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Results: 8

1.
Figure 3

Figure 3. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

Domain comparison of zebrafish β1 paralogs β1–1 and β1–2 with human β1 (% sequence identity). PSI, plexin/semaphorin/integrin; EGF, epidermal growth factor; βTD, β terminal domain; TM+ cyto, transmembrane and cytoplasmic domains.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.
2.
Figure 5

Figure 5. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

A. Domain comparison of zebrafish truncated β1 paralogs with human β1 (% sequence identity). B. Domain comparison of truncated β1 paralogs with β1–3 (% sequence identity). PSI, plexin/semaphorin/integrin; EGF, epidermal growth factor; βTD, β terminal domain; TM+ cyto, transmembrane and cytoplasmic domains. The sequence identities of the individual EGF repeats are shown in B.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.
3.
Figure 8

Figure 8. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

Expression profiling of zebrafish β1 paralogs in adult tissues. Expression of the different paralogs was analyzed by semiquantitative RT-PCR using primers designed against a portion of extracellular domains of the different paralogs. The amplification of zebrafish β-actin was monitored as a positive control. Br, brain; Fi, fin; Gi, gill; He, heart; In, intestine; Kd, kidney; Lv, liver; Mu, muscle; Sk, skin; Te, testis.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.
4.
Figure 1

Figure 1. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

Schematic diagram of the domain structure of integrin β subunits. Domain arrangement is based on crystal structures of the extracellular regions of α Vβ3 [13], α IIbβ3 [14] and β2 [15]. PSI, plexin/semaphorin/integrin; EGF, epidermal growth factor; TM, transmembrane. N-, amino terminus; C-, carboxyl terminus. Dotted line indicates the overall path of the polypeptide chain.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.
5.
Figure 6

Figure 6. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

Phylogenetic relationship of zebrafish (Dr) β1 integrin chains with representative deuterostome orthologs. Maximum Likelihood tree is shown with supporting Neighbor Joining bootstrap replicates (black), Maximum Parsimony bootstrap replicates (blue) and Bayesian clade credibility values (brown). Horizontal scale is amino acid replacements per site. Ciona intestinalis β1 (Ci_b1) was used to root the tree; homo sapiens β1 (Hs_b1) is shown as an example of tetrapod sequence.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.
6.
Figure 2

Figure 2. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

Alignment of zebrafish β1 sequences (β1–1, β1–2, β1–3, β1tr-1, β1tr-2 and β1tr-3) with human β1. The alignment was performed using ClustalW. Protein domains are annotated: PSI, plexin/semaphorin/integrin; EGF, epidermal growth factor; βTD, β terminal domain; TM transmembrane; cyto, cytoplasmic domain. MIDAS (M), ADMIDAS (A) and LIMBS (L) cation binding residues in the A domain are shown. Red underline indicates the position of the βB-βC loop, black underline indicates the position of the βD-α5 loop in the A domain. Sequence identities are indicated by *, conservative substitutions by :, semi-conservative substitutions by.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.
7.
Figure 7

Figure 7. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

Expression profiling of zebrafish β1 paralogs during development. Expression of the different paralogs at 2, 4, 6, 8, 12, 14, 24, 48, 56, 72 and 96 hpf (hours post fertilization) was analyzed by semiquantitative RT-PCR using primers designed against a portion of extracellular domains of the different paralogs. The amplification of zebrafish β-actin was monitored as a positive control.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.
8.
Figure 4

Figure 4. From: Identification of multiple integrin ?1 homologs in zebrafish (Danio rerio).

Alignment of zebrafish truncated β1 sequences. The alignment was performed using ClustalW. Protein domains are annotated: PSI, plexin/semaphorin/integrin; EGF, epidermal growth factor. Yellow bar indicates the position of a putative flexible linker region in EGF-2 [15]. Domain boundaries in the EGF repeats are as predicted by Takagi et al. [58]. Based on this prediction, the truncated β1 sequences contain four additional residues after the end of EGF-4. The position of an additional cysteine residue in EGF-4 (not seen in other β subunits) is indicated by tial. Sequence identities are indicated by *, conservative substitutions by :, semi-conservative substitutions by.

A Paul Mould, et al. BMC Cell Biol. 2006;7:24-24.

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