Hospital biosecurity capacitation: Analysis and recommendations for the prevention and control of COVID-19.

The outbreak of the coronavirus disease 2019 (COVID-19) in December 2019 highlighted several concerns regarding hospital biosafety capacitation in the People's Republic of China, although the epidemic is now under control. This study examined the primary problems related to hospital biosecurity, including the absence of a hospital emergency system, inadequate management and control of nosocomial infection, limited hospital laboratory capacity, and poor hospital admission capacity. Accordingly, this study puts forward the following countermeasures and suggestions for hospitals to deal with future biosecurity events, such as a major epidemic: first, biosecurity management systems and emergency response mechanisms in hospitals need to be set up; second, the investment and guarantee mechanisms for hospital biosecurity construction should be improved; third, the capacity building of biosecurity incident management requires special attention in general hospitals; and finally, comprehensive plans need to be developed for the integrated construction of medical treatment and prevention facilities through disease-control systems.

Nitrogen-doped graphene aerogel as both a sulfur host and an effective interlayer for high-performance lithium-sulfur batteries.

Lithium-sulfur batteries have attracted great concern because of the high theoretical capacity of sulfur (1675 mA h g). However, the poor electrical conductivity and volumetric expansion of sulfur along with the dissolution of lithium polysulfides largely limit their practical application. In this study, nitrogen-doped graphene aerogel (NGA) with high nitrogen content and porosity is used as a host for the impregnation of sulfur.

Division of Labor in an Oligomer of the DEAD-Box RNA Helicase Ded1p.

Most aspects of RNA metabolism involve DEAD-box RNA helicases, enzymes that bind and remodel RNA and RNA-protein complexes in an ATP-dependent manner. Here we show that the DEAD-box helicase Ded1p oligomerizes in the cell and in vitro, and unwinds RNA as a trimer. Two protomers bind the single-stranded region of RNA substrates and load a third protomer to the duplex, which then separates the strands.

Preparation and characterization of a composite hydrogel with graphene oxide as an acid catalyst.

In this study, a facile method for synthesizing a novel graphene oxide/pyrrole-formaldehyde (GOP-1) composite hydrogel was developed via in situ polymerization of pyrrole and formaldehyde in the presence of graphene oxide sheets without any additional catalyst. During the polymerization, graphene oxide can act as a two-dimensional template to regulate the aggregation state of polymer and as an acid catalyst to accelerate the reaction rate of pyrrole and formaldehyde. The morphology and microstructure were investigated by scanning electron microscopy, transmission electron microscopy, and X-ray diffraction, respectively.

Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro.

The DEAD-box proteins CYT-19 in Neurospora crassa and Mss116p in Saccharomyces cerevisiae are general RNA chaperones that function in splicing mitochondrial group I and group II introns and in translational activation. Both proteins consist of a conserved ATP-dependent RNA helicase core region linked to N and C-terminal domains, the latter with a basic tail similar to many other DEAD-box proteins. In CYT-19, this basic tail was shown to contribute to non-specific RNA binding that helps tether the core helicase region to structured RNA substrates.

DEAD-box proteins unwind duplexes by local strand separation.

DEAD-box proteins catalyze ATP-driven, local structural changes in RNA or RNA-protein complexes (RNP) during which only few RNA base pairs are separated. It is unclear how duplex unwinding by DEAD-box proteins differs from unwinding by canonical helicases, which can separate many base pairs by directional and processive translocation on the nucleic acid, starting from a helical end. Here, we show that two different DEAD-box proteins, Ded1p and Mss116p, can unwind RNA duplexes from internal as well as terminal helical regions and act on RNA segments as small as two nucleotides flanked by DNA.

Do DEAD-box proteins promote group II intron splicing without unwinding RNA?

The DEAD-box protein Mss116p promotes group II intron splicing in vivo and in vitro. Here we explore two hypotheses for how Mss116p promotes group II intron splicing: by using its RNA unwinding activity to act as an RNA chaperone or by stabilizing RNA folding intermediates. We show that an Mss116p mutant in helicase motif III (SAT/AAA), which was reported to stimulate splicing without unwinding RNA, retains ATP-dependent unwinding activity and promotes unfolding of a structured RNA.

Amelioration of osteoarthritis by intra-articular hyaluronan synthase 2 gene therapy.

Osteoarthritis (OA) is a chronic, degenerative disorder of multifactorial aetiology, characterized by loss of articular cartilage and periarticular bone remodelling. Goals of managing OA include controlling pain, maintaining and improving function and health-related quality of life, and limiting functional impairment. Although several managements had been proved to ameliorate the symptoms of osteoarthritis, no methods could cure it thoroughly.

DEAD-box-protein-assisted RNA structure conversion towards and against thermodynamic equilibrium values.

RNAs in biological processes often interconvert between defined structures. These RNA structure conversions are assisted by proteins and are frequently coupled to ATP hydrolysis. It is not well understood how proteins coordinate RNA structure conversions and which role ATP hydrolysis has in these processes.

Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity.

The RNA-catalyzed splicing of group I and group II introns is facilitated by proteins that stabilize the active RNA structure or act as RNA chaperones to disrupt stable inactive structures that are kinetic traps in RNA folding. In Neurospora crassa and Saccharomyces cerevisiae, the latter function is fulfilled by specific DEAD-box proteins, denoted CYT-19 and Mss116p, respectively. Previous studies showed that purified CYT-19 stimulates the in vitro splicing of structurally diverse group I and group II introns, and uses the energy of ATP binding or hydrolysis to resolve kinetic traps.

The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases.

Helicases unwind RNA or DNA duplexes and displace proteins from nucleic acids in an ATP-dependent fashion. To unwind duplexes, helicases typically load onto one of the two nucleic acid strands, usually at a single-stranded region, and then translocate on this strand in a unidirectional fashion, thereby displacing the complementary DNA or RNA. Here we show that the DEAD-box RNA helicase Ded1 unwinds duplexes in a different manner.

RNA helicases: versatile ATP-driven nanomotors.

RNA helicases are a large family of molecular motors that utilize nucleoside triphosphates to unwind RNA duplexes and to remodel RNA protein complexes. In this review, we discuss the structure and function of RNA helicases with an emphasis on the potential application of these enzymes to control conformational changes in nanoassemblies that contain RNA.

ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1.

DEAD-box RNA helicases, which are involved in virtually all aspects of RNA metabolism, are generally viewed as enzymes that unwind RNA duplexes or disrupt RNA-protein interactions in an ATP-dependent manner. Here, we show in vitro that the DEAD-box protein DED1 from Saccharomyces cerevisiae promotes not only RNA unwinding but also strand annealing, the latter in such a profound fashion that the physical limit for a bimolecular association rate constant is approached. We further demonstrate that DED1 establishes an ATP-dependent steady state between unwinding and annealing, which enables the enzyme to modulate the balance between the two opposing activities through ATP and ADP concentrations.

Cloning, expression, and genomic structure of a novel human Rap2 interacting gene (RPIP9).

During a large-scale screen of a human fetal brain cDNA library, a full-length cDNA encoding a novel Rap2 interacting protein was isolated and sequenced. The cDNA is 3397bp long and has a predicted open reading frame encoding a protein of 329 aa. The predicted protein shows high homology to mouse and human RPIP8, and has a RUN domain near its C-terminus.

Cloning and identification of a cDNA that encodes a novel human protein with thrombospondin type I repeat domain, hPWTSR.

A cDNA was isolated from the fetal brain cDNA library by high throughput cDNA sequencing. The 2390 bp cDNA with an open reading fragment (ORF) of 816 bp encodes a 272 amino acids putative protein with a thrombospondin type I repeat (TSR) domain and a cysteine-rich region at the N-terminus, so it is named hPWTSR. We used Northern blot detected two bands with length of about 3 kb and 4 kb respectively, which expressed in human adult tissues with different intensities.

Cloning and identification of a novel cDNA which may be associated with FKBP25.

A 1209 bp novel cDNA with a putative open reading frame of 627 bp that has an overlapped fragment of 527 bp with FKBP25 was isolated from a human fetal brain library. Northern Blot analysis detected a signal about 1.5 kb that suggests it is a full-length cDNA.

Cloning and expression of a novel retinoblastoma binding protein cDNA, RBBP10.

A 2860-bp cDNA was isolated from a human fetal brain cDNA library by high throughput cDNA sequencing, which encodes a putative protein with 186 amino acids. The putative protein shares 90.7% identity with rat pBOG (3403163) and shares 93.

Cloning and expression of a novel human galectin cDNA, predominantly expressed in placenta(1).

A novel human galectin cDNA (PPL13) was isolated by screening a human 18-week fetal brain library. The mRNA was predominantly expressed in placenta, while the expression of it was not or barely detectable in heart, brain, lung, liver, skeletal muscle, kidney, and pancreas by Northern blot. COS-7 cells transfected with cDNA encoding human PPL13 sequestered the protein in nuclei although it lacked any known nuclear localization signal.

Cloning and expression pattern of a spermatogenesis-related gene, BEX1, mapped to chromosome Xq22.

Through screening a human fetal brain cDNA library, a cDNA similar to the mouse Bex1 was isolated. This new gene was named brain expressed X-linked protein 1 (BEX1). Northern blot analysis revealed a 1.