Sort   by:  
 Page size 
ProteomicsMapping sites of O-fucose modification on mouse NOTCH2
The O-fucose modification sites on mouse NOTCH2 were determined by mass spectral glycoproteomic site mapping. The Extracellular Domain of mouse NOTCH2 was produced in HEK293T cells in the presence or absence of the three Fringe enzymes: Lunatic fringe, Manic fringe, or Radical fringe. The protein w...
ORGANISM(S): Homo sapiens (Human) 
2020-09-11 | PXD020431 | Pride
Notch2 Egf repeats O-fucose Fringe 
ProteomicsPOGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of FBN1
Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues including heart and lung. Through protein-protein interactions with latent TGF-beta binding protein 1 (LTBP1), microfibrils assist regulation of TGF-beta signa...
ORGANISM(S): Homo sapiens (Human) 
2021-08-06 | PXD025725 | Pride
Extracellular matrix protein Egf repeats Mass spectrometry Glycosylation Protein secretion Protein folding 
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 
ProteomicsAnalysis of endogenous NOTCH1 from POFUT1 S162L patient fibroblasts reveals the importance of the O-fucose modification on EGF12 in human development
NOTCH1 (N1) is a transmembrane receptor interacting with membrane-tethered ligands on opposing cells that mediate the direct cell-cell interaction necessary for many cell fate decisions. Protein O-fucosyltransferase 1 (POFUT1) adds O-fucose to Epidermal Growth Factor (EGF)-like repeats in the NOTCH ...
ORGANISM(S): Homo sapiens (Human) 
2024-08-02 | PXD050256 | Pride
Notch1 Mass spectrometry O-fucose Pofut1 
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 
ProteomicsModulation of the NOTCH1 pathway by LUNATIC FRINGE is dominant over that of MANIC or RADICAL FRINGE
Fringes are glycosyltransferases that transfer a GlcNAc to O-fucose residues on Epidermal Growth Factor-like (EGF) repeats. Three Fringes exist in mammals: LUNATIC FRINGE (LFNG), MANIC FRINGE (MFNG) and RADICAL FRINGE (RFNG). Fringe modification of O-fucose on EGF repeats in the NOTCH1 (N1) extracel...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-28 | PXD027619 | Pride
O-fucosylation Glycosylation Notch1 Fringe Egf-like domains 
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 
ProteomicsPoglut2/3 double knockout in mice results in neonatal lethality with reduced levels of fibrillin in lung tissues
Fibrillins, which are extensively O-glucosylated by POGLUT2 and 3, are crucial for development and cardiopulmonary function. Using primary dermal fibroblasts derived from our POGLUT 2 and 3 double knockout mouse model combined with proteomics analyses, we show that loss of O-glucose modifications on...
ORGANISM(S): Mus musculus (Mouse) 
2024-06-10 | PXD043730 | Pride
Mouse Q exactive Dermal fibroblasts Secretome Extracellular matrix 
ProteomicsLoss of POGLUT2 and 3 eliminates O-glucose at predicted sites but does not alter other modifications on EGFs
Fibrillins play a critical role in tissue/organ development and cardiopulmonary function. Here we showed that O-glucosylation of the fibrillins’ epidermal growth factor-like repeats by protein O-glucosyltransferase 2 (POGLUT2) and POGLUT3 was indispensable for in vivo function of mouse fibrillins. L...
ORGANISM(S): Mus Musculus 
2024-06-10 | PXD043827 | panorama
Sort   by:  
 Page size