ReviewBMC biology2012
The pupylation pathway and its role in mycobacteria.
Review in BMC biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed.
- Regulation of heme biosynthesis via the coproporphyrin dependent pathway in bacteria.Frontiers in microbiology · 2024Review
- Electrostatic interactions guide substrate recognition of the prokaryotic ubiquitin-like protein ligase PafA.Nature communications · 2023Article
- Identifying Pupylation Proteins and Sites by Incorporating Multiple Methods.Frontiers in endocrinology · 2022Article
- Protein degradation control and regulation of bacterial survival and pathogenicity: the role of protein degradation systems in bacteria.Molecular biology reports · 2021Review
- The Pup-Proteasome System Protects Mycobacteria from Antimicrobial Antifolates.Antimicrobial agents and chemotherapy · 2021Article
- PUP-Fuse: Prediction of Protein Pupylation Sites by Integrating Multiple Sequence Representations.International journal of molecular sciences · 2021Article
- The genetic proteome: Using genetics to inform the proteome of mycobacterial pathogens.PLoS pathogens · 2021Review
- PupStruct: Prediction of Pupylated Lysine Residues Using Structural Properties of Amino Acids.Genes · 2020Article
- New insights into the evasion of host innate immunity by Mycobacterium tuberculosis.Cellular & molecular immunology · 2020Review
- Deciphering Molecular Virulence Mechanism of Mycobacterium tuberculosis Dop isopeptidase Based on Its Sequence-Structure-Function Linkage.The protein journal · 2020Article
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- Potential of High-Affinity, Slow Off-Rate Modified Aptamer Reagents for Mycobacterium tuberculosis Proteins as Tools for Infection Models and Diagnostic Applications.Journal of clinical microbiology · 2017Article
- Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins.BMC structural biology · 2017Article
- The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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- The Absence of Pupylation (Prokaryotic Ubiquitin-Like Protein Modification) Affects Morphological and Physiological Differentiation in Streptomyces coelicolor.Journal of bacteriology · 2015Article
- Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius.Nature communications · 2015Article
- BB0323 and novel virulence determinant BB0238: Borrelia burgdorferi proteins that interact with and stabilize each other and are critical for infectivity.The Journal of infectious diseases · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pupylation is a post-translational protein modification occurring in actinobacteria through which the small, intrinsically disordered protein Pup (prokaryotic ubiquitin-like protein) is conjugated to lysine residues of proteins, marking them for proteasomal degradation. Although functionally related to ubiquitination, pupylation is carried out by different enzymes that are evolutionarily linked to bacterial carboxylate-amine ligases. Here, we compare the mechanism of Pup-conjugation to target proteins with ubiquitination, describe the evolutionary emergence of pupylation and discuss the importance of this pathway for survival of Mycobacterium tuberculosis in the host.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.