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Last update 08 May 2025

CA2 x CA1

Last update 08 May 2025

Basic Info

Related Targets

CA2CA1

Drugs associated with CA2 x CA1

CA inhibitor (Sakarya University)

Target

CA1 x CA2

Mechanism

CA1 inhibitors [+1]

Active Org.

Sakarya University

Originator Org.

Sakarya University

Active Indication-

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Ethinamate

Target

CA1 x CA2

Mechanism

CA1 inhibitors [+1]

Active Org.-

Originator Org.

Eli Lilly & Co. [+1]

Active Indication-

Inactive Indication

Sleep Initiation and Maintenance Disorders

Drug Highest PhaseWithdrawn

First Approval Ctry. / Loc.

United States

First Approval Date18 Mar 1955

100 Clinical Results associated with CA2 x CA1

100 Translational Medicine associated with CA2 x CA1

0 Patents (Medical) associated with CA2 x CA1

387

Literatures (Medical) associated with CA2 x CA1

01 Apr 2025·Molecular & Cellular Proteomics

Proteomic Analysis of Aqueous Humor Identified Clinically Relevant Molecular Targets for Neovascular Complications in Diabetic Retinopathy

Article

Author: Oh, Jae Won ; Kim, Kwang Pyo ; Jung, Jae Hun ; Kim, Tae Wan ; Ahn, Seong Joon

Diabetic retinopathy (DR) is a leading cause of blindness in adults under 40 in the developed world, with a significant proportion progressing to vision-threatening stages such as proliferative diabetic retinopathy (PDR) and neovascular glaucoma (NVG). This study aims to explore the molecular mechanisms underlying the progression from nonproliferative DR to PDR and NVG, focusing on identifying potential biomarkers and therapeutic targets. Utilizing discovery-based proteomics, specifically label-free quantification and tandem mass tag, we analyzed aqueous humor (AH) proteins obtained during cataract surgery or anterior chamber paracentesis from patients with nonproliferative DR, PDR, and NVG. Validation of marker candidates for each disease state was conducted using triple quadrupole-MS for targeted protein quantification. Our proteomic analysis identified 2255 proteins, and gene ontology analysis and functional annotation highlighted key biological processes implicated in DR, such as lens development, immune responses, and lipid metabolism. Validation of potential biomarkers identified 20 proteins with significant concentration changes, including several candidates with diagnostic utility based on ROC curve analysis. Further investigation into clinical relevance revealed that crystallin gamma-S is strongly associated with cataract severity, highlighting its role as a potential marker for ocular complications in DR. Importantly, we identified that the pathological factors driving DR progression have a much greater impact than age, a previously known variable, in shaping the proteomic landscape of AH. Additionally, proteins associated with macular degeneration (CA1, CA2, and HBA1) were uncovered, providing new insights into overlapping mechanisms between DR and other retinal diseases. Finally, proteins linked to panretinal photocoagulation treatment, including APOB and CST6, were identified, suggesting their involvement in the therapeutic response and post-treatment adaptation. These findings underscore the potential of AH proteomics in uncovering predictive biomarkers and elucidating the molecular pathogenesis of DR and its complications.

01 Mar 2025·The Plant Genome

Genome‐wide association mapping reveals novel genes and genomic regions controlling root‐lesion nematode resistance in chickpea mini core collection

Article

Author: Valluri, Vinod ; Sahu, Sunanda ; Channale, Sonal ; Ramakrishnan, R. S. ; Sharma, Radheshyam ; Varshney, Rajeev K. ; Gautam, Vedant ; Sharma, Stuti ; Naik, Yogesh Dashrath ; Kudapa, Himabindu ; Bhatt, Jayant ; Thudi, Mahendar ; Zwart, Rebecca S. ; Kumar, Ashish ; Punnuri, Somashekhar M.

AbstractRoot‐lesion nematodes (RLN) pose a significant threat to chickpea (Cicer arietinum L.) by damaging the root system and causing up to 25% economic losses due to reduced yield. Worldwide commercially grown chickpea varieties lack significant genetic resistance to RLN, necessitating the identification of genetic variants contributing to natural resistance. This study identifies genomic loci responsible for resistance to the RLN, Pratylenchus thornei Sher & Allen, in chickpea by utilizing high‐quality single nucleotide polymorphisms from whole‐genome sequencing data of 202 chickpea accessions. Phenotypic evaluations of the genetically diverse set of chickpea accessions in India and Australia revealed a wide range of responses from resistant to susceptible. Genome‐wide association studies (GWAS) employing Fixed and Random Model Circulating Probability Unification (FarmCPU) and Bayesian‐Information and Linkage‐Disequilibrium Iteratively Nested Keyway (BLINK) models identified 44 marker‐trait associations distributed across all chromosomes except Ca1. Crucially, genomic regions on Ca2 and Ca5 consistently display significant associations across locations. Of 25 candidate genes identified, five genes were putatively involved in RLN resistance response (glucose‐6‐phosphate dehydrogenase, heat shock proteins, MYB‐like DNA‐binding protein, zinc finger FYVE protein and pathogenesis‐related thaumatin‐like protein). One notably identified gene (Ca_10016) presents four haplotypes, where haplotypes 1–3 confer moderate susceptibility, and haplotype 4 contributes to high susceptibility to RLN. This information provides potential targets for marker development to enhance breeding for RLN resistance in chickpea. Additionally, five potential resistant genotypes (ICC3512, ICC8855, ICC5337, ICC8950, and ICC6537) to P. thornei were identified based on their performance at a specific location. The study's significance lies in its comprehensive approach, integrating multiple‐location phenotypic evaluations, advanced GWAS models, and functional genomics to unravel the genetic basis of P. thornei resistance. The identified genomic regions, candidate genes, and haplotypes offer valuable insights for breeding strategies, paving the way for developing chickpea varieties resilient to P. thornei attack.

01 Mar 2025·Biochemical and Biophysical Research Communications

Molecular dynamics simulation reveals structural insights into isozyme selectivity of carbonic anhydrase XII inhibitors in hypoxic tumor microenvironment

Article

Author: Gao, Quan-Ze ; Saravanan, Venkatesan ; Kumaradoss, Kathiravan Muthu ; Palani, Sathiya Priya ; Valsaladevi, Anjana Gopi ; Chagaleti, Bharath Kumar

Human carbonic anhydrase (CA) isoenzymes IX and XII are overexpressed in cancer cells, contributing to tumor microenvironment acidification and representing important targets for cancer therapy. In this study, we identified compound V35 (ZINC09419065) as a selective inhibitor of CA IX and CA XII with enhanced binding stability and selectivity compared to standard inhibitors. We analyzed conserved regions in CA I, CA II, CA IX, and CA XII to investigate their isozyme selectivity, revealing critical selectivity determinants at positions 95, 141, and 203. Molecular docking results indicated that V35 interacts robustly with CA XII, forming a metal ion coordination complex with Zn via HIS94, HIS96, HIS119, and THR199, similar to the interaction pattern of standard inhibitor SLC-0111. Molecular dynamics (MD) simulations conducted over 500 ns under hypoxic conditions showed that V35 has high binding stability, with root mean square deviation (RMSD) and fluctuation (RMSF) values comparable to SLC-0111, demonstrating its conformational stability in CA XII. Binding free energy calculations using the MMGBSA method showed that V35 achieves binding free energy of -44.17 kcal/mol with CA XII, closely matching SLC-0111 (-49.41 kcal/mol). Density functional theory (DFT) calculations further highlighted V35's electrostatic potential distribution, supporting its isozyme selectivity. Post-dynamics analysis indicated that the ester functional groups and the inward movement of HIS64 stabilize V35's interactions in CA XII, a feature absent in CA I.

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