Results 261 to 270 of about 315,883 (294)
Intracellular Delivery of Native Proteins by BioReversible Arginine Modification (BioRAM) on Amino Groups. [PDF]
Franke J +3 more
europepmc +1 more source
Transcription-replication conflict resolution by nuclear RNA interference. [PDF]
Cheng T +13 more
europepmc +1 more source
Structural insights into the coordinated regulation of the SLAH family in Arabidopsis thaliana. [PDF]
Zhang S +25 more
europepmc +1 more source
Mind the cap: Detecting degradation impurities in synthetic mRNAs. [PDF]
Nielsen D +3 more
europepmc +1 more source
Canonical transcription termination mechanisms explain a minority of operons in cyanobacteria
Cascino JA +6 more
europepmc +1 more source
Structure of theMethanothermobacter thermautotrophicusexosome RNase PH ring
The core of the exosome, a versatile multisubunit RNA-processing enzyme found in archaea and eukaryotes, includes a ring of six RNase PH subunits. This basic architecture is homologous to those of the bacterial and archaeal RNase PHs and the bacterial polynucleotide phosphorylase (PNPase). While all six RNase PH monomers are catalytically active in the
Chyan Leong Ng +3 more
openalex +3 more sources
In order to elucidate the mechanism of action of Rhizopus niveus RNase Rh, we investigated the pH profiles of the kinetic parameters of RNase RNAP Rh, a derivative of RNase Rh, and its mutant enzymes, i.e., RNase RNAP Rh H104F, RNase RNAP Rh E105Q, and RNase RNAP Rh D51N. Based on comparisons of their profiles we concluded that protonation of His104 is
Masachika Irie +9 more
openalex +3 more sources
The conformational stability of RNase Rs was determined with chemical and thermal denaturants over the pH range of 1-10. Equilibrium unfolding with urea showed that values of D(1/2) (5.7 M) and DeltaG(H(2)O) (12.8 kcal/mol) were highest at pH 5.0, its pI and the maximum conformational stability of RNase Rs was observed near pH 5.0.
Rajashree A. Deshpande +2 more
openalex +3 more sources
Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation
Equilibrium unfolding of A. niger RNase with chemical denaturants, for example GuHCl and urea, and thermal unfolding have been studied as a function of pH using fluorescence, far-UV, near-UV, and absorbance spectroscopy. Because of their ability to affect electrostatic interactions, pH and chemical denaturants have a marked effect on the stability ...
Gundampati Ravi Kumar +4 more
openalex +3 more sources
pH-Reversible Cationic RNase A Conjugates for Enhanced Cellular Delivery and Tumor Cell Killing
Intracellularly-acting therapeutic proteins are considered promising alternatives for the treatment of various diseases. Major limitations of their application are low efficiency of intracellular delivery and possible reduction of protein activity during derivatization.
Xiaowen Liu +7 more
openalex +3 more sources

