Results 41 to 50 of about 431,100 (179)
EnsemPseU: Identifying Pseudouridine Sites With an Ensemble Approach
Pseudouridine (Ψ) is the most prevalent RNA modification, which is formed from uridine through an isomerization reaction. With the increasing availability of genomic and proteomic samples, computer-aided pseudouridine-synthase-specific Ψ ...
Yue Bi, Dong Jin, Cangzhi Jia
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Pseudouridines and Pseudouridine Synthases of the Ribosome
psi are ubiquitous in ribosomal RNA. Eubacteria, Archaea, and eukaryotes all contain psi, although their number varies widely, with eukaryotes having the most. The small ribosomal subunit can apparently do without psi in some organisms, even though others have as many as 40 or more.
J, Ofengand +7 more
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Ribosomal RNA pseudouridines and pseudouridine synthases [PDF]
Pseudouridines are found in virtually all ribosomal RNAs but their function is unknown. There are four to eight times more pseudouridines in eukaryotes than in eubacteria. Mapping 19 Haloarcula marismortui pseudouridines on the three‐dimensional 50S subunit does not show clustering.
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The coding/non-coding overlapping architecture of the gene encoding the Drosophila pseudouridine synthase. [PDF]
Background: In eukaryotic cells, each molecule of H/ACA small nucleolar RNA (snoRNA) assembles with four evolutionarily conserved core proteins to compose a specific ribonucleoprotein particle. One of the four core components has pseudouridine synthase
Giuseppe Tortoriello +9 more
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Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a positive single-stranded RNA virus, engages in complex interactions with host cell proteins throughout its life cycle. While these interactions enable the host to recognize and inhibit viral
Roberto Giambruno +16 more
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Structure of the pseudouridine synthase RsuA fromHaemophilus influenzae [PDF]
The structure of the pseudouridine synthase RsuA from Haemophilus influenza, which catalyzes the conversion of uridine to pseudouridine at a single position within 16S ribosomal RNA, has been determined at 1.59 A resolution and compared with that of Escherichia coli RsuA. The H.
Matte, A. +4 more
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Pseudouridimycin is a microbial C-nucleoside natural product that specifically inhibits bacterial RNA polymerases by binding to the active site and competing with uridine triphosphate for the nucleoside triphosphate (NTP) addition site.
Robert Schnell (332808) +8 more
core +1 more source
MU-PseUDeep: A deep learning method for prediction of pseudouridine sites
Pseudouridine synthase binds to uridine sites and catalyzes the conversion of uridine to pseudouridine (Ψ). This binding takes place in a specific context and in the conformation of nucleotides. Most machine-learning methods for Ψ site classification use
Saad M. Khan +4 more
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The Pseudouridine Synthases Proceed through a Glycal Intermediate
The pseudouridine synthases isomerize (U) in RNA to pseudouridine (Ψ), and the mechanism that they follow has long been a question of interest. The recent elucidation of a product of the mechanistic probe 5-fluorouridine that had been epimerized to the arabino isomer suggested that the Ψ synthases might operate through a glycal intermediate formed by ...
Veerareddygari, Govardhan Reddy +2 more
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Pseudouridine synthases are proviral factors for Sindbis virus in insect and mammalian cells
Alphaviruses are positive-sense, single-stranded RNA (+ssRNA) viruses transmitted by arthropod vectors to vertebrate hosts. Pseudouridine is the most prevalent RNA modification in the prototype alphavirus, Sindbis virus (SINV) genome, but the location ...
Nicole Stark +6 more
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