An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
about
The GOLPH3 pathway regulates Golgi shape and function and is activated by DNA damageDistinct Biochemical Pools of Golgi Phosphoprotein 3 in the Human Breast Cancer Cell Lines MCF7 and MDA-MB-231The multiple cellular functions of the oncoprotein Golgi phosphoprotein 3GOLPH3 drives cell migration by promoting Golgi reorientation and directional trafficking to the leading edge.β-Galactoside α2,6-sialyltranferase 1 promotes transforming growth factor-β-mediated epithelial-mesenchymal transition.Integrin α5 Suppresses the Phosphorylation of Epidermal Growth Factor Receptor and Its Cellular Signaling of Cell Proliferation via N-GlycosylationExpression of N-Acetylglucosaminyltransferase III Suppresses α2,3-Sialylation, and Its Distinctive Functions in Cell Migration Are Attributed to α2,6-Sialylation Levels.Regulation of CD44 expression and focal adhesion by Golgi phosphatidylinositol 4-phosphate in breast cancer.Expression of GOLPH3 protein in colon cancer tissues and its association with the prognosis of patients.Relative versus absolute quantitation in disease glycomics.Significance of β-Galactoside α2,6 Sialyltranferase 1 in Cancers.Golgi phosphoprotein3 overexpression is associated with poor survival in patients with solid tumors: a meta-analysis.Emerging themes of regulation at the Golgi.Golgi-Related Proteins GOLPH2 (GP73/GOLM1) and GOLPH3 (GOPP1/MIDAS) in Cutaneous Melanoma: Patterns of Expression and Prognostic Significance.Golgi phosphoprotein 3 triggers signal-mediated incorporation of glycosyltransferases into coatomer-coated (COPI) vesicles.The Inhibitory Role of α2,6-Sialylation in Adipogenesis.MYO18A: An unusual myosin.COG7 deficiency in Drosophila generates multifaceted developmental, behavioral and protein glycosylation phenotypes.Drug resistance related to aberrant glycosylation in colorectal cancer.Immunosuppressive drugs affect high-mannose/hybrid N-glycans on human allostimulated leukocytes.
P2860
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P2860
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
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name
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
@ast
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
@en
type
label
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
@ast
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
@en
prefLabel
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
@ast
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
@en
P2093
P2860
P356
P1476
An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.
@en
P2093
Daisuke Takakura
Hiroyuki Miyoshi
Jianguo Gu
Nana Kawasaki
Noritaka Hashii
Qinglei Hang
Sanghun Im
Tomohiko Fukuda
Tomoya Isaji
P2860
P304
20694-20705
P356
10.1074/JBC.M113.542688
P407
P577
2014-07-01T00:00:00Z