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Structure of the toxic core of α-synuclein from invisible crystals.

Overview of attention for article published in Nature, September 2015
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About this Attention Score

  • In the top 5% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (97th percentile)
  • Above-average Attention Score compared to outputs of the same age and source (51st percentile)

Citations

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174 Dimensions

Readers on

mendeley
411 Mendeley
citeulike
4 CiteULike
Title
Structure of the toxic core of α-synuclein from invisible crystals.
Published in
Nature, September 2015
DOI 10.1038/nature15368
Pubmed ID
Authors

Jose A. Rodriguez, Magdalena I. Ivanova, Michael R. Sawaya, Duilio Cascio, Francis E. Reyes, Dan Shi, Smriti Sangwan, Elizabeth L. Guenther, Lisa M. Johnson, Meng Zhang, Lin Jiang, Mark A. Arbing, Brent L. Nannenga, Johan Hattne, Julian Whitelegge, Aaron S. Brewster, Marc Messerschmidt, Sébastien Boutet, Nicholas K. Sauter, Tamir Gonen, David S. Eisenberg, Rodriguez, Jose A, Ivanova, Magdalena I, Sawaya, Michael R, Cascio, Duilio, Reyes, Francis E, Shi, Dan, Sangwan, Smriti, Guenther, Elizabeth L, Johnson, Lisa M, Zhang, Meng, Jiang, Lin, Arbing, Mark A, Nannenga, Brent L, Hattne, Johan, Whitelegge, Julian, Brewster, Aaron S, Messerschmidt, Marc, Boutet, Sébastien, Sauter, Nicholas K, Gonen, Tamir, Eisenberg, David S

Abstract

The protein α-synuclein is the main component of Lewy bodies, the neuron-associated aggregates seen in Parkinson disease and other neurodegenerative pathologies. An 11-residue segment, which we term NACore, appears to be responsible for amyloid formation and cytotoxicity of human α-synuclein. Here we describe crystals of NACore that have dimensions smaller than the wavelength of visible light and thus are invisible by optical microscopy. As the crystals are thousands of times too small for structure determination by synchrotron X-ray diffraction, we use micro-electron diffraction to determine the structure at atomic resolution. The 1.4 Å resolution structure demonstrates that this method can determine previously unknown protein structures and here yields, to our knowledge, the highest resolution achieved by any cryo-electron microscopy method to date. The structure exhibits protofibrils built of pairs of face-to-face β-sheets. X-ray fibre diffraction patterns show the similarity of NACore to toxic fibrils of full-length α-synuclein. The NACore structure, together with that of a second segment, inspires a model for most of the ordered portion of the toxic, full-length α-synuclein fibril, presenting opportunities for the design of inhibitors of α-synuclein fibrils.

Twitter Demographics

The data shown below were collected from the profiles of 51 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 411 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 10 2%
United Kingdom 6 1%
Denmark 1 <1%
Poland 1 <1%
France 1 <1%
Japan 1 <1%
China 1 <1%
Chile 1 <1%
Canada 1 <1%
Other 0 0%
Unknown 388 94%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 134 33%
Researcher 110 27%
Student > Master 35 9%
Student > Bachelor 30 7%
Student > Doctoral Student 22 5%
Other 80 19%
Readers by discipline Count As %
Agricultural and Biological Sciences 146 36%
Biochemistry, Genetics and Molecular Biology 99 24%
Chemistry 61 15%
Neuroscience 28 7%
Unspecified 27 7%
Other 50 12%

Attention Score in Context

This research output has an Altmetric Attention Score of 67. 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 15 March 2016.
All research outputs
#180,190
of 11,326,849 outputs
Outputs from Nature
#12,400
of 58,936 outputs
Outputs of similar age
#6,481
of 237,847 outputs
Outputs of similar age from Nature
#446
of 918 outputs
Altmetric has tracked 11,326,849 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 98th percentile: it's in the top 5% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 58,936 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 70.6. This one has done well, scoring higher than 78% 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 237,847 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 97% of its contemporaries.
We're also able to compare this research output to 918 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 51% of its contemporaries.