Evidence map›Paper›PMID 39339186›Full record

ArticlePharmaceutics2024

An Innovative Inhibitor with a New Chemical Moiety Aimed at Biliverdin IXβ Reductase for Thrombocytopenia and Resilient against Cellular Degradation.

Hoe-Myung Jung, Jung-Hye Ha, Mark Vincent C Dela Cerna, Joseph A Burlison, Joonhyeok Choi, Bo-Ram Kim, Jeong Kyu Bang, Kyoung-Seok Ryu, Donghan Lee

Abstract read
In one paragraph

Article in Pharmaceutics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Hoe-Myung JungKorea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si 28119, Republic of Korea.
Jung-Hye HaNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation (DGMIF), 80 Cheombok-ro, Dong-gu, Daegu 41061, Republic of Korea.
Mark Vincent C Dela CernaDepartment of Biochemistry, Chemistry and Physics, Georgia Southern University, 11935 Abercorn Street, Savannah, GA 31419, USA.ORCID 0000-0001-5995-4667
Joseph A BurlisonDepartment of Medicine, James Graham Brown Cancer Center, University of Louisville, 505 S. Hancock St., Louisville, KY 40202, USA.
Joonhyeok ChoiKorea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si 28119, Republic of Korea.ORCID 0000-0002-3800-0394
Bo-Ram KimKorea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si 28119, Republic of Korea.
Jeong Kyu BangKorea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si 28119, Republic of Korea.ORCID 0000-0001-5916-0912
Kyoung-Seok RyuKorea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si 28119, Republic of Korea.
Donghan LeeKorea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si 28119, Republic of Korea.

Funding

Korea Basic Science Institute A439112Korea Basic Science Institute C030130Korea Basic Science Institute C130000Korea Basic Science Institute C140130Korea Basic Science Institute T39632
6 · The paper itself

Abstract

Biliverdin IXβ reductase (BLVRB) has emerged as a promising therapeutic target for thrombocytopenia due to its involvement in reactive oxygen species (ROS) mechanisms. During the pursuit of inhibitors targeting BLVRB, olsalazine (OSA) became apparent as one of the most potent candidates. However, the direct application of OSA as a BLVRB inhibitor faces challenges, as it is prone to degradation into 5-aminosalicylic acid through cleavage of the diazenyl bond by abundant azoreductase (AzoR) enzymes in gut microbiota and eukaryotic cells. To overcome this obstacle, we devised olsalkene (OSK), an inhibitor where the diazenyl bond in OSA has been substituted with an alkene bond. OSK not only matches the efficacy of OSA but also demonstrates improved stability against degradation by AzoR, presenting a promising solution to this limitation. Furthermore, we have found that both OSK and OSA inhibit BLVRB, regardless of the presence of nicotinamide adenine dinucleotide phosphate, unlike other known inhibitors. This discovery opens new avenues for investigating the roles of BLVRB in blood disorders, including thrombocytopenia.

Indexed as

azoreductase-resistant inhibitorbiliverdin IXβ reductase-inhibitor complex structureNMR spectroscopythrombocytopeniaX-ray crystallography

Identifiers

PMID39339186
PMCPMC11435328

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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.