Evidence map›Paper›PMID 27043297›Full record

ArticleNature structural & molecular biology2016

Structural basis for specific inhibition of Autotaxin by a DNA aptamer.

Kazuki Kato, Hisako Ikeda, Shin Miyakawa, Satoshi Futakawa, Yosuke Nonaka, Masatoshi Fujiwara, Shinichi Okudaira, Kuniyuki Kano, Junken Aoki, Junko Morita and 4 more

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.4field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Structure-based investigation of a DNA aptamer targeting PTK7 reveals an intricate 3D fold guiding functional optimization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Review
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  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Aptamer Applications in Neuroscience.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 2 institutions in 1 country.

Kazuki KatoDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
Hisako IkedaRibomic Inc., Tokyo, Japan.
Shin MiyakawaRibomic Inc., Tokyo, Japan.
Satoshi FutakawaRibomic Inc., Tokyo, Japan.
Yosuke NonakaRibomic Inc., Tokyo, Japan.
Masatoshi FujiwaraRibomic Inc., Tokyo, Japan.
Shinichi OkudairaGraduate School of Pharmaceutical Sciences, Tohoku University, Miyagi, Japan.
Kuniyuki KanoGraduate School of Pharmaceutical Sciences, Tohoku University, Miyagi, Japan.
Junken AokiGraduate School of Pharmaceutical Sciences, Tohoku University, Miyagi, Japan.
Junko MoritaDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
Ryuichiro IshitaniDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
Hiroshi NishimasuDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
Yoshikazu NakamuraRibomic Inc., Tokyo, Japan.ORCID 0000-0001-8763-0424
Osamu NurekiDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
Tohoku University · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATX is a plasma lysophospholipase D that hydrolyzes lysophosphatidylcholine (LPC) and produces lysophosphatidic acid. To date, no ATX-inhibition-mediated treatment strategies for human diseases have been established. Here, we report anti-ATX DNA aptamers that inhibit ATX with high specificity and efficacy. We solved the crystal structure of ATX in complex with the anti-ATX aptamer RB011, at 2.0-Å resolution. RB011 binds in the vicinity of the active site through base-specific interactions, thus preventing the access of the choline moiety of LPC substrates. Using the structural information, we developed the modified anti-ATX DNA aptamer RB014, which exhibited in vivo efficacy in a bleomycin-induced pulmonary fibrosis mouse model. Our findings reveal the structural basis for the specific inhibition of ATX by the anti-ATX aptamer and highlight the therapeutic potential of anti-ATX aptamers for the treatment of human diseases, such as pulmonary fibrosis.

Indexed as

AnimalsAptamers, NucleotideBase SequenceBinding SitesCrystallography, X-RayHEK293 CellsHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsInverted Repeat SequencesLysophospholipase DMaleMice, Inbred C57BLModels, MolecularPhosphodiesterase InhibitorsPhosphoric Diester HydrolasesAptamers, NucleotideLysophospholipase DPhosphodiesterase InhibitorsPhosphoric Diester Hydrolases

Identifiers

PMID27043297
OpenAlexW2319911082

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.