نتایج جستجو برای: rnase

تعداد نتایج: 8269  

Journal: :The Journal of biological chemistry 1979
P Blackburn B L Jailkhani

Several specific modifications, both proteolytic and chemical, have been performed on RNase A. The ability of each of these RNase A derivatives to bind the human placental RNase inhibitor has been determined in competition binding assays. The interaction depends upon the native conformation of the enzyme. Loss of active site residues His-12 and His-119, along with auxiliary residues Lys-7, Phe-...

Journal: :Analytica Chimica Acta 2021

Metal ions homeostasis plays an important role in biological processes. The ability to detect the concentration of metal fluids is often challenged by obvious interference or competitive binding nature other alkaline metals ions. Common analytical techniques employed for detection are electrochemical, fluorescence and colorimetric methods. However, most reported sensors complicated, time-consum...

Journal: :Trends in biochemical sciences 2006
Donald Evans Steven M Marquez Norman R Pace

Ribonuclease P (RNase P) is an endonuclease involved in processing tRNA. It contains both RNA and protein subunits and occurs in all three domains of life: namely, Archaea, Bacteria and Eukarya. The RNase P RNA subunits from bacteria and some archaea are catalytically active in vitro, whereas those from eukaryotes and most archaea require protein subunits for activity. RNase P has been characte...

Journal: :RNA 2006
Tim J M Welting Bastiaan J Kikkert Walther J van Venrooij Ger J M Pruijn

RNase MRP is a eukaryotic endoribonuclease involved in nucleolar and mitochondrial RNA processing events. RNase MRP is a ribonucleoprotein particle, which is structurally related to RNase P, an endoribonuclease involved in pre-tRNA processing. Most of the protein components of RNase MRP have been reported to be associated with RNase P as well. In this study we determined the association of thes...

Journal: :Journal of Horticultural Research 2022

Abstract Calcium ions are involved in plant self-incompatibility response as important signaling substances cells. In the sporophytic response, Ca 2+ enters stigma papilla cells and plays a key role inhibiting incompatible pollen tube growth. gametophytic reaction of Papaveraceae, female determinants style ( PrsS ) male PrpS recognize each other, promote extracellular influx into tube, destroy ...

Journal: :Angewandte Chemie 2021

SARS-CoV-2 In their Communication on page 21662, Xinjing Tang et al. report the efficient inhibition of using chimeric antisense oligonucleotides through RNase L activation.

2012
Mario Krehan Christian Heubeck Nicolas Menzel Peter Seibel Astrid Schön

RNase P processes the 5'-end of tRNAs. An essential catalytic RNA has been demonstrated in Bacteria, Archaea and the nuclei of most eukaryotes; an organism-specific number of proteins complement the holoenzyme. Nuclear RNase P from yeast and humans is well understood and contains an RNA, similar to the sister enzyme RNase MRP. In contrast, no protein subunits have yet been identified in the pla...

Journal: :Biological & pharmaceutical bulletin 2014
Hiroko Kobayashi Naomi Motoyoshi Tadashi Itagaki Norio Inokuchi

Here, we determined the sequence of a cDNA encoding a guanylic acid-specific ribonuclease (RNase He1) from Hericium erinaceus that exhibits high sequence identity (59%) with RNase Po1, an enzyme with anti-cancer activity and which is found in Pleurotus ostreatus. RNase He1 and RNase Po1 have similar structures and heat stabilities; hence, RNase He1 may also have potential as an anti-cancer agen...

Journal: :International journal of molecular sciences 2016
Franziska Rademacher Maren Simanski Jürgen Harder

RNase 7 belongs to the RNase A superfamily and exhibits a broad spectrum of antimicrobial activity against various microorganisms. RNase 7 is expressed in human skin, and expression in keratinocytes can be induced by cytokines and microbes. These properties suggest that RNase 7 participates in innate cutaneous defense. In this review, we provide an overview about the role of RNase 7 in cutaneou...

Journal: :Bioscience, biotechnology, and biochemistry 2004
Hyongi Chon Rikita Nakano Naoto Ohtani Mitsuru Haruki Kazufumi Takano Masaaki Morikawa Shigenori Kanaya

The gene encoding RNase HIII from the thermophilic bacterium Bacillus stearothermophilus was cloned and overexpressed in Escherichia coli, and the recombinant protein (Bst-RNase HIII) was purified and biochemically characterized. Bst-RNase HIII is a monomeric protein with 310 amino acid residues, and shows an amino acid sequence identity of 47.1% with B. subtilis RNase HIII (Bsu-RNase HIII). Th...

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