Proteome-wide identification of mycobacterial pupylation targets
about
PupDB: a database of pupylated proteinsBacterial ProteasomesThe pup-proteasome system of Mycobacterium tuberculosisEvolution and functional cross-talk of protein post-translational modificationsThe Pup-Proteasome System of MycobacteriaSystematic analysis and prediction of pupylation sites in prokaryotic proteinsProkaryotic ubiquitin-like protein modificationBacterial Proteasomes: Mechanistic and Functional InsightsProteasomal control of cytokinin synthesis protects Mycobacterium tuberculosis against nitric oxideProkaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteinsImproved mycobacterial protein production using a Mycobacterium smegmatis groEL1ΔC expression strainSurvival 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 coliPupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis.Uncovering ubiquitin and ubiquitin-like signaling networks.Computational 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-PupylationDatabase resources for the tuberculosis communityThe pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin.Characterization of differential pore-forming activities of ESAT-6 proteins from Mycobacterium tuberculosis and Mycobacterium smegmatisPositive-Unlabeled Learning for Pupylation Sites Prediction.Prokaryotic proteasomes: nanocompartments of degradation.A proteomic view of mycobacteria.The expanding universe of ubiquitin and ubiquitin-like modifiers.Production of recombinant proteins in Mycobacterium smegmatis for structural and functional studies.A versatile vector for mycobacterial protein production with a functional minimized acetamidase regulon.Proteomics for the Investigation of Mycobacteria.Bacterial self-resistance to the natural proteasome inhibitor salinosporamide A.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 Absence of Pupylation (Prokaryotic Ubiquitin-Like Protein Modification) Affects Morphological and Physiological Differentiation in Streptomyces coelicolor.Genetic and Proteomic Analyses of Pupylation in Streptomyces coelicolorAAA+ Machines of Protein Destruction in Mycobacteria.A further case of Dop-ing in bacterial pupylation.Position-specific analysis and prediction of protein pupylation sites based on multiple features.A kinetic model for the prevalence of mono- over poly-pupylation.CIPPN: computational identification of protein pupylation sites by using neural network.
P2860
Q21284316-FD98C681-B7F7-4B1D-BC5A-5333E05C4723Q26778726-6B13FB15-5A9C-4188-A616-BEB1AF30BE4AQ26823027-8B7BF97E-AD85-4097-8F55-E5E8E0AAFFE6Q26823238-5693FD04-30E2-4596-A139-D00FA6DFAF98Q26825089-67BB179B-BA01-4701-B36B-19BB81EB0235Q26830109-65B3C50D-C7AE-4E7A-8C89-53FDDF2618FFQ26998484-69BC7DEE-8372-42DA-BD9D-3361E6FB0400Q28073414-BA937F4C-1BC5-4DB5-8DA7-8A3FB340169DQ28487570-5F5D1F1D-1E49-4269-9B8D-7D3F3FADD744Q28817737-2A6FCB20-742D-4EAF-B7C7-7580E5E670C1Q33856372-E7C9DAC2-6893-4706-B213-1BC9373F11CBQ34332393-766C6C9D-C098-4C98-94AD-2FE0BF85A5E9Q34496647-F58A3F21-EE87-4AAF-80FE-22DAFED80AF6Q34517240-5CE9134C-1621-4C2F-A555-C4B90960786EQ35138440-4BE307AE-06AA-492F-8662-27DB833A200EQ35149828-F0B6F085-E437-4F00-AA61-9BE56766113CQ35615172-BF9AF3F1-E3C4-4EA6-8839-D38BD702EEEEQ35665107-7AF673AF-35EF-4384-88F3-617A3D51A32BQ35868210-534A67C7-3FD8-48F0-8C14-431FEA4D4937Q35949076-4126EDDB-418D-434A-828D-8FBDDC6D2A17Q36668680-5B711C1A-E235-451A-A299-8985D29855D4Q36866058-707FFF46-B353-43C8-8363-6D1C679DEE97Q37152006-F1844565-3505-4586-A69F-63681AD8C463Q37192556-5D7BF131-F1C3-4E5E-8F1C-8EF9AB586F64Q37606186-7CF89805-4909-480C-AFE0-CACFB0D2CD2CQ37897211-23FF79CC-67E0-480D-BA27-CB9DFA126929Q38018311-DCF7357F-91B0-45D0-9C85-F3F783709AC1Q38258837-C99DA4B9-6D7F-4D5D-ACA6-5B8182C723F2Q38635176-A2701DBA-2343-40D8-92EE-D36B2F166407Q38810017-4427BDC8-7B91-4111-B2FE-F3DC24CFA2E8Q39251583-FAC1405D-D50E-43B4-B15B-24EF42FC9A43Q39682745-5938803A-DD3F-4E70-8FED-A8C19C40A7F9Q39978378-0FF37305-6C3A-49BB-AE3F-041E894B849DQ40631540-B6E7B1AA-B184-4672-9DFF-A2D1EAFAE6C0Q40881763-1054C2E0-44B5-44D2-98D6-BC797549BEA6Q41050594-0BE4C59F-52E7-4D81-9603-7F811281573EQ41856812-12C36F3B-7DE4-4987-89AF-BF58F9D2B408Q41901575-8B74316C-5361-4391-8706-15FFB5214627Q46683867-75E38143-08C1-49C7-BA98-001168DF0DD2Q47192024-C4997342-B4CC-448D-A23C-D69E5309D290
P2860
Proteome-wide identification of mycobacterial pupylation targets
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
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
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh
2010年學術文章
@zh-hant
name
Proteome-wide identification of mycobacterial pupylation targets
@en
Proteome-wide identification of mycobacterial pupylation targets
@nl
type
label
Proteome-wide identification of mycobacterial pupylation targets
@en
Proteome-wide identification of mycobacterial pupylation targets
@nl
prefLabel
Proteome-wide identification of mycobacterial pupylation targets
@en
Proteome-wide identification of mycobacterial pupylation targets
@nl
P2093
P2860
P356
P1476
Proteome-wide identification of mycobacterial pupylation targets
@en
P2093
Amy Hye-Won Jeon
Anja Stefanski
Christian Poulsen
Gerold Schmitt-Ulms
Helmut E Meyer
Kai Stühler
Young-Hwa Song
P2860
P356
10.1038/MSB.2010.39
P577
2010-07-01T00:00:00Z