ReviewMolecular biology reports2025
Key post-translational modifications of crystallin: from mechanism to target exploration for cataract diagnosis and treatment.
Review in Molecular biology reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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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.
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.
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0 citing papers in PubMed.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The maintenance of lens transparency depends on the structural stability and functional integrity of crystallin, and post-translational modification (PTM) is the core link in regulating the conformation, solubility, and molecular chaperone activity of crystallin. This article systematically reviews the molecular mechanisms of key PTM types in crystallin, analyzes the synergistic and antagonistic effects among different PTMs, and clarifies that PTM imbalance promotes the occurrence and development of cataracts by inducing denaturation and aggregation of crystallin. Meanwhile, summarize the research progress of PTM as a diagnostic marker and therapeutic target for cataracts, providing a comprehensive theoretical reference for the study of cataract mechanisms and their application in diagnosis and treatment.
Indexed as
Identifiers
41329261What Socratic holds
Registered trials
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 Socratic graph.