Evidence map›Paper›PMID 28608415›Full record

ArticleProtein science : a publication of the Protein Society2017

Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1.

Toshiaki Hosaka, Masateru Okazaki, Tomomi Kimura-Someya, Yoshiko Ishizuka-Katsura, Kaori Ito, Shigeyuki Yokoyama, Kosuke Dodo, Mikiko Sodeoka, Mikako Shirouzu

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

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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.

Toshiaki HosakaDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Kanagawa, 230-0045, Japan.ORCID http://orcid.org/0000-0002-7652-8114
Masateru OkazakiSodeoka Live Cell Chemisty Project, ERATO, JST, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Tomomi Kimura-SomeyaDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Kanagawa, 230-0045, Japan.
Yoshiko Ishizuka-KatsuraDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Kanagawa, 230-0045, Japan.
Kaori ItoDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Kanagawa, 230-0045, Japan.
Shigeyuki YokoyamaRIKEN Structural Biology Laboratory, Yokohama, Kanagawa, 230-0045, Japan.
Kosuke DodoSodeoka Live Cell Chemisty Project, ERATO, JST, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Mikiko SodeokaSodeoka Live Cell Chemisty Project, ERATO, JST, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Mikako ShirouzuDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama, Kanagawa, 230-0045, Japan.
Japan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-dependent anion channel 1 (VDAC1), which is located in the outer mitochondrial membrane, plays important roles in various cellular processes. For example, oligomerization of VDAC1 is involved in the release of cytochrome c to the cytoplasm, leading to apoptosis. However, it is unknown how VDAC1 oligomerization occurs in the membrane. In the present study, we determined high-resolution crystal structures of oligomeric human VDAC1 (hVDAC1) prepared by using an Escherichia coli cell-free protein synthesis system, which avoided the need for denaturation and refolding of the protein. Broad-range screening using a bicelle crystallization method produced crystals in space groups C222 and P22

Indexed as

Crystallography, X-RayEscherichia coliHumansHydrophobic and Hydrophilic InteractionsLipid BilayersModels, MolecularProtein MultimerizationProtein SubunitsRecombinant ProteinsSurface PropertiesVoltage-Dependent Anion Channel 1Lipid BilayersProtein SubunitsRecombinant ProteinsVDAC1 protein, humanVoltage-Dependent Anion Channel 1cell-free protein synthesiscrystallizationoligomerization statesingle-channel gatingvoltage-dependent anion channel 1X-ray crystallographyβ-barrel structure

Identifiers

PMID28608415
PMCPMC5563135
OpenAlexW2625581241

What OpenQuestion holds

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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.