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the functional role of S100A4 in regulating endothelial cell growth and tumor metastasis involves interaction with the N-terminal half of Methionine Aminopeptidase 2.
activity is regulated by the transcription of clock genes within the clock feedback loops
The stability of p67 increases during myotube formation while inhibiting the phosphorylation of ERKs 1 and 2.
demonstrate an essential role for MetAP-2 in angiogenesis and indicate that MetAP-2 is responsible for the endothelial cell growth arrest induced by fumagillin and its derivatives
Data suggest that methionine aminopeptidase 2 plays a role in the proliferation of fibroblasts and myofibroblasts in fibrotic lung diseases and may serve as a novel pharmacologic target in idiopathic pulmonary fibrosis.
MetAP2 plays an important role in tumor cell growth and may contribute to tumorigenesis
Discovery, identification, and characterization of candidate pharmacodynamic markers of Metap2 inhibition are reported.
Results show that methionine aminopeptidase-2 (MetAP2) regulates angiogenesis in glioblastoma and identify MetAP2-specific substrates that may serve as candidates for clinical assay development.
MetAP1 and MetAP2 have roles in driving cell selectivity for a potent anti-cancer agent in synergy, by controlling glutathione redox state
Suggest MetAP2 as important regulator of proliferation/apoptosis in non-small cell lung cancers.
Nt-acetylation prevents the excision of the initiator methionine by MetAP2.
Data indicate that methionine aminopeptidase 2 (MetAP2) contains a single disulfide bond that exists in oxidized and reduced states and influences enzyme function.
The activity of unmodified, nitrated and oxidised METAP2 was assessed and it was found that nitration significantly reduced its ability to cleave a chromogenic substrate. Mass spectrometry analysis identified Tyr336 as a nitrated residue in METAP2.
Increased expression of METAP2 is associated with pilocytic astrocytoma.
This study demonstrated a hitherto-undescribed role of MetAP2 in definitive hematopoiesis and a possible link to noncanonical Wnt and ERK signaling.
the substrate specificities of Escherichia coli MetAP1, human MetAP1, and human MetAP2 were systematically profiled
Data indicate that MetAP2 expression and pp60c-src phosphorylation were decreased in NC2213 treated cells.
High expression in germinal center B cells and their neoplastic counterparts.
Divalent metal cofactors are physiologically relevant for activity of this enzyme.
MetAP protein has a role in colorectal adenocarcinoma progression
Expressed in colon cancer cells
MetAP-1 and MetAP-2 have essential functions in the control of mammalian cell proliferation
A comparison of the structual differences between Type I and Type II methionine aminopeptidases.
Discovery, identification, and characterization of candidate pharmacodynamic markers of METAP2 inhibition are reported.
This gene is a member of the methionyl aminopeptidase family and encodes a protein that binds 2 cobalt or manganese ions. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent protein. Increased expression of this gene is associated with various forms of cancer and the anti-cancer drugs fumagillin and ovalicin inhibit the protein by irreversibly binding to its active site. A pseudogene of this gene is located on chromosome 2.
methionine aminopeptidase 2
, methionyl aminopeptidase 2
, methionine aminopeptidase 2-like
, hypothetical protein
, MAP 2
, eIF-2-associated p67
, initiation factor 2-associated 67 kDa glycoprotein
, initiation factor 2-associated protein (p67)
, metAP 2
, peptidase M 2
, eIF-2-associated p67 homolog
, initiation factor 2 associated 67 kDa protein