๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Analysis of the presynaptic signaling mechanisms underlying the inhibition of LTP in rat dentate gyrus by the tyrosine kinase inhibitor, genistein

โœ Scribed by Daniela B. Pereira; Carlos B. Duarte


Publisher
John Wiley and Sons
Year
2003
Tongue
English
Weight
53 KB
Volume
13
Category
Article
ISSN
1050-9631

No coin nor oath required. For personal study only.

โœฆ Synopsis


In conclusion, the report by Casey and colleagues is based on the use of two pharmacological inhibitors that have nonspecific effects and no attempt was made to verify their specificity. This lead the authors to ambitious conclusions on the involvement of tyrosine kinases on LTP in perforant path-granule cell synapses, that cannot be inferred from the data presented in this article.


๐Ÿ“œ SIMILAR VOLUMES


Analysis of the presynaptic signaling me
โœ M. Casey; C. Maguire; ร. Kelly; M.A. Gooney; M.A. Lynch ๐Ÿ“‚ Article ๐Ÿ“… 2002 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 260 KB ๐Ÿ‘ 1 views

## Abstract A great deal of recent evidence points to a role for tyrosine kinase in expression of LTP. Data have been presented that are consistent with the idea that tyrosine phosphorylation of proteins occurs in both the presynaptic and postsynaptic areas. In this study, we set out to investigate

Analysis of the presynaptic signalling m
โœ Marina Lynch ๐Ÿ“‚ Article ๐Ÿ“… 2004 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 45 KB ๐Ÿ‘ 1 views

This study was one of a series designed to analyse signalling events in the hippocampus after induction of long-term potentiation (LTP). The specific purpose was to further analyse changes associated with tyrosine kinase activation after earlier observations. Among the earlier observations were the

Modulation of liver canalicular transpor
โœ W Jager; O Winter; B Halper; A Salamon; M Sartori; L Gajdzik; G Hamilton; G They ๐Ÿ“‚ Article ๐Ÿ“… 1997 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 305 KB

Rat liver cells express the multispecific organic anion trans-tition with other substrates at the sites of glucuronidation and transport via cmoat. (HEPATOLOGY 1997;26:1467-1476.) porter (cmoat, cmrp, mrp2) and P-glycoprotein (Pgp) in their canalicular membranes, proteins that are homologous to the