Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
1 to 16 of 16  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, DOMAIN.
    Category: Function, Interaction, Sequences, Family & Domains.
    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
    "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.

  5. 5
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2871 other entries.

  6. 6
    "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.

  7. 7
    "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, ACTIVE SITE, MUTAGENESIS OF THR-58.
    Category: Function, Pathology & Biotech.
    Strain: H37Rv.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  8. 8
    Cited for: PHOSPHORYLATION, PROCESSING.
    Category: PTM / Processing.
    Strain: H37Rv.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 other entries.

  9. 9
    "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 58-291 IN COMPLEXES WITH THE ALPHA SUBUNIT AND WITH THE MLN-273 INHIBITOR, SUBUNIT.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  10. 10
    Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEXES WITH WILD-TYPE AND OPEN-GATE ALPHA SUBUNIT MUTANT; 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.

  11. 11
    "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) OF 58-291 IN COMPLEX WITH ALPHA SUBUNIT AND FELLUTAMIDE B INHIBITOR, ACTIVITY REGULATION.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  12. 12
    "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 MUTANT ALA-58 IN COMPLEX WITH WILD-TYPE AND OPEN-GATE ALPHA SUBUNIT MUTANT, SUBUNIT, GATED STRUCTURE, PROTEASOME ASSEMBLY PROCESS.
    Category: Pathology & Biotech, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  13. 13
    "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.

  14. 14
    "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.

  15. 15
    "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.

  16. 16
    Category: Structure.
    Source: PDB:6ODE, PDB:6OCW, PDB:6OCZ.

    This publication is mapped to 1 other entry.

1 to 16 of 16  Show
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again