Evidence map›Paper›PMID 32421328›Full record

ArticleJournal of medicinal chemistry2020

Synthesis and Identification of a Novel Lead Targeting Survivin Dimerization for Proteasome-Dependent Degradation.

Robert Peery, Kwaku Kyei-Baffour, Zizheng Dong, Jianguo Liu, Pedro de Andrade Horn, Mingji Dai, Jing-Yuan Liu, Jian-Ting Zhang

Abstract read
In one paragraph

Article in Journal of medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Novel quinoxaline-based survivin degraders overcome docetaxel-resistance in castration-resistant prostate cancer.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2026
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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

8 authors.

Robert PeeryDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana 46202, United States.
Kwaku Kyei-BaffourDepartment of Chemistry and Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, United States.
Zizheng DongDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana 46202, United States.
Jianguo LiuDepartment of Cancer Biology, University of Toledo College of Medicine and Life Sciences, Toledo, Ohio 43614, United States.
Pedro de Andrade HornDepartment of Chemistry and Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, United States.
Mingji DaiDepartment of Chemistry and Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, United States.ORCID 0000-0001-7956-6426
Jing-Yuan LiuDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana 46202, United States.
Jian-Ting ZhangDepartment of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, Indiana 46202, United States.ORCID 0000-0002-2803-9914

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
Synthesis and Study of Medicinally Important MoleculesR35GM128570 · NIGMS · PURDUE UNIVERSITY · PI Mingji Dai · 2018 to 2026
$3.7M
Effective targeting survivin dimerization interface with small molecule inhibitorsR01GM127656 · NIGMS · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI LIU, JASMINE JINGYUAN · 2018 to 2023
$1.7M
NCI NIH HHS P30 CA023168NIGMS NIH HHS R01 GM127656NIGMS NIH HHS R35 GM128570
6 · The paper itself

Abstract

Survivin, a homodimeric member of the Inhibitor of Apoptosis Protein (IAP) family, is required for cancer cell survival and overexpressed in almost all solid tumors. However, targeting survivin has been challenging due to its "undruggable" nature. Recently, we used a novel approach to target the dimerization interface and identified inhibitors of two scaffolds that can directly bind to and inhibit survivin dimerization. One of the scaffolds, represented by the compound LQZ-7, contains an undesirable labile hydrazone linker and a potentially nonfunctional furazanopyrazine ring that we attempted to eliminate in this study. We found one compound,

Indexed as

Administration, OralAnimalsAntineoplastic AgentsCell SurvivalDose-Response Relationship, DrugDrug DesignHumansHydrazonesMaleMicePC-3 CellsProteasome Endopeptidase ComplexProtein MultimerizationSurvivinXenograft Model Antitumor AssaysAntineoplastic AgentsBIRC5 protein, humanHydrazonesProteasome Endopeptidase ComplexSurvivin

Identifiers

PMID32421328
PMCPMC8216492

What OpenQuestion holds

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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.