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Characterization of RasGRP2, a Plasma Membrane-targeted, Dual Specificity Ras/Rap Exchange Factor*

Overview of attention for article published in Journal of Biological Chemistry, October 2000
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  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (86th percentile)
  • High Attention Score compared to outputs of the same age and source (86th percentile)

Mentioned by

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2 patents
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2 Wikipedia pages

Citations

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109 Dimensions

Readers on

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52 Mendeley
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Title
Characterization of RasGRP2, a Plasma Membrane-targeted, Dual Specificity Ras/Rap Exchange Factor*
Published in
Journal of Biological Chemistry, October 2000
DOI 10.1074/jbc.m006087200
Pubmed ID
Authors

Jodi Clyde-Smith, Gint Silins, Michael Gartside, Sean Grimmond, Maria Etheridge, Ann Apolloni, Nick Hayward, John F. Hancock

Abstract

Ras proteins operate as molecular switches in signal transduction pathways downstream of tyrosine kinases and G-protein-coupled receptors. Ras is switched from the inactive GDP-bound state to the active GTP-bound state by guanine nucleotide exchange factors (GEFs). We report here the cloning and characterization of RasGRP2, a longer alternatively spliced form of the recently cloned RapGEF, CalDAG-GEFI. A unique feature of RasGRP2 is that it is targeted to the plasma membrane by a combination of N-terminal myristoylation and palmitoylation. In vivo, RasGRP2 selectively catalyzes nucleotide exchange on N- and Ki-Ras, but not Ha-Ras. RasGRP2 also catalyzes nucleotide exchange on Rap1, but this RapGEF activity is less potent than that associated with CalDAG-GEFI. The nucleotide exchange activity of RasGRP2 toward N-Ras is stimulated by diacylglycerol and inhibited by calcium. The effects of diacylglycerol and calcium are additive but are not accompanied by any detectable change in the subcellular localization of RasGRP2. In contrast, CalDAG-GEFI is localized predominantly to the cytosol and lacks Ras exchange activity in vivo. However, prolonged exposure to phorbol esters, or growth in serum, results in localization of CalDAG-GEFI to the cell membrane and restoration of Ras exchange activity. Expression of RasGRP2 or CalDAG-GEFI in NIH3T3 cells transfected with wild type N-Ras results in an accelerated growth rate but not morphologic transformation. Thus, under appropriate growth conditions, CalDAG-GEFI and RasGRP2 are dual specificity Ras and Rap exchange factors.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 52 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 2%
Unknown 51 98%

Demographic breakdown

Readers by professional status Count As %
Researcher 17 33%
Student > Ph. D. Student 13 25%
Professor 5 10%
Student > Master 5 10%
Student > Doctoral Student 2 4%
Other 5 10%
Unknown 5 10%
Readers by discipline Count As %
Agricultural and Biological Sciences 25 48%
Biochemistry, Genetics and Molecular Biology 13 25%
Medicine and Dentistry 4 8%
Neuroscience 2 4%
Pharmacology, Toxicology and Pharmaceutical Science 1 2%
Other 2 4%
Unknown 5 10%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 9. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 July 2018.
All research outputs
#3,798,945
of 25,374,647 outputs
Outputs from Journal of Biological Chemistry
#6,156
of 85,241 outputs
Outputs of similar age
#3,622
of 38,859 outputs
Outputs of similar age from Journal of Biological Chemistry
#50
of 1,016 outputs
Altmetric has tracked 25,374,647 research outputs across all sources so far. Compared to these this one has done well and is in the 83rd percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 85,241 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.1. This one has done well, scoring higher than 86% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 38,859 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 86% of its contemporaries.
We're also able to compare this research output to 1,016 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 86% of its contemporaries.