Hsp47 is a chaperone protein with a fundamental role in the folding, stability and intracellular transport of procollagen triple helices. A light-responsive Hsp47 recombinant protein, engineered to control in situ the production and assembly of cellular collagen is here demonstrated. This novel light-driven tool enables unprecedented fundamental studies of collagen biosynthesis and associated diseases
Heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that helps the molecular ma...
Heat shock protein 47 (HSP47), encoded by the SERPINH1 gene, is a molecular chaperone essential for ...
HSP47 is a stress protein (heat shock protein) which resides in the endoplasmic reticulum, and is po...
Hsp47 is a chaperone protein with a fundamental role in the folding, stability and intracellular tra...
Collagen is the most abundant structural protein in mammals and is crucial for the mechanical integr...
Although collagens are the most abundant proteins implicated in various disease pathways, essential ...
Background: Collagen is a structural protein that provides mechanical stability and defined architec...
HSP47 (heat shock protein 47) is a collagen-specific molecular chaperone that is essential for proco...
This project involves the study of heat shock protein 47 (HSP47), which is a molecular chaperone cru...
Abstract: HSP47 (Heat Shock Protein 47) is a collagen-specific molecular chaperone that is essential...
HSP47 (heat shock protein 47) is a collagen-specific molecular chaperone that is essential for proco...
AbstractCollagen biosynthesis involves a complex series of post-translational modifications, control...
Heat shock protein 47 kDa (HSP47), an ER-resident and collagen-specific molecular chaperone, recogni...
Collagen is the most abundant protein in mammals and is the main protein of connective tissue in ani...
HSP47 is a molecular chaperone that plays an unknown role during the assembly and transport of proco...
Heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that helps the molecular ma...
Heat shock protein 47 (HSP47), encoded by the SERPINH1 gene, is a molecular chaperone essential for ...
HSP47 is a stress protein (heat shock protein) which resides in the endoplasmic reticulum, and is po...
Hsp47 is a chaperone protein with a fundamental role in the folding, stability and intracellular tra...
Collagen is the most abundant structural protein in mammals and is crucial for the mechanical integr...
Although collagens are the most abundant proteins implicated in various disease pathways, essential ...
Background: Collagen is a structural protein that provides mechanical stability and defined architec...
HSP47 (heat shock protein 47) is a collagen-specific molecular chaperone that is essential for proco...
This project involves the study of heat shock protein 47 (HSP47), which is a molecular chaperone cru...
Abstract: HSP47 (Heat Shock Protein 47) is a collagen-specific molecular chaperone that is essential...
HSP47 (heat shock protein 47) is a collagen-specific molecular chaperone that is essential for proco...
AbstractCollagen biosynthesis involves a complex series of post-translational modifications, control...
Heat shock protein 47 kDa (HSP47), an ER-resident and collagen-specific molecular chaperone, recogni...
Collagen is the most abundant protein in mammals and is the main protein of connective tissue in ani...
HSP47 is a molecular chaperone that plays an unknown role during the assembly and transport of proco...
Heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that helps the molecular ma...
Heat shock protein 47 (HSP47), encoded by the SERPINH1 gene, is a molecular chaperone essential for ...
HSP47 is a stress protein (heat shock protein) which resides in the endoplasmic reticulum, and is po...