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  • 1
    Electronic Resource
    Electronic Resource
    Bacterial Toxins (1954)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 8 (1954), S. 411-428 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.mi.08.100154.002211
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  • 2
    Electronic Resource
    Electronic Resource
    A geometric hierarchy for the supersymmetry-breaking scale
    Amsterdam : Elsevier
    Physics Letters B 125 (1983), S. 59-62 
    Details
    ISSN: 0370-2693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0370-2693(83)91234-0
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  • 3
    Electronic Resource
    Electronic Resource
    Comparison of fiber types in skeletal muscles from ten animal species based on sensitivity of the myofibrillar actomyosin ATPase to acid or copper (1985)
    Springer
    Histochemistry and cell biology 82 (1985), S. 175-183 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Comparisons were made of the histochemical characteristics of skeletal muscle from 10 animal species. The basic comparison was made from the staining patterns for the myofibrillar actomyosin ATPase produced by preincubation of fresh frozen cross-sections of muscle at alkaline pH (10.30) or acid pH (4.60) with those produced by preincubation in media containing Cu2+ at alkaline pH (10.30), near neutral pH (7.40), or acid pH (4.60). Muscle sections were also stained for reduced nicotinamide adenine dinucleotide tetrazolium reductase and alpha-glycerophosphate dehydrogenase to provide an indication of the relative oxidative and glycolytic capacity of the different fiber types. Type II fibers in mixed fibered muscles were either very sensitive, moderately sensitive, or relatively insensitive to inactivation of the myofibrillar actomyosin ATPase after acid preincubation. These fibers were identified as type IIA1, IIA2, and IIA3, respectively. The myofibrillar actomyosin ATPase of the type I fibers of these muscles, with the exception of those in mouse muscle, was activated by pretreatment with acid. A separation of animal species was possible based on the stability of the IIA1 fibers to inclusion of Cu2+ in the preincubation medium. For one group of animals (rat, mouse, monkey, man, dog, rabbit, and cow), a reciprocal relationship existed between lability to acid and stability to Cu2+ for type IIA1 and IIA3 fibers, respectively. For the second group of animals (horse, ass, and cat) there was a parallel relationship between lability or stability of the type IIA1 and IIA3 fibers to pretreatment with either acid or Cu2+
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00708203
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  • 4
    Electronic Resource
    Electronic Resource
    Conversion of rat muscle fiber types (1985)
    Springer
    Histochemistry and cell biology 83 (1985), S. 555-560 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Rats were used in this study to determine the time course of conversion of muscle fiber types. The right or left gastrocnemius muscle was removed thereby causing an overload on the ipsilateral soleus and plantaris muscles. The contralateral limb served as a control. The type II to type I fiber conversion was followed histochemically in the soleus and plantaris muscles for one to six weeks following surgery. Muscle sections were stained for myofibrillar actomyosin ATPase and NADH tetrazolium reductase. The type I population in the soleus muscle was 99.3% six weeks after synergist removal. The plantaris muscle underwent a two fold increase in the percentage of type I fibers after six weeks. Transitional fibers were prominent in the plantaris muscle and reached their peak at 4% (P〈0.05) of the total population, four weeks after surgery.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00492460
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  • 5
    Electronic Resource
    Electronic Resource
    Identification of γ-tubulin, a new member of the tubulin superfamily encoded by mipA gene of Aspergillus nidulans (1989)
    [s.l.] : Nature Publishing Group
    Nature 338 (1989), S. 662-664 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Three mutant mipA alleles were isolated as extragenic suppressors of benA33, a heat-sensitive (hs~) /3-tubulin mutation1'2'3. The ben A gene encodes the major /3-tubulin expressed in hyphae4 and this /3-tubulin is essential to mitosis and nuclear migration2'5. Although the mutant mipA alleles ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/338662a0
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  • 6
    Electronic Resource
    Electronic Resource
    Differentiation of fiber types in skeletal muscle from the sequential inactivation of myofibrillar actomyosin ATPase during acid preincubation (1983)
    Springer
    Histochemistry and cell biology 77 (1983), S. 543-555 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A method is described for identifying fiber types of skeletal muscle from several mammalian species on the basis of the sequential inactivation of myofibrillar actomyosin ATPase during acid preincubation. When this method is used in combination with the standard alkaline preincubation at least 5 types of fibers can be identified. Of these, 2 are type I fibers with those of the slow twitch soleus muscle being different from those that exist in mixed muscles. The 3 subtypes of type II fibers exist independent of their metabolic properties. The need for careful standardization of histochemical methods for the visualization of myofibrillar actomyosin ATPase and the implication of the existence of different fiber types in apparently homogeneous muscle for the preparation of antibodies used for immunocytochemical methods of fiber identification are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495808
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  • 7
    Electronic Resource
    Electronic Resource
    Influence of exercise on the fiber composition of skeletal muscle (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 553-557 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Biopsy samples from the vastus lateralis muscle (VLM) of man were examined for fiber composition at rest and at selected intervals during prolonged exercise ranging in intensity from 40% to 75% of the total body maximal oxygen uptake (VO 2max) and one-min bouts of exercise at 150%VO 2max. Because of the heterogeneity of fibers in human VLM, studies were also completed where the effect of exercise on the fiber composition of the rat soleus muscle (SM) was examined. In some animals the SM from one hindlimb was removed 9 days prior to their being exercised after which the remaining SM was removed. Exercise reduced muscle glycogen in all experiments. In the studies with man, blood lactate exceeded 17 mmoles/l after the heavy exercise but was largely unchanged by endurance exercise. Colonic temperature of the exercised rats exceeded 40° C. In studies where fibers were identified only as type I and type II, type II fibers in the VLM of all samples (16) taken at rest averaged 61.2±12.5% as compared to 59.0±12.0% after exercise (54 biopsy samples). In a second series of studies with man where the subtypes of type II fibers were identified, there were also no differences in fiber composition of the VLM after varying periods of exercise. Glycogen content and percent fiber composition were the same in right and left SM obtained from rested rats. Exercise (30 to 40 min) did not alter the fiber composition of the rat SM. These data demonstrate that the histochemically demonstratable myofibrillar actomyosin ATPase of skeletal muscle is not altered by a single exercise bout.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02400971
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  • 8
    Electronic Resource
    Electronic Resource
    Influence of exercise on the fiber composition of skeletal muscle (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 553-557 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Biopsy samples from the vastus lateralis muscle (VLM) of man were examined for fiber composition at rest and at selected intervals during prolonged exercise ranging in intensity from 40% to 75% of the total body maximal oxygen uptake (VO 2max) and one-min bouts of exercise at 150%VO 2max. Because of the heterogeneity of fibers in human VLM, studies were also completed where the effect of exercise on the fiber composition of the rat soleus muscle (SM) was examined. In some animals the SM from one hindlimb was removed 9 days prior to their being exercised after which the remaining SM was removed. Exercise reduced muscle glycogen in all experiments. In the studies with man, blood lactate exceeded 17 mmoles/l after the heavy exercise but was largely unchanged by endurance exercise. Colonic temperature of the exercised rats exceeded 40° C. In studies where fibers were identified only as type I and type II, type II fibers in the VLM of all samples (16) taken at rest averaged 61.2±12.5% as compared to 59.0±12.0% after exercise (54 biopsy samples). In a second series of studies with man where the subtypes of type II fibers were identified, there were also no differences in fiber composition of the VLM after varying periods of exercise. Glycogen content and percent fiber composition were the same in right and left SM obtained from rested rats. Exercise (30 to 40 min) did not alter the fiber composition of the rat SM. These data demonstrate that the histochemically demonstratable myofibrillar actomyosin ATPase of skeletal muscle is not altered by a single exercise bout.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553716
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  • 9
    Electronic Resource
    Electronic Resource
    Topographic compensation: Guidance and directed locomotion of fibroblasts on grooved micromachined substrata in the absence of microtubules (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 45-58 
    Details
    ISSN: 0886-1544
    Keywords: colcemid ; kinesin ; actin ; topographic guidance ; micromachined substrata ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Fibroblats cultured on grooved substrata align themselves and migrate in the direction of the grooves, a phenomenon called contact guidance. Microtubules have been deemed important for cell polarization, directed locomotion, and contact guidance. Because microtubules were the first cytoskeletal element to align with the grooves when fibroblasts spread on grooved substrata, we investigated the consequences of eliminating the influence of microtubules by seeding fibro-blasts onto smooth and grooved micromachined substrata in the presence of colcemid. Fibroblasts were examined by time-lapse cinematography and epifluorescence or confocal microscopy to determine cell shape and orientation and the distribution of cytoskeletal or associated elements including actin filaments, vinculin, intermediate filaments, microtubules, and kinesin.As expected, cells spreading on smooth surfaces in the presence of colcemid did not polarize or locomote. Surprisingly however, by 24 hours, cells spread on grooves in the presence of colcemid were morphologically indistinguishable from controls spread on grooves. Both groups were aligned and polarized with the direction of the grooves and demonstrated directional locomotion along the grooves. In the absence of microtubules, kinesin localized to some of the aligned stress fibers and to leading edges of cells spreading on grooves. The grooved substratum compensated for the microtubule deficiency by organizing and maintaining an aligned actin filament framework. Thus, microtubules are not required to establish or maintain stable, polarized cell shapes or directed locomotion, provided an alternate oriented cytoskeletal component is available.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310106
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  • 10
    Electronic Resource
    Electronic Resource
    Conditionally lethal tubA α-tubulin mutations in Aspergillus nidulans (1987)
    Springer
    Molecular genetics and genomics 208 (1987), S. 135-144 
    Details
    ISSN: 1617-4623
    Keywords: Tubulin ; Microtubules ; Cytoskeleton ; Mitosis ; Motility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have mapped 17 extragenic suppressors of benA 33, a heat-sensitive β-tubulin mutation of Aspergillus nidulans, to the tubA α tubulin locus. Fifteen of these tubA mutations cause cold sensitivity in a genetic background with benA 33 and appear to cause lethality in a background with the wild-type benA allele. We examined the microtubule-mediated processes, nuclear division and nuclear migration, in seven different cold-sensitive double mutants, each carrying benA 33 and a different cold-sensitive tubA allele. Nuclear division and migration were inhibited at a restrictive temperature in each case, suggesting that cold sensitivity is due to the inhibition of microtubule function at low temperatures. A single allele, tubA4, suppressed the heat sensitivity conferred by benA33 but did not confer cold sensitivity in a benA33 background, however in a wildtype benA background, tubA4 conferred supersensitivity to antimicrotubule agents and weak cold sensitivity. TubA4 did not suppress the heat sensitivity conferred by two other benA alleles. The cold sensitivity conferred by tubA4 was suppressed by the microtubule stabilizing agent deuterium oxide, and the suppression of heat sensitivity conferred by four other tubA mutations was reversed by deuterium oxide. These results suggest that these mutations may affect hydrophobic interactions between α-and β-tubulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330434
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