Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Debra Gawler"'
Publikováno v:
Cell Biology International. 32:1388-1396
The plasma membrane of the heart muscle cell and its underlying cytoskeleton are vitally important to the function of the heart. Annexin A6 is a major cellular calcium and phospholipid binding protein. Here we show that annexin A6 copurifies with sar
Publikováno v:
Journal of Biological Chemistry. 271:24333-24336
The CaLB domain is a 43-amino acid sequence motif found in a number of functionally diverse signaling proteins including three Ras-specific GTPase activating proteins (GAPs). In the Ras GTPase activating protein, P120(GAP), this domain has the abilit
Publikováno v:
Cell biology international. 33(1)
The association of cytosolic phospholipase A(2)-alpha (cPLA(2)alpha) with intracellular membranes is central to the generation of free arachidonic acid and thromboxane A(2) in activated platelets. Despite this, the site and nature of this membrane as
Publikováno v:
Cardiovascular research. 69(2)
Objective: Src has been proposed to activate L-type calcium channel activity by binding to the a1c subunit. In the II–III linker region of this subunit there is a novel consensus sequence for Src binding. We have examined whether this site is a fun
Publikováno v:
Journal of Molecular and Cellular Cardiology. 40:986
Autor:
Andrea Varro, Shin-Ichi Fukuoka, Nichola Rockliffe, Angela Willshaw, Sailaja Ambavarapu, Jun Yan, Karen Grant, Debra Gawler, G Burdyga
Publikováno v:
FEBS Letters. (1-3):13-21
Rabphilin is a synaptic vesicle-associated protein proposed to play a role in regulating neurotransmitter release. Here we report the isolation and identification of a novel protein complex containing rabphilin, annexin A4 and synaptotagmin 1. We sho
Autor:
Debra Gawler, Nichola Rockliffe
Publikováno v:
FEBS Letters. (3):831-838
One prime candidate linking N-methyl-d-aspartate (NMDA) receptors to the regulation of the MAP kinase cascade is SynGAP, a negative regulator of Ras. In order to assess how a physiological stimulus can alter SynGAP activity, an appropriate whole cell