Evidence map›Paper›PMID 30704121›Full record

ArticleMolecules (Basel, Switzerland)2019

Transthyretin Amyloid Fibril Disrupting Activities of Extracts and Fractions from

Niraj Chaudhary, Ryoko Sasaki, Tsuyoshi Shuto, Masato Watanabe, Teppei Kawahara, Mary Ann Suico, Takeshi Yokoyama, Mineyuki Mizuguchi, Hirofumi Kai, Hari Prasad Devkota

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Frontiers in pharmacology · 2020
    Review
  3. Article
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

10 authors at 2 institutions in 1 country.

Niraj ChaudharyDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan. nirajchaudharypu@gmail.com.
Ryoko SasakiDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan. 188y1008@st.kumamoto-u.ac.jp.
Tsuyoshi ShutoDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan. tshuto@gpo.kumamoto-u.ac.jp.
Masato WatanabeDepartment of Medicinal Botany, Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973, Japan. wata-m@gpo.kumamoto-u.ac.jp.
Teppei KawaharaUseful and Unique Natural Products for Drug Discovery and Development (UpRoD), Program for Building Regional Innovation Ecosystems at Kumamoto University, Kumamoto 862-0973, Japan. teppei@kumamoto-u.ac.jp.ORCID 0000-0001-5140-4724
Mary Ann SuicoDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan. mann@gpo.kumamoto-u.ac.jp.
Takeshi YokoyamaGraduate School of Medicine and Pharmaceutical Sciences, University of Toyama, 2630 Sugitani, Toyama 930-0194, Japan. tyokoya3@pha.u-toyama.ac.jp.
Mineyuki MizuguchiGraduate School of Medicine and Pharmaceutical Sciences, University of Toyama, 2630 Sugitani, Toyama 930-0194, Japan. mineyuki@pha.u-toyama.ac.jp.
Hirofumi KaiDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan. hirokai@gpo.kumamoto-u.ac.jp.
Hari Prasad DevkotaProgram for Leading Graduate Schools, Health Life Science: Interdisciplinary and Glocal Oriented (HIGO) Program, Kumamoto University, Kumamoto 862-0973, Japan. devkotah@kumamoto-u.ac.jp.ORCID 0000-0002-0509-1621
Kumamoto University · JPUniversity of Toyama · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transthyretin-related amyloidosis is a slowly progressive disorder caused by deposition of insoluble amyloid plaques formed by fibrillization of mutant or defective transthyretin (TTR) monomers that leads to neurodegeneration and organ failure. Thus, any compound exhibiting TTR amyloid formation inhibitory activity or TTR amyloid fibril disrupting activity might be a potential candidate for the development of therapies for these disorders. Our aim in this study was the evaluation of the TTR amyloid fibril disrupting potential of extracts of leaves and immature fruits of two

Indexed as

AmyloidCell LineCell SurvivalFruitHumansJuglansLiquid-Liquid ExtractionMolecular StructurePlant ExtractsPlant LeavesPrealbuminProtein AggregatesProtein Aggregation, PathologicalAmyloidPlant ExtractsPrealbuminProtein AggregatesJuglans mandshurica var. cordiformisJuglans mandshurica var. sachalinensisjuglonenaphthoquinonetransthyretin protein (TTR)transthyretin-related amyloidosis

Identifiers

PMID30704121
PMCPMC6384717
OpenAlexW2912849535

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.