Ask about this productRelated genes to: PHOSPHO2 Blocking Peptide
- Gene:
- PHOSPHO2 NIH gene
- Name:
- phosphatase, orphan 2
- Previous symbol:
- -
- Synonyms:
- MGC22679
- Chromosome:
- 2q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-12-06
- Date modifiied:
- 2015-08-25
Related products to: PHOSPHO2 Blocking Peptide
Related articles to: PHOSPHO2 Blocking Peptide
- RNA 2'-phosphotransferase Tpt1 catalyzes the removal of an internal RNA 2'-PO4 via a two-step mechanism in which: (i) the 2'-PO4 attacks NAD+ C1'' to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii) transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-OH RNA and ADP-ribose-1'',2''-cyclic phosphate. Although Tpt1 enzymes are prevalent in bacteria, archaea, and eukarya, Tpt1 is uniquely essential in fungi, where it erases the 2'-PO4 mark installed by tRNA ligases during tRNA splicing. A Tpt1 "poison" that arrests the reaction after step 1 could aid in the design of antifungals that interdict tRNA biogenesis. Whereas our previous studies of 2''OMeNAD+ established its efficacy in poisoning Runella slithyformis Tpt1 (RslTpt1, a bacterial enzyme), its application was limited insofar as Tpt1 enzymes from fungal pathogens were unable to utilize 2''OMeNAD for step 1 catalysis. Here we report the chemical synthesis of 2''F-NAD, which proved to be a broad-spectrum poison against Tpt1 enzymes from five different taxa, including human pathogens Candida albicans and Candida auris. The resulting RNA-2'-phospho-(2''F-ADP-ribose) dead-end product remains stably trapped in a complex with Tpt1. A modified analog, 2''F-NAD-DTB, containing desthiobiotin (DTB) linked to adenine C2, provides an improved affinity-tag probe of RNA 2'-phosphate modification. - Source: PubMed
Publication date: 2026/09/03
Kasprzyk RenataGhosh ShreyaShuman Stewart - The response to lifestyle modification (LSM) in children with obesity is variable and difficult to predict. - Source: PubMed
Publication date: 2026/07/02
Gawlik-Starzyk Aneta MShmoish MichaelBereket AbdullahWasniewska Malgorzata GabrielaAntosz AleksandraSzeliga Kamila MagdalenaKırkgoz TarıkTuran SerapGuran TulayAversa TommasoCorica DomenicoWudy Stefan AHartmann Michaela FSobalska-Kwapis MartaStrapagiel DominikHochberg Ze Apos Ev - Air pollution exposure is increasingly recognized as a risk factor for chronic kidney disease (CKD), but the underlying mechanisms, especially the complex gene-environment interactions as reflected in genetic susceptibility, transcriptomic, and proteomic signatures, remain to be elucidated. - Source: PubMed
Publication date: 2026/05/09
Lu JianSun ShuaigangShang XinruDeng ZekaiWang ShunweiJiang ShiminLi Wenge - The dinucleotide molecule, 5'-phospho-2'-deoxyuridine-3'-pyrophosphate adenosine-3'-phosphate (pdUppA-3'-p) (PUA), is known to act as a highly potent inhibitor of bovine pancreatic ribonuclease A (RNase A) with = 27 nM (D. D. Leonidas , , 1999, , 10287-10297). In the present work, PUA is investigated to study the effect of different conformations on its residence time and dynamical interactions at the active site of RNase A. Two conformers of PUA, designated as closed and open in terms of their end-to-end distances, have been screened in different environments based on a wide range of global and local reactivity parameters computed using conceptual density functional theory (CDFT). In all the cases studied, the open conformation is found to be more flexible with its reactive sites predominantly localized at the terminal uracil nucleobase. The closed conformer, on the other hand, is associated more with intramolecular hydrogen bonding and van der Waals interactions at both nucleobase termini. When subjected to classical molecular dynamics (MD) simulation, the open conformer is found to dissociate rapidly from the active site of RNase A within 24-300 ns, while the closed conformer remained bound throughout the 5 µs long MD trajectory. The transition from open to closed conformation is found to stabilize the PUA-RNase A complex, lowering its free energy by nearly 25 kcal mol. The crystal structure of the PUA-RNase A complex reports the ligand molecule only in its open conformation at the active site of RNase A (N. Russo and R. Shapiro, , 1999, , 14902-14908). The closed conformer has not been detected experimentally as yet. Our results therefore indicate a hereto unexplored role of the closed conformation in the inhibition of RNase A by PUA. - Source: PubMed
Publication date: 2026/04/30
Priyadarsinee SudiptiDas ArunenduTaraphder Srabani - Skin color of poultry, an important economic trait, is related to breed, feed, environment, and other factors. In recent years, China's duck industry has developed rapidly, and duck products are welcomed by consumers. Different skin colors of ducks have different cooking methods. Black skinned duck, such as Yulin black duck, is more popular in China because they are considered more suitable for making soup, while other skin colors, such as Pekin duck, is used for roasting. In order to gain a deeper understanding of the genetic factors associated with differences in duck skin color, the transcriptomes and metabolomes of skin between Yulin black duck and Pekin duck from 15 (BSE15 vs. PSE15), 21 (BSE21 vs. PSE21) and 27 (BSE27 vs. PSE27) days of incubation were compared and analyzed. The transcriptome results showed that a total of 187 (118 up-regulated and 69 down-regulated), 417 (91 up-regulated and 326 down-regulated) and 137 (55 up-regulated and 82 down-regulated) differentially expressed genes (DEGs) were identified from BSE15 vs. PSE15, BSE21 vs. PSE21 and BSE27 vs. PSE27, respectively. The significantly enriched GO terms of biological process were positive regulation of melanin biosynthetic process, melanin biosynthetic process, cuticle development, melanin biosynthetic process from tyrosine, and melanocyte differentiation, which were potentially related to skin growth and development. Eleven significant pathways, highly enriched by DCT, TYR, ASIP, TYRP1, KIT, PHOSPHO2, CERS3, SGPP2, SPTLC3, DEGS2, PATJ, RBP7, AOX1, ETNPPL, HPGDS, and GAD1, were melanogenesis, tyrosine metabolism, vitamin B6 metabolism, sphingolipid metabolism, protein digestion and absorption, tight junction, alpha-linolenic acid metabolism, arachidonic acid metabolism, linoleic acid metabolism, nicotinate and nicotinamide metabolism, and alanine, aspartate and glutamate metabolism, which participated in regulating the development of duck skin during embryonic stage. The significantly different metabolites (SDMs) were mainly organoheterocyclic compounds, lipids and lipid-like molecules, organic oxygen compounds, organic acids and derivatives, including L-tyrosine, N-arachidonyl maleimide, glycerophospho-N-palmitoyl ethanolamine, LPE 22:4, and PC(0:0/18:0). which were mainly enriched in glycerophospholipid metabolism, arachidonic acid metabolism, linoleic acid metabolism, alpha-linoleic acid metabolism, and melanogenesis in metabolome, suggesting that these pathways may play important roles in skin development of duck during embryonic stage. Besides, the analysis of integrated transcriptome and metabolome indicated that the pathways, including glycerophospholipid metabolism, arachidonic acid metabolism, linoleic acid metabolism, and alpha-linolenic acid metabolism, could contribute to regulating skin development in embryonic duck. Our findings could help elucidate the genetic mechanisms underlying the development differences in duck skin color. Furthermore, the candidate genes and metabolites can be used to provide a valuable breeding strategy for the selection of specific duck breeds with ideal skin coloration. - Source: PubMed
Publication date: 2025/06/06
Hu ZhigangCai YingjieCao ChangHe HuaGuo ShunLi NaXin AiguoLiu Xiaolin