<p>The end of TB1, the unique region, and the EGF4 domain found characteristically in mammalian fibrillins are indicated on the bottom. For invertebrate organisms, the cbEGF-like (purple box), and the new cbEGF domain (orange box) are highlighted, and cysteine residues are circled in red in these domains. The relative numbers of the cysteine residues within the respective EGF domain is indicated on top. Note that the unique region does not exist in invertebrate fibrillin proteins, and is instead replaced by a cbEGF-like domain. The non-calcium binding EGF4 domain that typically follows the unique region is replaced in invertebrate fibrillins by a cbEGF domain.</p
Clustal omega alignment of (A) Human and P. furiosus PCNAs (B) P. furiosus PCNA and K. gabonensis be...
Fibrillin-1 is a mosaic protein mainly composed of 43 calcium binding epidermal growth factor-like (...
Fibrillin-1 is a mosaic protein mainly composed of 43 calcium binding epidermal growth factor-like (...
Abstract Fibrillins are large extracellular glycoproteins that form the principal component of micro...
glycoproteins that form 10–12 nm diameter microfibrils in connective tissues. They are found in the ...
<p>Relative numbering of the cysteine residues in the hybrid 2 domain as identified in human fibrill...
Fibrillins are modular, disulphide-rich glycoproteins that assemble into microfibrils in the extrace...
Nsus sequence was boxed with black in the alignment. The PHD secondary structure is shown above the ...
<div><p>Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and non-...
Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and non-elastic ...
Fibrillin-1 is a large extracellular matrix glycoprotein and the major constituent of fibrillin-rich...
<p>Only the relevant loop containing the RGD sequence is shown. RGD sequences are highlighted by a b...
The fibrillins and latent transforming growth factor-beta binding proteins (LTBPs) form a superfamil...
Jensen et al. report the crystal structure of a human fibrillin-1 hybrid domain in this issue of Str...
SummaryThe fibrillins and latent transforming growth factor-β binding proteins (LTBPs) form a superf...
Clustal omega alignment of (A) Human and P. furiosus PCNAs (B) P. furiosus PCNA and K. gabonensis be...
Fibrillin-1 is a mosaic protein mainly composed of 43 calcium binding epidermal growth factor-like (...
Fibrillin-1 is a mosaic protein mainly composed of 43 calcium binding epidermal growth factor-like (...
Abstract Fibrillins are large extracellular glycoproteins that form the principal component of micro...
glycoproteins that form 10–12 nm diameter microfibrils in connective tissues. They are found in the ...
<p>Relative numbering of the cysteine residues in the hybrid 2 domain as identified in human fibrill...
Fibrillins are modular, disulphide-rich glycoproteins that assemble into microfibrils in the extrace...
Nsus sequence was boxed with black in the alignment. The PHD secondary structure is shown above the ...
<div><p>Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and non-...
Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and non-elastic ...
Fibrillin-1 is a large extracellular matrix glycoprotein and the major constituent of fibrillin-rich...
<p>Only the relevant loop containing the RGD sequence is shown. RGD sequences are highlighted by a b...
The fibrillins and latent transforming growth factor-beta binding proteins (LTBPs) form a superfamil...
Jensen et al. report the crystal structure of a human fibrillin-1 hybrid domain in this issue of Str...
SummaryThe fibrillins and latent transforming growth factor-β binding proteins (LTBPs) form a superf...
Clustal omega alignment of (A) Human and P. furiosus PCNAs (B) P. furiosus PCNA and K. gabonensis be...
Fibrillin-1 is a mosaic protein mainly composed of 43 calcium binding epidermal growth factor-like (...
Fibrillin-1 is a mosaic protein mainly composed of 43 calcium binding epidermal growth factor-like (...