Expression of an engineered form of recombinant procollagen in mouse milk
Nature Biotechnology, ISSN: 1087-0156, Vol: 17, Issue: 4, Page: 385-389
1999
- 87Citations
- 32Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations87
- Citation Indexes86
- 86
- CrossRef67
- Patent Family Citations1
- Patent Families1
- Captures32
- Readers32
- 32
Article Description
We have examined the suitability of the mouse mammary gland for expression of novel recombinant procollagens that can be used for biomedical applications. We generated transgenic mouse lines containing cDNA constructs encoding recombinant procollagen, along with the α and β subunits of prolyl 4-hydroxylase, an enzyme that modifies the collagen into a form that is stable at body temperature. The lines expressed relatively high levels (50- 200 μg/ml) of recombinant procollagen in milk. As engineered, the recombinant procollagen was shortened and consisted of a proα2(I) chain capable of forming a triple-helical homotrimer not normally found in nature. Analysis of the product demonstrated that (1) the proα chains formed disulphide-linked trimers, (2) the trimers contained a thermostable triple- helical domain, (3) the N-propeptides were aligned correctly, and (4) the expressed procollagen was not proteolytically processed to collagen in milk.
Bibliographic Details
Springer Science and Business Media LLC
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