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  • Polymer and Materials Science  (127)
  • Cell & Developmental Biology  (59)
  • 1
    Electronic Resource
    Electronic Resource
    High gloss of extruded high impact polystyrene sheet. A microscopical study of sheet morphology (1963)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 7 (1963), S. S51 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1963.070070638
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  • 2
    Electronic Resource
    Electronic Resource
    High gloss of extruded high impact polystyrene sheet. A microscopical study of sheet morphology (1963)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 7 (1963), S. 1731-1741 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Morphological changes effected in the two-phase high impact polystyrene system by several methods of securing high surface gloss of extruded sheet were studied microscopically. In the glazing process changes occur in refractive index of the copolymer particles and in the matrix. Excessive glazing may result in oxidative damage. The effects of temperature and oxidation and temperature alone on the copolymer particles have been investigated.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1963.070070514
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  • 3
    Electronic Resource
    Electronic Resource
    The cytoskeleton of murine leukemia virus (MuLV)-infected mouse fibroblasts as observed under varying conditions of formaldehyde fixation (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 567-577 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; murine leukemia viruses ; formaldehyde fixation ; membrane permeability ; immunofluorescence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Mouse fibroblasts chronically infected with Moloney murine leukemia virus (MuLV) were fixed using variable amounts of formaldehyde, then examined by indirect immunofluorescence light microscopy. Several antisera were employed to detect both external and internal antigens associated with the cells, eg, MuLV gp70, tubulin, vimentin, and actin. Our results indicate that the cell membranes could be partially permeabilized to IgG molecules directed against the three cytoskeletal antigens only after 3.7%, but not 1%, formaldehyde treatment. Complete permeabilization was achieved by subsequent acetone treatment of cells after 3.7% formaldehyde fixation. In such cells, normal-appearing cytoskeletal networks of microtubules and intermediate filaments were observed. Stress fibers were also seen; however, they appeared less numerous and thinner than those of uninfected mouse fibroblasts. Further, a significant amounts of F-actin fluorescence was localized in granules in the cytoplasm of infected cells. Similar observations were made using JLS-V9 mouse cells chronically infected with 334C virus, another MuLV. These results taken together suggest that subtle differences exist in the organization of actin within MuLV-infected and uninfected mouse fibroblasts.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970030523
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  • 4
    Electronic Resource
    Electronic Resource
    Protein phosphorylation and dynamics of cytoskeletal structures associated with basal bodies in Paramecium (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 44-54 
    Details
    ISSN: 0886-1544
    Keywords: monoclonal antibody ; phosphoproteins ; basal bodies ; morphogenesis ; Paramecium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The presence of phosphorylated proteins associated with microtubule organizing centers in tissue culture cells during mitosis has been demonstrated by the use of monoclonal antibodies raised against mitotic HeLa cells [Vandre et al., Proc. Natl. Acad. Sci. U.S.A. 81:4439-4443, 1984]. We report here that in Paramecium two of the mitosis specific antibodies, MPM-1 and MPM-2, decorate throughtout the cell cycle all the microtubule organizing centers (MTOCs) located in the cortex and in the oral apparatus (gullet). Immuno-electron microscopy showed that these antibodies labeled the electron-dense material surrounding basal bodies from which several microtubule networks as well as kinetodesmal fibers originate. During mitosis, these antibodies also stained other cortical cytoskeletal structures, the kinetodesmal fibers (MPM-1 and MPM-2) and the epiplasm (MPM-1). Among the different polypeptides recognized by the antibodies on immunoblots, three major ones of 60, 63, and 116 kDa were found to be common to the cortex (where several thousand ciliary basal bodies are anchored) and the oral apparatus (which comprises several hundred basal bodies around which various arrays of cytoplasmic microtubules are organized). Alkaline phosphatase treatment abolished the immunoreactivity of the polypeptides and the labeling observed by immunofluorescence. These results demonstrate that phosphorylated proteins are associated with all the known active microtubule organizing centers present in the cortex throughout the cell cycle of Paramecium. Furthermore they indicate that in Paramecium phosphorylation of proteins could also be involved in the cell cycle dependent dynamics of cortical cytoskeletal structures other than microtubules.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080107
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  • 5
    Electronic Resource
    Electronic Resource
    Distribution of phosphorylated spindle-associated proteins in the diatom Stephanopyxis turris (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 33-41 
    Details
    ISSN: 0886-1544
    Keywords: phosphorylation ; MPM-2 ; mitotic spindle ; microtubule-associated protein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Mitotic spindles isolated from the diatom Stephanopyxis turris become thiophosphorylated in the presence of ATPγS at specific locations within the mitotic apparatus, resulting in a stimulation of ATP-dependent spindle elongation in vitro. Here, using indirect immunofluorescence, we compare the staining pattern of an antibody against thiophosphorylated proteins to that of MPM-2, an antibody against mitosis-specific phosphoproteins, in isolated spindles. Both antibodies label spindle poles, kinetochores, and the midzone. Neither antibody exhibits reduced labeling in salt-extracted spindles, although prior salt extraction inhibits thiophosphorylation in ATPγS. Furthermore, both antibodies recognize a 205 kd band on immunoblots of spindle extracts. Microtubule-organizing centers and mitotic spindles label brightly with the MPM-2 antibody in intact cells. These results show that functional mitotic spindles isolated from S. turris are phosphorylated both in vivo and in vitro. We discuss the possible role of phosphorylated cytoskeletal proteins in the control of mitotic spindle function.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120105
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  • 6
    Electronic Resource
    Electronic Resource
    Epitope mapping of monoclonal antibodies against caldesmon and their effects on the binding of caldesmon to Ca++/calmodulin and to actin or actin-tropomyosin filaments (1991)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 20 (1991), S. 95-108 
    Details
    ISSN: 0886-1544
    Keywords: actomyosin ; smooth muscle contraction ; nonmuscle cell motility ; microinjection ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of monoclonal anti-caldesmon antibodies, C2, C9, C18, C21, and C23, on the binding of caldesmon to F-actin/F-actin-tropomyosin filaments and to Ca++/calmodulin were examined in an in vitro reconstitution system. In addition, the antibody epitopes were mapped by Western blot analysis of NTCB (2-nitro-5-thiocyanobenzoic acid) and CNBr (cyanogen bromide) fragments of caldesmon. Both C9 and C18 recognize an amino terminal fragment composed of amino acid residues 19 to 153. The C23 epitope lies within a fragment ranging from residues 230 to 386. Included in this region is a 13-residue repeat sequence. Interestingly this repetitive sequence shares sequence similarity with a sequence found in nuclear lamin A, a protein which is also recognized by C23 antibody. Therefore, it is likely that the C23 epitope corresponds to this 13-residue repeat sequence. A carboxyl-terminal 10K fragment contains the epitopes for antibodies C2 and C21. Among these antibodies, only C21 drastically inhibits the binding of caldesmon to F-actin/F-actin-tropomyosin filaments and tc Ca++/calmodulin. When the molar ratio of monoclonal antibody C21 to caldesmon reached 1.0, a maximal inhibition (90%) on the binding of caldesmon to F-actin filaments was observed. However, it required double amounts of C21 antibody to exhibit a maximal inhibition of 70% on the binding of caldesmon to F-actin-tropomyosin filaments. These results suggest that the presence of tropomyosin in F-actin enhances caldesmon's binding. Furthermore, C21 antibody also effectively inhibits the caldesmon binding to Ca++/calmodolin. The kinetics of C21 inhibition on caldesmon's binding to Ca++/calmodulin is very similar to the inhibition obtained by preincubation of caldesmon with free Ca++/calmodulin. This result suggests that there is only one Ca++/calmodulin binding domain on caldesmon and this domain appears to be very close to the C21 epitope. Apparently, the Ca++/calmodulin-binding domain and the actin-binding domain are very close to each other and may interfere with each other. In an accompanying paper, we have further demonstrated that microinjection of C21 antibody into living chicken embryo fibroblasts inhibit intracellular granule movement, suggesting an in vivo interference with the functional domains [Hegmann et al., 1991: Cell Motil. Cytoskeleton 20:109-120].
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970200203
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  • 7
    Electronic Resource
    Electronic Resource
    Spectrin and ankyrin in brain (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 623-633 
    Details
    ISSN: 0886-1544
    Keywords: spectrin ; ankyrin ; brain membranes ; spectrin subunits ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Further similarity between mammalian erythrocyte spectrin and pig brain spectrin has been demonstrated by (a) formation of hybrid molecules with brain α-chains and erythrocyte β-chains and by (b) identification of an ankyrin protein in brain membranes. Hybrid spectrin molecules prepared from brain α-chains and erythrocyte β-chains were visualized by low-angle rotary shadowing as double-stranded rods (dimers) 100 nM in length. 125I-labeled brain α-chain that was hybridized with erythrocyte β-subunit acquired ability to bind to ankyrin sites on erythrocyte membranes. 125I-labeled brain α-chain bound only to β-subunits of erythrocyte and brain spectrin following transfer of these polypeptides to nitrocellulose paper from sodium dodecyl sulfate (SDS) gels. Thus brain spectrin and mammalian erythrocyte spectrin have shared functional sites involved in association of their subunits. Additional evidence for similarity of brain and erythrocyte membranes is the finding of a 210,000 Mr membrane protein in brain that cross-reacts with erythrocyte ankyrin and has a water-soluble domain of 72,000 Mr that is produced by protease digestion. The 72,000 Mr domain of brain ankyrin has been isolated by affinity chromatography on erythrocyte spectrin-Sepharose, and was demonstrated to bind directly to erythrocyte and brain spectrin. The brain 72,000 Mr fragment has distinct peptide maps from the erythrocyte 72,000 Mr ankyrin fragment and thus is not a result of erythrocyte contamination.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970030527
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  • 8
    Electronic Resource
    Electronic Resource
    β-Tubulin mutation suppresses microtubule dynamics in vitro and slows mitosis in vivo (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 285-300 
    Details
    ISSN: 0886-1544
    Keywords: microtubule dynamics ; β-tubulin ; mitosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule (MT) dynamics vary both spatially and temporally within cells and are thought to be important for proper MT cellular function. Because MT dynamics appear to be closely tied to the guanosine triphosphatase (GTPase) activity of β-tubulin subunits, we examined the importance of MT dynamics in the budding yeast S. cerevisiae by introducing a T107K point mutation into a region of the single β-tubulin gene, TUB2, known to affect the assembly-dependent GTPase activity of MTs in vitro. Analysis of MT dynamic behavior by video-enhanced differential interference contrast microscopy, revealed that T107K subunits slowed both the growth rates and catastrophic disassembly rates of individual MTs in vitro. In haploid cells tub2-T107K is lethal; but in tub2-T107K/tub2-590 heterozygotes the mutation is viable, dominant, and slows cell-cycle progression through mitosis, without causing wholesale disruption of cellular MTs. The correlation between the slower growing and shortening rates of MTs in vitro, and the slower mitosis in vivo suggests that MT dynamics are important in budding yeast and may regulate the rate of nuclear movement and segregation. The slower mitosis in mutant celis did not result in premature cytokinesis and cell death, further suggesting that cell-cycle control mechanisms “sense” the mitotic slowdown, possibly by monitoring MT dynamics directly. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970300406
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of crosslinking on the properties of poly(2-hydroxyethyl methacrylate) hydrogels (1991)
    Weinheim : Wiley-Blackwell
    Angewandte Makromolekulare Chemie 189 (1991), S. 195-205 
    Details
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: 2-Hydroxyethyl-methacrylat wurde durch Initiierung mit γ-Strahlung in Masse mit zwei verschiedenen tetrafunktionellen Monomeren (Ethylenglycol-dimethacrylat und 1,2-Bis(acryloxymethyl)-tetramethyldisiloxan) und einem hexafunktionellen Monomeren (1,1,1-Trimethylolpropan-trimethacrylat) als Vernetzungsmittel copolymerisiert. Die erhaltenen Xerogele wurden anschließend mit Wasser bis zum Erreichen der Gleichgewichtsquellung behandelt. Um die drei Vernetzungsmittel vergleichen zu können, wurde unter Berücksichtigung von Molmasse und Funktionalität der Xerogele die theoretische Konzentration an Vernetzungsstellen zwischen 0,032 und 0,644 mol/l variiert. Die relative Hydrophobie der drei Vernetzungsmittel hat einen ausschlaggebenden Einfluß sowohl auf die Gleichgewichtsquellung als auch auf den Elastizitätsmodul der gequollenen Gele. Der Gehalt an nicht-einfrierbarem Wasser in mit 1,1,1-Trimethylol-propan-trimethacrylat vernetzten Gelen wurde anhand von DSC-Untersuchungen analysiert. Das Verhältnis von nicht-einfrierbarem zum Gesamtgehalt an Wasser in den Gelen nimmt mit steigender Vernetzungsdichte zu.
    Notes: By means of γ-irradiation 2-hydroxyethyl methacrylate has been copolymerized in bulk with two different tetrafunctional monomers, ethylene glycol dimethacrylate and 1,3-bis(acryloxymethyl) tetramethyl disiloxane and with a hexafunctional monomer, 1,1,1-trimethylolpropane trimethacrylate. The resultant xerogels were subsequently swollen to equilibrium in water. In order to allow a comparison among the three crosslinkers, their molar masses and funtionalities were taken into account, the theoretical crosslink concentrations being varied from 0.032 to 0.644 mol dm-3. The relative hydrophobicity of the three crosslinkers was found to have a significant effect on both the equilibrium swelling and elastic modulus of the swollen gels. Non-freezing water in several gels crosslinked with 1,1,1-trimethylolpropane trimethacrylate was analysed by differential scanning calorimetry (DSC). The proportion of non-freezing water in the gel relative to the overall water content was found to increase with increasing crosslink density.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/apmc.1991.051890118
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  • 10
    Electronic Resource
    Electronic Resource
    A facile synthesis of polyamides from aromatic diisocyanates and dicarboxylic acid catalyzed by Lewis acids (1996)
    Weinheim : Wiley-Blackwell
    Macromolecular Rapid Communications 17 (1996), S. 897-903 
    Details
    ISSN: 1022-1336
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Aromatic polyamides were prepared by an AlCl3 or HCl-catalyzed polymerization of toluene diisocyanate or methylenebis(phenyl isocyanate) with adipic acid at low temperatures (≤100°C) in a short reaction time (3-4 h). The intrinsic viscosity of the polymers was approximately 1.1 dL/g as determined at 25°C with m-cresol as solvent, indicating that the polyamides obtained by this method have relatively high molecular weights. The polymers exhibit high glass transition temperatures and good thermal stability.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/marc.1996.030171208
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