AbstractCalponin is a smooth muscle specific, actin-, tropomyosin- and calmodulin-binding protein thought to be involved in some way in the regulation or modulation of contraction. Here we describe the cloning and bacterial expression of two calponin species from murine and porcine smooth muscle tissues. Primary and secondary structural analyses of the deduced amino acid sequences revealed a high degree of homology to avian calponin with the exception of a short and variable C-terminal segment. The sequence data demonstrate that the two mammalian calponin variants do not arise via alternative splicing but are encoded by different genes
AbstractCalponin is involved in the regulation of contractility and organization of the actin cytosk...
AbstractCalponin (4.1–5.9 μM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20–25% wi...
AbstractInteraction of smooth-muscle calponin and desmin was analyzed by means of ultracentrifugatio...
AbstractCalponin is a smooth muscle specific, actin-, tropomyosin- and calmodulin-binding protein th...
AbstractCalponin is an actin-, calmodulin-. and tropomyosin-binding protein that has been isolated f...
AbstractSmooth muscle cell calponin (h1 or basic isoform) is an actin-binding protein that inhibits ...
,binding proteins contains three genetic variants, a smooth muscle-specific variant termed h1 or bas...
AbstractTwo-dimensional gel analysis of basic proteins in developing human smooth muscle identifies ...
Calponin is an actin-, calmodulin-, and tropomyosin-binding protein that has been isolated from smoo...
Calponins (CaPs) are actin-binding proteins that stabilize actin filaments. Mammals express three ge...
AbstractLimited chymotryptic cleavage of turkey gizzard calponin yields a 13 kDa fragment which coul...
AbstractCalponin, a novel homologue of troponin T, purified from chicken gizzard was found to be one...
AbstractCalponin is a thin filament-associated protein in smooth muscle that has been shown to bind ...
AbstractWe have tested the hypothesis of Winder and Walsh [(1990) J. Biol. Chem. 256, 10148] that th...
Calponins (CaPs) are actin-binding proteins that stabilize actin filaments. Mammals express three ge...
AbstractCalponin is involved in the regulation of contractility and organization of the actin cytosk...
AbstractCalponin (4.1–5.9 μM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20–25% wi...
AbstractInteraction of smooth-muscle calponin and desmin was analyzed by means of ultracentrifugatio...
AbstractCalponin is a smooth muscle specific, actin-, tropomyosin- and calmodulin-binding protein th...
AbstractCalponin is an actin-, calmodulin-. and tropomyosin-binding protein that has been isolated f...
AbstractSmooth muscle cell calponin (h1 or basic isoform) is an actin-binding protein that inhibits ...
,binding proteins contains three genetic variants, a smooth muscle-specific variant termed h1 or bas...
AbstractTwo-dimensional gel analysis of basic proteins in developing human smooth muscle identifies ...
Calponin is an actin-, calmodulin-, and tropomyosin-binding protein that has been isolated from smoo...
Calponins (CaPs) are actin-binding proteins that stabilize actin filaments. Mammals express three ge...
AbstractLimited chymotryptic cleavage of turkey gizzard calponin yields a 13 kDa fragment which coul...
AbstractCalponin, a novel homologue of troponin T, purified from chicken gizzard was found to be one...
AbstractCalponin is a thin filament-associated protein in smooth muscle that has been shown to bind ...
AbstractWe have tested the hypothesis of Winder and Walsh [(1990) J. Biol. Chem. 256, 10148] that th...
Calponins (CaPs) are actin-binding proteins that stabilize actin filaments. Mammals express three ge...
AbstractCalponin is involved in the regulation of contractility and organization of the actin cytosk...
AbstractCalponin (4.1–5.9 μM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20–25% wi...
AbstractInteraction of smooth-muscle calponin and desmin was analyzed by means of ultracentrifugatio...