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Comment
. 2006 Dec;169(6):1910-2.
doi: 10.2353/ajpath.2006.060923.

Zebrafish as a novel model system to study the function of caveolae and caveolin-1 in organismal biology

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Comment

Zebrafish as a novel model system to study the function of caveolae and caveolin-1 in organismal biology

Philippe G Frank et al. Am J Pathol. 2006 Dec.
No abstract available

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Figures

Figure 1
Figure 1
Evolutionary conservation of the caveolin-1 (Cav-1) protein. Alignment of the Cav-1 protein sequences from C. elegans (accession no. Q94051), D. rerio (accession no. Q6YLH9), and Homo sapiens (accession no. Q2TNI1) was produced using CINEMA. Note that the β-isoform uses an internal methionine (M32 in humans; M34 in zebrafish) as an initiation codon, as indicated (α versus β). As such, only the α-isoform undergoes tyrosine phosphorylation [Y14 in humans and zebrafish; see asterisk], since the β-isoform lacks tyrosine 14. The positions of the caveolin-signature-sequence (SQ) and the caveolin-scaffolding-domain (CSD) are highlighted. Palmitoylated cysteine residues have been boxed, in the case of the human and zebrafish sequences. Color coding is as follows: white, hydrophobic residues; blue, positively charged residues; red, negatively charged residues; green, small hydrogen bonding residues; brown, glycine/proline residues; yellow, cysteine residues; and cyan, aromatic residues.

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