Fibronectin consists of a series of three internal homology repeats (types I, II, and III [(1983) Proc. Natl. Acad. Sci. USA 80, 137-141]). The type III units are each coded for by two exons with the exception of the alternatively spliced extra domain type III [(1984) EMBO J. 3, 2511-2516]. To investigate the gene organisation of the type I and II repeats, genomic clones covering the collagen-binding domain of human fibronectin have been isolated and characterised. The results show that each of the type I and II homology units in this region corresponds to an exon. Taken together with the previous data concerning the type III units, the data lend support to a gene fusion model of fibronectin evolution
Type XIX collagen is a newly discovered member of rikko, 1993; Inoguchi et al., 1995). The collagen ...
AbstractAnalysis of the structure of the 3′-end of the human α2(IV) gene demonstrated that the α1(IV...
A) Binding site of FnbpB primers used in this study showed variation in the length of C-terminal fib...
AbstractFibronectin consists of a series of three internal homology repeats (types I, II, and III [(...
Type III homologies of human fibronectin are generally encoded by two exons, with the exception of t...
AbstractWe have sequenced that area of a human fibronectin gene clone which codes for a connecting s...
Type I collagen is the fundamental component of the extracellular matrix. Its α1 gene is the direct ...
Recombinant fibronectin (FN) fragments and their mutant proteins were produced to elucidate the role...
The nucleotide sequence of the human procollagen α1(II) collagen gene extending from within the firs...
The collagen-binding domain of human fibronectin has been expressed as a cro/beta-galactosidase fusi...
AbstractWe have determined the 2.0 Å crystal structure of a fragment of human fibronectin encompassi...
Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abunda...
AbstractThe fibronectin monomer is comprised of three types of homologous repeating units, the types...
Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abunda...
Fibronectin is an extracellular multidomain glycoprotein that directs and regulates a variety of cel...
Type XIX collagen is a newly discovered member of rikko, 1993; Inoguchi et al., 1995). The collagen ...
AbstractAnalysis of the structure of the 3′-end of the human α2(IV) gene demonstrated that the α1(IV...
A) Binding site of FnbpB primers used in this study showed variation in the length of C-terminal fib...
AbstractFibronectin consists of a series of three internal homology repeats (types I, II, and III [(...
Type III homologies of human fibronectin are generally encoded by two exons, with the exception of t...
AbstractWe have sequenced that area of a human fibronectin gene clone which codes for a connecting s...
Type I collagen is the fundamental component of the extracellular matrix. Its α1 gene is the direct ...
Recombinant fibronectin (FN) fragments and their mutant proteins were produced to elucidate the role...
The nucleotide sequence of the human procollagen α1(II) collagen gene extending from within the firs...
The collagen-binding domain of human fibronectin has been expressed as a cro/beta-galactosidase fusi...
AbstractWe have determined the 2.0 Å crystal structure of a fragment of human fibronectin encompassi...
Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abunda...
AbstractThe fibronectin monomer is comprised of three types of homologous repeating units, the types...
Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abunda...
Fibronectin is an extracellular multidomain glycoprotein that directs and regulates a variety of cel...
Type XIX collagen is a newly discovered member of rikko, 1993; Inoguchi et al., 1995). The collagen ...
AbstractAnalysis of the structure of the 3′-end of the human α2(IV) gene demonstrated that the α1(IV...
A) Binding site of FnbpB primers used in this study showed variation in the length of C-terminal fib...