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| Untersuchte Arbeit: Seite: 17, Zeilen: 17-17 |
Quelle: Fukunaga et al 1991 Seite(n): 2862, Zeilen: figure |
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B: Schematic representation of the homo- and hetero-dimeric structures of functional receptors for IL-6, G-CSF, GM-CSF and IL-2. The CRH domains containing the conserved cysteine residues (thin bars) and the WSXWS motif (thick bar) are indicated by shaded boxes. The gp130 (the β-chain of the IL-6 receptor) has a remarkable similarity to the G-CSFR. The numbers indicate the percentage of identical amino acids in each subdomain23. 23. Basu S, Hodgson G, Katz M, Dunn AR. Evaluation of role of G-CSF in the production, survival, and release of neutrophils from bone marrow into circulation. Blood. 2002;100:854-861. |
Datei:17b source.png
Fig. 8. Schematic representation of homo- and heterodimeric structures of functional, high affinity receptors for G-CSF, GM-CSF, IL-2 and IL-6. The CRH domains containing the conserved cysteine residues (thin bars) and the 'WSXWS' motif (thick bar) are indicated by shaded boxes. The gpl30 protein (the (-chain of the IL-6 receptor) shows remarkable homology with the G-CSF receptor except for a C-terminal part of the cytoplasmic domain. The numbers indicate the percentage of identical amino acids in each subdomain. |
The source is not given. None of the copied material can be found in Basu et al. (2002) |
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