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ProteomicsEpitope fine mapping by mass spectrometry: Investigations of immune complexes consisting of monoclonal anti-HpTGEKP antibody and zinc finger protein linker phospho-hexapeptides.
We describe the mass spectrometric analysis of the binding strength of a monoclonal mouse antibody (clone 18E9.D9, BioLegend, London, England) which was raised against the predominantly occuring phosphorylated linker sequence, HpTGEKP, of C2H2 zinc finger proteins (ZNF proteins) using a synthetic ...
ORGANISM(S): Homo sapiens (Human) 
2022-08-15 | PXD031150 | Pride
Item-two Off-line esi-ms Zinc finger-phosphopeptide Antiphosphopeptide-antibody Binding strength characterization 
ProteomicsCharacterization of Phosphorylation-dependent Antibody Binding to Cancer-mutated Linkers of C2H2 Zinc Finger Proteins by Intact Transition Epitope Mapping - Thermodynamic Weak-force Order Analysis.
We describe mass spectrometric antibody-peptide binding motif analyses of a monoclonal antibody (clone 18E9.D9, BioLegend, London, England) from mouse which was raised against the predominantly occuring phosphorylated linker sequence HpTGEKP of human C2H2 zinc finger proteins. As the anti-HpTGEKP an...
ORGANISM(S): Homo sapiens (Human) 
2023-01-25 | PXD035818 | Pride
Item-two Off-line esi-ms Uterine corpus endometrial carcinoma Skin cutaneous melanoma Zinc finger-phosphopeptide Antiphosphopeptide-antibody Colon and rectal adenocarcinomas 
ProteomicsQuantitative phosphoproteomics analysis uncovers the regulatory networks of ZNF322A in lung cancer cells
Cys2His2 (C2H2)-type zinc finger (ZNF) is one of the most common DNA-binding motif and plays a major role as transcription factors, which encoded by 2% of human genes. C2H2 type ZNFs are reported as proteins of great versatility, such as regulation of differentiation, development, metabolism, cell s...
ORGANISM(S): Homo sapiens (Human) 
2021-09-08 | PXD015936 | Pride
Znf322a Phosphoproteomics Human lung cancer 
UnknownIdentification of a major phosphopeptide in human tristetraprolin by phosphopeptide mapping and mass spectrometry.
Not available
S-EPMC4091943 | biostudies-literature
UnknownPhosphorylation site analysis of the anti-inflammatory and mRNA-destabilizing protein tristetraprolin.
Not available
S-EPMC2674331 | biostudies-literature
UnknownZNF322A-mediated protein phosphorylation induces autophagosome formation through modulation of IRS1-AKT glucose uptake and HSP-elicited UPR in lung cancer.
Not available
S-EPMC7310457 | biostudies-literature
UnknownPhosphoproteomic analysis of lung tissue from patients with pulmonary arterial hypertension.
Not available
S-EPMC8711668 | biostudies-literature
ProteomicsNuclear phosphoproteomics analysis of resting and IL-2-stimulated T lymphocytes
The aim of the present project was to study in detail the site-specific phosphorylation events occurring both in resting as well as in T lymphocytes stimulated with IL-2 for five minutes. For that purpose we combined SILAC-based quantitative mass spectrometry analysis with phosphopeptide enrichment ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080773 | MassIVE
ProteomicsComparative phosphoproteomic analysis of barley grains during imbibition
Seed dormancy is an indispensable trait for plants. It of barley is gradually decayed by a period of dry storage (after-ripening) or certain environmental condition. Freshly harvested (FH) and after-ripened (AR) grains have been differentially characterized by numerous studies, such as light, temper...
ORGANISM(S): Cellular Organisms 
2019-09-29 | PXD011232 | JPOST Repository
ProteomicsJPST000370-4 Dark and Bright sides of TMT tag for phosphoproteome analysis [Reanalysis: JPST000370]
The aim of this study is to figure out the mechanism of the loss of TMT labeling phosphopeptides during phosphopeptides purification by using TiO2 and IMAC and report the dark (cons) and bright (pros) sites of TMT tag for phosphoproteome analysis. [Original project description]
ORGANISM(S): Epithelial Cell 
2023-03-25 | RPXD034681 | JPOST Repository
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