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Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B

Overview of attention for article published in Nature Structural & Molecular Biology, November 2008
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Title
Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B
Published in
Nature Structural & Molecular Biology, November 2008
DOI 10.1038/nsmb.1512
Pubmed ID
Authors

Dong Yang, Neggy Rismanchi, Benoît Renvoisé, Jennifer Lippincott-Schwartz, Craig Blackstone, James H Hurley

Abstract

The endosomal sorting complex required for transport (ESCRT) machinery, including ESCRT-III, localizes to the midbody and participates in the membrane-abscission step of cytokinesis. The ESCRT-III protein charged multivesicular body protein 1B (CHMP1B) is required for recruitment of the MIT domain-containing protein spastin, a microtubule-severing enzyme, to the midbody. The 2.5-A structure of the C-terminal tail of CHMP1B with the MIT domain of spastin reveals a specific, high-affinity complex involving a noncanonical binding site between the first and third helices of the MIT domain. The structural interface is twice as large as that of the MIT domain of the VPS4-CHMP complex, consistent with the high affinity of the interaction. A series of unique hydrogen-bonding interactions and close packing of small side chains discriminate against the other ten human ESCRT-III subunits. Point mutants in the CHMP1B binding site of spastin block recruitment of spastin to the midbody and impair cytokinesis.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 174 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 4 2%
France 2 1%
Portugal 1 <1%
United Kingdom 1 <1%
Switzerland 1 <1%
Japan 1 <1%
Canada 1 <1%
Unknown 163 94%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 48 28%
Researcher 37 21%
Student > Master 17 10%
Student > Bachelor 14 8%
Student > Doctoral Student 12 7%
Other 23 13%
Unknown 23 13%
Readers by discipline Count As %
Agricultural and Biological Sciences 81 47%
Biochemistry, Genetics and Molecular Biology 45 26%
Neuroscience 7 4%
Immunology and Microbiology 5 3%
Chemistry 4 2%
Other 9 5%
Unknown 23 13%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. 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 02 January 2009.
All research outputs
#17,285,036
of 25,371,288 outputs
Outputs from Nature Structural & Molecular Biology
#3,615
of 4,186 outputs
Outputs of similar age
#89,383
of 104,427 outputs
Outputs of similar age from Nature Structural & Molecular Biology
#21
of 30 outputs
Altmetric has tracked 25,371,288 research outputs across all sources so far. This one is in the 21st percentile – i.e., 21% of other outputs scored the same or lower than it.
So far Altmetric has tracked 4,186 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 15.5. This one is in the 6th percentile – i.e., 6% of its peers scored the same or lower than it.
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 104,427 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 8th percentile – i.e., 8% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 30 others from the same source and published within six weeks on either side of this one. This one is in the 6th percentile – i.e., 6% of its contemporaries scored the same or lower than it.