Pupylation as a signal for proteasomal degradation in bacteria-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

Pupylation as a signal for proteasomal degradation in bacteria

Published:2014-01 Issue:1 Volume:1843 Page:103-113
ISSN:0167-4889
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Author:

Striebel Frank,Imkamp Frank,Özcelik Dennis,Weber-Ban Eilika

Funder

Swiss National Science Foundation (SNSF)

National Center of Excellence in Research (NCCR) Structural Biology program of the SNSF

ETH

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference80 articles.

1. Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein;Burns;J. Biol. Chem.,2009

2. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis;Pearce;Science,2008

3. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes;Striebel;Nat. Struct. Mol. Biol.,2009

4. “Depupylation” of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates;Burns;Mol. Cell,2010

5. Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway;Imkamp;EMBO Rep.,2010

Cited by 65 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Plasticity of the proteasome-targeting signal Fat10 enhances substrate degradation;eLife;2024-07-10

2. Toxin-based screening of C-terminal tags in Escherichia coli reveals the exceptional potency of ssrA-like degrons;2024-06-14

3. Toxin-based screening of C-terminal tags in Escherichia coli reveals the exceptional potency of ssrA-like degrons;2024-06-14

4. Regulation of heme biosynthesis via the coproporphyrin dependent pathway in bacteria;Frontiers in Microbiology;2024-03-21

5. Lysine deserts and cullin-RING ligase receptors: Navigating untrodden paths in proteostasis;iScience;2023-11

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号京ICP备18003416号-3