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By Monique M. Tirion, Daniel ben-Avraham, Kenneth C. Holmes (auth.), James E. Estes, Paul J. Higgins (eds.)

During the interval August 5-9, 1992, and instantly previous the 1992 Gordon study convention on Motile and Contractile structures, the "Third foreign convention at the constitution and serve as of Ubiquitous mobile Protein Actin" used to be held on the Emma Willard university in Troy, manhattan, below the identify "ACTIN '92". This convention involved in the elemental houses and mobile services of actin and actin­ established microfilament platforms. the 1st convention during this sequence was once held in 1982, in Sydney, Australia, and hosted via Dr. Cristobal G. dos Remedios and Dr. Julian A. Barden, either from the college of Sydney (New South Wales, Austrailia). the second one convention convened in Monza, Italy in June 1987, and was once equipped through Dr. Roberto Colombo, collage of Milan (Italy). This 3rd collecting of researchers dedicated to the examine of actin and actin-associated proteins was once geared up by way of Dr. James E. Estes, Albany Stratton V A scientific heart and Dr. Paul 1. Higgins, Albany clinical collage, who have been assisted through an Organizing Committee inclusive of Dr. Edward D. Korn (National middle, Lung and Blood Institute, NIH), Dr. Thomas P. Stossel (Massachusetts normal Hospital), Dr. Fumio Matsumura (Rutgers University), and Dr. Stephen Farmer (Boston University). This assembly used to be devoted to the various pioneering contributions of Professor Fumio Oosawa to the sector of actin research.

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Additional resources for Actin: Biophysics, Biochemistry, and Cell Biology

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1992). Then Konno and Morales (1985) reported that two thiol groups in actin, normally unreactive, became exposed at very low Ca ++ concentrations, suggesting that the Ca ++-binding affinity of actin might be much stronger than previously thought. , 1992). , 1992). In this experiment, the fluorescent Ca ++ chelator Quin 2 is used to induce and 36 monitor the dissociation of tightly-bound Ca ++ from actin. The slow increase in fluorescence intensity up to the first plateau is due to the release of Ca ++ from the high affinity site.

Gershman. 1987. Tight Binding of Divalent Cations to Monomeric Actin. 1. Bioi. Chem. 262:4952-4957. , LA. J. C. Gershman. 1992. Tightly-bound divalent cation of actin. I. Muse. Res. Cell Mot. 13:272-284. , D. Lieberman, and Helen R. Gilbert. 1980. A Fluorescent Probe for Conformational Changes in Skeletal Muscle G-Actin. I. Bioi. Chem. 255:8991-8993. Frieden, C. 1982. The Mg-induced Conformational Change in Rabbit Skeletal Muscle G-actin. 1. Bioi. Chem. 257:2882-2886. Frieden, C. and K. Patane.

1972, Effect of calcium ions on the flexibility of reconstituted thin filaments of muscle studied by quasi-electric scattering oflaser light, 1. Mol. Bioi. 68:511-522. F. , 1990, Atomic structure of the actin:DNase I complex, Nature 347:37-44. , Nakano, E. , 1965, Polymerisation of actin free from nucleotides and divalent cations, Biochim. Biophys. Acta 94:494-503. Kasai, M. , 1969, Behaviour of divalent cations and nucleotides bound to F-actin, Biochim. Biophys. Acta 172:300-310. , Polzar, B.

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