Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells
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Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinasesIntegrin alpha5beta1 and ADAM-17 interact in vitro and co-localize in migrating HeLa cellsThe cysteine-rich domain regulates ADAM protease function in vivo.Syndecans in tumor cell adhesion and signalingIdentification of SH3 domain proteins interacting with the cytoplasmic tail of the a disintegrin and metalloprotease 10 (ADAM10)The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cellsPreferred SH3 domain partners of ADAM metalloproteases include shared and ADAM-specific SH3 interactions.Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1.ADAM12 and alpha9beta1 integrin are instrumental in human myogenic cell differentiation.Intracellular processing of metalloprotease disintegrin ADAM12.Activation of phosphatidylinositol 3-kinase signaling by a mutant thyroid hormone beta receptor.Nongenomic activation of phosphatidylinositol 3-kinase signaling by thyroid hormone receptors.Breast cancer-associated mutations in metalloprotease disintegrin ADAM12 interfere with the intracellular trafficking and processing of the protein.Insights into the activity, differential expression, mutual regulation, and functions of matrix metalloproteinases and a disintegrin and metalloproteinases in hypertension and cardiac disease.Role of metalloprotease disintegrin ADAM12 in determination of quiescent reserve cells during myogenic differentiation in vitro.Aberrant alternative exon use and increased copy number of human metalloprotease-disintegrin ADAM15 gene in breast cancer cells.Regulation of ADAM12 cell-surface expression by protein kinase C epsilon.Proteomic screening identifies the zonula occludens protein ZO-1 as a new partner for ADAM12 in invadopodia-like structures.
P2860
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P2860
Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
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2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@ast
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@en
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@nl
type
label
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@ast
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@en
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@nl
prefLabel
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@ast
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@en
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@nl
P2093
P2860
P356
P1476
Direct interaction between the ...... ositol 3-kinase in C2C12 cells
@en
P2093
P2860
P304
P356
10.1074/JBC.M101162200
P407
P577
2001-07-06T00:00:00Z