Evidence map›Paper›PMID 14517264›Full record

ArticleThe EMBO journal2003

Transglutaminase 2 inhibits Rb binding of human papillomavirus E7 by incorporating polyamine.

Ju-Hong Jeon, Kyung-Ho Choi, Sung-Yup Cho, Chai-Wan Kim, Dong-Myung Shin, Joon-Cheol Kwon, Kye-Yong Song, Sang-Chul Park, In-Gyu Kim

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 59 citations in OpenAlex.

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  14. Transglutaminase is a therapeutic target for oxidative stress, excitotoxicity and stroke: a new epigenetic kid on the CNS block.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2013
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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

9 authors at 1 institution in 1 country.

Ju-Hong JeonDepartment of Biochemistry and Molecular Biology/Aging and Apoptosis Research Center, Seoul National University College of Medicine, 28 Yongon Dong, Seoul 110-799, Korea.
Kyung-Ho Choi
Sung-Yup Cho
Chai-Wan Kim
Dong-Myung Shin
Joon-Cheol Kwon
Kye-Yong Song
Sang-Chul Park
In-Gyu Kim
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transglutaminase 2 (TGase 2) is one of a family of enzymes that catalyze protein modification through the incorporation of polyamines into substrates or the formation of protein crosslinks. However, the physiological roles of TGase 2 are largely unknown. To elucidate the functions of TGase 2, we have searched for its interacting proteins. Here we show that TGase 2 interacts with E7 oncoprotein of human papillomavirus type 18 (HPV18) in vitro and in vivo. TGase 2 incorporates polyamines into a conserved glutamine residue in the zinc-binding domain of HPV18 E7 protein. This modification mediates the inhibition of E7's Rb binding ability. In contrast, TGase 2 does not affect HPV16 E7, due to absence of a glutamine residue at this polyamination site. Using E7 mutants, we demonstrate that TGase 2-dependent inhibition of HPV E7 function correlates with the presence of the polyamination site. Our results indicate that TGase 2 is an important cellular interfering factor and define a novel host-virus interaction, suggesting that the inability of TGase 2 to inactivate HPV16 E7 could explain the high prevalence of HPV16 in cervical cancer.

Indexed as

DNA-Binding ProteinsGTP-Binding ProteinsHumansOncogene Proteins, ViralPapillomavirus E7 ProteinsPolyaminesProtein Glutamine gamma Glutamyltransferase 2Retinoblastoma ProteinTransglutaminasesDNA-Binding ProteinsE7 protein, Human papillomavirus type 18GTP-Binding Proteinsoncogene protein E7, Human papillomavirus type 16Oncogene Proteins, ViralPapillomavirus E7 ProteinsPolyaminesProtein Glutamine gamma Glutamyltransferase 2Retinoblastoma ProteinTransglutaminases

Identifiers

PMID14517264
PMCPMC204478
OpenAlexW2036668686

What OpenQuestion 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 OpenQuestion graph.