Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate.
about
PupDB: a database of pupylated proteinsBacterial ProteasomesThe pup-proteasome system of Mycobacterium tuberculosisThe Pup-Proteasome System of MycobacteriaSystematic analysis and prediction of pupylation sites in prokaryotic proteinsProkaryotic ubiquitin-like protein modificationStructures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathwayBacterial Proteasomes: Mechanistic and Functional InsightsProkaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteinsSurvival of mycobacteria depends on proteasome-mediated amino acid recycling under nutrient limitationThe pupylation pathway and its role in mycobacteria.Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system.Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coliComputational Identification of Protein Pupylation Sites by Using Profile-Based Composition of k-Spaced Amino Acid Pairs.Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation.The Mechanism of Mycobacterium smegmatis PafA Self-PupylationMycobacterium tuberculosis prokaryotic ubiquitin-like protein-deconjugating enzyme is an unusual aspartate amidase.Game of 'Somes: Protein Destruction for Mycobacterium tuberculosis Pathogenesis.Enzyme-catalyzed protein crosslinking.Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase.The natural history of ubiquitin and ubiquitin-related domains.Pupylation-dependent and -independent proteasomal degradation in mycobacteria.Pupylation: proteasomal targeting by a protein modifier in bacteria.Fluorescent probes reveal a minimal ligase recognition motif in the prokaryotic ubiquitin-like protein from Mycobacterium tuberculosis.The regulatory significance of tag recycling in the mycobacterial Pup-proteasome system.Genetic and Proteomic Analyses of Pupylation in Streptomyces coelicolorMycobacterium tuberculosis Proteasome Accessory Factor A (PafA) Can Transfer Prokaryotic Ubiquitin-Like Protein (Pup) between SubstratesPosition-specific analysis and prediction of protein pupylation sites based on multiple features.Synthesis and evaluation of a selective fluorogenic Pup derived assay reagent for Dop, a potential drug target in Mycobacterium tuberculosis.Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis.A kinetic model for the prevalence of mono- over poly-pupylation.Identification of Serine 119 as an Effective Inhibitor Binding Site of M. tuberculosis Ubiquitin-like Protein Ligase PafA Using Purified Proteins and M. smegmatis.Identification of Protein Pupylation Sites Using Bi-Profile Bayes Feature Extraction and Ensemble Learning
P2860
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P2860
Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate.
description
2010 nî lūn-bûn
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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
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2010年学术文章
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2010年學術文章
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name
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@ast
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@en
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@nl
type
label
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@ast
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@en
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@nl
prefLabel
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@ast
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@en
Mycobacterial ubiquitin-like p ...... osphorylated pup intermediate.
@nl
P2860
P356
P1476
Mycobacterial ubiquitin-like p ...... hosphorylated pup intermediate
@en
P2093
Ethan Guth
P2860
P304
P356
10.1074/JBC.M110.189282
P407
P577
2010-11-16T00:00:00Z