Evidence map›Paper›PMID 27879017›Full record

ArticleProtein science : a publication of the Protein Society2017

Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release.

Tetsuya Kadonosono, Wanaporn Yimchuen, Takuya Tsubaki, Tadashi Shiozawa, Yasuhiro Suzuki, Takahiro Kuchimaru, Yasufumi Sato, Shinae Kizaka-Kondoh

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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Loss of function of SVBP leads to autosomal recessive intellectual disability, microcephaly, ataxia, and hypotonia.Genetics in medicine : official journal of the American College of Medical Genetics · 2019
    Article
  5. Article
  6. Article
  7. Review
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 2 institutions in 1 country.

Tetsuya KadonosonoDepartment of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Wanaporn YimchuenDepartment of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Takuya TsubakiDepartment of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Tadashi ShiozawaDepartment of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Yasuhiro SuzukiDepartment of Vascular Biology, Institute of Development, Aging, and Cancer, Tohoku University, Sendai, 980-8575, Japan.
Takahiro KuchimaruDepartment of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Yasufumi SatoDepartment of Vascular Biology, Institute of Development, Aging, and Cancer, Tohoku University, Sendai, 980-8575, Japan.
Shinae Kizaka-KondohDepartment of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Tokyo Institute of Technology · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vasohibins (VASH1 and VASH2) are recently identified regulators of angiogenesis and cancer cell functions. They are secreted proteins without any classical secretion signal sequences, and are thought to be secreted instead via an unconventional protein secretion (UPS) pathway in a small vasohibin-binding protein (SVBP)-dependent manner. However, the precise mechanism of SVBP-dependent UPS is poorly understood. In this study, we identified a novel UPS regulatory system in which essential domain architecture (VASH-PS) of VASHs, comprising regions VASH1

Indexed as

Angiogenic ProteinsCarrier ProteinsCell Cycle ProteinsCytosolHeLa CellsHumansMolecular ChaperonesProtein DomainsAngiogenic ProteinsCarrier ProteinsCell Cycle ProteinsMolecular ChaperonesSVBP protein, humanVASH1 protein, humanVASH2 protein, humanmolecular chaperonpunctate structure formationunconventional protein secretionvasohibins

Identifiers

PMID27879017
PMCPMC5326560
OpenAlexW2549181864

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.