-
1“…The heterodimeric adenosine deaminases acting on tRNAs (ADAT2-ADAT3, or ADAT) are enzymes present in eukaryotes that convert adenine (A) to inosine (I) in the first anticodon base (position 34) by hydrolytic deamination. …”
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
2por Ramos-Morales, Elizabeth, Bayam, Efil, Del-Pozo-Rodríguez, Jordi, Salinas-Giegé, Thalia, Marek, Martin, Tilly, Peggy, Wolff, Philippe, Troesch, Edouard, Ennifar, Eric, Drouard, Laurence, Godin, Juliette D, Romier, Christophe“…The eukaryotic wobble adenosine-to-inosine modification is catalysed by the ADAT (ADAT2/ADAT3) complex that modifies up to eight tRNAs, requiring a full tRNA for activity. …”
Publicado 2021
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
3por Cheung, Foo, Fantoni, Giovanna, Conner, Maria, Sellers, Brian A, Kotliarov, Yuri, Candia, Julián, Stagliano, Katherine, Biancotto, Angélique“…Experimental data resulting from the assay is provided by SomaLogic in a proprietary text-based format called ADAT. This manuscript describes a user-friendly point and click open source, platform-independent software tool designed to be used for navigating and plotting data from an ADAT file. …”
Publicado 2017
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
4por Liu, Xiwen, Chen, Ruoyu, Sun, Yujie, Chen, Ran, Zhou, Jie, Tian, Qingnan, Tao, Xuan, Zhang, Zhang, Luo, Guan-zheng, Xie, Wei“…This modification is produced via deamination on A34 and catalyzed by the adenosine deaminase acting on tRNA (ADAT) enzyme. Eukaryotic ADATs are heterodimers composed of the catalytic subunit ADAT2 and the structural subunit ADAT3, but their molecular assemblies and catalytic mechanisms are largely unclear. …”
Publicado 2020
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
5“…RESULTS: readat is an R package for working with the SomaLogic ADAT file format. It provides functionality for importing, transforming and annotating data from these files. …”
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
6por Dorosteh, Ameneh Pooresmaeil, Ghaffari, Mohtasham, Rakhshanderou, Sakineh, Mehrabi, Yadollah, Ramezankhani, AliEnlace del recurso
Publicado 2023
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
7por Salehi Chaleshtori, Ahmad Reza, Miyake, Noriko, Ahmadvand, Mohammad, Bashti, Oranous, Matsumoto, Naomichi, Noruzinia, Mehrdad“…A heterodimer consists of ADAT3 and ADAT2 and is involved in the adenosine-to-inosine conversion in tRNA. …”
Publicado 2018
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
8por Roura Frigolé, Helena, Camacho, Noelia, Castellví Coma, Maria, Fernández-Lozano, Carla, García-Lema, Jorge, Rafels-Ybern, Àlbert, Canals, Albert, Coll, Miquel, Ribas de Pouplana, Lluís“…Adenosine deaminase acting on transfer RNA (ADAT) is an essential eukaryotic enzyme that catalyzes the deamination of adenosine to inosine at the first position of tRNA anticodons. …”
Publicado 2019
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
9por Dolce, Luciano G., Zimmer, Aubree A., Tengo, Laura, Weis, Félix, Rubio, Mary Anne T., Alfonzo, Juan D., Kowalinski, Eva“…Here, using cryo-EM, we present the structure of a eukaryotic ADAT2/3 deaminase bound to a full-length tRNA, revealing that the enzyme distorts the anticodon loop, but in contrast to the bacterial enzymes, selects its substrate via sequence-independent contacts of eukaryote-acquired flexible or intrinsically unfolded motifs distal from the conserved catalytic core. …”
Publicado 2022
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
10
-
11
-
12
-
13
-
14
-
15por Dumbrava, E.E., Call, S.G., Huang, H.J., Stuckett, A.L., Madwani, K., Adat, A., Hong, D.S., Piha-Paul, S.A., Subbiah, V., Karp, D.D., Fu, S., Naing, A., Tsimberidou, A.M., Moulder, S.L., Koenig, K.H., Barcenas, C.H., Kee, B.K., Fogelman, D.R., Kopetz, E.S., Meric-Bernstam, F., Janku, F.Enlace del recurso
Publicado 2021
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
16por Ramos, Jillian, Han, Lu, Li, Yan, Hagelskamp, Felix, Kellner, Stefanie M., Alkuraya, Fowzan S., Phizicky, Eric M., Fu, Dragony“…The formation of inosine at the wobble position of eukaryotic tRNAs is an essential modification catalyzed by the ADAT2/ADAT3 complex. In humans, a valine-to-methionine mutation (V144M) in ADAT3 that originated ∼1,600 years ago is the most common cause of autosomal recessive intellectual disability (ID) in Arabia. …”
Publicado 2019
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
17por Gao, Zhan, Jiang, Wanyue, Zhang, Yu, Zhang, Liping, Yi, Mengmeng, Wang, Haitao, Ma, Zengyu, Qu, Baozhen, Ji, Xiaohan, Long, Hongan, Zhang, Shicui“…We show that amphioxus (Branchiostoma japonicum) ADAT2 (BjADAT2) contains the active site ‘HxE-PCxxC’ and the key residues for target-base-binding, and amphioxus ADAT3 (BjADAT3) harbors both the N-terminal positively charged region and the C-terminal pseudo-catalytic domain important for recognition of substrates. …”
Publicado 2023
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
18por Ramos, Jillian, Proven, Melissa, Halvardson, Jonatan, Hagelskamp, Felix, Kuchinskaya, Ekaterina, Phelan, Benjamin, Bell, Ryan, Kellner, Stefanie M., Feuk, Lars, Thuresson, Ann-Charlotte, Fu, Dragony“…In humans, the wobble inosine modification is catalyzed by the heterodimeric ADAT2/3 complex. Here, we describe novel pathogenic ADAT3 variants impairing adenosine deaminase activity through a distinct mechanism that can be corrected through expression of the heterodimeric ADAT2 subunit. …”
Publicado 2020
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
19“…In eukarya, wobble inosine modification is catalyzed by the heterodimeric ADAT complex containing ADAT2 and ADAT3. Human individuals homozygous for loss of function variants in ADAT3 exhibit intellectual disability disorders. …”
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto -
20por Torres, Adrian Gabriel, Piñeyro, David, Rodríguez-Escribà, Marta, Camacho, Noelia, Reina, Oscar, Saint-Léger, Adélaïde, Filonava, Liudmila, Batlle, Eduard, Ribas de Pouplana, Lluís“…The modification in eukaryotes results from a deamination reaction of adenine that is catalyzed by the heterodimeric enzyme adenosine deaminase acting on tRNA (hetADAT), composed of two subunits: ADAT2 and ADAT3. …”
Publicado 2015
Enlace del recurso
Enlace del recurso
Enlace del recurso
Online Artículo Texto