Evidence map›Paper›PMID 36548224›Full record

ArticlePloS one2022

Importance of annexin V N-terminus for 2D crystal formation and quick purification protocol of recombinant annexin V.

Ryusei Yamada, Tran Ngoc Trang, Holger Flechsig, Toshiki Takeda, Noriyuki Kodera, Hiroki Konno

Abstract read
In one paragraph

Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Ryusei YamadaCollege of Science and Engineering, School of Biological Science and Technology, Kanazawa University, Kanazawa, Japan.
Tran Ngoc TrangGraduate School of Frontier Science Initiative, Kanazawa University, Kanazawa, Japan.ORCID 0000-0002-7083-5770
Holger FlechsigWPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Toshiki TakedaCollege of Science and Engineering, School of Natural System, Kanazawa University, Kanazawa, Japan.
Noriyuki KoderaWPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Hiroki KonnoWPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID 0000-0002-1712-171X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Annexin V forms trimeric structures which further assemble into two-dimensional crystal (2D crystal) lattices on negatively charged phospholipid bilayer in a Ca2+-dependent manner. It is also known that annexin V 2D crystals show two types of symmetric patterns with six-fold symmetry (p6) and three-fold symmetry (p3). The p6 lattice also contains additional trimers in the gaps between the p6 axes, which are also referred to as non-p6 trimers because they do not participate in the formation of the p6 lattice. We here show that the annexin V N-terminal has significant influence on 2D crystal formation using high-speed atomic force microscopy (HS-AFM) observations. We also present a quick purification method to purify recombinant annexin V without any residual affinity tag after protein purification in ~3h.

Indexed as

CalciumPhospholipidsAnnexin A5Annexin A5CalciumPhospholipids

Identifiers

PMID36548224
PMCPMC9778525

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.