Results 51 to 60 of about 20,593,893 (291)

RNase P-Mediated Sequence-Specific Cleavage of RNA by Engineered External Guide Sequences

open access: yesBiomolecules, 2015
The RNA cleavage activity of RNase P can be employed to decrease the levels of specific RNAs and to study their function or even to eradicate pathogens. Two different technologies have been developed to use RNase P as a tool for RNA knockdown.
Merel Derksen   +2 more
doaj   +1 more source

Modular Architecture of Bacterial RNase P Ribozymes as a Structural Platform for RNA Nanostructure Design

open access: yesCHIMIA, 2018
Ribonuclease P (RNase P) is a class of enzymes involved in the processing of precursor tRNAs to remove their 5'-leader sequences. Ribonuclease P enzymes are classified into two completely distinct classes, i.e.
Yuri Nozawa   +3 more
doaj   +1 more source

The deduced amino acid sequence alignment for the S-RNase (PcS34-RNase),

open access: yes, 2011
S-RNase (PdoS5-RNase), . S-RNase (PaS1-RNase), . S-RNase (PdS11-RNase), and . S-RNase (PtS8-RNase). The asterisks indicate the five amino acid residues that are different between . S-RNase and . S-RNase. Conserved nucleotides are shown on a darkened
Daniel Potter (52965)   +5 more
core   +1 more source

Playing RNase P evolution: swapping the RNA catalyst for a protein reveals functional uniformity of highly divergent enzyme forms.

open access: yesPLoS Genetics, 2014
The RNase P family is a diverse group of endonucleases responsible for the removal of 5' extensions from tRNA precursors. The diversity of enzyme forms finds its extremes in the eukaryal nucleus where RNA-based catalysis by complex ribonucleoproteins in ...
Christoph Weber   +3 more
doaj   +1 more source

Inhibition of antimicrobial resistance by RNase 3/1 chimeras in biofilm cultures of Acinetobacter baumannii

open access: yes, 2023
reservedThe worldwide spread of bacterial resistance against conventional antibiotics motivates the development of novel antimicrobial drugs. Bacterial biofilms are highly present in the hospital setting and are responsible for several types of ...
CENERE, GIOVANNI
core  

The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions

open access: yesBiomolecules, 2016
Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5’ end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life ...
Bradley P. Klemm   +6 more
doaj   +1 more source

PPR proteins shed a new light on RNase P biology. [PDF]

open access: yes, 2013
A fast growing number of studies identify pentatricopeptide repeat (PPR) proteins as major players in gene expression processes. Among them, a subset of PPR proteins called PRORP possesses RNase P activity in several eukaryotes, both in nuclei and ...
Hammani, K. (K)   +14 more
core   +1 more source

Engineered extracellular vesicles enriched with the miR‐214/199a cluster enhance the efficacy of chemotherapy in ovarian cancer

open access: yesMolecular Oncology, EarlyView.
Loss of the miR‐214/199a cluster is associated with recurrence in ovarian cancer. Engineered small extracellular vesicles (m214‐sEVs) elevate miR‐214‐3p/miR‐199a‐5p in tumor cells, suppress β‐catenin, TLR4, and YKT6 signaling, reprogram tumor‐derived sEV cargo, reduce chemoresistance and migration, and enhance carboplatin efficacy and survival in ...
Weida Wang   +12 more
wiley   +1 more source

CCDC80 suppresses high‐grade serous ovarian cancer migration via negative regulation of B7‐H3

open access: yesMolecular Oncology, EarlyView.
PAX8 is a lineage‐specific master regulator of transcription in high‐grade serous ovarian cancer (HGSC) progression. We show for the first time that PAX8 facilitates proliferation and metastasis by repressing the cell autonomous tumor suppressor CCDC80 and inducing B7‐H3 expression.
Aya Saleh   +12 more
wiley   +1 more source

Loss of IGF‐1R impairs DNA‐PKcs recruitment to chromatin leading to defective end‐joining

open access: yesMolecular Oncology, EarlyView.
IGF‐1R promotes radioresistance by facilitating DNA‐PKcs recruitment to chromatin, enabling non‐homologous end‐joining (NHEJ) repair of double‐strand breaks. Inhibition or loss of IGF‐1R disrupts this recruitment to damage sites, driving compensatory reliance on microhomology‐mediated end‐joining (MMEJ) repair.
Matthew O. Ellis   +3 more
wiley   +1 more source

Home - About - Disclaimer - Privacy