HUGO ID Detailed Result 391

PMID	Match String	Actual String	Score	Flanking text	Edited by	Edit
11679167	AKT	Akt	0.0	is an homologue of the mammalian protein kinase B/Akt, B Akt which is involved in insulin signalling apoptosis and cellular proliferation
11679167	AKT	Akt	0.0	Sch9/Rim15 Sch9 Rim15 and the C elegans DAF-2/AGE-1/Akt/DAF16 DAF-2 AGE-1 Akt DAF16 pathways play similar roles in regulating ageing and stress
12654515	AKT	Akt	0.1	Furthermore VEGF-induced downstream Akt activation promoted motor neuron-like NSC34 cell survival in the presence
12654515	AKT	Akt	0.3	neuron-like cell death from mutant G93A-SOD1 effects via PI3-K/Akt PI3-K Akt activation
12654515	AKT	Akt	0.0	In addition we show that Akt activation promotes NSC34 motor neuron-like cell survival in the presence
12654515	AKT	Akt	0.3	cell survival is mediated by activation of the PI3-K/Akt PI3-K Akt pathway 2
12654515	AKT	Akt	0.0	Constitutively active (myristoylated) myristoylated and dominant negative Akt (K179M-Akt) K179M-Akt were kindly provided by Dr Alfonso Bellacosa Fox
12654515	AKT	Akt	0.0	Akt activation assay
12654515	AKT	Akt	0.0	Akt activation was examined by Western blotting with phosphorylation specific Akt
12654515	AKT	Akt	0.0	Akt activation was examined by Western blotting with phosphorylation specific Akt antibody (Cell Cell Signaling
12654515	AKT	Akt	0.1	Activation of Akt by VEGF contributes to the protection from mutant SOD1-mediated motor
12654515	AKT	Akt	0.1	One of the downstream effectors of PI3-K is Akt activation
12654515	AKT	Akt	0.0	examined whether VEGF treatment of NSC34 cells was associated with Akt phosphorylation
12654515	AKT	Akt	0.0	Indeed cells exposed to VEGF displayed concentration- and time-dependent Akt activation ( Fig 5D and E
12654515	AKT	Akt	0.0	Overexpression of the dominant negative mutant of Akt resulted in a significant reduction in the protective effect by
12654515	AKT	Akt	0.0	In contrast expression of constitutively active Akt increased cell survival despite the presence of mutant G93A-SOD1 (
12654515	AKT	Akt	0.1	Taken together the data indicate that activation of Akt by VEGF contributes to the protection from NSC34 motor neuron-like
12654515	AKT	Akt	0.3	Thus it is possible that the PI3-K/Akt PI3-K Akt signaling module recruited by VEGF in our experiments is associated
12654515	AKT	Akt	0.0	Our experiments further revealed that Akt activation is essential for implementation of the protective effect by
12654515	AKT	Akt	0.0	Indeed expression of dominant negative Akt blocked the protective function of VEGF while the expression of
12654515	AKT	Akt	0.0	protective function of VEGF while the expression of constitutively active Akt partially prevented mutant SOD1-mediated motor neuron-like cell death even in
12654515	AKT	Akt	0.0	These findings are not surprising since Akt is now well established as a critical protein activated by
12654515	AKT	Akt	0.0	Once phosphorylated Akt has been demonstrated to promote cell survival by inactivation of
12654515	AKT	Akt	0.3	However several lines of evidence suggest that the VEGF/Akt VEGF Akt pathway is particularly important to neuronal survival
12654515	AKT	Akt	0.1	a pre-conditioning hypoxic stimulus up-regulated the expression of VEGF and Akt and the activity of the latter was critical to increased
12654515	AKT	Akt	0.0	Similarly expression of active Akt suppressed mouse hippocampal neuronal death induced by hypoxia glutamate or
12654515	AKT	Akt	0.0	In addition activation of Akt was tightly linked to neuronal cell survival after traumatic brain
12654515	AKT	Akt	0.3	We now demonstrate that the activation of PI3-K/Akt PI3-K Akt signaling pathways by VEGF can promote motor neuron-like cell survival
12654515	AKT	Akt	0.3	However since the activation of PI3-K/Akt PI3-K Akt is a transient event ( Fig 4 the long-lasting protective
12654515	AKT	Akt	0.3	and molecular genetic approaches we have demonstrated that PI3-K/Akt PI3-K Akt activation is the primary contributor to the neuroprotective function of
12654515	AKT	Akt	0.3	Activation of PI3-K/Akt PI3-K Akt pathways by VEGF contributed to the protection from mutant G93A-SOD1-mediated
12654515	AKT	Akt	0.0	of time (30_amp_#x2013;180 30_amp_#x2013 180 min and then assayed for Akt activation as described in Materials and methods
12654515	AKT	Akt	0.0	(E) E The increase of Akt activation in three independent experiments compared to that of vector
12654515	AKT	Akt	0.0	(F) F Constitutively active Akt enhanced while dominant negative Akt partially abolished the protective function
12654515	AKT	Akt	0.0	(F) F Constitutively active Akt enhanced while dominant negative Akt partially abolished the protective function of VEGF on NSC34 motor
16877542	AKT	Akt	0.3	indicate that such an oxidative modification hinders the IGF1/Akt IGF1 Akt survival pathway in motor neurons
16877542	AKT	Akt	0.2	Keywords Akt ALS microglia oxidation non-cell autonomous
16877542	AKT	Akt	0.0	Phosphorylation of Akt and cell viability in response to IGF1 recombinant and to
16877542	AKT	Akt	0.3	NADPH Oxidase Impairs the Insulin-Like Growth Factor 1 (IGF1)/Akt IGF1 Akt Pathway in Transgenic SOD1 G93A Mice
16877542	AKT	Akt	0.0	findings oxidation indices in the intracellular serine/threonine serine threonine kinase Akt which transduces IGF1 receptor signaling ( 15 did not differ
16877542	AKT	Akt	0.0	There were also smaller phospho-Akt total Akt ratios ( Fig 4 F and G as well as
16877542	AKT	Akt	0.0	fewer cells that were immunoreactive for a downstream target of Akt phospho-BAD ( Fig 4 H _amp_#x02013 J and smaller phospho-BAD
16877542	AKT	Akt	0.3	Microglial-Derived ROS Recapitulate the IGF1/Akt IGF1 Akt Pathway Defect in Vitro
16877542	AKT	Akt	0.0	H 2 O 2 IGF1 pathway responsiveness was monitored by Akt phosphorylation
16877542	AKT	Akt	0.0	Exposure to IGF1 caused a dose-dependent phosphorylation of Akt in SH-SY5Y cells ( Fig 5 A and B and
16877542	AKT	Akt	0.0	Conversely IGF1 barely increased Akt phosphorylation in the neuroblastoma cell lines that were exposed to
16877542	AKT	Akt	0.2	H 2 O 2 ( Fig 5 E attenuated IGF1-mediated Akt phosphorylation in the neuroblastoma cell line ( Fig 5 C
16877542	AKT	Akt	0.0	Upon longer exposure to LPS-activated microglial-conditioned medium the Akt phosphorylation response to the IGF1 recombinant remained depressed and at
16877542	AKT	Akt	0.2	However both the alteration of IGF1-mediated Akt phosphorylation and the loss of cell viability mediated by LPS-activated
16877542	AKT	Akt	0.0	elicited by ligation of the IGF1 receptor including autophosphorylation and Akt phosphorylation were indeed abated by ROS in a microglial NADPH
16877542	AKT	Akt	0.3	Modulation of the IGF1/Akt IGF1 Akt pathway by NADPH oxidase-derived ROS
16877542	AKT	Akt	0.2	Glucose oxidase- and microglial-derived ROS impair the IGF1 Akt pathway in vitro
16877542	AKT	Akt	0.0	( A Phospho-Akt (upper upper blot and total Akt (lower lower blot immunoblots of IGF1-treated SH-SY5Y cells exposed or
17105868	AKT1	Akt-1	0.0	that result in activation of the serine/threonine serine threonine kinase Akt-1 and phospholipase C gamma (Chalecka-Franaszek Chalecka-Franaszek and Chuang 1999 ~0.425
17496232	AKT	Akt	0.5	caspases increase of HSPs and Bcl-2 and activation of Akt/PKB, Akt PKB which induces cytoprotective gene expression through NF-kappaB activation (
17496232	PKB	PKB	0.5	increase of HSPs and Bcl-2 and activation of Akt/PKB, Akt PKB which induces cytoprotective gene expression through NF-kappaB activation ( 85
17496232	AKT	Akt	0.5	H 2 O 2 ss with differential activation of MAPKs Akt and cyclin D In this sense very low NO inhibits
17956327	AKT	Akt	0.8	ERK (extracellular-signal-regulated extracellular-signal-regulated kinase MAPKs (mitogen-activated mitogen-activated protein kinases and Akt also called PKB (protein protein kinase B
17956327	PKB	PKB	0.8	kinase MAPKs (mitogen-activated mitogen-activated protein kinases and Akt also called PKB (protein protein kinase B
17956327	PKB	PKB	0.8	for pLTF 42 and activated forms of both ERK and PKB (Akt) Akt are increased in the ventral cervical spinal cord
17956327	AKT	Akt	0.8	42 and activated forms of both ERK and PKB (Akt) Akt are increased in the ventral cervical spinal cord following intermittent
17956327	PKB	PKB	0.8	LTF long-term facilitation pLTF phrenic LTF PKA protein kinase A PKB protein kinase B PKC protein kinase C ROS reactive oxygen
18219386	RAC	Rac	0.0	members of the Rho family of small GTPases including the Rac family
18219386	RAC	Rac	0.0	Members of the Rac family are not strictly NADPH subunits as they regulate other
18219386	RAC	Rac	0.0	Rac acts to coordinate the translocation of the p47 phox /p67
18219386	RAC	Rac	0.0	Inactivation of Rac is mediated via GTPase-activating proteins which stimulate the intrinsic ability
18219386	RAC	Rac	0.0	mediated via GTPase-activating proteins which stimulate the intrinsic ability of Rac to hydrolyze GTP to GDP
18219386	RAC	Rac	0.0	partners but Nox1 and Nox2 are both p47 phox and Rac dependent ( 15
18422522	AKT	Akt	0.0	of sphingosine-1-phosphate stimulation of its membrane receptors and activation of Akt as determined using small interference RNA and dominant negative constructs
11679167	protein kinase b	protein kinase b	1.0	sch9p is an homologue of the mammalian protein kinase b/akt which is involved in insulin signalling apoptosis and cellular proliferation and functions in a pathway that regulates ageing and stress resistance paradis et al. 1999 .
17956327	protein kinase b	protein kinase b	1.0	igh affinity receptor trkb tropomyosin receptor kinase b resulting in the phosphorylation of erk extracellular signal regulated kinase mapks mitogen activated protein kinases and akt [also called pkb protein kinase b ].
17956327	protein kinase b	protein kinase b	1.0	ermittent hypoxia; bdnf brain derived neurotrophic factor; erk extracellular signal regulated kinase; 5 ht 5 hydroxytryptamine; ltf long term facilitation; pltf phrenic ltf; pka protein kinase a; pkb protein kinase b; pkc protein kinase c; ros reactive oxygen species; sod superoxide dismutase; trkb tropomyosin receptor kinase b.