Results 51 to 60 of about 4,003 (181)

Many Facets of PNPase - Uncovering the Role of PNPase in the Mitochondria [PDF]

, 2018
PNPase is a conserved 3’-5’ exoribonuclease localized in the mammalian mitochondria. Its expression is essential for embryonic development and mitochondrial homeostasis.
Shimada, Eriko
core   +1 more source

Polynucleotide phosphorylase regulates multiple virulence factors and the stabilities of small RNAs RsmY/Z in Pseudomonas aeruginosa

Frontiers in Microbiology, 2016
Post-transcriptional regulation enables bacteria to quickly response to environmental stresses. Polynucleotide phosphorylase (PNPase), which contains an N-terminal catalytic core and C-terminal RNA binding KH-S1 domains, is involved in RNA processing ...
Ronghao eChen, Yuding eWeng, Feng eZhu, Yongxin eJin, Chang eLiu, XiaoLei ePan, Bin eXia, Zhihui eCheng, Shouguang eJin, Shouguang eJin, Weihui eWu   +10 more
doaj   +1 more source

Phenotypic Characterization of PNPase Mutation and Overexpression in C. elegans [PDF]

, 2019
PNPase, polynucleotide phosphorylase, is a multifunctional exoribonuclease protein with 3` terminal oligonucleotide polymerase activity. Coded by the PNPT1 gene, the protein is associated with mitochondrial homeostasis and functions as a possible target ...
Hur, Brian J
core   +1 more source

The exoribonuclease Polynucleotide Phosphorylase influences the virulence and stress responses of yersiniae and many other pathogens

Frontiers in Cellular and Infection Microbiology, 2013
Microbes are incessantly challenged by both biotic and abiotic stressors threatening their existence. Therefore, bacterial pathogens must possess mechanisms to successfully subvert host immune defenses as well as overcome the stress associated with host ...
Jason A. Rosenzweig, Ashok K Chopra
doaj   +1 more source

RliB interacts with PNPase.

, 2014
A) Protein affinity purification using 3′ biotinylated RliB. Two biotinylated bait RNAs were used: full length RliB (RliB-B) and a control RNA (S. aureus RNAIII). Coomassie stained SDS-PAGE gel of the two elution fractions is shown.
José Marques Andrade (275739), Eduardo P. C. Rocha (7388), Cecilia Maria Arraiano (5657536), Nina Sesto (507623), Pascale Cossart (25004), Pascale Romby (155460), Éric Westhof (5657539), Marie Touchon (118515), Jiro Kondo (14526), Cristel Archambaud (507624)   +9 more
core   +1 more source

Phenotypic characterization of PNPase knockdown in C. elegans [PDF]

, 2015
The multifunctional exoribonuclease protein PNPase is implicated as a potential target for cancer therapy as well as causing mitochondrial disorders in humans, but there has yet to be a whole animal knockdown model created. In this study, C. elegans was
Lambert, Laura A
core   +1 more source

miRNA Sensor HuR Compartmentalizes Ago2‐Uncoupled miRNAs to Lipid Droplets to Buffer miRNA Activity in Mammalian Cells

The FASEB Journal, Volume 40, Issue 11, 15 June 2026.
This study revealed a dose‐dependent miRNA buffering mechanism involving extracellular export and storage of miRNA on lipid droplets. The protein HuR facilitates miRNA buffering by dissociating miRNAs from Ago2 and promoting miRNA accumulation on lipid droplets or its extracellular export, depending on cellular requirements.
Sreemoyee Chakraborty, Diptankar Bandyopadhyay, Kamalika Mukherjee, Suvendra N. Bhattacharyya   +3 more
wiley   +1 more source

Pathological PNPase variants with altered RNA binding and degradation activity affect the phenotype of bacterial and human cell models

bioRxiv
Human PNPase (hPNPase) is an essential RNA exonuclease located in mitochondria, where it contributes to RNA import from the cytoplasm, degradation of mitochondrial RNA, and R-loop homeostasis. Biallelic mutations in the hPNPase PNPT1 gene cause different
Roberto Pizzoccheri, Federica A. Falchi, Andrea Alloni, Marianna Caldarulo, Tania Camboni, Federico Zambelli, Giulio Pavesi, Cristina Visentin, C. Camilloni, S. Sertic, Federica Briani   +10 more
semanticscholar   +1 more source

Uncovering a previously unknown function of polyphosphate in polyadenylated RNA‐induced amyloidogenesis of Hfq

The FEBS Journal, Volume 293, Issue 12, Page 3588-3600, June 2026.
Polyphosphate interaction with Hfq and RNA drives phase separation and amyloid self‐assembly, uncovering a previously unrecognized role for polyP in bacterial stress responses. Our findings reveal new insights into the molecular mechanisms of RNA‐mediated phase separation, highlighting the role of polyP as a key modulator of this process. Polyphosphate
Kevin Mosca, Florian Turbant, Sambhasan Banerjee, Frank Wien, Richard R. Sinden, Véronique Arluison   +5 more
wiley   +1 more source

8‐Aminoguanine Induces Diuresis, Natriuresis, and Glucosuria by Inhibiting Purine Nucleoside Phosphorylase and Reduces Potassium Excretion by Inhibiting Rac1

Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2018
Background 8‐Aminoguanosine and 8‐aminoguanine are K+‐sparing natriuretics that increase glucose excretion. Most effects of 8‐aminoguanosine are due to its metabolism to 8‐aminoguanine.
Edwin K. Jackson, Zaichuan Mi, Thomas R. Kleyman, Dongmei Cheng   +3 more
doaj   +1 more source