Evidence map›Paper›PMID 28631011›Full record

ReviewAmino acids2017

Isoprenyl carboxyl methyltransferase inhibitors: a brief review including recent patents.

Woo Seok Yang, Seung-Gu Yeo, Sungjae Yang, Kyung-Hee Kim, Byong Chul Yoo, Jae Youl Cho

Open access · hybridAbstract readReview
In one paragraph

Review in Amino acids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Current computer-aided drug design · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Ras and exosome signaling.Seminars in cancer biology · 2019
    Review
  15. Review
  16. 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

6 authors at 3 institutions in 1 country.

Woo Seok YangDepartment of Genetic Engineering, Sungkyunkwan University, 2066 Seobu-ro, Jang-gu, Suwon, 16419, Republic of Korea.
Seung-Gu YeoDepartment of Radiation Oncology, Soonchunhyang University College of Medicine, Soonchunhyang University Hospital, Cheonan, 31151, Republic of Korea.
Sungjae YangDepartment of Genetic Engineering, Sungkyunkwan University, 2066 Seobu-ro, Jang-gu, Suwon, 16419, Republic of Korea.
Kyung-Hee KimBiomarker Branch, Research Institute, National Cancer Center, Goyang, 10408, Republic of Korea.
Byong Chul YooBiomarker Branch, Research Institute, National Cancer Center, Goyang, 10408, Republic of Korea. yoo_akh@ncc.re.kr.
Jae Youl ChoDepartment of Genetic Engineering, Sungkyunkwan University, 2066 Seobu-ro, Jang-gu, Suwon, 16419, Republic of Korea. jaecho@skku.edu.
Sungkyunkwan University · KRNational Cancer Center · KRSoonchunhyang University Hospital · KR

Funding

The National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and future Planning 1731210-1
6 · The paper itself

Abstract

Among the enzymes involved in the post-translational modification of Ras, isoprenyl carboxyl methyltransferase (ICMT) has been explored by a number of researchers as a significant enzyme controlling the activation of Ras. Indeed, inhibition of ICMT exhibited promising anti-cancer activity against various cancer cell lines. This paper reviews patents and research articles published between 2009 and 2016 that reported inhibitors of ICMT as potential chemotherapeutic agents targeting Ras-induced growth factor signaling. Since ICMT inhibitors can modulate Ras signaling pathway, it might be possible to develop a new class of anti-cancer drugs targeting Ras-related cancers. Researchers have discovered indole-based small-molecular ICMT inhibitors through high-throughput screening. Researchers at Duke University identified a prototypical inhibitor, cysmethynil. At Singapore University, Ramanujulu and his colleagues patented more potent compounds by optimizing cysmethynil. In addition, Rodriguez and Stevenson at Universidad Complutense De Madrid and Cancer Therapeutics CRC PTY Ltd., respectively, have developed inhibitors based on formulas other than the indole base. However, further optimization of chemicals targeted to functional groups is needed to improve the characteristics of ICMT inhibitors related to their application as drugs, such as solubility, effectiveness, and safety, to facilitate clinical use.

Indexed as

Gene Expression Regulation, NeoplasticProtein Processing, Post-TranslationalAnimalsAntineoplastic AgentsDrug DesignEnzyme InhibitorsHumansIndolesIntercellular Signaling Peptides and ProteinsNeoplasmsPatents as TopicProtein Methyltransferasesras ProteinsSignal TransductionStructure-Activity RelationshipAntineoplastic AgentscysmethynilEnzyme InhibitorsIndolesIntercellular Signaling Peptides and ProteinsProtein Methyltransferasesprotein-S-isoprenylcysteine O-methyltransferaseras ProteinsCancerCysmethynilICMT inhibitorMethylationRas

Identifiers

PMID28631011
PMCPMC5561173
OpenAlexW2629359470

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.