AbstractA sequence motif of about 100 amino acids, termed the `calponin homology domain' has been suggested to confer actin binding to a variety of cytoskeletal and signalling molecules. Here we analyse and compare the sequences of all calponin homology domain-containing proteins identified to date. We propose that single calponin homology domains do not confer actin-binding per se and that the actin-binding motifs of cross-linking proteins, which comprise two disparate calponin homology domains, represent a unique protein module
ABSTRACT Dystrophin has been shown to be associated in cells with actin bundles. Dys-246, an N-termi...
AbstractIn this issue of Structure, polymorphism of an actin binding protein is revealed in the stru...
The assembly of actin filaments into distinct cytoskeletal structures plays a critical role in cell ...
AbstractA sequence motif of about 100 amino acids, termed the `calponin homology domain' has been su...
AbstractBackground: The actin-binding site of several cytoskeletal proteins is comprised of two calp...
AbstractWith the refinement of algorithms for the identification of distinct motifs from sequence da...
Tandem calponin-homology (CH) domains are the most common actin-binding domains in proteins. However...
AbstractCalponin is involved in the regulation of contractility and organization of the actin cytosk...
Tandem calponin homology (CH1-CH2) domains are common actin-binding domains in proteins that interac...
Tandem calponin homology (CH1-CH2) domains are common actin-binding domains in proteins that interac...
Tandem calponin homology (CH1-CH2) domains are common actin-binding domains in proteins that interac...
IQGAPs are eukaryotic proteins which integrate signals from various sources and pass these on the cy...
Dystrophin and utrophin are two muscle proteins involved in Duchenne/Becker muscular dystrophy. Both...
Calponins (CaPs) are actin-binding proteins that stabilize actin filaments. Mammals express three ge...
AbstractAn actin-binding protein domain we call here ‘calponin-homology’ or CH is present in signall...
ABSTRACT Dystrophin has been shown to be associated in cells with actin bundles. Dys-246, an N-termi...
AbstractIn this issue of Structure, polymorphism of an actin binding protein is revealed in the stru...
The assembly of actin filaments into distinct cytoskeletal structures plays a critical role in cell ...
AbstractA sequence motif of about 100 amino acids, termed the `calponin homology domain' has been su...
AbstractBackground: The actin-binding site of several cytoskeletal proteins is comprised of two calp...
AbstractWith the refinement of algorithms for the identification of distinct motifs from sequence da...
Tandem calponin-homology (CH) domains are the most common actin-binding domains in proteins. However...
AbstractCalponin is involved in the regulation of contractility and organization of the actin cytosk...
Tandem calponin homology (CH1-CH2) domains are common actin-binding domains in proteins that interac...
Tandem calponin homology (CH1-CH2) domains are common actin-binding domains in proteins that interac...
Tandem calponin homology (CH1-CH2) domains are common actin-binding domains in proteins that interac...
IQGAPs are eukaryotic proteins which integrate signals from various sources and pass these on the cy...
Dystrophin and utrophin are two muscle proteins involved in Duchenne/Becker muscular dystrophy. Both...
Calponins (CaPs) are actin-binding proteins that stabilize actin filaments. Mammals express three ge...
AbstractAn actin-binding protein domain we call here ‘calponin-homology’ or CH is present in signall...
ABSTRACT Dystrophin has been shown to be associated in cells with actin bundles. Dys-246, an N-termi...
AbstractIn this issue of Structure, polymorphism of an actin binding protein is revealed in the stru...
The assembly of actin filaments into distinct cytoskeletal structures plays a critical role in cell ...