Article
Publicly Available
GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways
-
Stefan Hart
Published/Copyright:
September 9, 2005
Received: 2005-5-19
Accepted: 2005-7-25
Published Online: 2005-9-9
Published in Print: 2005-9-1
©2005 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Paper of the Year 2004: Award to Yin Wang and Iris Lorenzi
- Improving the levels of essential amino acids and sulfur metabolites in plants
- Symmetry at the active site of the ribosome: structural and functional implications
- GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways
- Developing an effective RNA interference strategy against a plus-strand RNA virus: silencing of coxsackievirus B3 and its cognate coxsackievirus-adenovirus receptor
- NF-κB contributes to transcription of placenta growth factor and interacts with metal responsive transcription factor-1 in hypoxic human cells
- Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP
- Role of the N-terminal region and of β-sheet residue Thr29 on the activity of the ω2 global regulator from the broad-host range Streptococcus pyogenes plasmid pSM19035
- Lysine 3 acetylation regulates the phosphorylation of yeast 6-phosphofructo-2-kinase under hypo-osmotic stress
- Determination of the specificity of monoclonal antibodies against Schistosoma mansoni CAA glycoprotein antigen using neoglycoconjugate variants
- Cholesterol is the major component of native lipoproteins activating the p38 mitogen-activated protein kinases
- Focal adhesion kinase is redistributed to focal complexes and mediates cell spreading in macrophages in response to M-CSF
- Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease
- Activation processing of cathepsin H impairs recognition by its propeptide
Keywords for this article
ADAM;
breast cancer;
cross-talk;
HB-EGF;
shedding;
sphingosine kinase (SPHK)
Articles in the same Issue
- Paper of the Year 2004: Award to Yin Wang and Iris Lorenzi
- Improving the levels of essential amino acids and sulfur metabolites in plants
- Symmetry at the active site of the ribosome: structural and functional implications
- GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways
- Developing an effective RNA interference strategy against a plus-strand RNA virus: silencing of coxsackievirus B3 and its cognate coxsackievirus-adenovirus receptor
- NF-κB contributes to transcription of placenta growth factor and interacts with metal responsive transcription factor-1 in hypoxic human cells
- Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP
- Role of the N-terminal region and of β-sheet residue Thr29 on the activity of the ω2 global regulator from the broad-host range Streptococcus pyogenes plasmid pSM19035
- Lysine 3 acetylation regulates the phosphorylation of yeast 6-phosphofructo-2-kinase under hypo-osmotic stress
- Determination of the specificity of monoclonal antibodies against Schistosoma mansoni CAA glycoprotein antigen using neoglycoconjugate variants
- Cholesterol is the major component of native lipoproteins activating the p38 mitogen-activated protein kinases
- Focal adhesion kinase is redistributed to focal complexes and mediates cell spreading in macrophages in response to M-CSF
- Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease
- Activation processing of cathepsin H impairs recognition by its propeptide