{"title":"Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle.","authors":"T Wallimann, H M Eppenberger","doi":"10.1007/978-1-4757-4723-2_8","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_8","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-1-4757-4723-2_8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15004186","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Sarcomere-associated cytoskeletal lattices in striated muscle. Review and hypothesis.","authors":"K Wang","doi":"10.1007/978-1-4757-4723-2_10","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_10","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15004188","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle.","authors":"T. Wallimann, Eppenberger Hm","doi":"10.3929/ETHZ-A-000370124","DOIUrl":"https://doi.org/10.3929/ETHZ-A-000370124","url":null,"abstract":"S: T. Wallimann, D.C. Turner, and H.M. Eppenberger. Localization of creatine kinase at the M-line of skeletal muscle myofibrils. Abstracts for 5th Annual Meeting of the Union for Swiss Societies for Experimental Biology in Basel, Switzerland (USGEB) (1973), p. 23 H.M. Eppenberger, D.C. Turner, and T. Wallimann. Evidenz für das Vorhandensein strukturell gebundener M-TypKreatinkinase (E.C. 2.7.3.2.) im Bereich der A-Bande lm quergestreiften Skelettmuskel. Hoppe-Seyler's Zeitschrift für Physiol. Chemie 354: 228 (1973) T. Wallimann, and H.M. Eppenberger. Ultrastructural localization of the M-line protein creatine kinase in chicken pectoralis muscle. Abstracts of the American Society for Cell Biology 17th Annual Meeting 15-18 Nov. 1977, San Diego, Cal. in: J.Cell Biol. 75: 326a (1977) W.F. Stafford 111, E.M. Szentkiralyi, T. Wallimann, and A.G. Szent-Gyprgyi. Interaction of light chains with scallop myosin. Abstract of the Intl. Meeting on Muscle in Alpbach, Austria (1976) A.G. Szent-Györgyi, P.D. Chantler, J. Sellers, W.F. Stafford, E.M. Szentkiralyi, and T. Wallimann. Myosin-linked calcium regulation. Abstracts of the sixth Intl. Biophysics Congress, Kyoto, Japan, 3-9 Sept. (1978), p. 86 T. Wallimann, and A.G. Szent-Györgyi. Effectsof anti-scallop myosin light-chain antibodies on myosin linked regulation. 23rd Annual Meeting of the Biophysical Society, 25-28 Febr. (1979) in: Biophys. J. 25: 72a (1979) T. Wallimann, and A.E. Szent-Györgyi. Immunological comparison of heavy and light-chains from different myosins by indirect, competitive radioimmunobinding assay, a novel IC RIBA technique. Abstract for ASBC!BS Meeting in Atlanta. in: Federation Proceedings 39: 2167, abstract 2956 (1980) Paula Flicker, Theo Wallimann, and Peter Vibert. Location of regulatory light chais in scallop myosin. Biophys. J. 33: 279a (1981) P.M.D. Harwicke, Theo Wallimann, and Andrew G. Szent-Györgyi. Proximity of the regulatory and essential light chains in scallop myosin. Biophys. J. 33: 279a (1981) H.M. Eppenberger, T.D. Doetschman, J.C. Perriard, E.E. Strehler, D. Studer, and T. Wallimann. Myomesin in cross-striated muscle cells. Cold Spring Harbor Symposium on: Molecular and Cel1ular Control of Muscle Deveelopment. 8-13 Sept. (1981) p.l0l. T. Schlösser, T. Wallimann, and H.M. Eppenberger. Physiological significance of M-line-bound creatine kinase (CK). Experientia ~: 731 (1982) E.E. Strehler, T. Wallimann, and H.M. Eppenberger. Interaction between M-line Proteins and Myosin. 22n Annual Meeting of the American Society for Cell Biology, Baltimore, 30 Nov. 4 Dec. (1982) in: J. Cell Biol. 95: 360a (1982) Walzthöny, D., M. Bähler, T. Wallimann, H. Gross, H.M. Eppenberger, and H. Moor. Improved techniques for the visualization of myosin molecules. 10th Intl. Congress on Electron Microscopy, Hamburg, 17-24 Aug. (1982) M. Bähler, E.E. Strehler, D. Walzthöny, H.M. Eppenberger, and T. Wallimann. Myosin Binding Proteins. 11th Europ. Congress on Muscle and Motility, Leicester, 14-18 ","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70170207","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cytoskeletal events during calcium- or EGF-induced initiation of DNA synthesis in cultured cells. Role of protein phosphorylation and clues in the transformation process.","authors":"N Marceau, S H Swierenga","doi":"10.1007/978-1-4757-4723-2_5","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_5","url":null,"abstract":"<p><p>The possible relationship between cytoskeletal events and growth regulation in response to stimulation by calcium and by growth factors such as EGF can be summarized as follows: An elaborate interaction exists between calcium and serum growth factors, such as EGF, in the initiation of DNA synthesis in quiescent cells. This implies that many processes between the external signals delivered at the cell surface and the sequential intracellular events that lead to chromosomal replication, and ultimately to cell division, must be coordinated in a reproducible manner. It is now apparent that because of its possible role as a dynamic integrator of the cytoplasm, the cytoskeleton could represent the coordinator of the events that lead to replication. Calcium (with its intracellular acceptor, calmodulin) and cAMP (which can act by opposing mechanisms) are extensively involved in the control of the integrity of the cytoskeleton. Distinct protein kinases are activated by calcium/calmodulin, EGF, and cAMP as aspects of the prereplicative response, and many of the substrates for phosphorylation are cytoskeletal proteins. The emerging picture seems to include a direct involvement of these protein kinases in the cascade of regulatory events that leads to the initiation of DNA synthesis. Thus, the cytoskeleton has a direct role in the transmission of proliferative signals from external receptor sites to the nucleus. A means by which neoplastic cells can bypass the normal regulatory pathways is proposed in the light of recent data showing that the product of oncogenes are protein kinases or proteins that intimately interact with cellular protein kinases.</p>","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14120774","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Tropomyosin. Structural and functional diversity.","authors":"M R Payne, S E Rudnick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15004184","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cell shape, the complex cellular networks, and gene expression. Cytoskeletal protein genes as a model system.","authors":"A Ben-Ze'ev","doi":"10.1007/978-1-4757-4723-2_2","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_2","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13723630","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}