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GenomicsQuantitative glycoproteomics reveals cellular substrate selectivity of the endoplasmic reticulum protein quality control sensors UGGT1 and UGGT2
Quantitative glycoproteomics reveals cellular substrate selectivity of the endoplasmic reticulum protein quality control sensors UGGT1 and UGGT2
PRJNA681212 | ENA
ProteomicsIdentification of Glycoproteins Associated with HIV Latently Infected Cells Using Quantitative Glycoproteomics
HIV infection is not curable due to viral latency. Compelling reports studying proteins such as CD2, PD-1, LAG-3 and TIGIT suggest that there is a distinct profile of surface proteins that can be used for targeting latently infected cells. We have recently reported that glycoproteins were differenti...
ORGANISM(S): Homo sapiens (Human) 
2016-05-23 | PXD003561 | Pride
Latency Hiv Speg Quantitative glycoproteomics 
UnknownQuantitative proteome-wide O-glycoproteomics analysis with FragPipe.
Not available
S-EPMC11648966 | biostudies-literature
UnknownLarge-scale quantitative glycoproteomics analysis of site-specific glycosylation occupancy.
Not available
S-EPMC3463725 | biostudies-literature
TranscriptomicsQuantitative glycoproteomics reveals cellular substrate selectivity of the endoplasmic reticulum protein quality control sensors UGGT1 and UGGT2
The protein quality control sensors UDP-glucose: glycoprotein glucosyltransferase (UGGT) 1 and 2 are proposed to act as gatekeepers of the early secretory pathway. They initiate rebinding to the carbohydrate-dependent chaperones calnexin and calreticulin that associate with proteins possessing monog...
ORGANISM(S): Homo sapiens 
2020-11-28 | GSE162262 | GEO
ProteomicsBloodstream infection N-glycoproteomics
Here we have performed targeted quantitative N-glycoproteomics from plasma samples of patients with confirmed positive blood culture together with age and sex matched febrile controls with negative blood culture reports. Three hundred and sixty eight potential N-glycopeptides were quantified by mass...
ORGANISM(S): Homo sapiens (Human) 
2018-04-09 | PXD009048 | Pride
Sepsis Human plasma Bloodstream infection N-glycoproteomics 
ProteomicsGlyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries
We report a LC-MS/MS O-glycoproteomics strategy using Data Independent Acquisition (DIA) mode that holds the potential for enabling direct analysis of O-glycoproteins with characterization of sites and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries. To explor...
ORGANISM(S): Homo sapiens (Human) 
2019-11-19 | PXD011063 | Pride
Glycoproteomics Mass spectrometry O-glycosylation Data independent acquisition Human serum 
ProteomicsN-glycoproteomics and proteomics in NGLY1 deficient patient-derived dermal fibroblasts
In the biological systems, several genes are involved in protein glycosylation and deglycosylation pathways. Congenital disorders of deglycosylation (CDDG) are a set of disorders which occur due to the defect in genes involved in deglycosylation pathways. The only known CDDG so far is the defect in ...
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD034364 | Pride
Proteomics Fibroblasts Human Glycoproteomics Mass spectrometry Ngly1 Congenital disorder of glycosylation Congenital disorder of deglycosylation 
UnknownQuantitative glycoproteomics of human milk and association with atopic disease.
Not available
S-EPMC9106177 | biostudies-literature
UnknownQuantitative glycoproteomics analysis identifies novel FUT8 targets and signaling networks critical for breast cancer cell invasiveness.
Not available
S-EPMC8932202 | biostudies-literature
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