Results 261 to 270 of about 315,883 (294)

Transcription-replication conflict resolution by nuclear RNA interference. [PDF]

open access: yesMol Cell
Cheng T   +13 more
europepmc   +1 more source

Structural insights into the coordinated regulation of the SLAH family in Arabidopsis thaliana. [PDF]

open access: yesNat Commun
Zhang S   +25 more
europepmc   +1 more source

Mind the cap: Detecting degradation impurities in synthetic mRNAs. [PDF]

open access: yesMol Ther Nucleic Acids
Nielsen D   +3 more
europepmc   +1 more source

Canonical transcription termination mechanisms explain a minority of operons in cyanobacteria

open access: yes
Cascino JA   +6 more
europepmc   +1 more source

Structure of theMethanothermobacter thermautotrophicusexosome RNase PH ring

open access: closedActa Crystallographica Section D Biological Crystallography, 2010
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

pH Profile of Kinetic Constants of RNase Rh from Rhizopus niveus and Its Mutant Enzymes towards UpU, and Possible Mechanisms of RNase Rh

open access: closedThe Journal of Biochemistry, 1994
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

Equilibrium unfolding of RNase Rs from Rhizopus stolonifer: pH dependence of chemical and thermal denaturation

open access: closedBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
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

open access: closedEuropean Biophysics Journal, 2011
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

open access: closedBiomacromolecules, 2015
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

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