Evidence map›Paper›PMID 40070060›Full record

ReviewCurrent protein & peptide science2025

Inhibitors of Type II NADH Dehydrogenase Enzyme: A Review.

Guangzhou Sun, Quanshan Shi, Yuting Song, Lingkai Tang, Siyao Li, Tiantian Yang, Kaixuan Hu, Liang Ma, Xiaodong Shi, Jianping Hu

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current protein & peptide science, 2025. 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

10 authors.

Guangzhou SunKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Quanshan ShiKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Yuting SongLaboratory of Tumor Targeted and Immune Therapy, Clinical Research Center for Breast, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center for Biotherapy, Chengdu, China.
Lingkai TangKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Siyao LiKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Tiantian YangKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Kaixuan HuKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Liang MaKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Xiaodong ShiKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.
Jianping HuKey Laboratory of Medicinal and Edible Plants Resources Development of Sichuan Education Department, School of Pharmacy, Chengdu University, Chengdu, 610106, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are organelles in eukaryotic organisms with an electron transport chain consisting of four complexes (i.e., CI, CII, CIII, and CIV) on the inner membrane, which have functions such as providing energy, electron transport, and generating proton gradients. NADH dehydrogenase type 2 (NDH-2), widely found in bacterial, plant, fungal and protist mitochondria, is a nonproton-pumping single-subunit enzyme bound to the surface of the inner mitochondrial membrane that partially replaces NDH-1. NDH-2 has a crucial role in the energy metabolism of pathogenic microorganisms, and the lack of NDH-2 or its homologs in humans makes NDH-2 an essential target for the development of antimicrobial drugs. There is a wide variety of pathogenic microorganisms that invade the human body and cause diseases; therefore, more and more inhibitors targeting NDH-2 of different pathogenic microorganisms continue to be reported. This paper first reviews the structure and function of NDH-2 and summarizes the classification of compounds targeting NDH-2. Given the relative paucity of inhibition mechanisms for NDH-2, which has greatly hindered the development of targeted drugs, the article concludes with a summary of two possible mechanisms in action: allosteric inhibition and competitive inhibition. This review will provide theoretical support for the subsequent molecular design and modification of drugs targeting the pathogenic microorganism NDH-2.

Indexed as

Enzyme InhibitorsNADH DehydrogenaseAllosteric RegulationAnimalsHumansMitochondriaEnzyme InhibitorsNADH DehydrogenaseNADH dehydrogenase IIinhibition mechanisminhibitorMitochondriamolecular designNDH-2pathogenic microorganisms.

Identifiers

What Socratic 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 Socratic graph.