Evidence map›Paper›PMID 34729300›Full record

ReviewActa pharmaceutica Sinica. B2021

Natural compounds in the regulation of proteostatic pathways: An invincible artillery against stress, ageing, and diseases.

Arun Upadhyay

Abstract readReview
In one paragraph

Review in Acta pharmaceutica Sinica. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Miquelianin and spiraeoside fromFrontiers in pharmacology · 2025
    Article
  4. Article
  5. Macrophage senescence in health and diseases.Acta pharmaceutica Sinica. B · 2024
    Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. 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

1 author.

Arun UpadhyayDepartment of Biochemistry, Central University of Rajasthan, Bandar Sindari, Kishangarh, Ajmer, Rajasthan 305817, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells have different sets of molecules for performing an array of physiological functions. Nucleic acids have stored and carried the information throughout evolution, whereas proteins have been attributed to performing most of the cellular functions. To perform these functions, proteins need to have a unique conformation and a definite lifespan. These attributes are achieved by a highly coordinated protein quality control (PQC) system comprising chaperones to fold the proteins in a proper three-dimensional structure, ubiquitin-proteasome system for selective degradation of proteins, and autophagy for bulk clearance of cell debris. Many kinds of stresses and perturbations may lead to the weakening of these protective cellular machinery, leading to the unfolding and aggregation of cellular proteins and the occurrence of numerous pathological conditions. However, modulating the expression and functional efficiency of molecular chaperones, E3 ubiquitin ligases, and autophagic proteins may diminish cellular proteotoxic load and mitigate various pathological effects. Natural medicine and small molecule-based therapies have been well-documented for their effectiveness in modulating these pathways and reestablishing the lost proteostasis inside the cells to combat disease conditions. The present article summarizes various similar reports and highlights the importance of the molecules obtained from natural sources in disease therapeutics.

Indexed as

17-AAG, 17-allylamino-geldanamycinAgeingAPC, anaphase-promoting complexAutophagyBAG, BCL2-associated athanogeneCancerCAP, chaperone-assisted proteasomal degradationCASA, chaperone-assisted selective autophagyChaperonesCHIP, carboxy-terminus of HSC70 interacting proteinCMA, chaperone-mediated autophagyDrug discoveryDUBs, deubiquitinasesEGCG, epigallocatechin-3-gallateESCRT, endosomal sorting complexes required for transportHECT, homologous to the E6-AP carboxyl terminusHSC70, heat shock cognate 70HSF1, heat shock factor 1HSP, heat shock proteinKFERQ, lysine-phenylalanine-glutamate-arginine-glutamineLAMP2a, lysosome-associated membrane protein 2aLC3, light chain 3Natural moleculesNBR1, next to BRCA1 gene 1NeurodegenerationPQC, protein quality controlProteinopathiesProteostasisRING, really interesting new geneUbiquitin proteasome systemUb, ubiquitinUPS, ubiquitin–proteasome system

Identifiers

PMID34729300
PMCPMC8546668

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.