Evidence map›Paper›PMID 17290225›Full record

ArticleThe EMBO journal2007

Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding.

Kazuya Honbou, Reiko Minakami, Satoru Yuzawa, Ryu Takeya, Nobuo N Suzuki, Sachiko Kamakura, Hideki Sumimoto, Fuyuhiko Inagaki

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.3field-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

27 citing papers in PubMed, 67 citations in OpenAlex.

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  12. Molecular analysis of protein-phosphoinositide interactions.Current topics in microbiology and immunology · 2012
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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 at 3 institutions in 1 country.

Kazuya HonbouLaboratory of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Reiko Minakami
Satoru Yuzawa
Ryu Takeya
Nobuo N Suzuki
Sachiko Kamakura
Hideki Sumimoto
Fuyuhiko Inagaki
Hokkaido University · JPJapan Science and Technology Agency · JPKyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The superoxide-producing phagocyte NADPH oxidase is activated during phagocytosis to destroy ingested microbes. The adaptor protein p40phox associates via the PB1 domain with the essential oxidase activator p67phox, and is considered to function by recruiting p67phox to phagosomes; in this process, the PX domain of p40phox binds to phosphatidylinositol 3-phosphate [PtdIns(3)P], a lipid abundant in the phagosomal membrane. Here we show that the PtdIns(3)P-binding activity of p40phox is normally inhibited by the PB1 domain both in vivo and in vitro. The crystal structure of the full-length p40phox reveals that the inhibition is mediated via intramolecular interaction between the PB1 and PX domains. The interface of the p40phox PB1 domain for the PX domain localizes on the opposite side of that for the p67phox PB1 domain, and thus the PB1-mediated PX regulation occurs without preventing the PB1-PB1 association with p67phox.

Indexed as

Models, MolecularProtein Structure, TertiaryAnimalsCrystallizationHeLa CellsHumansImmunoprecipitationMiceMicroscopy, ConfocalNADPH OxidasesPhagocytosisPhagosomesPhosphatidylinositol PhosphatesPhosphoproteinsProtein BindingNADPH OxidasesNCF4 protein, humanneutrophil cytosol factor 67Kphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesPhosphoproteins

Identifiers

PMID17290225
PMCPMC1852833
OpenAlexW2160690435

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.