Calcium, thin filaments, and the integrative biology of cardiac contractility

T Kobayashi, RJ Solaro - Annu. Rev. Physiol., 2005 - annualreviews.org
▪ Abstract Although well known as the location of the mechanism by which the cardiac
sarcomere is activated by Ca2+ to generate force and shortening, the thin filament is now …

Thin filament mutations: developing an integrative approach to a complex disorder

JC Tardiff - Circulation research, 2011 - Am Heart Assoc
Sixteen years ago, mutations in cardiac troponin (Tn) T and α-tropomyosin were linked to
familial hypertrophic cardiomyopathy, thus transforming the disorder from a disease of the β …

Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions

NJ Greenfield - Nature protocols, 2006 - nature.com
Circular dichroism (CD) is an excellent spectroscopic technique for following the unfolding
and folding of proteins as a function of temperature. One of its principal applications is to …

Structure of the mid-region of tropomyosin: bending and binding sites for actin

JH Brown, Z Zhou, L Reshetnikova… - Proceedings of the …, 2005 - National Acad Sciences
Tropomyosin is a two-chain α-helical coiled coil whose periodic interactions with the F-actin
helix are critical for thin filament stabilization and the regulation of muscle contraction. Here …

[HTML][HTML] Gestalt-binding of tropomyosin to actin filaments

KC Holmes, W Lehman - Journal of muscle research and cell motility, 2008 - Springer
We argue that the overall behavior of tropomyosin on F-actin cannot be easily discerned by
examining thin filaments reduced to their smallest interacting units. In isolation, the …

The shape and flexibility of tropomyosin coiled coils: implications for actin filament assembly and regulation

XE Li, KC Holmes, W Lehman, HS Jung… - Journal of molecular …, 2010 - Elsevier
Wrapped superhelically around actin filaments, the coiled-coil α-helices of tropomyosin
regulate muscle contraction by cooperatively blocking or exposing myosin-binding sites on …

[HTML][HTML] Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded α-helical coiled-coils

SC Kwok, RS Hodges - Journal of Biological Chemistry, 2004 - ASBMB
Detailed sequence analyses of the hydrophobic core residues of two long two-stranded α-
helical coiled-coils that differ dramatically in sequence, function, and length were performed …

Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation

NJ Greenfield, YJ Huang, GVT Swapna… - Journal of molecular …, 2006 - Elsevier
Tropomyosin is a coiled-coil protein that binds head-to-tail along the length of actin filaments
in eukaryotic cells, stabilizing them and providing protection from severing proteins …

Tropomyosin structure, function, and interactions: a dynamic regulator

SE Hitchcock-DeGregori, B Barua - Fibrous proteins: structures and …, 2017 - Springer
Tropomyosin is the archetypal-coiled coil, yet studies of its structure and function have
proven it to be a dynamic regulator of actin filament function in muscle and non-muscle cells …

Regulation of muscle contraction by tropomyosin and troponin: how structure illuminates function

JH Brown, C Cohen - Advances in protein chemistry, 2005 - Elsevier
Publisher Summary This chapter provides a brief description of tropomyosin's periodic and
aperiodic structural features related to their function. The chapter describes the structure of …