DrugBank ID: db15073
DrugCentral: ribose
Synonymous :aldehydo-d-ribose | d-ribo-2,3,4,5-tetrahydroxyvaleraldehyde | d-ribose | ribose

Drug Sentece Context

Table 1. Analysis of context sentence of ribose gene in 3 abstracts.

pmid sentence
32266873 Two druggable targets, namely 3C-like proteinase (3CLpro) and 2’-O-ribose methyltransferase (2’-O-MTase) were selected in this study due to their indispensable nature in the viral life cycle. […] 3CLpro is a cysteine protease responsible for the proteolysis of replicase polyproteins resulting in the formation of various functional proteins, whereas 2’-O-MTase methylates the ribose 2’-O position of the first and second nucleotide of viral mRNA, which sequesters it from the host immune system.
32283108 Interestingly, GS-441524 addresses both enzyme active sites in a manner consistent with significant incorporation, delayed chain termination, and altered excision due to the ribose 1’-CN group, which may account for the increased antiviral effect compared to other available analogues.
32397643 The nsp16 catalytic subunit of the 2’-O-MTase is unusual in its requirement for a stimulatory subunit (nsp10) to catalyze the ribose 2’-O-methylation of the viral RNA cap.
32408699 A molecular docking analysis was carried out using 171 essential oil components with SARS-CoV-2 main protease (SARS-CoV-2 Mpro), SARS-CoV-2 endoribonucleoase (SARS-CoV-2 Nsp15/NendoU), SARS-CoV-2 ADP-ribose-1″-phosphatase (SARS-CoV-2 ADRP), SARS-CoV-2 RNA-dependent RNA polymerase (SARS-CoV-2 RdRp), the binding domain of the SARS-CoV-2 spike protein (SARS-CoV-2 rS), and human angiotensin-converting enzyme (hACE2).
32461321 For coronaviruses, RNA cap structure is first methylated at guanine N-7 (G-N-7) position by nonstructural protein 14 (nsp14), which facilitates and precedes the subsequent ribose 2’-O methylation by nsp16-nsp10 complex.
32578982 Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those observed in other coronaviruses, biochemical and structural data reveal that the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses and a potential therapeutic target.