ScholarLens Back to search
2018•Unpublished venueRequires access

Impact of the P6- and P8/ P18-interactions in cleavage of model substrates by RNase P RNA with and without the specificity domain

Guanzhong Mao

Open publisher page 0 citations

Abstract

Abstract The natural trans-acting ribozyme RNase P RNA (RPR) is composed of two domains in which the catalytic (C-) domain mediates cleavage of various substrates. The C-domain alone, after removal ...

About this research paper

What this paper is about

Abstract The natural trans-acting ribozyme RNase P RNA (RPR) is composed of two domains in which the catalytic (C-) domain mediates cleavage of various substrates. The C-domain alone, after removal ...

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Abstract The natural trans-acting ribozyme RNase P RNA (RPR) is composed of two domains in which the catalytic (C-) domain mediates cleavage of various substrates. The C-domain alone, after removal ...

Key concepts: Ribozyme, Cleavage (geology), RNase P, RNA, RNase H, Chemistry, Mammalian CPEB3 ribozyme, Domain (mathematical analysis)

Related papers

Related paper 1Related paper 2Related paper 3
Back to paper searchBrowse research topicsOriginal source
Impact of the P6- and P8/ P18-interactions in cleavage of model substrates by RNase P RNA with and without the specificity domain — Research Paper | ScholarLens