mAm methyltransferase PCIF1 is essential for aggressiveness of gastric cancer cells by inhibiting TM9SF1 mRNA translation.

PCIF1 (phosphorylated CTD interacting factor 1) is the first reported RNA N6,2'-O-dimethyladenosine (mAm) methyltransferase. However, the pathological significance of PCIF1 and mAm modification remains unknown. Here we find that both PCIF1 expression and mAm modification are significantly elevated in gastric cancer tissues.

Colorimetric detection of ATP by inhibiting the Peroxidase-like activity of carbon dots.

Adenosine triphosphate (ATP) is the main energy currency for cells and an important biomolecule involved in cellular reactions, whose abnormal levels are closely related to physical disease, thus it is extremely important to establish a convenient, fast and simple ATP monitoring method. Toward this end, we developed a facile method for colorimetric detection of ATP on the basis of the inhibiting effect of ATP on the peroxidase-like activity of carbon dots (CDs). The detection principle of this method was utilizing the peroxidase-like activity of CDs, which catalyze the oxidation of 3,3',5,5'-tetramethylbenzidine (TMB) by HO to generate blue products.

Metal-free colorimetric detection of pyrophosphate ions by the peroxidase-like activity of ATP.

Pyrophosphate (PO, PPi) plays a vital role in ecological environment. Its elevated levels in water bodies can lead to eutrophication. Hence, its detection is extremely significant.

Integrated characterization of SARS-CoV-2 genome, microbiome, antibiotic resistance and host response from single throat swabs.

The ongoing coronavirus disease 2019 (COVID-19) pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection, poses a severe threat to humanity. Rapid and comprehensive analysis of both pathogen and host sequencing data is critical to track infection and inform therapies. In this study, we performed unbiased metatranscriptomic analysis of clinical samples from COVID-19 patients using a recently developed RNA-seq library construction method (TRACE-seq), which utilizes tagmentation activity of Tn5 on RNA/DNA hybrids.

Enhancing the peroxidase activity and decreasing the protease activity of ficin with rational modification and its application to one-step colorimetric detection of glucose.

Ficin has dual enzyme activity, i.e., protease and peroxidase-like activity.

Transposase-assisted tagmentation of RNA/DNA hybrid duplexes.

Tn5-mediated transposition of double-strand DNA has been widely utilized in various high-throughput sequencing applications. Here, we report that the Tn5 transposase is also capable of direct tagmentation of RNA/DNA hybrids in vitro. As a proof-of-concept application, we utilized this activity to replace the traditional library construction procedure of RNA sequencing, which contains many laborious and time-consuming processes.

Ficin encapsulated in mesoporous metal-organic frameworks with enhanced peroxidase-like activity and colorimetric detection of glucose.

Ficin has been reported to possess peroxidase activity, but its applications in some respects have been limited because of its relatively low activity. Herein, a mesoporous metal-organic framework, PCN-333(Fe), was synthesized, which was selected to encapsulate ficin to form ficin@PCN-333(Fe). Compared with ficin, the peroxidase-like activity of ficin@PCN-333(Fe) toward 3,3',5,5'-tetramethylbenzidine (TMB) oxidation was about 3 times increase in the presence of HO, and followed classical Michaelis-Menten model.

Enhancing the peroxidase-like activity of ficin by rational blocking thiol groups for colorimetric detection of biothiols.

The peroxidase-like activity of ficin is relatively low, which limits its application. It was found that thiol groups of ficin could inhibit its peroxidase-like activity. So, two procedures, i.

Base-Resolution Mapping Reveals Distinct mA Methylome in Nuclear- and Mitochondrial-Encoded Transcripts.

Gene expression can be post-transcriptionally regulated via dynamic and reversible RNA modifications. N-methyladenosine (mA) is a recently identified mRNA modification; however, little is known about its precise location and biogenesis. Here, we develop a base-resolution mA profiling method, based on mA-induced misincorporation during reverse transcription, and report distinct classes of mA methylome in the human transcriptome.