HUGO ID Detailed Result 12513

PMID	Match String	Actual String	Score	Flanking text	Edited by	Edit
16043017	UCHL1	UCH-L1	2.2	translationally controlled tumor protein (TCTP), TCTP ubiquitin carboxyl-terminal hydrolase-L1 (UCH-L1), UCH-L1 and possibly B-crystallin
16043017	UCHL1	UCH-L1	2.2	activity decline our current study suggests that oxidative modification of UCH-L1 TCTP SOD1 and possibly B-crystallin may play an important role
16043017	UCHL1	UCH-L1	2.2	Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) UCH-L1 assay
16043017	UCHL1	UCH-L1	2.2	The activities of UCH-L1 in the spinal cord were measured by determining the rate
16043017	UCHL1	UCH-L1	2.2	UCH-L1 activities of each individual were assayed by the change of
16043017	UCHL1	UCH-L1	2.2	The average UCH-L1 activities of six transgenic animals were compared to those of
16043017	UCHL1	UCH-L1	2.2	were identified as SOD1 translationally controlled tumor protein (TCTP), TCTP UCH-L1 and B-crystallin
16043017	UCHL1	UCH-L1	2.2	here that the specific carbonyl levels of human SOD1 TCTP UCH-L1 and possibly B-crystallin are significantly increased in the spinal cord
16043017	UCHL1	UCH-L1	2.2	oxidative modification inactivated protein activity we compared the activity of UCH-L1 in the G93A-SOD1 transgenic mice to that in the control
16043017	UCHL1	UCH-L1	2.2	of activity of oxidatively modified proteins 49 50 and 51 UCH-L1 activity was significantly decreased (29%) 29% in the G93A-SOD1 transgenic
16043017	UCHL1	UCH-L1	2.2	compared to those of the nontransgenic mice as SOD1 TCTP UCH-L1 and B-crystallin
16043017	UCHL1	UCH-L1	2.2	UCH-L1 belongs to a family of ubiquitin carboxyl-terminal hydrolases that play
16043017	UCHL1	UCH-L1	2.2	Loss of UCH-L1 function causes neuroaxonal dystrophy 74 75 and 76 significant protein
16043017	UCHL1	UCH-L1	2.2	Similarly decreased UCH-L1 activity by mutation also enhances protein aggregation in Escherichia coli
16043017	UCHL1	UCH-L1	2.2	Therefore based on the prior literature oxidative inactivation of UCH-L1 presented in the current study possibly contributes to both the
16043017	UCHL1	UCH-L1	2.2	notion and consistent with our finding ( Fig 4 that UCH-L1 activity is decreased in G93A-SOD1 mouse spinal cord the inclusions
16043017	UCHL1	UCH-L1	2.2	on our current observations the increased oxidative modification of SOD1 UCH-L1 and B-crystallin plays a significant role in the protein aggregation
16043017	UCHL1	UCH-L1	2.2	(TCTP) TCTP and proteins involved in inclusion formation (SOD1, SOD1 UCH-L1 and B-crystallin suggesting a potential relationship between protein oxidation protein
16043017	UCHL1	UCH-L1	2.2	( B-crystallin Ca 2 binding (TCTP), TCTP protein degradation (UCH-L1), UCH-L1 and antioxidant capacity (SOD1) SOD1
16043017	UCHL1	UCH-L1	2.2	Fig 4._amp_#xa0 Activity of UCH-L1 in G93A-SOD1 transgenic mice as a percentage of the nontransgenic
16043017	UCHL1	UCH-L1	2.2	The activity of UCH-L1 is significantly decreased in the spinal cord of G93A-SOD1 transgenic
16043017	uch l1	uch l1	1.0	these proteins are sod1 translationally controlled tumor protein tctp ubiquitin carboxyl terminal hydrolase l1 uch l1 and possibly b crystallin.
16043017	uch l1	uch l1	1.0	because oxidative modification can lead to structural alteration and activity decline our current study suggests that oxidative modification of uch l1 tctp sod1 and possibly b crystallin may play an important role in the neurodegeneration of als.
16043017	uch l1	uch l1	1.0	ubiquitin carboxyl terminal hydrolase l1 uch l1 assay
16043017	uch l1	uch l1	1.0	the activities of uch l1 in the spinal cord were measured by determining the rate of conversion of ubiquitin c terminal 7 amido 4 methylcoumarin ub amc calbiochem to ubiquitin and free amc [48] .
16043017	uch l1	uch l1	1.0	uch l1 activities of each individual were assayed by the change of _amp_#x3bb; em 460 nm over time.
16043017	uch l1	uch l1	1.0	the average uch l1 activities of six transgenic animals were compared to those of six control animals using student's t test.
16043017	uch l1	uch l1	1.0	these proteins were identified as sod1 translationally controlled tumor protein tctp uch l1 and b crystallin.
16043017	uch l1	uch l1	1.0	we report here that the specific carbonyl levels of human sod1 tctp uch l1 and possibly b crystallin are significantly increased in the spinal cord of g93a sod1 transgenic mice compared to that of nontransgenic mice.
16043017	uch l1	uch l1	1.0	in order to confirm that oxidative modification inactivated protein activity we compared the activity of uch l1 in the g93a sod1 transgenic mice to that in the control mice.
16043017	uch l1	uch l1	1.0	consistent with our prior studies that demonstrate loss of activity of oxidatively modified proteins [49] [50] and [51] uch l1 activity was significantly decreased 29% in the g93a sod1 transgenic mice compared to that of nontransgenic control fig 4 .
16043017	uch l1	uch l1	1.0	in the current study we identified the proteins that demonstrate increased carbonyl levels compared to those of the nontransgenic mice as sod1 tctp uch l1 and b crystallin.
16043017	uch l1	uch l1	1.0	uch l1 belongs to a family of ubiquitin carboxyl terminal hydrolases that play important roles in the ubiquitin_amp_#x2013;proteolytic pathway [71] .
16043017	uch l1	uch l1	1.0	loss of uch l1 function causes neuroaxonal dystrophy [74] [75] and [76] significant protein oxidization [45] and accumulation of synuclein protein in gracile axonal dystrophy mice [77] .
16043017	uch l1	uch l1	1.0	similarly decreased uch l1 activity by mutation also enhances protein aggregation in escherichia coli [78] .
16043017	uch l1	uch l1	1.0	therefore based on the prior literature oxidative inactivation of uch l1 presented in the current study possibly contributes to both the protein aggregation and the oxidative stress observed in g93a sod1 transgenic mice and als patients.
16043017	uch l1	uch l1	1.0	consistent with this notion and consistent with our finding fig 4 that uch l1 activity is decreased in g93a sod1 mouse spinal cord the inclusions of human als and msod1 including g93a mice are excessively ubiquitinated [79] [80] [81] and [82] .
16043017	uch l1	uch l1	1.0	based on our current observations the increased oxidative modification of sod1 uch l1 and b crystallin plays a significant role in the protein aggregation in the spinal cords of g93a sod1 transgenic mice.
16043017	uch l1	uch l1	1.0	study provides insight into the mechanism of g93a sod1 neurotoxicity in vivo which involves oxidative modification of a ca 2+ regulating protein tctp and proteins involved in inclusion formation sod1 uch l1 and b crystallin suggesting a potential relationship between protein oxidation protein aggregation and ca 2+ regulation in als.
16043017	uch l1	uch l1	1.0	moreover one can speculate that the oxidative modification of these proteins impairs protein stability b crystallin ca 2+ binding tctp protein degradation uch l1 and antioxidant capacity sod1 .
16043017	uch l1	uch l1	1.0	fig. 4._amp_#xa0;activity of uch l1 in g93a sod1 transgenic mice as a percentage of the nontransgenic control.
16043017	uch l1	uch l1	1.0	the activity of uch l1 is significantly decreased in the spinal cord of g93a sod1 transgenic mice compared to nontransgenic control.