Results 201 to 210 of about 67,577 (255)

RNase A is inhibited by the cysteine-rich protein thionein but not by the metal-containing form metallothionein. [PDF]

Mol Cell Biochem
Trujillo-González F, Muñoz-Granados IA, Sanchez-Gaytan BL, Brambila E, Perez-Aguilar JM.   +4 more
europepmc   +1 more source

Characterisation of RT Connection and RNase H Polymorphisms in HIV-1 Subtype C in Botswana. [PDF]

Viruses
Zuze BJL, Choga WT, Moraka-Mankge NO, Choga OT, Bhebhe L, Maruapula D, Phuthego T, Mokomane M, Moyo S, Gaseitsiwe S.   +9 more
europepmc   +1 more source

YhfH functions as a tri-function RNA in Bacillus thuringiensis BMB171. [PDF]

Nucleic Acids Res
Qin J, Cai X, Zhang Y, Wang Z, Pan F, Yan B, Cai J.   +6 more
europepmc   +1 more source

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The varieties of ribonuclease P

Trends in Biochemical Sciences, 1992
Ribonuclease P is a ribozyme involved in tRNA processing that is present in all cells and organelles that synthesize tRNA. Most of our understanding of ribonuclease P derives from studies of the bacterial enzyme. This enzyme has been characterized biochemically and a secondary structure for the RNA subunit has been proposed.
S C, Darr, J W, Brown, N R, Pace
openaire   +2 more sources

Human Ribonuclease P

2001
Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
N, Jarrous, S, Altman
openaire   +2 more sources

Ribonuclease P: a ribonucleoprotein enzyme

Current Opinion in Chemical Biology, 2000
The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5' end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA-P-protein and RNase-P-RNA-precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the ...
J C, Kurz, C A, Fierke
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The enigma of ribonuclease P evolution

Trends in Genetics, 2003
The 5'-end maturation of tRNAs is catalyzed by the ribonucleoprotein enzyme ribonuclease P (RNase P) in all organisms. Here we provide, for the first time, a comprehensive overview on the representation of individual RNase P protein homologs within the Eukarya and Archaea.
Enno, Hartmann, Roland K, Hartmann
openaire   +2 more sources

Modifications of ribonuclease A induced by p-benzoquinone

Bioorganic Chemistry, 2012
The nature of ribonuclease A (RNase) modifications induced by p-benzoquinone (pBQ) was investigated using several analysis methods. SDS-PAGE experiments revealed that pBQ was efficient in producing oligomers and polymeric aggregates when RNase was incubated with pBQ.
Jisook, Kim, Albert R, Vaughn, Chris, Cho, Titus V, Albu, Ethan A, Carver   +4 more
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Structure of ribonuclease P — a universal ribozyme

Current Opinion in Structural Biology, 2006
Ribonuclease P (RNase P) is one of only two known universal ribozymes and was one of the first ribozymes to be discovered. It is involved in RNA processing, in particular the 5' maturation of tRNA. Unlike most other natural ribozymes, it recognizes and cleaves its substrate in trans. RNase P is a ribonucleoprotein complex containing one RNA subunit and
Alfredo, Torres-Larios, Kerren K, Swinger, Tao, Pan, Alfonso, Mondragón   +3 more
openaire   +2 more sources