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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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发表于 2025-3-21 16:41:37 | 显示全部楼层 |阅读模式
书目名称Elastic Filaments of the Cell
编辑Henk L. Granzier,Gerald H. Pollack
视频video
丛书名称Advances in Experimental Medicine and Biology
图书封面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
描述Elastic filaments refer mainly to titin, the largest of allknown proteins. Titin was discovered initially in muscle cells, whereit interconnects 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 found inchromosomes of neurons and also in blood platelets. This topic is fastbecoming a focal point for research in understanding viscoelasticproperties at the molecular, cellular, and tissue levels. In titin maylie a generic basis for biological viscoelasticity. It has becomeclear that titin may hold the key to certain clinical anomalies. Forexample, it is clear that titin-based ventricular stiffness ismodulated by calcium and that titin is responsible for the alteredstiffness in cardiomyopathies. It is also clear from evidence from agroup of Finnish families that titin mutations may underlie somemuscular dystrophies and that with other mutations chromatids fail toseparate during mitosis. Thus, it is clear that this protein will haveimportant clini
出版日期Book 2000
关键词Activation; Calcium; Drosophila; cell; chromosome; mutation; protein; protein structure; proteins; tissue
版次1
doihttps://doi.org/10.1007/978-1-4615-4267-4
isbn_softcover978-1-4613-6916-5
isbn_ebook978-1-4615-4267-4Series ISSN 0065-2598 Series E-ISSN 2214-8019
issn_series 0065-2598
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
The information of publication is updating

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发表于 2025-3-21 21:53:27 | 显示全部楼层
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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发表于 2025-3-22 06:13:43 | 显示全部楼层
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.
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发表于 2025-3-22 16:36:53 | 显示全部楼层
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.
发表于 2025-3-22 20:02:06 | 显示全部楼层
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
发表于 2025-3-22 22:14:19 | 显示全部楼层
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.
发表于 2025-3-23 03:43:46 | 显示全部楼层
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.
发表于 2025-3-23 05:45:29 | 显示全部楼层
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.
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