Evidence map›Paper›PMID 26141743›Full record

ReviewBiochimica et biophysica acta2016

Alpha-crystallin-derived peptides as therapeutic chaperones.

Murugesan Raju, Puttur Santhoshkumar, K Krishna Sharma

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Small Heat Shock Proteins in Retinal Diseases.Frontiers in molecular biosciences · 2022
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Murugesan RajuDepartment of Ophthalmology, University of Missouri School of Medicine, Columbia, MO 65212, USA.
Puttur SanthoshkumarDepartment of Ophthalmology, University of Missouri School of Medicine, Columbia, MO 65212, USA.
K Krishna SharmaDepartment of Ophthalmology, University of Missouri School of Medicine, Columbia, MO 65212, USA; Department of Biochemistry, University of Missouri School of Medicine, Columbia, MO 65212, USA. Electronic address: sharmak@health.missouri.edu.
University of Missouri · US

Funding

Metastable Crystallins: Structure and StabilizationR01EY023219 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI KRISHNA K SHARMA · 2013 to 2026
$5.9M
Crystallin-Derived Anti-Chaperones in the LensR01EY019878 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 2010 to 2013
$1.4M
NEI NIH HHS EY023219NEI NIH HHS EY19878NEI NIH HHS R01 EY019878NEI NIH HHS R01 EY023219
6 · The paper itself

Abstract

backgroundThe demonstration of chaperone-like activity in peptides (mini-chaperones) derived from α-crystallin's chaperone region has generated significant interest in exploring the therapeutic potential of peptide chaperones in diseases of protein aggregation. Recent studies in experimental animals show that mini-chaperones could reach intended targets and alter the disease phenotype. Although mini-chaperones show potential benefits against protein aggregation diseases, they do tend to form aggregates on storage. There is thus a need to fine-tune peptide chaperones to increase their solubility, pharmacokinetics, and biological efficacy. SCOPE OF REVIEW: This review summarizes the properties and the potential therapeutic roles of mini-chaperones in protein aggregation diseases and highlights some of the refinements needed to increase the stability and biological efficacy of mini-chaperones while maintaining or enhancing their chaperone-like activity against precipitation of unfolding proteins. MAJOR

conclusionsMini-chaperones suppress the aggregation of proteins, block amyloid fibril formation, stabilize mutant proteins, sequester metal ions, and exhibit antiapoptotic properties. Much work must be done to fine-tune mini-chaperones and increase their stability and biological efficacy. Peptide chaperones could have a great therapeutic value in diseases associated with protein aggregation and apoptosis. GENERAL SIGNIFICANCE: Accumulation of misfolded proteins is a primary cause for many age-related diseases, including cataract, macular degeneration, and various neurological diseases. Stabilization of native proteins is a logical therapeutic approach for such diseases. Mini-chaperones, with their inherent antiaggregation and antiapoptotic properties, may represent an effective therapeutic molecule to prevent the cascade of protein conformational disorders. Future studies will further uncover the therapeutic potential of mini-chaperones. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease.

Indexed as

alpha-CrystallinsAnimalsAntioxidantsGlaucomaMolecular ChaperonesPeptidesProtein Aggregation, PathologicalRetinal Diseasesalpha-CrystallinsAntioxidantsMolecular ChaperonesPeptidesCrystallinsMini-chaperonesPeptideProtein aggregationTherapeutics

Identifiers

PMID26141743
PMCPMC4673008
OpenAlexW843422225

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.