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Expression, purification, crystallization, and preliminary X-ray crystallographic studies of the human adiponectin receptors, AdipoR1 and AdipoR2

Overview of attention for article published in Journal of Structural and Functional Genomics, January 2015
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About this Attention Score

  • Good Attention Score compared to outputs of the same age (74th percentile)

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9 tweeters

Citations

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35 Mendeley
Title
Expression, purification, crystallization, and preliminary X-ray crystallographic studies of the human adiponectin receptors, AdipoR1 and AdipoR2
Published in
Journal of Structural and Functional Genomics, January 2015
DOI 10.1007/s10969-014-9192-z
Pubmed ID
Authors

Hiroaki Tanabe, Kanna Motoyama, Mariko Ikeda, Motoaki Wakiyama, Takaho Terada, Noboru Ohsawa, Toshiaki Hosaka, Masakatsu Hato, Yoshifumi Fujii, Yoshihiro Nakamura, Satoshi Ogasawara, Tomoya Hino, Takeshi Murata, So Iwata, Miki Okada-Iwabu, Masato Iwabu, Kunio Hirata, Yoshiaki Kawano, Masaki Yamamoto, Tomomi Kimura-Someya, Mikako Shirouzu, Toshimasa Yamauchi, Takashi Kadowaki, Shigeyuki Yokoyama

Abstract

The adiponectin receptors (AdipoR1 and AdipoR2) are membrane proteins with seven transmembrane helices. These receptors regulate glucose and fatty acid metabolism, thereby ameliorating type 2 diabetes. The full-length human AdipoR1 and a series of N-terminally truncated mutants of human AdipoR1 and AdipoR2 were expressed in insect cells. In small-scale size exclusion chromatography, the truncated mutants AdipoR1Δ88 (residues 89-375) and AdipoR2Δ99 (residues 100-386) eluted mostly in the intact monodisperse state, while the others eluted primarily as aggregates. However, gel filtration chromatography of the large-scale preparation of the tag-affinity-purified AdipoR1Δ88 revealed the presence of an excessive amount of the aggregated state over the intact state. Since aggregation due to contaminating nucleic acids may have occurred during the sample concentration step, anion-exchange column chromatography was performed immediately after affinity chromatography, to separate the intact AdipoR1Δ88 from the aggregating species. The separated intact AdipoR1Δ88 did not undergo further aggregation, and was successfully purified to homogeneity by gel filtration chromatography. The purified AdipoR1Δ88 and AdipoR2Δ99 proteins were characterized by thermostability assays with 7-diethylamino-3-(4-maleimidophenyl)-4-methyl coumarin, thin layer chromatography of bound lipids, and surface plasmon resonance analysis of ligand binding, demonstrating their structural integrities. The AdipoR1Δ88 and AdipoR2Δ99 proteins were crystallized with the anti-AdipoR1 monoclonal antibody Fv fragment, by the lipidic mesophase method. X-ray diffraction data sets were obtained at resolutions of 2.8 and 2.4 Å, respectively.

Twitter Demographics

The data shown below were collected from the profiles of 9 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 35 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Japan 1 3%
Bangladesh 1 3%
Unknown 33 94%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 10 29%
Researcher 8 23%
Student > Bachelor 4 11%
Student > Doctoral Student 3 9%
Student > Master 3 9%
Other 7 20%
Readers by discipline Count As %
Agricultural and Biological Sciences 19 54%
Unspecified 5 14%
Biochemistry, Genetics and Molecular Biology 4 11%
Chemistry 3 9%
Medicine and Dentistry 2 6%
Other 2 6%

Attention Score in Context

This research output has an Altmetric Attention Score of 4. 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 06 February 2016.
All research outputs
#3,087,747
of 12,321,253 outputs
Outputs from Journal of Structural and Functional Genomics
#17
of 94 outputs
Outputs of similar age
#66,066
of 267,055 outputs
Outputs of similar age from Journal of Structural and Functional Genomics
#1
of 1 outputs
Altmetric has tracked 12,321,253 research outputs across all sources so far. This one has received more attention than most of these and is in the 74th percentile.
So far Altmetric has tracked 94 research outputs from this source. They receive a mean Attention Score of 3.1. This one has done well, scoring higher than 81% 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 267,055 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 74% of its contemporaries.
We're also able to compare this research output to 1 others from the same source and published within six weeks on either side of this one. This one has scored higher than all of them