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Mendeley readers
Chapter title |
Cloning, Expression, and Purification of the Glycosylated Transmembrane Protein, Cation-Dependent Mannose 6-Phosphate Receptor, from Sf9 Cells Using the Baculovirus System
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Chapter number | 7 |
Book title |
The Surfaceome
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Published in |
Methods in molecular biology, January 2018
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DOI | 10.1007/978-1-4939-7553-2_7 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7551-8, 978-1-4939-7553-2
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Authors |
Linda J. Olson, Nancy M. Dahms |
Abstract |
The cation-dependent mannose 6-phosphate receptor (CD-MPR) is a single-pass type I membrane protein. This protein functions to transport lysosomal enzymes displaying phosphomannosyl residues from the Golgi complex and the cell surface to the lysosome. This glycosylated protein contains three disulfide bridges in its 159-residue extracytoplasmic domain. One of the problems with studying eukaryotic membrane proteins is isolating sufficient quantities. Structural studies typically require several hundred milligrams of highly purified protein. Here we present a method to isolate milligram quantities of CD-MPR/Asn81 suitable for structural studies. |
Mendeley readers
The data shown below were compiled from readership statistics for 6 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 6 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 2 | 33% |
Professor | 1 | 17% |
Student > Ph. D. Student | 1 | 17% |
Student > Postgraduate | 1 | 17% |
Student > Master | 1 | 17% |
Other | 0 | 0% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 5 | 83% |
Chemistry | 1 | 17% |