Request Demo

Last update 08 May 2025

CRYAA

Last update 08 May 2025

Basic Info

Synonyms

Alpha-crystallin A chain, Alpha-crystallin A(1-162), Alpha-crystallin A(1-168)

+ [6]

Introduction

Contributes to the transparency and refractive index of the lens (PubMed:18302245). In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions (PubMed:18199971, PubMed:19595763, PubMed:22120592, PubMed:31792453). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373).

Drugs associated with CRYAA

VP1-001

Target

CRYAA

Mechanism

CRYAA modulators

Active Org.

Viewpoint Therapeutics, Inc.

Originator Org.

Viewpoint Therapeutics, Inc.

Active Indication

Cataract [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

US20240327439

Patent Mining

Target

CRYAA x TTR

Mechanism-

Active Org.

Plex Pharmaceuticals, Inc.

Originator Org.

Plex Pharmaceuticals, Inc.

Active Indication

Eye Diseases [+1]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

TBA-61

Target

CRYAA

Mechanism

CRYAA inhibitors

Active Org.-

Originator Org.

Finlay Institute of Cuba

Active Indication-

Inactive Indication

Tuberculosis

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with CRYAA

100 Translational Medicine associated with CRYAA

0 Patents (Medical) associated with CRYAA

1,287

Literatures (Medical) associated with CRYAA

01 Jul 2025·Archives of Biochemistry and Biophysics

The p.K90N mutation in human HSPB5 highlights the critical role of lysine 90 in chaperone function and structural integrity

Article

Author: Moosavi-Movahedi, Ali Akbar ; Yousefi, Reza ; Stroylova, Yulia Y ; Saboury, Ali Akbar ; Shahsavani, Mohammad Bagher ; Somee, Leila Rezaei ; Amanlou, Massoud ; Mirzaei, Zahra ; Habibi-Rezaei, Mehran ; Muronetz, Vladimir I ; Ghaffari, Ahmad Reza ; Barinova, Ksenia V

HSPB5 (αB-crystallin), a small heat shock protein, stabilizes proteins and prevents misfolded protein aggregation through dynamic oligomer formation. Mutations in HSPB5 can result in diseases such as myopathy and cataracts. This study focuses on the myopathy-associated p.K90N mutation in the α-crystallin domain and its impact on the structure and function of human HSPB5. The recombinant mutated protein was expressed and purified for analysis using spectroscopy, microscopy, and molecular dynamics simulations. Our results reveal that the p.K90N mutation induces significant structural alterations, including an increase in β-sheet content and a reduction in α-helical structure compared to the wild-type protein. Molecular dynamics simulations showed an increased angle between dimers and decreased accessible surface area in the mutant protein. Additionally, the mutant exhibited a higher propensity for forming larger oligomers and amyloid fibrils, and enhanced thermal stability. These structural changes lead to reduced chaperone activity and impaired protein aggregation prevention, likely contributing to cell death and myopathy. Overall, the p.K90N mutation significantly alters the structural and functional properties of HSPB5, highlighting its pathogenic role and providing insights into disease mechanisms.

01 May 2025·International Journal of Biological Macromolecules

Impact of crowding on aggregation of UV-irradiated βL-crystallin and chaperone like activity of α-crystallin depends of the nature of a crowding agent

Article

Author: Muranov, Konstantin O ; Poliansky, Nikolay B ; Borzova, Vera A

The effect of crowding on the aggregation of UV irradiated β_L-crystallin and the chaperone-like activity of α-crystallin has been studied. PEG-20000, BSA and γ-crystallin were used as crowders. It was shown that the initial rate of aggregation of UV irradiated β_L-crystallin depended on the type of crowder: the rate did not change in the presence of BSA, doubled when the concentration of γ-crystallin reached 30 mg/ml, and increased linearly with increasing PEG concentration. It was found that PEG is not an inert compound, but causes additional destabilization and denaturation of UV irradiated β_L-crystallin. The nucleation time of UV irradiated β_L-crystallin aggregation in the presence of BSA and γ-crystallin decreased linearly with an increase in the excluded volume up to 5 %, then remained constant. It was found that BSA and γ-crystallin reduced the initial adsorption capacity of α-crystallin, which was used to quantify chaperone-like activity, in a concentration-dependent manner. g-crystallin demonstrated a greater ability to suppress chaperone-like activity compared to BSA. This difference is due to γ-crystallin ability to interact with α-crystallin. The obtained results indicate the importance of using the exact same crowders that in vivo create the environment of the biochemical process for study in vitro.

01 May 2025·Ophthalmology and Therapy

Comprehensive Analysis of Congenital Aniridia and Differential Diagnoses: Genetic Insights and Clinical Manifestations

Review

Author: Suiwal, Shweta ; Stachon, Tanja ; Szentmáry, Nóra ; Obst, Jessica ; Hall, Jonathan ; Jávorszky, Eszter ; Corton, Marta ; Maka, Erika ; Amini, Maryam ; Seitz, Berthold ; Waizel, Maria Della Volpe ; Fries, Fabian Norbert ; Tory, Kálmán ; Grünauer-Kloevekorn, Clara

INTRODUCTIONCongenital aniridia (CA) is a severe and complex disorder involving the entire eye, primarily characterized by iris anomalies alongside other clinical features that pose significant risks to vision. This study seeks to offer a comprehensive overview of CA by detailing its clinical presentations, genetic underpinnings, associated phenotypes, and differential diagnoses. Additionally, it proposes a diagnostic framework to distinguish CA from other conditions that present with similar iris abnormalities.METHODSWe conducted a comprehensive literature review to compile and analyze clinical and genetic data related to CA and its differential diagnoses. We included all studies describing the clinical characteristics, pathogenic variants, and associated syndromes of congenital aniridia.RESULTSCA presents a wide range of ocular symptoms. Pathogenic variants in the PAX6 gene are the primary genetic cause of CA, though variations in other genes, including FOXC1, PITX2, CYP1B1, FOXD3, PITX3, CPAMD8, ITPR1, TENM3, TRIM44, COL4A1, CRYAA, and PXDN may also be implicated. The differential diagnosis of CA requires careful consideration of conditions with overlapping symptoms, such as WAGR syndrome (which involves deletions affecting the PAX6 and WT1 genes on chromosome 11p13, and potentially BDNF on 11p14.1), Axenfeld-Rieger syndrome (FOXC1/PITX2), ring-chromosome 6 syndrome (which involves FOXC1 microdeletion), COL4A1-related anterior segment dysgenesis, Gillespie syndrome (ITPR1 gene) or Peters anomaly. Accurate diagnosis can be achieved by evaluating specific clinical features-including iris anomalies, aniridia-associated keratopathy, cataracts, glaucoma, foveal hypoplasia, nystagmus, and optic nerve head abnormalities-supplemented by genetic testing.CONCLUSIONSUnderstanding the diverse clinical presentations and genetic basis of diseases associated with iris abnormalities is essential for accurate diagnosis and effective management. Integrating genetic diagnostics into the evaluation process enables the development of tailored treatment strategies, which can significantly improve patient outcomes.

Analysis

Perform a panoramic analysis of this field.

view full example data

Hiro LS Researcher

The AI Search Engine Built to Accelerate Biopharma Decisions

Search across billion-scale life sciences data to uncover signals, validate evidence, and act with confidence.

Ask any biopharma research question→

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, Patsnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Discover Synapse Data Servers

Synapse data is now integrated into the PatSnap LS Model Context Protocol (MCP) service. Customize your LLM agent now using our MCP server!

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

CRYAA

Basic Info

Related

Analysis