Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation.
about
The Pup-Proteasome System of MycobacteriaProkaryotic ubiquitin-like protein modificationProteasomal control of cytokinin synthesis protects Mycobacterium tuberculosis against nitric oxideProkaryotic 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.Fate of pup inside the Mycobacterium proteasome studied by in-cell NMR.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.The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin.Prokaryotic proteasomes: nanocompartments of degradation.Fluorescent probes reveal a minimal ligase recognition motif in the prokaryotic ubiquitin-like protein from Mycobacterium tuberculosis.AAA+ Machines of Protein Destruction in Mycobacteria.CIPPN: computational identification of protein pupylation sites by using neural network.Pupylation of PafA or Pup inhibits components of the Pup-Proteasome System.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
Q26825089-C4662F40-50D8-42AC-BDE1-2FEF2AC494CCQ26998484-C054476C-69FF-4E75-A380-17E9CC9F8D37Q28487570-96D046C3-0EAF-48D5-B427-7A15A2BB112CQ28817737-98B6D07D-498B-4F11-854F-EB63B7C12B2BQ34332393-D36A8646-1811-4D55-BAB4-5E2DFC854188Q34496647-178D9127-C1D9-4626-940D-C5F378723E72Q34517240-97E6E622-9FD6-420D-9078-2800D4657DCEQ34990156-CBD4AAFE-889D-4C38-9970-02B56C833639Q35949076-28A957D0-13DB-4F89-B969-78901326A415Q36347883-707F774E-57C9-4529-A328-AE49230FF81CQ36421483-67FCB1E1-2387-41E3-BC2C-2B0E1E216957Q36866058-76D2A8A6-783E-46C2-8732-45A0D2153647Q37606186-D40114BE-BA9F-489E-A158-FB49D25DDBFCQ39978378-7BC763EF-6090-4E7E-8E10-34F032542126Q41050594-730A91D0-F2DC-4B36-B687-D9AEDAF5888EQ47192024-6F5F8038-EAEA-42DF-BEFD-1A12DB85A8F2Q47339289-08A3E464-028B-4CBF-9C80-9BB2C3B72F56Q53698033-B8720FED-C2F2-43DE-B781-B488E61606D2
P2860
Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Activity of the mycobacterial ...... sibly regulated by pupylation.
@ast
Activity of the mycobacterial ...... sibly regulated by pupylation.
@en
type
label
Activity of the mycobacterial ...... sibly regulated by pupylation.
@ast
Activity of the mycobacterial ...... sibly regulated by pupylation.
@en
prefLabel
Activity of the mycobacterial ...... sibly regulated by pupylation.
@ast
Activity of the mycobacterial ...... sibly regulated by pupylation.
@en
P2093
P2860
P356
P1476
Activity of the mycobacterial ...... sibly regulated by pupylation.
@en
P2093
Cyrille L Delley
Dennis Özcelik
Frank Striebel
Franziska M Heydenreich
P2860
P304
P356
10.1074/JBC.M111.331124
P407
P577
2011-12-30T00:00:00Z