Results 91 to 100 of about 20,593,893 (291)
Adenosine triphosphate as a modulator of protein interactions and stability
FEBS Open Bio, EarlyView.ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source
Inhibition of Bacterial RNase P RNA by Phenothiazine Derivatives
Biomolecules, 2016 There is a need to identify novel scaffolds and targets to develop new antibiotics. Methylene blue is a phenothiazine derivative, and it has been shown to possess anti-malarial and anti-trypanosomal activities.
Shiying Wu +2 more
doaj +1 more source
Towards reconstitution of human RNase P protein subunits with human and bacterial RNase P RNAs [PDF]
, 2011 2011 Denman Undergraduate Research Forum Winner,1st PlaceRNase P is an endoribonuclease that catalyzes the removal of 5'-leaders in precursor tRNAs (pre-tRNAs), and it functions in all three domains of life as a ribonucleoprotein (RNP).
Ekeke, Chigozirim
core
Protocol for quantifying miRNA trafficking across the endosomal membrane
FEBS Open Bio, EarlyView.An in vitro protocol measures miRNA uptake into endosomes isolated from mammalian cell extracts, which are free of subcellular contaminants. Performed at 37 °C in the presence of ATP, it ensures the import of single‐stranded miRNA into the endosomal lumen.
Syamantak Ghosh +2 more
wiley +1 more source
hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes. [PDF]
, 1999 RNase MRP is a ribonucleoprotein particle involved in the processing of pre-rRNA. The RNase MRP particle is structurally highly related to the RNase P particle, which is involved in pre-tRNA processing.
Venrooij, W.J.W. van +2 more
core +1 more source
Fusogenic RNA Nanomodules for Fusion‐Mediated and Multiplexed siRNA Delivery
Advanced Functional Materials, EarlyView.A fusogenic lipid‐layered RNA nanomodules (L‐CRAMs) enable high‐capacity and long‐lasting siRNA delivery through membrane fusion. These nanomodules carry exceptionally large siRNA payloads, avoid conventional endosomal uptake, and release multiple functional siRNAs through Dicer‐mediated processing.
Sunghyun Moon +5 more
wiley +1 more source
Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components
Cell ReportsSummary: Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities. It is an endonuclease related to RNase P, which processes pre-tRNAs and pre-tRNA-like substrates.
Rui Che +5 more
doaj +1 more source
Characterization of one new non-S-RNase of Armeniaca cathayana
Czech Journal of Genetics and Plant Breeding, 2019 Armeniaca cathayana, a new species described in 2010, belongs to gametophytic self-incompatibility (GSI) system which is under S-allele control. One new non-S-ribonuclease (non-S-RNase) was found in A. cathayana through comparing its nucleotide and amino
Mengpei Liu +4 more
doaj +1 more source
Nanomaterial Strategies for Pulmonary Delivery of Immunotherapeutics in Lung Cancer Treatment
Advanced Healthcare Materials, EarlyView.Inhalable immunotherapeutic nanomedicines enable organ‐selective immune modulation by overcoming pulmonary delivery barriers and concentrating therapy within lung tumors. This Review defines how nanomaterial properties govern airway deposition, retention, cellular partitioning, and immune activation across vaccines, checkpoint blockade, STING agonists,
Han Zhang, Wei Tang
wiley +1 more source
Discovery of a mini-RNase P in archaea [PDF]
Proceedings of the National Academy of Sciences, 2010 The remarkable and unexpected finding of an abbreviated version of archaeal RNase P RNA reported by Lai et al. in PNAS (1) raises the proverbial question: Which came first, the chicken or the egg? However, given nature's tinkering ability, this finding hints at the possibility of independent evolution of domains in biological catalysts. Lai et al.
openaire +2 more sources