ISSN:
1476-4687
Source:
Nature Archives 1869 - 2009
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
Notes:
[Auszug] It has been shown that the FGF receptor can phosphorylate itself on Tyr766 and that a recombinant SH2 domain (src-homologous domain 2) of PLCy can bind to a tryptic fragment of the receptor containing this tyrosine11. We reasoned that if Tyr766 were the main site of interaction between the FGF ...
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1038/358678a0