Evidence map›Paper›PMID 31216785›Full record

ReviewInternational journal of molecular sciences2019

Diagnostic and Treatment Approaches Involving Transthyretin in Amyloidogenic Diseases.

Gil Yong Park, Angelo Jamerlan, Kyu Hwan Shim, Seong Soo A An

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  10. Review
  11. Article
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  14. Article
  15. Treatment With Diflunisal in Domino Liver Transplant Recipients With Acquired Amyloid Neuropathy.Transplant international : official journal of the European Society for Organ Transplantation · 2022
    Article
  16. Article
  17. Review
  18. 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

4 authors at 1 institution in 1 country.

Gil Yong ParkDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Korea. gilyong8472@gmail.com.ORCID 0000-0002-7529-0423
Angelo JamerlanDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Korea. angelojamerlan@gmail.com.ORCID 0000-0002-5669-8386
Kyu Hwan ShimDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Korea. smuller0305@gmail.com.
Seong Soo A AnDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Korea. seongaan@gachon.ac.kr.
Gachon University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transthyretin (TTR) is a thyroid hormone-binding protein which transports thyroxine from the bloodstream to the brain. The structural stability of TTR in tetrameric form is crucial for maintaining its original functions in blood or cerebrospinal fluid (CSF). The altered structure of TTR due to genetic mutations or its deposits due to aggregation could cause several deadly diseases such as cardiomyopathy and neuropathy in autonomic, motor, and sensory systems. The early diagnoses for hereditary amyloid TTR with cardiomyopathy (ATTR-CM) and wild-type amyloid TTR (ATTRwt) amyloidosis, which result from amyloid TTR (ATTR) deposition, are difficult to distinguish due to the close similarities of symptoms. Thus, many researchers investigated the role of ATTR as a biomarker, especially its potential for differential diagnosis due to its varying pathogenic involvement in hereditary ATTR-CM and ATTRwt amyloidosis. As a result, the detection of ATTR became valuable in the diagnosis and determination of the best course of treatment for ATTR amyloidoses. Assessing the extent of ATTR deposition and genetic analysis could help in determining disease progression, and thus survival rate could be improved following the determination of the appropriate course of treatment for the patient. Here, the perspectives of ATTR in various diseases were presented.

Indexed as

BiomarkersAmyloidogenic ProteinsAmyloidosisDiagnosis, DifferentialDisease ManagementHumansMutationPrealbuminProtein AggregatesProtein Aggregation, PathologicalStructure-Activity RelationshipWorkflowAmyloidogenic ProteinsBiomarkersPrealbuminProtein Aggregatesamyloidamyloidosismutationprotein aggregationtransthyretin

Identifiers

PMID31216785
PMCPMC6628571
OpenAlexW2950021910

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.