynamics to simulate diffusion mechanisms of the hydronium ion in a model PEM. In order to mimic a precise polymer with a layered morphology, as recently introduced by Trigg, et al., Nat. Mater., 2018, 17, 725, a nano-confined environment was created composed of graphane bilayers to which sulfonate end groups (SO₃⁻) are attached, and the space between the bilayers was subsequently filled with water and hydronium ions up to λ values of 3 and 4, where λ denotes the water-to-anion ratio. We find that for the low λ value, the water distribution is not homogeneous, which results in an incomplete second solvation shell for H₃O⁺, fewer water molecules in the vicinity of SO₃⁻, and a higher probability of obtaining a coordination number of ∼1 for the nearest oxygen neighbor to SO₃⁻. These conditions increase the probability that H₃O⁺ will react with SO₃⁻ according to the reaction SO₃⁻ + H₃O⁺ ↔ SO₃H + H₂O, which was found to be an essential part of the hydronium diffusion mechanism. This suggests there are optimal hydration conditions that allow the sulfonate end groups to take an active part in the hydronium diffusion mechanism, resulting in high hydronium conductivity. We expect that the results of this study could help guide synthesis and experimental characterization used to design new PEM materials with high hydronium conductivity.
    Keywords fuel cells ; molecular dynamics ; oxygen ; polymers ; power generation ; probability ; solvation ; sulfonates ; water distribution
    Language English
    Dates of publication 2021-0202
    Size p. 2448-2458.
    Publishing place The Royal Society of Chemistry
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 2702232-8
    ISSN 2050-7496 ; 2050-7488
    ISSN (online) 2050-7496
    ISSN 2050-7488
    DOI 10.1039/d0ta10565a
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Microtubule-associated proteins and motors required for ectopic microtubule array formation in Saccharomyces cerevisiae.

    King, Brianna R / Meehl, Janet B / Vojnar, Tamira / Winey, Mark / Muller, Eric G / Davis, Trisha N

    Genetics

    2021  Volume 218, Issue 2

    Abstract: The mitotic spindle is resilient to perturbation due to the concerted, and sometimes redundant, action of motors and microtubule-associated proteins. Here, we utilize an inducible ectopic microtubule nucleation site in the nucleus of Saccharomyces ... ...

    Abstract The mitotic spindle is resilient to perturbation due to the concerted, and sometimes redundant, action of motors and microtubule-associated proteins. Here, we utilize an inducible ectopic microtubule nucleation site in the nucleus of Saccharomyces cerevisiae to study three necessary steps in the formation of a bipolar array: the recruitment of the γ-tubulin complex, nucleation and elongation of microtubules (MTs), and the organization of MTs relative to each other. This novel tool, an Spc110 chimera, reveals previously unreported roles of the microtubule-associated proteins Stu2, Bim1, and Bik1, and the motors Vik1 and Kip3. We report that Stu2 and Bim1 are required for nucleation and that Bik1 and Kip3 promote nucleation at the ectopic site. Stu2, Bim1, and Kip3 join their homologs XMAP215, EB1 and kinesin-8 as promoters of microtubule nucleation, while Bik1 promotes MT nucleation indirectly via its role in SPB positioning. Furthermore, we find that the nucleation activity of Stu2 in vivo correlates with its polymerase activity in vitro. Finally, we provide the first evidence that Vik1, a subunit of Kar3/Vik1 kinesin-14, promotes microtubule minus end focusing at the ectopic site.
    MeSH term(s) Cell Nucleus/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Mitosis ; Molecular Motor Proteins/genetics ; Molecular Motor Proteins/metabolism ; Mutation ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Spindle Apparatus/metabolism
    Chemical Substances Microtubule-Associated Proteins ; Molecular Motor Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2021-03-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2167-2
    ISSN 1943-2631 ; 0016-6731
    ISSN (online) 1943-2631
    ISSN 0016-6731
    DOI 10.1093/genetics/iyab050
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  7. Article ; Online: Motile Cilia

    Brian A. Bayless / Francesca M. Navarro / Mark Winey

    Frontiers in Cell and Developmental Biology, Vol

    Innovation and Insight From Ciliate Model Organisms

    2019  Volume 7

    Abstract: Ciliates are a powerful model organism for the study of basal bodies and motile cilia. These single-celled protists contain hundreds of cilia organized in an array making them an ideal system for both light and electron microscopy studies. Isolation and ... ...

    Abstract Ciliates are a powerful model organism for the study of basal bodies and motile cilia. These single-celled protists contain hundreds of cilia organized in an array making them an ideal system for both light and electron microscopy studies. Isolation and subsequent proteomic analysis of both cilia and basal bodies have been carried out to great success in ciliates. These studies reveal that ciliates share remarkable protein conservation with metazoans and have identified a number of essential basal body/ciliary proteins. Ciliates also boast a genetic and molecular toolbox that allows for facile manipulation of ciliary genes. Reverse genetics studies in ciliates have expanded our understanding of how cilia are positioned within an array, assembled, stabilized, and function at a molecular level. The advantages of cilia number coupled with a robust genetic and molecular toolbox have established ciliates as an ideal system for motile cilia and basal body research and prove a promising system for future research.
    Keywords motile cilia ; basal body ; ciliate ; doublet microtubules ; ciliary array ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2019-11-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
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  8. Article ; Online: Building Cell Structures in Three Dimensions: Electron Tomography Methods for Budding Yeast.

    O'Toole, Eileen T / Giddings, Thomas H / Winey, Mark

    Cold Spring Harbor protocols

    2017  Volume 2017, Issue 3

    Abstract: Saccharomyces ... ...

    Abstract Saccharomyces cerevisiae
    MeSH term(s) Electron Microscope Tomography/methods ; Freeze Substitution ; Freezing ; Fungal Structures/ultrastructure ; Imaging, Three-Dimensional/methods ; Preservation, Biological ; Saccharomyces cerevisiae/ultrastructure
    Language English
    Publishing date 2017-03-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.top077685
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  9. Article ; Online: Yeast pericentrin/Spc110 contains multiple domains required for tethering the γ-tubulin complex to the centrosome.

    Alonso, Annabel / Fabritius, Amy / Ozzello, Courtney / Andreas, Mike / Klenchin, Dima / Rayment, Ivan / Winey, Mark

    Molecular biology of the cell

    2020  Volume 31, Issue 14, Page(s) 1437–1452

    Abstract: ... ...

    Abstract The
    MeSH term(s) Antigens/genetics ; Antigens/metabolism ; Binding Sites ; Calmodulin/metabolism ; Calmodulin-Binding Proteins/genetics ; Calmodulin-Binding Proteins/metabolism ; Cell Nucleus/metabolism ; Centrosome/metabolism ; Centrosome/physiology ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubule-Organizing Center/metabolism ; Microtubules/metabolism ; Nuclear Proteins/metabolism ; Phosphoproteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Spindle Apparatus/metabolism ; Spindle Pole Bodies/metabolism ; Tubulin/metabolism ; Tubulin/physiology
    Chemical Substances Antigens ; CMD1 protein, S cerevisiae ; Calmodulin ; Calmodulin-Binding Proteins ; Cytoskeletal Proteins ; Microtubule-Associated Proteins ; Nuclear Proteins ; Phosphoproteins ; SPC110 protein, S cerevisiae ; SPC42 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Spc29 protein, S cerevisiae ; Tubulin ; pericentrin
    Language English
    Publishing date 2020-05-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E20-02-0146
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    In stock of ZB MED Cologne/Königswinter

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    Zs.MO 410: Show issues

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  10. Article ; Online: Cryopreparation and Electron Tomography of Yeast Cells.

    O'Toole, Eileen T / Giddings, Thomas H / Winey, Mark

    Cold Spring Harbor protocols

    2017  Volume 2017, Issue 3

    Abstract: Three-dimensional imaging of cells using electron tomography enables analysis of cell structure at unprecedented resolution. The preparation of cells for tomography using rapid freezing followed by freeze-substitution is an essential first step to ensure ...

    Abstract Three-dimensional imaging of cells using electron tomography enables analysis of cell structure at unprecedented resolution. The preparation of cells for tomography using rapid freezing followed by freeze-substitution is an essential first step to ensure the optimal preservation of the cell structure for 3D studies. This protocol outlines a method for obtaining well-preserved cells using high-pressure freezing followed by freeze-substitution. We have found that this method is particularly well suited for electron tomography studies and has the added bonus of preserving antigenicity for immuno-electron microscopy. The steps involved in imaging cells and performing tomographic analysis of cellular structures are also outlined.
    MeSH term(s) Electron Microscope Tomography/methods ; Freeze Substitution ; Freezing ; Fungal Structures/ultrastructure ; Hydrostatic Pressure ; Imaging, Three-Dimensional ; Preservation, Biological ; Saccharomyces cerevisiae/ultrastructure
    Language English
    Publishing date 2017-03-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.prot085589
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