Evidence map›Paper›PMID 26859714›Full record

ReviewCurrent opinion in chemical biology2016

A current pharmacologic agent versus the promise of next generation therapeutics to ameliorate protein misfolding and/or aggregation diseases.

Aleksandra Baranczak, Jeffery W Kelly

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.3field-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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Biosensors for Studying Neuronal Proteostasis.Frontiers in molecular neuroscience · 2022
    Review
  4. Article
  5. From Kuru to Alzheimer: A personal outlook.Protein science : a publication of the Protein Society · 2021
    Review
  6. Review
  7. The proteostasis network and its decline in ageing.Nature reviews. Molecular cell biology · 2019
    Review
  8. Review
  9. Small molecule probes of protein aggregation.Current opinion in chemical biology · 2017
    Review
  10. 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

2 authors at 1 institution in 1 country.

Aleksandra BaranczakDepartment of Chemistry and The Skaggs Institute for Chemical Biology, La Jolla, CA 92037, USA; Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: Aleksandra.baranczak@abbvie.com.
Jeffery W KellyDepartment of Chemistry and The Skaggs Institute for Chemical Biology, La Jolla, CA 92037, USA; Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: jkelly@scripps.edu.
Scripps Research Institute · US

Funding

Probing the Biochemical Mechanisms of Amyloid DiseaseR01DK046335 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 1998 to 2025
$8.8M
Discovering small molecules activators of stress responsive signalingR01AG046495 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI JEFFERY W KELLY, Rockland Luke Wiseman · 2013 to 2026
$6.0M
Probing the biochemical mechanism of amyloid diseaseR37DK046335 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 2006 to 2015
$5.9M
NIA NIH HHS R01 AG046495NIDDK NIH HHS R01 DK046335NIDDK NIH HHS R37 DK046335
6 · The paper itself

Abstract

The list of protein aggregation-associated degenerative diseases is long and growing, while the portfolio of disease-modifying strategies is very small. In this review and perspective, we assess what has worked to slow the progression of an aggregation-associated degenerative disease, covering the underlying mechanism of pharmacologic action and what we have learned about the etiology of the transthyretin amyloid diseases and likely amyloidoses in general. Next, we introduce emerging therapies that should apply more generally to protein misfolding and/or aggregation diseases, approaches that rely on adapting the protein homeostasis or proteostasis network for disease amelioration.

Indexed as

Protein FoldingHumansProteostasis Deficiencies

Identifiers

PMID26859714
PMCPMC4907839
OpenAlexW2268900877

What OpenQuestion holds

Textmetadata
LicenceTDM
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.