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ProteomicsA “Two birds One Stone” Strategy for Site-specific Analysis of the Core Fucosylation and O-GlcNAcylation
Core fucosylation and O-GlcNAcylation are two most famous protein glycosylations and regulate diverse physiological and pathological processes in living organism. Core fucosylation is a protein glycosylation in which a L-fucose residue attaches to the innermost N-acetylglucosamine (GlcNAc) of N-glyc...
ORGANISM(S): Homo Sapiens 
2023-12-04 | PXD047486 |
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
ProteomicsCancer-associated Notch receptor variants lead to O-fucosylation defects that can deregulate Notch signaling
NOTCH1 is a transmembrane receptor that initiates the Notch signaling pathway involved in embryonic development and maintenance of adult tissue homeostasis. The extracellular part of NOTCH1 is composed largely of EGF-like domains (EGFs) many of which can be O-fucosylated by protein O-fucosyltransfer...
ORGANISM(S): Homo sapiens (Human) 
2022-10-21 | PXD036345 | Pride
O-fucosylation Egf repeat Cancer Notch Pofut1 
ProteomicsDefective O-fucosylation of EDIL3 attenuates invasion and vascular remodeling of trophoblasts via LIFR signaling pathway in preeclampsia
Preeclampsia(PE)is a severe placental disorder that affects 3%-5% of all pregnancies worldwide. The primary cause of PE is abnormal placentationduring eanly pregnancy, including poor trophoblast invasion and insutficientapiral arteriole remodeling, Protein O-ucosylation is a type of protein posttran...
ORGANISM(S): Homo Sapiens 
2025-12-25 | PXD072416 |
ProteomicsSPY mediates O-fucose modification of hundreds of proteins and sugar-dependent growth in Arabidopsis_(Part 1: HCD)
The recent discovery of SPY-catalyzed protein O-fucosylation reveals a novel mechanism for regulating nucleocytoplasmic protein functions in plants. Genetic evidence indicates important roles of SPY in diverse developmental and physiological processes, however, the upstream signal controlling SPY ac...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-05-10 | PXD038490 | Pride
O-fucosylation Aal Mass spectrometry O-glycosylation Proteomics. 
ProteomicsSPY mediates O-fucose modification of hundreds of proteins and sugar-dependent growth in Arabidopsis_(Part 2: EtHCD)
The recent discovery of SPY-catalyzed protein O-fucosylation reveals a novel mechanism for regulating nucleocytoplasmic protein functions in plants. Genetic evidence indicates important roles of SPY in diverse developmental and physiological processes, however, the upstream signal controlling SPY ac...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-05-10 | PXD038491 | Pride
O-fucosylation Proteomics Aal Mass spectrometry O-glycosylation 
ProteomicsO-Fucosylation of ADAMTSL2 Thrombospondin Type 1 Repeats is Required for Secretion and is Impacted by Geleophysic Dysplasia-Causing Mutations
A disintegrin-like and metalloprotease domain with thrombospondin type 1 repeats-like 2 (ADAMTSL2) is a matricellular protein that interacts with latent TGF-b binding protein 1 and fibrillin-1. ADAMTSL2 mutations cause an autosomal recessive connective tissue disorder named geleophysic dysplasia 1 (...
ORGANISM(S): Mus musculus (Mouse) 
2020-10-01 | PXD018902 | Pride
Geleophysic dysplasia Thrombospondin type 1 repeats Tsr glycosylation Adamtsl2 o-fucosylation 
ProteomicsO-Fucosylation of CPN20 by SPINDLY Derepresses Abscisic Acid Signaling during Seed Germination and Seedling Development--Partial Submission
We utilized ETD (Electron Transfer Dissociation)-MS/MS analysis to identify O-fucosylation sites in ectopically expressed CPN20 in mammalian cells and Arabidopsis.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-02-17 | PXD027272 | Pride
O-fucosylation Etd Lc-ms/ms Cpn20 
UnknownProtein O-fucosylation: structure and function.
Not available
S-EPMC6656592 | biostudies-literature
ProteomicsO-fucosylation of Thrombospondin Type I Repeats on Thrombospondin 1 is dispensable for trafficking to Platelets
Thrombospondin 1 (THBS1) is a secreted extracellular matrix glycoprotein that regulates a variety of cellular and physiological processes. THBS1’s diverse functions are attributed to interactions between the modular domains of THBS1 with an array of proteins found in the extracellular matrix. THBS1’...
ORGANISM(S): Mus musculus (Mouse) 
2023-02-02 | PXD037158 | Pride
Pofut2/o-fucosylation/c-mannosylation/thrombospondin 1/protein trafficking 
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