Evidence map›Paper›PMID 24389582›Full record

ArticleNature communications2014

The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein.

Jungwon Hwang, Hyun-Woo Suh, Young Ho Jeon, Eunha Hwang, Loi T Nguyen, Jeonghun Yeom, Seung-Goo Lee, Cheolju Lee, Kyung Jin Kim, Beom Sik Kang and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

88 citing papers in PubMed, 187 citations in OpenAlex.

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  16. The desert woodrat (Neotoma lepida) induces a diversity of biotransformation genes in response to creosote bush resin.Comparative biochemistry and physiology. Toxicology & pharmacology : CBP · 2024
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28 more citing papers are in PubMed but not listed here.

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

15 authors at 8 institutions in 1 country.

Jungwon Hwang1] Department of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea [2] Infection and Immunity Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Hyun-Woo SuhImmunotherapy Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Young Ho JeonCollege of Pharmacy, Korea University, Sejong 339-700, Korea.
Eunha HwangDivision of Magnetic Resonance, Korea Basic Science Institute, Ochang, Chungbuk 363-883, Korea.
Loi T NguyenInfection and Immunity Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Jeonghun Yeom1] BRI, Korea Institute of Science and Technology, Seoul 136-791, Korea [2] Department of Biological Chemistry, University of Science and Technology, Daejeon 305-333, Korea.
Seung-Goo LeeBiochemicals and Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Cheolju Lee1] BRI, Korea Institute of Science and Technology, Seoul 136-791, Korea [2] Department of Biological Chemistry, University of Science and Technology, Daejeon 305-333, Korea.
Kyung Jin KimSchool of Life Science and Biotechnology, Kyungpook National University, Daegu 702-701, Korea.
Beom Sik KangSchool of Life Science and Biotechnology, Kyungpook National University, Daegu 702-701, Korea.
Jin-Ok JeongDivision of Cardiology, Department of Internal Medicine, Chungnam National University School of Medicine, Daejeon 301-721, Korea.
Tae-Kwang OhInfection and Immunity Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Inpyo ChoiImmunotherapy Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Jie-Oh LeeDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Myung Hee Kim1] Infection and Immunity Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea [2] Biosystems and Bioengineering Program, University of Science and Technology, Daejeon 305-333, Korea.
Korea Research Institute of Bioscience and Biotechnology · KRKorea Advanced Institute of Science and Technology · KRKorea Institute of Science and Technology · KRKyungpook National University · KRChungnam National University · KRKorea Basic Science Institute · KRKorea University · KRKorea University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The redox-dependent inhibition of thioredoxin (TRX) by thioredoxin-interacting protein (TXNIP) plays a pivotal role in various cancers and metabolic syndromes. However, the molecular mechanism of this regulation is largely unknown. Here, we present the crystal structure of the TRX-TXNIP complex and demonstrate that the inhibition of TRX by TXNIP is mediated by an intermolecular disulphide interaction resulting from a novel disulphide bond-switching mechanism. Upon binding to TRX, TXNIP undergoes a structural rearrangement that involves switching of a head-to-tail interprotomer Cys63-Cys247 disulphide between TXNIP molecules to an interdomain Cys63-Cys190 disulphide, and the formation of a de novo intermolecular TXNIP Cys247-TRX Cys32 disulphide. This disulphide-switching event unexpectedly results in a domain arrangement of TXNIP that is entirely different from those of other arrestin family proteins. We further show that the intermolecular disulphide bond between TRX and TXNIP dissociates in the presence of high concentrations of reactive oxygen species. This study provides insight into TRX and TXNIP-dependent cellular regulation.

Indexed as

Oxidation-ReductionReactive Oxygen SpeciesCarrier ProteinsCrystallography, X-RayDisulfidesHumansModels, MolecularProtein Structure, TertiaryThioredoxinsCarrier ProteinsDisulfidesReactive Oxygen SpeciesThioredoxinsTXNIP protein, humanTXN protein, human

Identifiers

PMID24389582
PMCPMC3941024
OpenAlexW1993760584

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.