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Last update 08 May 2025

A34

Last update 08 May 2025

Basic Info

Synonyms-

Introduction-

Drugs associated with A34

RebmAb400

Target

A34

Mechanism

A34 inhibitors

Active Org.

Recepta Biopharma SA

Originator Org.

Recepta Biopharma SA

Active Indication

Adenocarcinoma [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with A34

100 Translational Medicine associated with A34

0 Patents (Medical) associated with A34

Literatures (Medical) associated with A34

01 Apr 2025·Biochemistry

Mechanism of Conformational Selection of tRNA^Arg2 by Bacterial Deaminase TadA

Article

Author: Porathoor, Sini ; Mariam, Jessy ; Anand, Ruchi

Base editing is a common mechanism by which organisms expand their genetic repertoire to access new functions. Here, we explore the mechanism of tRNA recognition in the bacterial deaminase TadA, which exclusively recognizes tRNA^Arg2 and converts the wobble base adenosine (A34) to inosine. We quantitatively evaluate the dynamics of tRNA binding by incorporating the fluorescent adenine analogue 2-aminopurine (2-AP) at position 34 in the wobble base of the anticodon loop. Time-resolved fluorescence and anisotropy studies revealed that the recognition process is finely tuned. Mutations in residues directly involved in facilitating deamination, such as E55A and N42A, showed a minimal impact on binding dynamics. In contrast, mutations in the "capping residues", notably R149, unique to prokaryotic TadAs and located 12-15 Å away from the catalytic center, significantly disrupted binding and consequently catalytic activity. The capping residues play a critical role in enabling tRNA recognition, thereby underscoring their importance in enzyme function. Moreover, for effective catalysis, peripheral positively charged residues (R70, R94) that are part of the adjacent subunit in the dimeric assembly are important to splay out the tRNA, assisting in A34 attaining a flipped-out conformation. Perturbations in these extended regions, although 15-20 Å away from the active site, disrupt the binding dynamics and consequently the function, emphasizing the fine regulation of the tRNA recognition process. Analysis reveals that the C-terminal end of the extended helix where R149 is positioned, acts as a selectivity filter imparting exclusivity toward the deamination of tRNA^Arg2 by TadA.

05 Mar 2025·Journal of Agricultural and Food Chemistry

Identification and Validation of Key Amino Acids in IgE Linear Epitopes of β-Lactoglobulin: Comparison of Recognition Patterns of Chinese Bovine Milk-Allergic Sera with Different Symptoms

Article

Author: Chen, Hongbing ; Wu, Zhihua ; Yang, Anshu ; Meng, Xuanyi ; Wu, Yong ; Gao, Jinyan ; Hu, Wei ; Li, Xin ; Xie, Fen

β-lactoglobulin (BLG) is the primary allergen in bovine milk allergy. The identification of key amino acids in the BLG epitopes has not been comprehensive due to differences in identification methods, patient symptoms, and population characteristics. In this study, bioinformatics predictions were conducted for key amino acids based on two potential IgE linear epitopes in BLG. Then, the peptide AA30-43 was confirmed as an IgE linear epitope through alanine scanning mutagenesis and peptide microarray assays, with four key amino acids (A³⁴, A³⁷, R⁴⁰, and V⁴¹) common to different symptoms being identified. Moreover, symptom-specific key amino acids were identified. Serine (S³⁰) and aspartic acid (D³³) are the key amino acids for cutaneous allergy, while food allergy sera showed a preference for recognizing leucines in different positions (L³¹ and L³⁹). Additionally, mutant peptides (R⁴⁰, V⁴¹, L³⁹, and D³³) showed an obvious decrease in digestive stability compared with the epitope. Finally, the results of the KU812 cell degranulation model validated the critical role of the amino acids in allergenicity. These findings offer significant advantages for advancing both immune tolerance therapies and hypoallergenic milk product development, which hold significant implications for further research, prevention, and treatment of bovine milk allergy.

01 Aug 2024·Parasitology International

Detection of Blastocystis sp. and Dientamoeba fragilis using conventional and molecular methods in patients with celiac disease

Article

Author: Sarzhanov, Fakhriddin ; Dogruman-Al, Funda ; Demirel, Filiz ; Mızrak, Muzaffer ; Filik, Levent ; Dinç, Bedia

Blastocystis sp. and Dientamoeba fragilis are intestinal protists, which are common worldwide, but the pathogenic role of these organisms in gastrointestinal diseases is still controversial. This study aimed to investigate the frequency of Blastocystis sp. and D. fragilis in stool samples from adult patients with celiac disease (CD) by using conventional and molecular methods. A total of 75 patients with CD and 75 healthy individuals were included in this study. Fresh stool specimens collected from each individual were analyzed by conventional and molecular methods. The overall prevalence of Blastocystis sp. and D. fragilis was 41.3% (31/75) and 24% (18/75) in patients with CD, and 46.7% (35/75) and 13.3% (10/75) in healthy controls, respectively. There was no statistically significant difference in the prevalence of Blastocystis sp. and D. fragilis between CD patients and healthy individuals. Blastocystis sp. subtypes were identified in 20 CD and 16 control patients and the overall subtype distribution was observed as ST1 13.9%, ST2 30.6%, and ST3 55.6%. The prevalence of Blastocystis sp. and D. fragilis in adults with CD is similar to the prevalence of protozoa in healthy adults. In this study, the most prevalent Blastocystis subtype was ST3 and the most frequent allele was a34 in both CD patients and healthy individuals. No significant difference was found between the two groups in terms of the detection rates of Blastocystis sp. and D. fragilis, and it is thought that both protists may be colonisers of the intestinal microbiome.

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A34

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