| scholarly article | Q13442814 |
| P356 | DOI | 10.1111/FEBS.14086 |
| P698 | PubMed publication ID | 28440944 |
| P50 | author | Eyal Gur | Q43273511 |
| Nir Hecht | Q85416091 | ||
| P2093 | author name string | Michael M Meijler | |
| Shai Schlussel | |||
| Yifat Elharar | |||
| P2860 | cites work | Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway | Q27671633 |
| The ubiquitin code | Q28265104 | ||
| Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis | Q28486486 | ||
| Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes | Q28486639 | ||
| "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates | Q28486654 | ||
| Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway | Q28486761 | ||
| The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus | Q28486892 | ||
| Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis | Q28487196 | ||
| Prokaryotic ubiquitin-like protein pup is intrinsically disordered | Q28487221 | ||
| The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide | Q28487442 | ||
| Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo | Q28501857 | ||
| The Mycobacterium tuberculosis proteasome active site threonine is essential for persistence yet dispensable for replication and resistance to nitric oxide | Q33658714 | ||
| Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates | Q33876875 | ||
| Survival of mycobacteria depends on proteasome-mediated amino acid recycling under nutrient limitation | Q34332393 | ||
| Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system. | Q34517240 | ||
| Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate. | Q34575916 | ||
| Fate of pup inside the Mycobacterium proteasome studied by in-cell NMR. | Q34990156 | ||
| Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein. | Q34990851 | ||
| Recombineering mycobacteria and their phages | Q36414625 | ||
| Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase. | Q36779637 | ||
| Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli | Q37600115 | ||
| Regulated proteolysis in Gram-negative bacteria--how and when? | Q37948597 | ||
| Pupylation-dependent and -independent proteasomal degradation in mycobacteria | Q38583466 | ||
| The increasing complexity of the ubiquitin code | Q38845500 | ||
| Bacterial proteasome and PafA, the pup ligase, interact to form a modular protein tagging and degradation machine | Q43902826 | ||
| A kinetic model for the prevalence of mono- over poly-pupylation | Q46683867 | ||
| Development of a fluorescence anisotropy-based assay for Dop, the first enzyme in the pupylation pathway. | Q46712078 | ||
| P433 | issue | 12 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 1804-1814 | |
| P577 | publication date | 2017-04-25 | |
| P1433 | published in | FEBS Journal | Q1388041 |
| P1476 | title | The regulatory significance of tag recycling in the mycobacterial Pup-proteasome system | |
| P478 | volume | 284 |
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