High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor
摘要：
Nerve growth factor (NGF) interacts with two different low-affinity receptors that can be distinguished by affinity crosslinking. Reconstitution experiments by membrane fusion and transient transfection into heterologous cells indicate that high-affinity NGF binding requires coexpression and binding to both the low-affinity NGF receptor and the tyrosine kinase trk gene product. These studies reveal a new growth factor receptor-mediated mechanism of cellular differentiation involving trk and the low-affinity NGF receptor.
展开
关键词：
Animals Cell Line Cell Membrane Cross-Linking Reagents Kinetics Membrane Fusion Models, Biological Nerve Growth Factors Protein-Tyrosine Kinases Proto-Oncogene Proteins
DOI：
10.1038/350678a0
被引量：
年份：
1991
Nature
Nature
(全网免费下载)
Springer
EBSCO
万方医学
查看更多
Semantic Scholar
dx.doi.org
Europe PMC
NCBI
Oxford Univ Press
NCBI
JBC
adsabs.harvard.edu
ResearchGate
ProQuest
EBSCO
EBSCO
cghjournal.org
scripts.iucr.org
jneurosci.org
emboj.embopress.org
scienceopen.com
press.endocrine.org
molpharm.aspetjournals.org
aem.asm.org
clinsci.org
jasn.asnjournals.org
jcs.biologists.org
onAcademic
jcb.rupress.org
physrev.physiology.org
cshperspectives.cshlp.org
jacionline.org
readcube.com
mendeley.com
Nature
(全网免费下载)
通过文献互助平台发起求助，成功后即可免费获取论文全文。
相似文献
参考文献
引证文献
辅助模式
引用
文献可以批量引用啦~
欢迎点我试用！
