Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway - Wikidata - wikimedia - TriplyDB

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

http://www.wikidata.org/entity/Q28486761

about

Bacterial Proteasomes The pup-proteasome system of Mycobacterium tuberculosis The Pup-Proteasome System of Mycobacteria Prokaryotic ubiquitin-like protein modification Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway Bacterial Proteasomes: Mechanistic and Functional Insights Proteasomal control of cytokinin synthesis protects Mycobacterium tuberculosis against nitric oxide Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins Deubiquitinating enzymes as promising drug targets for infectious diseases.Survival of mycobacteria depends on proteasome-mediated amino acid recycling under nutrient limitation The pupylation pathway and its role in mycobacteria.Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system.Fate of pup inside the Mycobacterium proteasome studied by in-cell NMR.Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli Pupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis.Computational Identification of Protein Pupylation Sites by Using Profile-Based Composition of k-Spaced Amino Acid Pairs.Proteasomes and protein conjugation across domains of life.Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation.The Mechanism of Mycobacterium smegmatis PafA Self-Pupylation Mycobacterium tuberculosis prokaryotic ubiquitin-like protein-deconjugating enzyme is an unusual aspartate amidase.The archaeal proteasome is regulated by a network of AAA ATPases The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin.Trojan horse strategies used by pathogens to influence the small ubiquitin-like modifier (SUMO) system of host eukaryotic cells Prokaryotic proteasomes: nanocompartments of degradation.Pupylation-dependent and -independent proteasomal degradation in mycobacteria.Pupylation: proteasomal targeting by a protein modifier in bacteria.The regulatory significance of tag recycling in the mycobacterial Pup-proteasome system.Sumoylation as an Integral Mechanism in Bacterial Infection and Disease Progression.The Absence of Pupylation (Prokaryotic Ubiquitin-Like Protein Modification) Affects Morphological and Physiological Differentiation in Streptomyces coelicolor.Mycobacterium tuberculosis Proteasome Accessory Factor A (PafA) Can Transfer Prokaryotic Ubiquitin-Like Protein (Pup) between Substrates A further case of Dop-ing in bacterial pupylation.Synthesis and evaluation of a selective fluorogenic Pup derived assay reagent for Dop, a potential drug target in Mycobacterium tuberculosis.Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius.Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response Rhodococcus prokaryotic ubiquitin-like protein (Pup) is degraded by deaminase of pup (Dop).Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis.A kinetic model for the prevalence of mono- over poly-pupylation.Molecular Mechanisms of Intrinsic Streptomycin Resistance in Mycobacterium abscessus.Targeting the Proteostasis Network for Mycobacterial Drug Discovery.Identification of Serine 119 as an Effective Inhibitor Binding Site of M. tuberculosis Ubiquitin-like Protein Ligase PafA Using Purified Proteins and M. smegmatis.

P2860

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P2860

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

http://www.wikidata.org/entity/Q28486761

description

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 2010

@ast

im August 2010 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2010/10/01)

@sk

vědecký článek publikovaný v roce 2010

@cs

wetenschappelijk artikel (gepubliceerd op 2010/10/01)

@nl

наукова стаття, опублікована в жовтні 2010

@uk

مقالة علمية (نشرت في أكتوبر 2010)

@ar

name

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@ast

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@en

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@nl

type

label

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@ast

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@en

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@nl

prefLabel

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@ast

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@en

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@nl

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Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

@en

P2093

Frank Imkamp

http://www.w3.org/2001/XMLSchema#string

Frank Striebel

http://www.w3.org/2001/XMLSchema#string

Natalie Zimmermann

http://www.w3.org/2001/XMLSchema#string

P2860

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes

Structural Insights on the Mycobacterium tuberculosis Proteasomal ATPase Mpa

Modification of proteins by ubiquitin and ubiquitin-like proteins

Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein

Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes

The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus

Identification of substrates of the Mycobacterium tuberculosis proteasome

Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis

Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo

Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate

P304

791-797

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scholarly article

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10.1038/EMBOR.2010.119

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10

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11

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Eilika Weber-Ban

Dennis Özcelik

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2010-08-27T00:00:00Z

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46009896

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20798673

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2948181

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