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1 to 19 of 19  Show
  1. 1
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3992 other entries.

  2. 2
    "Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity."
    Lin G., Hu G., Tsu C., Kunes Y.Z., Li H., Dick L., Parsons T., Li P., Chen Z., Zwickl P., Weich N., Nathan C.
    Mol. Microbiol. 59:1405-1416(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, ACTIVITY REGULATION, KINETIC PARAMETERS, MUTAGENESIS OF 1-MET--SER-8.
    Category: Function, Pathology & Biotech, Interaction, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  3. 3
    "Identification of substrates of the Mycobacterium tuberculosis proteasome."
    Pearce M.J., Arora P., Festa R.A., Butler-Wu S.M., Gokhale R.S., Darwin K.H.
    EMBO J. 25:5423-5432(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SUBSTRATES.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 6 other entries.

  4. 4
    "Experimental determination of translational starts using peptide mass mapping and tandem mass spectrometry within the proteome of Mycobacterium tuberculosis."
    Rison S.C., Mattow J., Jungblut P.R., Stoker N.G.
    Microbiology 153:521-528(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, DETERMINATION OF TRANSLATIONAL START SITE, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    Category: Function, PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 12 other entries.

  5. 5
    "In vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice."
    Gandotra S., Schnappinger D., Monteleone M., Hillen W., Ehrt S.
    Nat. Med. 13:1515-1520(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN VIRULENCE, DISRUPTION PHENOTYPE.
    Category: Function, Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  6. 6
    "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 323 other entries.

  7. 7
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2871 other entries.

  8. 8
    "Stoichiometric protein complex formation and over-expression using the prokaryotic native operon structure."
    Poulsen C., Holton S., Geerlof A., Wilmanns M., Song Y.H.
    FEBS Lett. 584:669-674(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY, SUBUNIT.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 13 other entries.

  9. 9
    "The Mycobacterium tuberculosis proteasome active site threonine is essential for persistence yet dispensable for replication and resistance to nitric oxide."
    Gandotra S., Lebron M.B., Ehrt S.
    PLoS Pathog. 6:E1001040-E1001040(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN PERSISTENCE, DISRUPTION PHENOTYPE.
    Category: Function, Pathology & Biotech.
    Strain: H37Rv.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  10. 10
    Cited for: PHOSPHORYLATION AT THR-84; THR-178 AND THR-202.
    Category: PTM / Processing.
    Strain: H37Rv.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 other entries.

  11. 11
    "Bacterial proteasome activator Bpa (Rv3780) is a novel ring-shaped interactor of the mycobacterial proteasome."
    Delley C.L., Laederach J., Ziemski M., Bolten M., Boehringer D., Weber-Ban E.
    PLoS ONE 9:E114348-E114348(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BPA.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 other entries.

  12. 12
    "Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate."
    Hu G., Lin G., Wang M., Dick L., Xu R.-M., Nathan C., Li H.
    Mol. Microbiol. 59:1417-1428(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 2-248 IN COMPLEXES WITH THE BETA SUBUNIT AND WITH THE MLN-273 INHIBITOR, SUBUNIT.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  13. 13
    Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF WILD-TYPE AND OPEN-GATE MUTANT IN COMPLEXES WITH BETA SUBUNIT; INHIBITOR HT1171 AND INHIBITOR GL1, ACTIVITY REGULATION, BIOTECHNOLOGY.
    Category: Function, Pathology & Biotech, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  14. 14
    "Fellutamide B is a potent inhibitor of the Mycobacterium tuberculosis proteasome."
    Lin G., Li D., Chidawanyika T., Nathan C., Li H.
    Arch. Biochem. Biophys. 501:214-220(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND FELLUTAMIDE B INHIBITOR, ACTIVITY REGULATION.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  15. 15
    "Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome."
    Li D., Li H., Wang T., Pan H., Lin G., Li H.
    EMBO J. 29:2037-2047(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF WILD-TYPE AND OPEN-GATE MUTANT IN COMPLEX WITH BETA SUBUNIT, SUBUNIT, GATED STRUCTURE, PROTEASOME ASSEMBLY PROCESS.
    Category: Pathology & Biotech, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  16. 16
    "Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome."
    Bolten M., Delley C.L., Leibundgut M., Boehringer D., Ban N., Weber-Ban E.
    Structure 24:2138-2151(2016) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:5LZP.

    This publication is mapped to 2 other entries.

  17. 17
    "Structural Basis for the Species-Selective Binding of N,C-Capped Dipeptides to the Mycobacterium tuberculosis Proteasome."
    Hsu H.C., Singh P.K., Fan H., Wang R., Sukenick G., Nathan C., Lin G., Li H.
    Biochemistry 56:324-333(2017) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:5THO, PDB:5TRY, PDB:5TS0, PDB:5TRG, PDB:5TRR, PDB:5TRS.

    This publication is mapped to 1 other entry.

  18. 18
    "Proteasome substrate capture and gate opening by the accessory factor PafE from Mycobacterium tuberculosis."
    Hu K., Jastrab J.B., Zhang S., Kovach A., Zhao G., Darwin K.H., Li H.
    J. Biol. Chem. 293:4713-4723(2018) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:6BGL, PDB:6BGO.

    This publication is mapped to 2 other entries.

  19. 19
    Category: Structure.
    Source: PDB:6ODE, PDB:6OCW, PDB:6OCZ.

    This publication is mapped to 1 other entry.

1 to 19 of 19  Show
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