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MetabolomicsSerum protein N-glycosylation changes in multiple myeloma

BACKGROUND: Multiple myeloma is characterized by clonal proliferation of malignant plasma cells in the bone marrow that produce monoclonal immunoglobulins. N-glycosylation changes of these monoclonal immunoglobulins have been reported in multiple myeloma, but previous studies on...

2022-04-27 | MTBLS676 | MetaboLights
MetabolomicsA low protein diet drives short and long-term improvements in metabolic health in a mouse model of sleeve gastrectomy

Despite the largely beneficial impact of bariatric surgery on obesity and metabolic disease, many patients continue to suffer from obesity after surgery and weight recurrence is common. The success of bariatric surgery may be impacted by diet. While bariatric surgery guidelines recommend a high-p...

2025-10-13 | MTBLS13046 | MetaboLights
MetabolomicsLow-Protein Diet Enhances Anti-Tumor Immunity in Pancreatic Cancer through Microbiota-Derived Uridine Diphosphate-Galactose
Low-protein diets (LPD) have been linked to improved metabolic health, but their role in pancreatic ductal adenocarcinoma (PDAC) immunotherapy remains unclear. Here we show that an LPD suppresses PDAC progression in male mice by remodeling the gut microbiota and activating anti-tumor immunity. LPD p...
2026-07-09 | MTBLS14989 | MetaboLights
MetabolomicsIntegration of magnetic resonance imaging and protein and metabolite CSF measurements to enable early diagnosis of secondary progressive multiple sclerosis

Molecular networks in neurological diseases are complex. Despite this fact, contemporary biomarkers are in most cases interpreted in isolation, leading to a significant loss of information and power. We present an analytical approach to scrutinize and combine information from biomarkers originati...

2018-08-13 | MTBLS558 | MetaboLights
MetabolomicsOGFOD1 enables AML chemo- and nutrient stress resistance by regulating protein synthesis

Acute Myeloid Leukemia (AML) commonly relapses after initial chemotherapy response. We assessed metabolic adaptations in chemoresistant cells in vivo before overt relapse, identifying altered branched-chain amino acid (BCAA) levels in patient-derived xenografts (PDX) and immunophenotypically iden...

2025-07-19 | MTBLS10255 | MetaboLights
ProteomicsSurveyance of chaperone-client interactions via thiol labelling
Census of apparent chaperone-client interaction using thiol reactivity probe tetraphenylethene maleimide (TPE-MI).
ORGANISM(S): Homo sapiens (Human) Sus scrofa domesticus (domestic pig) 
2022-05-19 | PXD022587 | Pride
Molecular chaperone Tetraphenylethene maleimide (tpe-mi) Denaturation Protein folding 
ProteomicsStructural probing of Hsp26 activation and client binding by quantitative cross-linking mass spectrometry
Small heat-shock proteins (sHSP) are important members of the cellular stress response in all species. Their best described function is the binding of early unfolding states and the resulting prevention of protein aggregation. All sHSPs exist as oligomers but vary in size and subunit organization. S...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-08-13 | PXD026244 | Pride
Chaperones Hsp26 Shsps Ssa1 Qxl-ms Xl-ms Refolding complex Ydj1 
ProteomicsChaperone Activation and Client Binding of a 2-Cysteine Peroxiredoxin
Many 2-Cys-peroxiredoxins (2-Cys-Prxs) serve as dual-function proteins. Active as peroxidases under non-stress conditions, they convert into effective chaperones under stress conditions. While their peroxidase activity has been extensively studied and shown to involve cycles of redox-mediated oligom...
ORGANISM(S): Leishmania infantum Photinus pyralis (Common eastern firefly) (Lampyris pyralis) 
2019-02-19 | PXD010281 | Pride
Cross-linking  chaperone activation  chaperone-client complex 
UnknownLate Embryogenesis Abundant Protein-Client Protein Interactions.
Not available
S-EPMC7412488 | biostudies-literature
ProteomicsIntramembrane client recognition potentiates the chaperone functions of calnexin
One-third of the human proteome is comprised of membrane proteins, which are particularly vulnerable to misfolding and often require folding assistance by molecular chaperones. Calnexin (CNX), which engages client proteins via its sugar-binding lectin domain, is one of the most abundant ER chaperone...
ORGANISM(S): Homo sapiens (Human) 
2022-11-09 | PXD031140 | Pride
Membrane proteins Protein quality control Molecular chaperones Calnexin 
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