Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
出版年份 2017 全文链接
标题
Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
作者
关键词
Pupylation, Prokaryotic ubiquitin-like protein Pup, <em class=EmphasisTypeItalic >Mycobacterium tuberculosis</em>, NMR, Intrinsically disordered proteins
出版物
BMC STRUCTURAL BIOLOGY
Volume 17, Issue 1, Pages -
出版商
Springer Nature
发表日期
2017-02-01
DOI
10.1186/s12900-017-0072-1
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system
- (2016) Yifat Elharar et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Crystal Structure of the Complex between Prokaryotic Ubiquitin-like Protein and Its Ligase PafA
- (2013) Jonas Barandun et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Ubiquitin-Binding Proteins: Decoders of Ubiquitin-Mediated Cellular Functions
- (2012) Koraljka Husnjak et al. Annual Review of Biochemistry
- The pupylation pathway and its role in mycobacteria
- (2012) Jonas Barandun et al. BMC BIOLOGY
- Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway
- (2012) Dennis Özcelik et al. Nature Communications
- Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli
- (2011) Francisca A Cerda-Maira et al. EMBO REPORTS
- Activity of the Mycobacterial Proteasomal ATPase Mpa Is Reversibly Regulated by Pupylation
- (2011) Cyrille L. Delley et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Proteome-wide identification of mycobacterial pupylation targets
- (2011) Christian Poulsen et al. Molecular Systems Biology
- The mycobacterial Mpa–proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus
- (2010) Frank Striebel et al. EMBO JOURNAL
- Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway
- (2010) Frank Imkamp et al. EMBO REPORTS
- Mycobacterial Ubiquitin-like Protein Ligase PafA Follows a Two-step Reaction Pathway with a Phosphorylated Pup Intermediate
- (2010) Ethan Guth et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Prokaryotic Ubiquitin-like Protein (Pup) Is Coupled to Substrates via the Side Chain of Its C-Terminal Glutamate
- (2010) Markus Sutter et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Expansion of the mycobacterial “PUPylome”
- (2010) Jeramie Watrous et al. Molecular BioSystems
- “Depupylation” of Prokaryotic Ubiquitin-like Protein from Mycobacterial Proteasome Substrates
- (2010) Kristin E. Burns et al. MOLECULAR CELL
- Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation
- (2010) Tao Wang et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Prokayrotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium tuberculosis
- (2010) Richard A. Festa et al. PLoS One
- Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein
- (2009) Shanhui Liao et al. BIOCHEMICAL JOURNAL
- A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa
- (2009) Markus Sutter et al. FEBS LETTERS
- Prokaryotic Ubiquitin-Like Protein Pup Is Intrinsically Disordered
- (2009) Xiang Chen et al. JOURNAL OF MOLECULAR BIOLOGY
- Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
- (2009) Frank Striebel et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis
- (2008) M. J. Pearce et al. SCIENCE
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreFind the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
Search