Evidence map›Paper›PMID 24212136›Full record

ArticleNature chemical biology2014

Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction.

Dae Gyu Kim, Jin Young Lee, Nam Hoon Kwon, Pengfei Fang, Qian Zhang, Jing Wang, Nicolas L Young, Min Guo, Hye Young Cho, Ameeq Ul Mushtaq and 25 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemical biology, 2014. 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
3.3field-weighted citation impact, top 8% 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, 63 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Competitive Inhibition of Okanin againstInternational journal of molecular sciences · 2024
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Roles of Aminoacyl-tRNA Synthetases in Cancer.Frontiers in cell and developmental biology · 2020
    Review
  19. Aminoacyl-tRNA synthetases as therapeutic targets.Nature reviews. Drug discovery · 2019
    Review
  20. Review
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

35 authors at 11 institutions in 3 countries.

Dae Gyu Kim1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea. [3].
Jin Young Lee1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea. [3].
Nam Hoon Kwon1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Pengfei FangDepartment of Cancer Biology, The Scripps Research Institute, Scripps Florida, Jupiter, Florida, USA.
Qian ZhangDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida, USA.
Jing WangDepartment of Cancer Biology, The Scripps Research Institute, Scripps Florida, Jupiter, Florida, USA.
Nicolas L YoungIon Cyclotron Resonance Program, National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida, USA.
Min GuoDepartment of Cancer Biology, The Scripps Research Institute, Scripps Florida, Jupiter, Florida, USA.
Hye Young ChoCollege of Pharmacy, Korea University, Sejong, Korea.
Ameeq Ul MushtaqCollege of Pharmacy, Korea University, Sejong, Korea.
Young Ho JeonCollege of Pharmacy, Korea University, Sejong, Korea.
Jin Woo Choi1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Wellman Center for Photomedicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Jung Min Han1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Ho Woong KangYuhan Research Institute, Yongin, Korea.
Jae Eun JooYuhan Research Institute, Yongin, Korea.
Youn HurYuhan Research Institute, Yongin, Korea.
Wonyoung KangDepartment of Neurosurgery, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Korea.
Heekyoung YangDepartment of Neurosurgery, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Korea.
Do-Hyun NamDepartment of Neurosurgery, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Korea.
Mi-Sook LeeResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Jung Weon LeeResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Eun-Sook KimCollege of Pharmacy, Duksung Women's University, Seoul, Korea.
Aree MoonCollege of Pharmacy, Duksung Women's University, Seoul, Korea.
Kibom Kim1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Doyeun Kim1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Eun Joo KangMedicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea.
Youngji MoonMedicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea.
Kyung Hee RheeResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Byung Woo HanResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Jee Sun YangTranslational Research Center for Protein Function Control, Department of Biotechnology and WCU Department of Biomedical Sciences, Yonsei University, Seoul, Korea.
Gyoonhee HanTranslational Research Center for Protein Function Control, Department of Biotechnology and WCU Department of Biomedical Sciences, Yonsei University, Seoul, Korea.
Won Suk Yang1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Cheolju LeeBRI, Korea Institute of Science and Technology, Seoul, Korea.
Ming-Wei WangThe National Center for Drug Screening, Zhangjiang High-Tech Park, Shanghai, China.
Sunghoon Kim1] Medicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea. [2] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea. [3] World Class University Department of Molecular Medicine and Biopharmaceutical Sciences, Seoul National University, Seoul, Korea.
Seoul National University · KRKorea University · KRSamsung Medical Center · KRScripps Research Institute · USYuhan University · KRDuksung Women's University · KRYonsei University · KRFlorida State University · USKorea Institute of Science and Technology · KRNational Center for Drug Screening · CNNational High Magnetic Field Laboratory · US

Funding

Structural and Functional Studies of LysRS in Mast Cell ActivationR01GM100136 · NIGMS · SCRIPPS FLORIDA · PI KODADEK, THOMAS J. · 2012 to 2016
$1.9M
Development of Assays for Inhibitors of LysRS in Mast Cell ActivationR01GM106134 · NIGMS · SCRIPPS FLORIDA · PI GUO, MIN · 2013 to 2015
$1.1M
NIGMS NIH HHS GM100136NIGMS NIH HHS R01 GM100136NIGMS NIH HHS R01 GM106134
6 · The paper itself

Abstract

Lysyl-tRNA synthetase (KRS), a protein synthesis enzyme in the cytosol, relocates to the plasma membrane after a laminin signal and stabilizes a 67-kDa laminin receptor (67LR) that is implicated in cancer metastasis; however, its potential as an antimetastatic therapeutic target has not been explored. We found that the small compound BC-K-YH16899, which binds KRS, impinged on the interaction of KRS with 67LR and suppressed metastasis in three different mouse models. The compound inhibited the KRS-67LR interaction in two ways. First, it directly blocked the association between KRS and 67LR. Second, it suppressed the dynamic movement of the N-terminal extension of KRS and reduced membrane localization of KRS. However, it did not affect the catalytic activity of KRS. Our results suggest that specific modulation of a cancer-related KRS-67LR interaction may offer a way to control metastasis while avoiding the toxicities associated with inhibition of the normal functions of KRS.

Indexed as

Neoplasm MetastasisCell MembraneLysine-tRNA LigaseProtein TransportReceptors, LamininLysine-tRNA LigaseReceptors, Laminin

Identifiers

PMID24212136
PMCPMC4021855
OpenAlexW1965591024

What OpenQuestion holds

Textmetadata
LicenceTDM
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.