Titlebook: Elastic Filaments of the Cell; Henk L. Granzier,Gerald H. Pollack Book 2000 The Editor(s) (if applicable) and The Author(s), under exclusi

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書目名稱Elastic Filaments of the Cell影響因子(影響力)




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Getreide / Hülsenfrüchte / Hopfen und Malzlament system in the sarcomere, in particular to titin interactions with thick and thin filaments. The branching of titin network near the PEVK-region suggests that, in addition to conferring extensibility, it may also be important in facilitating the transition of titin intermolecular interactions between the arrays of thick and thin filaments.

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Assembly of Myofibrils in Cardiac Muscle Cellslocalized in the N-terminus of titin. This region of titin binds alpha-actinin and less avidly vinculin. Thus the N-terminus of titin via its binding to alpha-actinin, and vinculin could also help mediate the costameric attachment of the Z-bands of mature myofibrils to the nearest cell surfaces.

constitutional

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Titin as a Chromosomal Protein of chromosomes that may function to determine chromosome structure and provide elasticity, playing a role similar to that proposed for titin in muscle. We have identified mutations in . (.) and are characterizing phenotypes in muscle and chromosomes.

demote

0065-2598 ects the thick filament with the Z-line. Titin forms amolecular spring that is responsible for maintaining the structuralintegrity of contracting muscle, ensuring efficient musclecontraction. More recently, it has become clear that titin is notrestricted to muscle cells alone. For example, titin is

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Flat Growth: The Case of wirDesignn cardiac rest tension could not be ascribed to differences in the PEVK length of the N2B titin isoform. The low rest tension generated by dog cardiac muscle also does not appear to be explained by the N2 and PEVK segment lengths in the N2A titin isoform.

minimal

Einleitung und Zielsetzung der Studie,duced from thermodynamic measurements. A comparison between the unfolding forces measured in Ig domains of the muscle protein titin and those measured in fibronectin Type III domains reveals an extraordinarily high stability of titin domains.

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https://doi.org/10.1007/978-3-662-11875-7semble striated muscle titin in molecular size and morphology but differ in their interactions with myosin II filaments and in the structural contexts in which they exist .. Divergence of these titins from the muscle titin paradigm demonstrates the versatility of this remarkable family of giant proteins.