1999
DOI: 10.1210/edrv.20.6.0382
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The Insulin-Like Growth Factor-Binding Protein (IGFBP) Superfamily*

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Cited by 453 publications
(317 citation statements)
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References 203 publications
(284 reference statements)
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“…2 It can be seen from the CD results ( Fig. 2A) apparently significant differences in amplitude, the secondary structure estimates (given in Table I) are broadly similar, exhibiting a strong negative band with a minimum close to 200 nm in each case.…”
Section: Resultsmentioning
confidence: 64%
See 2 more Smart Citations
“…2 It can be seen from the CD results ( Fig. 2A) apparently significant differences in amplitude, the secondary structure estimates (given in Table I) are broadly similar, exhibiting a strong negative band with a minimum close to 200 nm in each case.…”
Section: Resultsmentioning
confidence: 64%
“…In turn, IGFs are regulated by a family of six IGF-binding proteins (IGFBPs) that form high affinity complexes with both IGF-I and IGF-II (reviewed in Ref. 2). Because the affinity constants of the IGFBPs are between 2-and 50-fold greater for binding IGFs than that of the IGF type 1 receptor, it is thought that the IGFBPs are able to regulate the bioavailability of IGFs in different biological fluids.…”
mentioning
confidence: 99%
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“…IGFBPs 1-6 are generally thought to consist of three structural domains of approximately equal length (4,5). All six IGFBPs are characterized by highly conserved cysteine-rich amino-and carboxyl-terminal domains, joined by a linker domain unique to each IGFBP species.…”
Section: Igfsmentioning
confidence: 99%
“…Although these fragments demonstrate IGF binding properties, there is a distinct loss of affinity, suggesting a requirement for additional components. Interestingly, IGFBPrelated proteins, which share sequence similarities with the amino-terminal domain of the high affinity IGFBPs, have also been reported to bind IGF-I, IGF-II, and insulin (4,(13)(14)(15).…”
Section: Igfsmentioning
confidence: 99%