Results 151 to 160 of about 16,394 (180)
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Angewandte Chemie International Edition, 2018
AbstractProtein allostery, a chemical‐to‐mechanical effect that can precisely regulate protein structure, exists in many proteins. Herein, we demonstrate that protein allostery can be used to drive self‐assembly for the construction of tunable protein architectures. Calmodulin (CaM) was chosen as a model allosteric protein. Ca2+‐mediated contraction of
Miaomiao Xu, Lianxiao Liu, Qiang Yan
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AbstractProtein allostery, a chemical‐to‐mechanical effect that can precisely regulate protein structure, exists in many proteins. Herein, we demonstrate that protein allostery can be used to drive self‐assembly for the construction of tunable protein architectures. Calmodulin (CaM) was chosen as a model allosteric protein. Ca2+‐mediated contraction of
Miaomiao Xu, Lianxiao Liu, Qiang Yan
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Journal of Cell Science, 1986
ABSTRACT Fluorescently labelled contractile proteins (alpha-actinin and filamin) were used to study the dynamic nature of three types of microfilament bundles: myofibrils, stress fibres and polygonal networks. Cultured muscle and non-muscle cells that were microinjected with fluorescent alphaactinin rapidly incorporated the labelled ...
J M, Sanger +3 more
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ABSTRACT Fluorescently labelled contractile proteins (alpha-actinin and filamin) were used to study the dynamic nature of three types of microfilament bundles: myofibrils, stress fibres and polygonal networks. Cultured muscle and non-muscle cells that were microinjected with fluorescent alphaactinin rapidly incorporated the labelled ...
J M, Sanger +3 more
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Staurosporine induces dissolution of microfilament bundles by a protein kinase C-independent pathway
Experimental Cell Research, 1990The protein kinase C (PKC) inhibitor staurosporine was found to dramatically alter the actin microfilament cytoskeleton of a variety of cultured cells, including PTK2 epithelial cells, Swiss 3T3 fibroblasts, and human foreskin fibroblasts. For example, PTK2 cells exposed to 20 nM staurosporine exhibited a progressive thinning and loss of cytoplasmic ...
K K, Hedberg +3 more
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Molecular Reproduction and Development, 1991
AbstractSperm from the decapod crustacean Rhynchocinetes typus undergo dramatic shape changes as they pass from the vas deferens to seawater and interact with the oocyte envelopes. Using FITC‐phalloidin and antitubulin antibodies, we were able to localize microfilaments and a tubulin‐like protein in R. typus spermatozoon. Microfilaments and the tubulin‐
PEREZ, C +5 more
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AbstractSperm from the decapod crustacean Rhynchocinetes typus undergo dramatic shape changes as they pass from the vas deferens to seawater and interact with the oocyte envelopes. Using FITC‐phalloidin and antitubulin antibodies, we were able to localize microfilaments and a tubulin‐like protein in R. typus spermatozoon. Microfilaments and the tubulin‐
PEREZ, C +5 more
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Experimental Cell Research, 1987
A specific polyclonal antibody has been raised against a basic cytoplasmic protein (p27) which is induced by serum in growth-arrested NIH 3T3 cells but is constitutively expressed in nonestablished fibroblasts. Immunoblotting analysis and [35S]methionine labeling show that p27 is absent in tissues and established cell lines of different types. However,
J F, Santarén +3 more
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A specific polyclonal antibody has been raised against a basic cytoplasmic protein (p27) which is induced by serum in growth-arrested NIH 3T3 cells but is constitutively expressed in nonestablished fibroblasts. Immunoblotting analysis and [35S]methionine labeling show that p27 is absent in tissues and established cell lines of different types. However,
J F, Santarén +3 more
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Biochemical Society Transactions, 1991
Fulton, A. €3.. Wan, K. M. & I’enman. S. (10x0) Cell (Cambridge. Mass.) 20, 840-X.57 I m k . K.. Kansom, I,., Kaufmann. Y. 81 I’enman. S. (1077) Cell (Cambridge, Mass.) 10,67-7X Cervera, M., Llreyfuss, G. 81 I’enman, S. (10x1) Cell (Cambridge, Mass.) 23, 1 13120 Zumbe. A., Stahli. C. 81 Trachsel, 11. (10x2) I’roc. Natl. Acad. Sci. lI.S.A. 79.
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Fulton, A. €3.. Wan, K. M. & I’enman. S. (10x0) Cell (Cambridge. Mass.) 20, 840-X.57 I m k . K.. Kansom, I,., Kaufmann. Y. 81 I’enman. S. (1077) Cell (Cambridge, Mass.) 10,67-7X Cervera, M., Llreyfuss, G. 81 I’enman, S. (10x1) Cell (Cambridge, Mass.) 23, 1 13120 Zumbe. A., Stahli. C. 81 Trachsel, 11. (10x2) I’roc. Natl. Acad. Sci. lI.S.A. 79.
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Microfilaments and protein synthesis; effects of insulin
International Journal of Biochemistry, 1993E K, Kirkeeide, I F, Pryme, A, Vedeler
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[Effects of methamidophos on microtubule and microfilament proteins in sciatic nerve of hens].
Zhonghua lao dong wei sheng zhi ye bing za zhi = Zhonghua laodong weisheng zhiyebing zazhi = Chinese journal of industrial hygiene and occupational diseases, 2007To investigate the dynamic changes of alpha-tubulin, beta-tubulin and beta-actin in sciatic nerve of hen with organophosphorus ester-induced delayed neuropathy (OPIDN).OPIDN was induced in 10-month-old Roman hens by daily subcutaneous administration of 30 mg/kg methamidophos for 15 days.
Xiu-lan, Zhao +6 more
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The Journal of protozoology, 1992
Microtubules and microfilaments are highly conserved cytoskeletal polymers hypothesized to play essential biomechanical roles in the unusual gliding motility of Apicomplexan zoites and in their invasion of, and development within, host epithelial cells. We have identified and isolated Cryptosporidium parvum genes encoding the microtubule proteins alpha-
R G, Nelson +4 more
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Microtubules and microfilaments are highly conserved cytoskeletal polymers hypothesized to play essential biomechanical roles in the unusual gliding motility of Apicomplexan zoites and in their invasion of, and development within, host epithelial cells. We have identified and isolated Cryptosporidium parvum genes encoding the microtubule proteins alpha-
R G, Nelson +4 more
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Microfilament gel rigidity cooperates negatively with the binding of actin gelling proteins.
Biochemistry international, 1990At 37 degrees C, in the presence of 0.1 M KC1 and 2 mM MgCl2, the binding of alpha-actinin to F-actin increases with the concentration of alpha-actinin but not with the concentration of F-actin. This implies that binding is determined by additional factors, beside the alpha-actinin - F-actin association constant. We propose that one of these factors is
E, Grazi, G, Trombetta, M, Guidoboni
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