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ProteomicsProfiling of ADAM12S regulated proteins in H1688 cells
In this project, we used SILAC quantitative proteomics to identify proteins that are differentially regulated by the short secreted form of A Disintegrin And Metalloproteinase 12, ADAM12S, in a small cell lung cancer cell line H1688. The aim of this study is to discover the proteins that are respons...
ORGANISM(S): Homo sapiens (Human) 
2021-02-15 | PXD013242 | Pride
Human Silac quantification Orbitrap elite H1688 Adam12s Lc-ms/ms 
ProteomicsIdentification of ADAM12S-interacting proteins in HeLa cells
ADAM12 is an A Disintegrin And Metalloproteinases (ADAMs). It is composed of signaling sequence, prodomain, metalloproteinase, disintegrin, cysteine-rich, EGF-like, transmembrane domains, and a cytoplasmic tail. ADAM12 is highly expressed in multiple cancers and is a diagnostic and prognostic biomar...
ORGANISM(S): Homo sapiens (Human) 
2022-02-28 | PXD009078 | Pride
Hela Interacting proteins Lc-ms/ms Adam12s Label free quantification 
ProteomicsSPECS and proteomics analysis of secreted glycosylated proteins regulated by ADAM12S
We used the secretome protein enrichment with click sugars (SPECS) method to purify the secreted glycosylated proteins and performed quantitative proteomics to identify the secreted proteins that were regulated by ADAM12S.
ORGANISM(S): Homo Sapiens 
2022-02-06 | PXD031470 |
UnknownMetalloproteinase-disintegrin ADAM12 is associated with a breast tumor-initiating cell phenotype.
Not available
S-EPMC3844617 | biostudies-literature
UnknownThe Disintegrin and Metalloprotease ADAM12 Is Associated with TGF-β-Induced Epithelial to Mesenchymal Transition.
Not available
S-EPMC4583281 | biostudies-literature
UnknownADAM12-directed ectodomain shedding of E-cadherin potentiates trophoblast fusion.
Not available
S-EPMC4816105 | biostudies-literature
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