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References from Ubiquitylation by the GID/CTLH complex regulates the metabolic and innate immune response of macrophages to infection by Mycobacterium tuberculosis. Local targets link to admitted publications; unresolved targets remain external evidence.
Macrophages in tuberculosis: Friend or foe
10.1007/s00281-013-0388-2 · 2013 · External reference
Tuberculosis and the art of macrophage manipulation
10.1093/femspd/fty037 · 2018 · External reference
How macrophage heterogeneity affects tuberculosis disease and therapy
10.1038/s41577-024-01124-3 · 2025 · External reference
Post-translational modification control of innate immunity
10.1016/j.immuni.2016.06.020 · 2016 · External reference
Tissue macrophages: Heterogeneity and functions
10.1186/s12915-017-0392-4 · 2017 · External reference
Bag it, tag it: Ubiquitin ligases and host resistance to Mycobacterium tuberculosis
10.1016/j.tim.2022.03.010 · 2022 · External reference
The ubiquitin ligase Smurf1 functions in selective autophagy of Mycobacterium tuberculosis and anti-tuberculous host defense
10.1016/j.chom.2016.11.002 · 2017 · External reference
The ubiquitin ligase parkin mediates resistance to intracellular pathogens
10.1038/nature12566 · 2013 · External reference
An expanded lexicon for the ubiquitin code
10.1038/s41580-022-00543-1 · 2023 · External reference
E3 ubiquitin ligases: Styles, structures and functions
10.1186/s43556-021-00043-2 · 2021 · External reference
The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism
10.1091/mbc.e08-03-0328 · 2008 · External reference
Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in eukaryotic cells and dominated by homologous components, the muskelin/RanBPM/CTLH complex
10.1371/journal.pone.0075217 · 2013 · External reference
The many faces of the GID/CTLH E3 ligase complex
10.1042/bst20253074 · 2025 · External reference
Structural and functional insights into GID/CTLH E3 ligase complexes
10.3390/ijms23115863 · 2022 · External reference
Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis
2021 · External reference
Non-canonical substrate recognition by the human WDR26-CTLH E3 ligase regulates prodrug metabolism
10.1016/j.molcel.2024.04.014 · 2024 · External reference
mTORC1-CTLH E3 ligase regulates the degradation of HMG-CoA synthase 1 through the Pro/N-degron pathway
2024 · External reference
The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan
10.1080/15548627.2019.1695399 · 2020 · External reference
The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation
10.7554/elife.35528 · 2018 · External reference
The CTLH complex in cancer cell plasticity
10.1155/2019/4216750 · 2019 · External reference
Pivotal role of RanBP9 in integrin-dependent focal adhesion signaling and assembly
10.1096/fj.11-194423 · 2012 · External reference
The hGIDGID4 E3 ubiquitin ligase complex targets ARHGAP11A to regulate cell migration
10.26508/lsa.202403046 · 2024 · External reference
FAM72A degrades UNG2 through the GID/CTLH complex to promote mutagenic repair during antibody maturation
10.1038/s41467-024-52009-x · 2024 · External reference
Loss of CTLH component MAEA impairs DNA repair and replication and leads to developmental delay
10.1038/s44321-025-00352-x · 2026 · External reference
Genome-wide screen of Mycobacterium tuberculosis-infected macrophages revealed GID/CTLH complex-mediated modulation of bacterial growth
10.1038/s41467-024-53637-z · 2024 · External reference
Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes
10.1074/jbc.m112.363762 · 2012 · External reference
Using clusterProfiler to characterize multiomics data
10.1038/s41596-024-01020-z · 2024 · External reference
Pathogenicity of Mycobacterium tuberculosis is expressed by regulating metabolic thresholds of the host macrophage
10.1371/journal.ppat.1004265 · 2014 · External reference
Mitochondrial metabolism in macrophages
10.1152/ajpcell.00126.2021 · 2021 · External reference
Structural insights into the catalysis and regulation of E3 ubiquitin ligases
10.1038/nrm.2016.91 · 2016 · External reference
In search of a new paradigm for protective immunity to TB
10.1038/nrmicro3230 · 2014 · External reference
Large-scale identification of ubiquitination sites by mass spectrometry
10.1038/nprot.2013.120 · 2013 · External reference
Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
10.1038/nbt.1654 · 2010 · External reference
The ubiquitin ligase CBL and Fas-associated factor 2 cooperate to regulate the innate immune response to M. tuberculosis
10.1371/journal.ppat.1013974 · 2026 · External reference
Dynamic post-translational modification profiling of Mycobacterium tuberculosis-infected primary macrophages
10.7554/elife.51461 · 2020 · External reference
Comparative analysis of macrophage post-translational modifications during intracellular bacterial pathogen infection
2020 · External reference
Systematic and quantitative assessment of the ubiquitin-modified proteome
10.1016/j.molcel.2011.08.025 · 2011 · External reference
Meta-analysis fails to show any correlation between protein abundance and ubiquitination changes
10.1002/2211-5463.70197 · 2026 · External reference
Global proteome and ubiquitinome changes in the soluble and insoluble fractions of Q175 huntington mice brains
10.1074/mcp.ra119.001486 · 2019 · External reference
UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites
10.1038/s41594-018-0084-y · 2018 · External reference
Rewiring of the ubiquitinated proteome determines ageing in C. elegans
10.1038/s41586-021-03781-z · 2021 · External reference
An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes
2017 · External reference
Role of ubiquitination in PTEN cellular homeostasis and its implications in GB drug resistance
10.3389/fonc.2020.01569 · 2020 · External reference
Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: Implications for Alzheimer’s disease
10.1186/s13024-023-00674-9 · 2023 · External reference
Akt signaling in macrophage polarization, survival, and atherosclerosis
10.3390/ijms20112703 · 2019 · External reference
Impaired fatty acid import or catabolism in macrophages restricts intracellular growth of Mycobacterium tuberculosis
10.7554/elife.102980.3 · 2025 · External reference
SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells
10.4049/jimmunol.0902844 · 2010 · External reference
The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood
10.1182/blood.v89.6.1876 · 1997 · External reference
INPP5D regulates inflammasome activation in human microglia
10.1038/s41467-023-42819-w · 2023 · External reference
Immunometabolism governs dendritic cell and macrophage function
10.1084/jem.20151570 · 2016 · External reference
Macrophage immunometabolism: Where are we (going)?
10.1016/j.it.2017.03.001 · 2017 · External reference
Metabolic pathways in immune cell activation and quiescence
10.1016/j.immuni.2013.04.005 · 2013 · External reference
Growth of Mycobacterium tuberculosis in vivo segregates with host macrophage metabolism and ontogeny
10.1084/jem.20172020 · 2018 · External reference
Immunometabolism at the interface between macrophages and pathogens
10.1038/s41577-019-0124-9 · 2019 · External reference
Dual RNA-seq of Mtb-infected macrophages in vivo reveals ontologically distinct host-pathogen interactions
10.1016/j.celrep.2019.12.033 · 2020 · External reference
Ubiquitinomics: History, methods, and applications in basic research and drug discovery
10.1002/pmic.202200074 · 2022 · External reference
Proteomic approaches to study ubiquitinomics
10.1016/j.bbagrm.2023.194940 · 2023 · External reference
Beyond K48 and K63: Non-canonical protein ubiquitination
10.1186/s11658-020-00245-6 · 2021 · External reference
Non-proteolytic ubiquitylation in cellular signaling and human disease
10.1038/s42003-022-03060-1 · 2022 · External reference
Exploitation of Mycobacterium tuberculosis reporter strains to probe the impact of vaccination at sites of infection
10.1371/journal.ppat.1004394 · 2014 · External reference
Optimisation of bioluminescent reporters for use with mycobacteria
10.1371/journal.pone.0010777 · 2010 · External reference
Mitochondrial respiration contributes to the interferon gamma response in antigen-presenting cells
10.7554/elife.65109 · 2021 · External reference
Incorporation of macrophage immune stresses into an intracellular assay of drug tolerance in Mycobacterium tuberculosis
10.1128/aac.00795-25 · 2025 · External reference
Growing and handling of Mycobacterium tuberculosis for macrophage infection assays
10.1007/978-1-4939-6581-6_22 · 2017 · External reference
MSFragger: Ultrafast and comprehensive peptide identification in mass spectrometry-based proteomics
10.1038/nmeth.4256 · 2017 · External reference
Fast quantitative analysis of timsTOF PASEF data with MSFragger and IonQuant
10.1074/mcp.tir120.002048 · 2020 · External reference
Proteome-wide identification of ubiquitin interactions using UbIA-MS
10.1038/nprot.2017.147 · 2018 · External reference
Meta-analysis fails to show any correlation between protein abundance and ubiquitination changes
10.1002/2211-5463.70197 · ExternalCitation · doi-reference
Ubiquitinomics: History, methods, and applications in basic research and drug discovery
10.1002/pmic.202200074 · ExternalCitation · doi-reference
Growing and handling of Mycobacterium tuberculosis for macrophage infection assays
10.1007/978-1-4939-6581-6_22 · ExternalCitation · doi-reference
Macrophages in tuberculosis: Friend or foe
10.1007/s00281-013-0388-2 · ExternalCitation · doi-reference
Proteomic approaches to study ubiquitinomics
10.1016/j.bbagrm.2023.194940 · ExternalCitation · doi-reference
Dual RNA-seq of Mtb-infected macrophages in vivo reveals ontologically distinct host-pathogen interactions
10.1016/j.celrep.2019.12.033 · ExternalCitation · doi-reference
The ubiquitin ligase Smurf1 functions in selective autophagy of Mycobacterium tuberculosis and anti-tuberculous host defense
10.1016/j.chom.2016.11.002 · ExternalCitation · doi-reference
Metabolic pathways in immune cell activation and quiescence
10.1016/j.immuni.2013.04.005 · ExternalCitation · doi-reference
Post-translational modification control of innate immunity
10.1016/j.immuni.2016.06.020 · ExternalCitation · doi-reference
Macrophage immunometabolism: Where are we (going)?
10.1016/j.it.2017.03.001 · ExternalCitation · doi-reference
Systematic and quantitative assessment of the ubiquitin-modified proteome
10.1016/j.molcel.2011.08.025 · ExternalCitation · doi-reference
Non-canonical substrate recognition by the human WDR26-CTLH E3 ligase regulates prodrug metabolism
10.1016/j.molcel.2024.04.014 · ExternalCitation · doi-reference
Bag it, tag it: Ubiquitin ligases and host resistance to Mycobacterium tuberculosis
10.1016/j.tim.2022.03.010 · ExternalCitation · doi-reference
The ubiquitin ligase parkin mediates resistance to intracellular pathogens
10.1038/nature12566 · ExternalCitation · doi-reference
Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
10.1038/nbt.1654 · ExternalCitation · doi-reference
MSFragger: Ultrafast and comprehensive peptide identification in mass spectrometry-based proteomics
10.1038/nmeth.4256 · ExternalCitation · doi-reference
Large-scale identification of ubiquitination sites by mass spectrometry
10.1038/nprot.2013.120 · ExternalCitation · doi-reference
Proteome-wide identification of ubiquitin interactions using UbIA-MS
10.1038/nprot.2017.147 · ExternalCitation · doi-reference
Structural insights into the catalysis and regulation of E3 ubiquitin ligases
10.1038/nrm.2016.91 · ExternalCitation · doi-reference
In search of a new paradigm for protective immunity to TB
10.1038/nrmicro3230 · ExternalCitation · doi-reference
INPP5D regulates inflammasome activation in human microglia
10.1038/s41467-023-42819-w · ExternalCitation · doi-reference
FAM72A degrades UNG2 through the GID/CTLH complex to promote mutagenic repair during antibody maturation
10.1038/s41467-024-52009-x · ExternalCitation · doi-reference
Genome-wide screen of Mycobacterium tuberculosis-infected macrophages revealed GID/CTLH complex-mediated modulation of bacterial growth
10.1038/s41467-024-53637-z · ExternalCitation · doi-reference
Immunometabolism at the interface between macrophages and pathogens
10.1038/s41577-019-0124-9 · ExternalCitation · doi-reference
How macrophage heterogeneity affects tuberculosis disease and therapy
10.1038/s41577-024-01124-3 · ExternalCitation · doi-reference
An expanded lexicon for the ubiquitin code
10.1038/s41580-022-00543-1 · ExternalCitation · doi-reference
Rewiring of the ubiquitinated proteome determines ageing in C. elegans
10.1038/s41586-021-03781-z · ExternalCitation · doi-reference
UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites
10.1038/s41594-018-0084-y · ExternalCitation · doi-reference
Using clusterProfiler to characterize multiomics data
10.1038/s41596-024-01020-z · ExternalCitation · doi-reference
Non-proteolytic ubiquitylation in cellular signaling and human disease
10.1038/s42003-022-03060-1 · ExternalCitation · doi-reference
Loss of CTLH component MAEA impairs DNA repair and replication and leads to developmental delay
10.1038/s44321-025-00352-x · ExternalCitation · doi-reference
The many faces of the GID/CTLH E3 ligase complex
10.1042/bst20253074 · ExternalCitation · doi-reference
Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes
10.1074/jbc.m112.363762 · ExternalCitation · doi-reference
Global proteome and ubiquitinome changes in the soluble and insoluble fractions of Q175 huntington mice brains
10.1074/mcp.ra119.001486 · ExternalCitation · doi-reference
Fast quantitative analysis of timsTOF PASEF data with MSFragger and IonQuant
10.1074/mcp.tir120.002048 · ExternalCitation · doi-reference
The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan
10.1080/15548627.2019.1695399 · ExternalCitation · doi-reference
Immunometabolism governs dendritic cell and macrophage function
10.1084/jem.20151570 · ExternalCitation · doi-reference
Growth of Mycobacterium tuberculosis in vivo segregates with host macrophage metabolism and ontogeny
10.1084/jem.20172020 · ExternalCitation · doi-reference
The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism
10.1091/mbc.e08-03-0328 · ExternalCitation · doi-reference
Tuberculosis and the art of macrophage manipulation
10.1093/femspd/fty037 · ExternalCitation · doi-reference
Pivotal role of RanBP9 in integrin-dependent focal adhesion signaling and assembly
10.1096/fj.11-194423 · ExternalCitation · doi-reference
Incorporation of macrophage immune stresses into an intracellular assay of drug tolerance in Mycobacterium tuberculosis
10.1128/aac.00795-25 · ExternalCitation · doi-reference
Mitochondrial metabolism in macrophages
10.1152/ajpcell.00126.2021 · ExternalCitation · doi-reference
The CTLH complex in cancer cell plasticity
10.1155/2019/4216750 · ExternalCitation · doi-reference
The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood
10.1182/blood.v89.6.1876 · ExternalCitation · doi-reference
Beyond K48 and K63: Non-canonical protein ubiquitination
10.1186/s11658-020-00245-6 · ExternalCitation · doi-reference
Tissue macrophages: Heterogeneity and functions
10.1186/s12915-017-0392-4 · ExternalCitation · doi-reference
Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: Implications for Alzheimer’s disease
10.1186/s13024-023-00674-9 · ExternalCitation · doi-reference
E3 ubiquitin ligases: Styles, structures and functions
10.1186/s43556-021-00043-2 · ExternalCitation · doi-reference
Optimisation of bioluminescent reporters for use with mycobacteria
10.1371/journal.pone.0010777 · ExternalCitation · doi-reference
Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in eukaryotic cells and dominated by homologous components, the muskelin/RanBPM/CTLH complex
10.1371/journal.pone.0075217 · ExternalCitation · doi-reference
Pathogenicity of Mycobacterium tuberculosis is expressed by regulating metabolic thresholds of the host macrophage
10.1371/journal.ppat.1004265 · ExternalCitation · doi-reference
Exploitation of Mycobacterium tuberculosis reporter strains to probe the impact of vaccination at sites of infection
10.1371/journal.ppat.1004394 · ExternalCitation · doi-reference
The ubiquitin ligase CBL and Fas-associated factor 2 cooperate to regulate the innate immune response to M. tuberculosis
10.1371/journal.ppat.1013974 · ExternalCitation · doi-reference
The hGIDGID4 E3 ubiquitin ligase complex targets ARHGAP11A to regulate cell migration
10.26508/lsa.202403046 · ExternalCitation · doi-reference
Role of ubiquitination in PTEN cellular homeostasis and its implications in GB drug resistance
10.3389/fonc.2020.01569 · ExternalCitation · doi-reference
Akt signaling in macrophage polarization, survival, and atherosclerosis
10.3390/ijms20112703 · ExternalCitation · doi-reference
Structural and functional insights into GID/CTLH E3 ligase complexes
10.3390/ijms23115863 · ExternalCitation · doi-reference
SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells
10.4049/jimmunol.0902844 · ExternalCitation · doi-reference
Impaired fatty acid import or catabolism in macrophages restricts intracellular growth of Mycobacterium tuberculosis
10.7554/elife.102980.3 · ExternalCitation · doi-reference
The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation
10.7554/elife.35528 · ExternalCitation · doi-reference
Dynamic post-translational modification profiling of Mycobacterium tuberculosis-infected primary macrophages
10.7554/elife.51461 · ExternalCitation · doi-reference
Mitochondrial respiration contributes to the interferon gamma response in antigen-presenting cells
10.7554/elife.65109 · ExternalCitation · doi-reference
