Identification of a cytoskeleton-associated glycoprotein from isolated microvilli of a mammary ascites tumor
Experimental Cell Research, ISSN: 0014-4827, Vol: 143, Issue: 2, Page: 303-308
1983
- 14Citations
- 3Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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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
- Citations14
- Citation Indexes14
- 14
- CrossRef11
- Captures3
- Readers3
Article Description
Microvilli isolated from MAT-C1 13762 ascites tumor cells were extracted with Triton X-100 in phosphate-buffered saline (PBS) to yield cytoskeletal residues. Analysis of the residues by two-dimensional isoelectric focusing-dodecyl sulfate electrophoresis and silver staining suggested that one of the major components is a glycoprotein (CAG). Neuraminidase treatments and glucosamine labeling demonstrated that CAG is a glycoprotein, and lactoperoxidase iodination showed its presence at the microvillar surface. DNase treatments and myosin affinity analysis suggested an association between CAG and the microvillar microfilaments. Thus, CAG has the properties expected of a transmembrane-linking molecule connecting the cell surface to the cytoskeleton.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0014482783900551; http://dx.doi.org/10.1016/0014-4827(83)90055-1; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0020586234&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/6682044; https://linkinghub.elsevier.com/retrieve/pii/0014482783900551; http://dx.doi.org/10.1016/0014-4827%2883%2990055-1; https://dx.doi.org/10.1016/0014-4827%2883%2990055-1
Elsevier BV
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