A mini-hairpin shaped nascent peptide blocks translation termination by a distinct mechanism
收藏Mendeley Data2026-04-18 收录
官方服务：
资源简介：
Plasmids used in the study.
本研究中使用的质粒（Plasmids）
应用场景：
创建时间：
2025-02-17
相关数据集
Structure of a drug-like compound stalled human translation termination complex
Structure of a drug-like compound stalled human translation termination complex Descriptor: 18S rRNA, 28S rRNA, 40S ribosomal protein S10, ... Authors: Li, W, Cate, J. Deposit date: 2020-06-03 Release
Protein Data Bank Japan2026-07-01 更新50
Genome-wide effects of the antimicrobial peptide apidaecin on translation termination
The proline-rich antimicrobial peptide apidaecin (Api) inhibits bacterial protein synthesis in a distinctive way. In vitro biochemical and structural studies showed that Api binds in the nascent pepti
NIAID Data Ecosystem30
A mini-hairpin shaped nascent peptide blocks translation termination by a distinct mechanism
The mini-hairpin shaped nascent peptide that blocks translation termination was found by comprehensive proteomics approach for small ORFs overexpression.
NIAID Data Ecosystem00
Nascent polypeptide within the exit tunnel stabilizes the ribosome to counteract risky translation. Nascent polypeptide within the exit tunnel stabilizes the ribosome to counteract risky translation
Continuous translation elongation, irrespective of amino acid sequences, is a prerequisite for living organisms to produce their proteomes. However, the risk of elongation abortion is concealed within
NIAID Data Ecosystem40
Sequence diversity of apidaecin-like peptides arresting the terminating ribosome
The Proline-rich Antimicrobial Peptide (PrAMP) apidaecin (Api) inhibits translation by binding in the ribosomal nascent peptide exit tunnel, trapping release factors RF1 or RF2, and arresting ribosome
NIAID Data Ecosystem20
