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ProteomicsMiT/TFE factors control ER-phagy via transcriptional regulation of FAM134B
Lysosomal degradation of the endoplasmic reticulum (ER) via autophagy (ER-phagy) is emerging as a critical regulator of ER homeostasis and function1. The selective incorporation of ER fragments into nascent autophagosomes is facilitated by ER resident proteins, ER-phagy receptors, that bind the auto...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-07-15 | PXD015130 | Pride
Erphagy secretome 
ProteomicsElucidating the Linezolid response of Staphylococcus aureus USA300 (metabolic labelling)
The translation inhibitor Linezolid is an important antibiotic of last resort against multiresistant gram-positive pathogens including MRSA. Linezolid is reported to specifically inhibit extracellular virulence factors, but the molecular cause is unknown. To elucidate the physiological response of S...
ORGANISM(S): Staphylococcus aureus (strain USA300) 
2016-03-18 | PXD001622 | Pride
Metabolic labelling Linezolid Transertion Staphylococcus aureus 
ProteomicsElucidating the Linezolid response of Staphylococcus aureus USA300 (Hi3 quantification)
The translation inhibitor Linezolid is an important antibiotic of last resort against multiresistant gram-positive pathogens including MRSA. Linezolid is reported to specifically inhibit extracellular virulence factors, but the molecular cause is unknown. To elucidate the physiological response of S...
ORGANISM(S): Staphylococcus aureus 
2016-03-18 | PXD001659 | Pride
Linezolid Absolute quantification 
ProteomicsProteomic analysis of triple negative breast cancer cell lines
We analysed aquired chemotherapeutic resistance of two different triple negative breast cancer cell lines BT-549 (Doxorubicin resistance) and MDA-MB-468 (5-Fluorouracil) by comparing the proteome of the parental cell line with the resistant cell line.
ORGANISM(S): Homo sapiens (Human) 
2018-02-23 | PXD008522 | Pride
Chemotherapy resistance Triple negative breast cancer 
ProteomicsUSP32 regulates non-proteolytic LAMTOR1 ubiquitination and Ragulator function
Ubiquitination is among the most prevalent post-translational modifications regulating a great number of cellular functions, and defects in such processes contribute to many diseases. Deubiquitinating enzymes (DUBs) are essential to control the precise outcome of ubiquitin signals. The ubiquitin-spe...
ORGANISM(S): Homo sapiens (Human) 
2022-12-16 | PXD024227 | Pride
Lysosomes Ubiquitin 
ProteomicsUSP32 regulates non-proteolytic LAMTOR1 ubiquitination and Ragulator function
Ubiquitination is among the most prevalent post-translational modifications regulating a great number of cellular functions, and defects in such processes contribute to many diseases. Deubiquitinating enzymes (DUBs) are essential to control the precise outcome of ubiquitin signals. The ubiquitin-spe...
ORGANISM(S): Homo sapiens (Human) 
2022-12-16 | PXD024211 | Pride
Ubiquitin Digly Lysosome 
ProteomicsATO and Gossypol for GSC treatment
Glioblastoma is one of the deadliest malignancies worldwide and is virtually incurable due to its highly infiltrative growth and limited sensitivity to conventional treatment by radiochemotherapy. It is hypothesized that a small population of cells with a stem-like phenotype is the major culprit of ...
ORGANISM(S): Homo sapiens (Human) 
2019-03-13 | PXD009249 | Pride
Chemotherapy Gliablastoma 
ProteomicsAsparagine hydroxylation of the UBA domain in Cezanne (OTUD7B)
by DUBs need to be tightly controlled. Here, we identify asparagine hydroxylation as a novel posttranslational modification involved in the regulation of Cezanne (OTUD7B), a DUB that controls key cellular functions and signaling pathways. We demonstrate that Cezanne is a substrate for FIH1- and oxyg...
ORGANISM(S): Homo sapiens (Human) 
2020-01-24 | PXD015216 | Pride
Otu7b Deubiquitinases Hydroxylation Cezanne 
ProteomicsMass-Spectrometric analysis of SdeA Ubiquitin modification and Ubiquitination
Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C-terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transf...
ORGANISM(S): Homo sapiens (Human) 
2016-12-07 | PXD005240 | Pride
Legionella pneumophila Etd Orbitrap fusion 
ProteomicsAnalysis of SdeA modification by SidJ
Legionella pneumophila is a pathogenic gram-negative bacterium that evades host defense pathways to establish its intracellular replicative niche1. SidE family (SidEs) effectors mediate phosphoribosyl (PR)-dependent ubiquitination of host substrates and promote bacterial infection. Legionella effect...
ORGANISM(S): Homo sapiens (Human) Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) 
2019-07-16 | PXD014362 | Pride
Glutamylation Legionella pneumophila 
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