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  • Chemistry  (272)
  • Life and Medical Sciences  (121)
  • SPACECRAFT DESIGN, TESTING AND PERFORMANCE  (19)
  • 11
    Electronic Resource
    Electronic Resource
    Experimental manipulation of γ-tubulin distribution in arabidopsis using anti-microtubule drugs (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 113-129 
    Details
    ISSN: 0886-1544
    Keywords: Arabidopsis ; centrosome ; CIPC ; colchicine ; cytokinesis ; γ-tubulin ; microtubule ; mitosis ; phragmoplast ; taxol ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: γ-Tubulin-specific antibodies stain the microtubule (Mt) arrays of Arabidopsis suspension cells in a punctate or patchy manner. During division, staining of kinetochore fibers and the phragmoplast is extensive, except in the vicinity of the plus ends at the metaphase plate and cell plate. γ-Tubulin localization responds to low levels of colchicine, with staining receding farther toward the minus (pole) ends of kinetochore fibers. At higher drug concentrations, γ-tubulin also associates with abnormal Mt foci as well as with the surface of the daughter nuclei facing the phragmoplast. During UV-induced recovery from colchicine, γ-tubulin increases along the presumptive minus ends of mitotic Mts as well as the phragmoplast near the daughter nuclei. With CIPC, immunostaining is concentrated around the centers of focal Mt arrays in multipolar spindles. In the presence of taxol, Mts are more prominent but the mitotic apparatus and phragmoplast are abnormal. As with CIPC, γ-tubulin is concentrated at focal arrays. Increased punctate staining is also present in interphase arrays, with fluorescent dots often located at the ends of Mts. These results support a preferential association between γ-tubulin and Mt minus ends, but are also consistent with more general binding along the walls of Mts. Thus, minus ends (and Mt nucleation sites) may be present throughout plant Mt arrays, but γ-tubulin may also serve another function, such as in structural stabilization.
    Additional Material: 21 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310204
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  • 12
    Electronic Resource
    Electronic Resource
    Structure/Reactivity relationships for high-performance polyamides: Kinetics of the reactions of N,N′-dihexylphthalamides in the presence of added copper iodide and water (1995)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 33 (1995), S. 533-545 
    Details
    ISSN: 0887-624X
    Keywords: polyamides ; model compound ; thermolysis ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An experimental study to determine the effect of copper(I) iodide and water on the rate and product distribution of aliphatic-aromatic polyamide degradation was carried out by using N,N′-dihexylterephthalamide (DHT) and N,N′-dihexylisophthalamide (DHI) as models of the amide functionality. DHT was reacted in an inert argon atmosphere at 350°C in the presence of CuI added in amounts ranging from 0-5% by weight. The rate of disappearance of DHT was enhanced by a factor of three with the addition of 0.5% CuI. Increases to 5 wt % did not change the disappearance kinetics further. Comparison of the behavior of DHT and DHI revealed that changes in rate of disappearance and product yields were dependent on the relative positions of the amide substituents. Reaction of DHI was enhanced more significantly at a given CuI loading. The rate of disappearance of DHI and DHT and the selectivity to N-hexylbenzamide increased with the addition of water in loadings ranging from 0.148M to 0.193M. The reactivity of DHI was more greatly enhanced at a given water loading. These differences were attributed to electronic effects, as evaluated by differences in atomic partial charges, and physical effects. © 1995 John Wiley & Sons, Inc.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1995.080330320
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  • 13
    Electronic Resource
    Electronic Resource
    A mass spectrometric investigation of the water-soluble oligomers remaining after the emulsion polymerization of methyl methacrylate (1995)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 33 (1995), S. 2297-2304 
    Details
    ISSN: 0887-624X
    Keywords: methyl methacrylate ; emulsion polymerization ; in situ surfactant ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A “surfactant-free” emulsion polymerization of methyl methacrylate was conducted at 80°C with ammonium persulfate initiator. The water-soluble MMA-based oligomers re-maining were isolated and analyzed both as-produced and after hydrolysis. NMR analysis revealed that the mole ratio of MMA repeat units to sulfate end groups in the former is 6.5. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and gel permeation chromatography both showed that the mean number of MMA repeat units comprising the extracted material is 8-9. The hydrolysis procedure rids the oligomers of their terminal groups and converts some of the methyl ester groups to acid, greatly sim-plifying the mass spectrum. This appears to be the first direct measurement of “surfactants” produced in situ from monomer and persulfate initiator. © 1995 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1995.080331402
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  • 14
    Electronic Resource
    Electronic Resource
    Dynamics of keratin filaments and the intermediate filament distribution center during shape change in PtK1 cells (1984)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 4 (1984), S. 169-181 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; motility ; cell spreading ; epithelial cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Reorganization of intermediate filaments during cell spreading is examined by immunofluorescence, electron microscopy, and time-lapse video microscopy. A juxtanuclear cap, believed to correspond to the intermediate filament distribution center, was observed to be spatially related to the organization of the intermediate filament network as cells spread. A keratin cap was observed, which appeared spontaneously in motile PtK1 cells. Cap formation may be a consequence of retraction of intermediate filaments from the cytoplasm as cells move. The position of this juxtanuclear cap is related to the direction of movement, located on the side of the nucleus near the advancing edge of the cell. As the cell spreads, the cap disappears as the keratin filament network returns to the cytoplasm. Evidence presented here is consistent with the hypothesis that the distribution center mediates keratin filament organization during cell shape change.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970040303
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  • 15
    Electronic Resource
    Electronic Resource
    Alteration of the distribution of intermediate filaments in PtK1 cells by acrylamide II: Effect on the organization of cytoplasmic organelles (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 15-24 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; keratin ; vimentin ; microtubules ; saltatory movements ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The distribution and motility of cytoplasmic particles was examined in PtK1 cells in which intermediate filament networks had been disrupted by acrylamide. In these cells, particles (mitochondria and vesicles) accumulated near the cell center although saltatory movements continued. This left a broad sheet of agranular cytoplasm at the periphery of the cell. Particles were capable of movement into this sheet. Intermediate filaments were absent in the peripheral cytoplasm although microtubules remained in a normal configuration. Particles apparently move along the microtubules. These results indicate that particle movement along microtubules is not dependent upon the normal configuration of intermediate filaments. It is suggested that intermediate filaments are necessary for normal organelle distribution and serve as a matrix with which particles can associate to maintain position.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060104
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  • 16
    Electronic Resource
    Electronic Resource
    Cytoskeletal alterations in cultured cardiomyocytes following exposure to the lipid peroxidation product, 4-hydroxynonenal (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 28 (1994), S. 119-134 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; vinculin ; desmin ; sarcolemmal damage ; free radicals ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Damage to the cardiac myocyte sarcolemma following any of several pathological insults such as ischemia (anoxia) alone or followed by reperfusion (reoxygenation), is most apparent as progressive sarcolemmal blebbing, an event attributed by many investigators to a disruption in the underlying cytoskeletal scaffolding. Scanning electron microscopic observation of tissue cultured rat neonatal cardiomyocytes indicates that exposure of these cells to the toxic aldehyde 4-hydroxynonenal (4-HNE), a free radical--induced, lipid peroxidation product, results in the appearance of sarcolemmal blebs, whose ultimate rupture leads to cell death. Indirect immunofluorescent localization of a number of cytoskeletal components following exposure to 4-HNE reveals damage to several, but not all, key cytoskeletal elements, most notably microtubules, vinculin-containing costameres, and intermediate filaments. The exact mechanism underlying the selective disruption of these proteins cannot be ascertained at this time. Colocalization of actin indicated that whereas elements of the cytoskeleton were disrupted by increasing length of exposure to 4-HNE, neither the striated appearance of the myofibrils nor the lateral register of neighboring myofibrils was altered. Monitoring systolic and diastolic levels of intracellular calcium ([Ca2+]i) indicated that increases in [Ca2+]i occurred after considerable cytoskeletal changes had already taken place, suggesting that damage to the cytoskeleton, at least in early phases of exposure to 4-HNE, does not involve Ca2+ -dependent proteases. However, 4-HNE-induced cytoskeletal alterations coincide with the appearance of, and therefore suggest linkage to, sarcolemmal blebs in cardiac myocytes.Although free radicals produced by reperfusion or reoxygenation of ischemic tissue have been implicated in cellular damage, these studies represent the first evidence linking cardiomyocyte sarcolemmal damage to cytoskeletal disruption produced by a free radical product. © 1994 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970280204
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  • 17
    Electronic Resource
    Electronic Resource
    Cytochalasin-Induced reorganization of actin in allium root cells (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 9 (1988), S. 283-298 
    Details
    ISSN: 0886-1544
    Keywords: colchicine ; microtubule ; mitosis ; rhodamine-phalloidin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effect of cytochalasins on F-actin was investigated in Allium root cells stained with rhodamine-phalloidin. With cytochalasin D (CD), the normal interphase network of actin fibers is replaced by dispersed rods and specks similar to those seen in animal cells. However, during division, the specks accumulate at the poles in the form of one to a few large aggregates. The effects intensify with increasing concentration (0.5-5 m̈g/ml) and exposure time (0.5-3 hr). Further, similar behavior is observed with cytochalasin B, but dihydroCB has little effect. Double localizations show that during preprophase, aggregates cluster in association with microtubule foci at the new poles located near the nuclear envelope. From metaphase through anaphase, the aggregates are often found near the tips of kinetochore fibers, while in telophase they are often appressed to the pole side of the daughter nuclei. No association is seen between actin and the other microtubule arrays. The reorganization of F-actin into small specks is unaffected by sodium azide, but aggregation at the poles is very sensitive to this agent. Polar clustering is also blocked by oryzalin, colchicine, and isopropyl n-(3-chlorophenyl) carbamate, but taxol has no effect. Experiments with scleroderma serum 5051 show that CD-induced aggregates are embedded in centrosomal material at the poles. The results reveal that the reorganization of actin in response to cytochalasins differs during the cell cycle. Furthermore, the aggregation of actin during division is probably governed by an energy-dependent interaction with microtubules.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970090402
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  • 18
    Electronic Resource
    Electronic Resource
    Acrylamide treatment of PtKl cells causes dephosphorylation of keratin polypeptides (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 11 (1988), S. 24-30 
    Details
    ISSN: 0886-1544
    Keywords: intermediate filaments ; phosphorylation ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Treatment of PtKl cells with 5 mM acrylamide for 4 hr results in alterations in the distribution of keratin filaments within the cells. This effect is reversible within 18 hr. Labeling of PtKl cells with 32P demonstrates that there are four phosphorylated keratins, having Mr of 56 k, 53 k, 45 k, and 40 k. Phosphate associated with these polypeptides appears to turn over with a t1/2 of 12 hr. Incubation of labeled cells in 5 mM acrylamide results in approximately 50% dephosphorylation of keratins within 2 hr, which is 3 times faster than normal turnover. Recovery of cells from acrylamide is accompanied by rephosphorylation of keratins within 18 hr. Analysis by 31P NMR spectroscopy shows that acrylamide treatments are accompanied by a transient decrease in soluble inorganic phosphate. This is followed by a rapid increase in Pi which gradually returns to normal levels. These studies show a strong correlation between phosphorylation of PtKl cell keratins and morphological response of keratin filaments to acrylamide. These observations suggest that normal distribution of keratin filaments may be, in part, mediated by protein phosphorylation.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970110104
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  • 19
    Electronic Resource
    Electronic Resource
    Effect of cytochalasins on actin in dividing root tip cells of Allium and Triticum: A comparative immunocytochemical study (1991)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 18 (1991), S. 107-112 
    Details
    ISSN: 0886-1544
    Keywords: cell division ; cytoskeleton ; root cell ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A collaborative effort was initiated to resolve differences in two recent papers on the effects of cytochalasins in root cells. While both studies reported similar effects on interphase cells (i.e., replacement of microfilaments by many small specks and rods), Palevitz (Cell Motil. Cytoskeleton 9:283-298, 1988) maintained that cytochalasins B and D induce actin aggregation at the poles of dividing Allium root cells at a concentration of 10 μM with rhodamine phalloidin as a reporter probe, whereas McCurdy and Gunning (Cell Motil. Cytoskeleton 15:76-87, 1990) could not find these aggregates following antiactin immunocytochemistry in Triticum roots treated with CB at 50 μM. Employing identical methods and materials in the same laboratory, we found that CD induces polar actin aggregates in dividing cells of both species. However, the aggregates in Triticum are smaller and occur less frequently than those in Allium. A similar pattern is seen with CB.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970180205
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  • 20
    Electronic Resource
    Electronic Resource
    Microtubule reorganization during the cell cycle in synchronized BY-2 tobacco suspensions (1991)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 18 (1991), S. 94-106 
    Details
    ISSN: 0886-1544
    Keywords: Nicotiana tabacum ; microfilament ; nuclear envelope ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Tobacco BY-2 suspension cultures were synchronized with aphidicolin in order to assess the relationship between microtubules (MTs), microfilaments (MFs), and the nuclear envelope (NE) at different stages of the cell cycle. Using immunofluorescence techniques, ordered MT arrays were found in the cortex in G1; few MTs are evident deeper in the cytoplasm or near the nucleus. However, MTs radiate from the surface of the nucleus during S and G2 as the interphase cortical array is replaced by the preprophase band. Perinuclear fluorescence is also visible at the end of cytokinesis but does not overlap with new ordered cortical arrays early in G1. When isolated nuclei are examined, associated MTs are again evident in S and G2, but not in G1. Microfilaments are colocalized with the MTs in the radiating arrays, as ascertained by dual staining of cells with rhodamine phalloidin. Propyzamide treatment leads to the loss of MTs at all stages, while cytoplasmic and perinuclear MF networks persist. Conversely, cytochalasin D disrupts MFs, including those radiating from the nucleus during S and G2, without any apparent effect on MTs. The results cast doubt on a proposed role for the NE in the generation of cortical MTs in plants. A universal role for MFs in the deployment of MTs is also in question.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970180204
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