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March 27, 2001Biochemistry

A Structural Characterization of the Interactions between Titin Z-Repeats and the α-Actinin C-Terminal Domain

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Authors

CJCatherine JosephBaylor College of Medicine GSGünter StierHeidelberg University RORonan O’BrienLimerick Institute of Technology

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Implication

Novel Z-band interaction mapping extends sarcomere models; leaves open functional validation in cardiac disease.

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Cite This Study

Joseph et al. (2001) studied this question.

synapsesocial.com/papers/6a73dbd35e45dc7750a8be0a https://doi.org/10.1021/bi002739r

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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1A survey of interactions made by the giant protein titin1993 · 147 citations
2Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle.1989 · 100 citations
3Targeting of cardiac muscle titin fragments to the Z-bands and dense bodies of living muscle and non-muscle cells2000 · 47 citations
4ZASP: A New Z-band Alternatively Spliced PDZ-motif Protein1999 · 225 citations
5Binding of the N‐terminal 63 kDa portion of connectin/titin to α‐actinin as revealed by the yeast two‐hybrid system1997 · 86 citations