Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis
@article{Fulton1991TitinAH,
title={Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis},
author={Alice Bordwell Fulton and William B. Isaacs},
journal={BioEssays},
year={1991},
volume={13}
}Titin, the largest protein identified to date (over 1 μm long, almost 3 million daltons in mass) is the third most abundant component of the sarcomere. In the mature myofibril, titin molecules span from M line to Z line, forming a third filament system which provides sarcomeric alignment and elastic recoil. In the developing sarcomere, accumulating evidence from studies both in vivo and in vitro implicates titin as part of a morphogenetic scaffolding, upon which critical events in…
83 Citations
Immunoglobulin-type domains of titin: same fold, different stability?
- BiologyBiochemistry
- 1994
The stability of the modules over a range of conditions was investigated by measuring key thermodynamic parameters for both thermal and chemical denaturation and by monitoring amide proton exchange as a function of time.
Titin role in muscle homeostasis : the kinase domain
- Biology
- 2014
It was demonstrated that TK is a catalytically inactive pseudokinase acting as a molecular scaffold and TK and MuRF1 signaling modules are structurally interconnected and genetic perturbation of this link might lead to dilated cardiomyopathy.
The anatomy of a molecular giant: how the sarcomere cytoskeleton is assembled from immunoglobulin superfamily molecules.
- Biology, ChemistryJournal of molecular and cellular cardiology
- 1995
The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity.
- BiologyBiophysical journal
- 1995
Actin Motility
- Biology, Chemistry
- 2005
In vitro binding assays and electrophoretic analyses revealed that the inhibition is most likely caused by interaction between the actin filament and the titin 1-11 fragment, and the physiological relevance of the novel finding of motility inhibition by titin fragments is discussed.
Nonuniform elasticity of titin in cardiac myocytes: a study using immunoelectron microscopy and cellular mechanics.
- BiologyBiophysical journal
- 1996
Biochemical and Structural Properties of Titin , Nebulin and Intermediate Filaments in Muscle
- Biology
- 2001
The Z-line is a key structure of the myofibrils and of the overall skeletal muscle cell cytoskeleton and can be considered as “representing,” or taking the place of, the microfilaments of non-muscle cells.
Dissecting titin into its structural motifs: identification of an alpha-helix motif near the titin N-terminus.
- BiologyBiochemistry
- 1995
A study of a stretch located in the titin N-terminus and part of a linker between two modules is presented, drawn toward this region because it shows 100% probability to form a coiled coil when analyzed by a prediction program.
Titin and Nebulin: Giant Multitasking Protein Rulers in Muscle
- Biology
- 1995
Recent studies of sarcomere-associated cytoskeletal lattices begin to shed light on how contracted muscle restores its length and how resting muscle responds to stretch and compression.
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