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  1. Book: Primary cilia

    Sloboda, Roger D.

    (Methods in cell biology ; 94)

    2009  

    Author's details ed. by Roger D. Sloboda
    Series title Methods in cell biology ; 94
    Collection
    Language English
    Size XVI, 386 S., [10] Bl. : Ill., graph. Darst.
    Edition 1. ed.
    Publisher Elsevier, Acad. Press
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT016217319
    ISBN 978-0-12-375024-2 ; 0-12-375024-5
    Database Catalogue ZB MED Medicine, Health

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    2010 A 2154 order for loan Magazin

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  2. Article ; Online: Purification and Localization of Intraflagellar Transport Particles and Polypeptides.

    Sloboda, Roger D

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

    2016  Volume 1365, Page(s) 119–137

    Abstract: The growth and maintenance of almost all cilia and flagella are dependent on the proper functioning of the process of intraflagellar transport (IFT). This includes the primary cilia of most human cells that are in the Go phase of the cell cycle. The ... ...

    Abstract The growth and maintenance of almost all cilia and flagella are dependent on the proper functioning of the process of intraflagellar transport (IFT). This includes the primary cilia of most human cells that are in the Go phase of the cell cycle. The model system for the study of IFT is the flagella of the biflagellate green alga Chlamydomonas. It is in this organism that IFT was first discovered, and genetic data from a Chlamydomonas mutant first linked the process of IFT to polycystic kidney disease in humans. The information provided in this chapter addresses procedures to purify IFT particles from flagella and localize these particles, and their associated motor proteins, in flagella using light and electron microscopic approaches.
    MeSH term(s) Cell Line ; Cell Proliferation ; Chlamydomonas/cytology ; Chlamydomonas/ultrastructure ; Cilia/metabolism ; Cilia/ultrastructure ; Electrophoresis, Polyacrylamide Gel ; Flagella/metabolism ; Flagella/ultrastructure ; Immunoblotting ; Immunohistochemistry ; Microscopy, Electron, Scanning ; Peptides/metabolism ; Protein Transport
    Chemical Substances Peptides
    Language English
    Publishing date 2016
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-3124-8_6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Separation of tubulin and microtubule-associated proteins by ion exchange chromatography.

    Sloboda, Roger D

    Cold Spring Harbor protocols

    2015  Volume 2015, Issue 1, Page(s) pdb.prot081208

    Abstract: Conventional liquid chromatography on phosphocellulose (PC) can be used to separate tubulin and microtubule-associated proteins (MAPs). Tubulin is a highly acidic protein and thus does not bind to PC. MAPs, however, do bind to PC and can be eluted with a ...

    Abstract Conventional liquid chromatography on phosphocellulose (PC) can be used to separate tubulin and microtubule-associated proteins (MAPs). Tubulin is a highly acidic protein and thus does not bind to PC. MAPs, however, do bind to PC and can be eluted with a subsequent salt wash of the column.
    MeSH term(s) Animals ; Chromatography, Ion Exchange ; Microtubule-Associated Proteins/chemistry ; Microtubule-Associated Proteins/metabolism ; Tubulin/isolation & purification
    Chemical Substances Microtubule-Associated Proteins ; Tubulin
    Language English
    Publishing date 2015-01-05
    Publishing country United States
    Document type Journal Article
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.prot081208
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Isolation of microtubules and microtubule-associated proteins using Paclitaxel.

    Sloboda, Roger D

    Cold Spring Harbor protocols

    2015  Volume 2015, Issue 1, Page(s) pdb.prot081190

    Abstract: Paclitaxel binds to tubulin, strongly promotes microtubule assembly from subunits, and stabilizes the assembled polymer against disassembly. Because of its ability to drive the assembly reaction almost completely toward microtubules, the paclitaxel- ... ...

    Abstract Paclitaxel binds to tubulin, strongly promotes microtubule assembly from subunits, and stabilizes the assembled polymer against disassembly. Because of its ability to drive the assembly reaction almost completely toward microtubules, the paclitaxel-dependent procedure outlined here is particularly useful for the isolation of microtubules from tissues in which the intracellular concentration of tubulin is low (e.g., nonneuronal sources, cultured cells, and invertebrate tissues). The microtubule-associated proteins (MAPs) remain bound to the paclitaxel-stabilized microtubules. The isolation of these MAPs by salt extraction is also described here.
    MeSH term(s) Animals ; Dose-Response Relationship, Drug ; Microtubule-Associated Proteins/isolation & purification ; Microtubules/metabolism ; Paclitaxel/metabolism ; Paclitaxel/pharmacology ; Protein Binding/drug effects ; Tubulin Modulators/metabolism ; Tubulin Modulators/pharmacology
    Chemical Substances Microtubule-Associated Proteins ; Tubulin Modulators ; Paclitaxel (P88XT4IS4D)
    Language English
    Publishing date 2015-01-05
    Publishing country United States
    Document type Journal Article
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.prot081190
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Observation of microtubule-based motor protein activity.

    Sloboda, Roger D

    Cold Spring Harbor protocols

    2015  Volume 2015, Issue 2, Page(s) 205–209

    Abstract: It is possible to detect the presence of motor proteins that have the ability to translocate particles along microtubules. The two procedures described here were developed to detect microtubule-dependent motor protein activity in cell lysates or of ... ...

    Abstract It is possible to detect the presence of motor proteins that have the ability to translocate particles along microtubules. The two procedures described here were developed to detect microtubule-dependent motor protein activity in cell lysates or of purified proteins. In the first procedure, latex beads bound to the putative motor protein are assayed for their ability to translocate along microtubules in an ATP-dependent fashion. If motor protein activity is present, it will bind to the beads and translocate them unidirectionally along the microtubules. In the second procedure, motor proteins induce microtubule gliding over a glass coverslip surface that is coated with active motor protein. Because the mass of a microtubule is negligible compared to that of a coverslip or slide, the microtubule glides over the glass surface when the surface is coated with active motor protein. Also included here are descriptions of assays designed to determine the directionality of movement of microtubule-based motor proteins.
    MeSH term(s) Microtubules/metabolism ; Molecular Motor Proteins/metabolism
    Chemical Substances Molecular Motor Proteins
    Language English
    Publishing date 2015-02-02
    Publishing country United States
    Document type Journal Article
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.prot081224
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Isolation and analysis of microtubules and associated proteins.

    Sloboda, Roger D

    Cold Spring Harbor protocols

    2015  Volume 2015, Issue 2, Page(s) 152–154

    Abstract: Microtubules, microtubule-associated proteins (MAPs), and motor proteins are essential components of all eukaryotic cells. They are all involved in mitosis and in the movement of organelles, proteins, and vesicles in cells. MAPs act as structural ... ...

    Abstract Microtubules, microtubule-associated proteins (MAPs), and motor proteins are essential components of all eukaryotic cells. They are all involved in mitosis and in the movement of organelles, proteins, and vesicles in cells. MAPs act as structural elements of the microtubule component of the cytoskeleton, whereas molecular motors propel cargo along microtubule tracks or translocate microtubules in the cytoplasm. This introduction provides an overview of procedures developed by many labs to isolate microtubules from cell homogenates, purify tubulin, MAPs, and motor proteins from microtubules preparations, and analyze kinesin and cytoplasmic dynein activity by video-enhanced differential interference contrast microscopy and fluorescence microscopy. These ingenious microscope-based assays, which were developed to determine the motility characteristics of kinesin and dynein, reveal, in clear and dramatic fashion, the activity of these amazing nanomachines in real time.
    MeSH term(s) Microtubule-Associated Proteins/isolation & purification ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism
    Chemical Substances Microtubule-Associated Proteins
    Language English
    Publishing date 2015-02-02
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.top074526
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Isolation of microtubule-based motor proteins by ATP release from paclitaxel-stabilized microtubules.

    Sloboda, Roger D

    Cold Spring Harbor protocols

    2015  Volume 2015, Issue 2, Page(s) 200–204

    Abstract: The α-β-tubulin heterodimer is asymmetric, and when asymmetric subunits assemble in a head-to-tail fashion, they produce a polymer that is itself asymmetric. Microtubules are therefore polar polymers having a head (or plus) end and a tail (or minus) end. ...

    Abstract The α-β-tubulin heterodimer is asymmetric, and when asymmetric subunits assemble in a head-to-tail fashion, they produce a polymer that is itself asymmetric. Microtubules are therefore polar polymers having a head (or plus) end and a tail (or minus) end. Both ends can be distinguished kinetically because they add and lose subunits at different rates. Because of this inherent asymmetry, translocation of a particle along a microtubule from the head to the tail is a different molecular event than is translocation from the minus to the plus end. Currently, two classes of microtubule-dependent motor proteins are recognized: Those that are plus-end-directed (i.e., kinesin-like) and those that are minus-end-directed (dynein-like). The kinesin family of proteins in humans contains at least 14 classes of kinesins, a grouping based on tertiary and quaternary structure considerations, as well as on enzymatic activity. The dyneins are organized into two groups: Axonemal dyneins and cytoplasmic dyneins. This protocol provides methods for the enrichment of kinesin or cytoplasmic dynein, based on the differential interactions of each type of motor protein with microtubules in the presence of different nucleotides. For a cleaner preparation of motor proteins, the protocol includes steps for the further separation of kinesin and dynein from one another by sucrose gradient centrifugation.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Antineoplastic Agents, Phytogenic/chemistry ; Antineoplastic Agents, Phytogenic/pharmacology ; Microtubules/chemistry ; Microtubules/metabolism ; Molecular Motor Proteins/isolation & purification ; Molecular Motor Proteins/metabolism ; Paclitaxel/chemistry ; Paclitaxel/pharmacology
    Chemical Substances Antineoplastic Agents, Phytogenic ; Molecular Motor Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Paclitaxel (P88XT4IS4D)
    Language English
    Publishing date 2015-02-02
    Publishing country United States
    Document type Journal Article
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.prot081216
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Isolation of microtubules by assembly/disassembly methods.

    Sloboda, Roger D

    Cold Spring Harbor protocols

    2015  Volume 2015, Issue 1, Page(s) pdb.prot081182

    Abstract: The microtubule-isolation procedures described here are based on the ability of the investigator to control the dimer-polymer distribution of tubulin by varying the temperature of the extract. In general, the extract is warmed to induce microtubule ... ...

    Abstract The microtubule-isolation procedures described here are based on the ability of the investigator to control the dimer-polymer distribution of tubulin by varying the temperature of the extract. In general, the extract is warmed to induce microtubule assembly, the polymer is collected by centrifugation, cooled to induce disassembly, clarified by centrifugation, and then warmed again to produce polymer. As long as the GTP supply is sufficient, the microtubules that result can be taken through numerous rounds of this in vitro assembly and disassembly reaction. Many microtubule-associated proteins (MAPs) associate with microtubules assembled in vitro. Some reagents can skew the equilibrium of assembly and disassembly toward formation of polymer. The inclusion of glycerol, for instance, promotes microtubule assembly by disrupting the hydration shell around the tubulin dimers. The result is a greater yield of tubulin per gram of starting material. However, the ratio of MAPs to tubulin is slightly lower, presumably because the glycerol also decreases the binding of MAPs to tubulin. Two methods are described here: The first uses buffer lacking assembly-promoting components, and the second uses buffer containing glycerol. These procedures are most efficient with vertebrate brain tissue, where the soluble protein can be up to 15%-20% tubulin. The first produces satisfactory yields when using chick or pig brain; the second is recommended for calf or cow brain. The second procedure may also be useful for studies of nonneuronal tissues where the relative concentration of tubulin per gram of wet weight is considerably lower than that of brain.
    MeSH term(s) Animals ; Brain/metabolism ; Cattle ; Chickens ; Electrophoresis, Polyacrylamide Gel ; Microtubules/metabolism ; Swine ; Tubulin/isolation & purification
    Chemical Substances Tubulin
    Language English
    Publishing date 2015-01-05
    Publishing country United States
    Document type Journal Article
    ISSN 1559-6095
    ISSN (online) 1559-6095
    DOI 10.1101/pdb.prot081182
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  9. Article ; Online: The

    Bloodgood, Robert A / Tetreault, Joseph / Sloboda, Roger D

    Journal of cell science

    2019  Volume 132, Issue 16

    Abstract: In addition to bend propagation for swimming, ...

    Abstract In addition to bend propagation for swimming,
    MeSH term(s) Chlamydomonas/genetics ; Chlamydomonas/metabolism ; Chlamydomonas/ultrastructure ; Flagella/genetics ; Flagella/metabolism ; Flagella/ultrastructure ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Plant Proteins/genetics ; Plant Proteins/metabolism
    Chemical Substances Glycoproteins ; Plant Proteins
    Language English
    Publishing date 2019-08-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.233429
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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  10. Article ; Online: Protein arginine methyltransferases interact with intraflagellar transport particles and change location during flagellar growth and resorption.

    Mizuno, Katsutoshi / Sloboda, Roger D

    Molecular biology of the cell

    2017  Volume 28, Issue 9, Page(s) 1208–1222

    Abstract: Changes in protein by posttranslational modifications comprise an important mechanism for the control of many cellular processes. Several flagellar proteins are methylated on arginine residues during flagellar resorption; however, the function is not ... ...

    Abstract Changes in protein by posttranslational modifications comprise an important mechanism for the control of many cellular processes. Several flagellar proteins are methylated on arginine residues during flagellar resorption; however, the function is not understood. To learn more about the role of protein methylation during flagellar dynamics, we focused on protein arginine methyltransferases (PRMTs) 1, 3, 5, and 10. These PRMTs localize to the tip of flagella and in a punctate pattern along the length, very similar, but not identical, to that of intraflagellar transport (IFT) components. In addition, we found that PRMT 1 and 3 are also highly enriched at the base of the flagella, and the basal localization of these PRMTs changes during flagellar regeneration and resorption. Proteins with methyl arginine residues are also enriched at the tip and base of flagella, and their localization also changes during flagellar assembly and disassembly. PRMTs are lost from the flagella of
    MeSH term(s) Animals ; Arginine/metabolism ; Axoneme/metabolism ; Axoneme/physiology ; Biological Transport ; Chlamydomonas/metabolism ; Chlamydomonas reinhardtii/metabolism ; Flagella/metabolism ; Flagella/physiology ; Methylation ; Protein Processing, Post-Translational ; Protein Transport ; Protein-Arginine N-Methyltransferases/metabolism ; Protein-Arginine N-Methyltransferases/physiology
    Chemical Substances Arginine (94ZLA3W45F) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319)
    Language English
    Publishing date 2017-05-01
    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.E16-11-0774
    Database MEDical Literature Analysis and Retrieval System OnLINE

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