HUGO ID Detailed Result 4553

PMID	Match String	Actual String	Score	Flanking text	Edited by	Edit
11050436	GPX1	GPX-1	0.9	peroxide in both compartments is achieved by glutathione peroxidase (GPX-1), GPX-1 which exists both in the cytosol and in the mitochondrial
14648077	GPX1	GPx1	2.2	including peroxiredoxin2 (Prx2, Prx2 thioredoxin peroxidase and glutathione peroxidase1 (GPx1): GPx1 SOD1 converts superoxide radicals into hydrogen peroxide (H H 2
14648077	GPX1	GPx1	2.2	2 O and oxygen (O O 2 by Prx2 and GPx1 that directly regulate the redox system
14648077	GPX1	GPx1	2.2	significance of the interaction of the redox system (Prx2/GPx1) Prx2 GPx1 with SOD1 in SOD1-mutated motor neurons in vivo we produced
14648077	GPX1	GPx1	2.2	against Prx2 and investigated the immunohistochemical localization of Prx2 and GPx1 in neuronal Lewy body-like hyaline inclusions (LBHIs) LBHIs in the
14648077	GPX1	GPx1	2.2	patients and transgenic rats showed identical immunoreactivities for Prx2 and GPx1 the reaction product deposits with the antibodies against Prx2 and
14648077	GPX1	GPx1	2.2	the reaction product deposits with the antibodies against Prx2 and GPx1 were localized in the LBHIs
14648077	GPX1	GPx1	2.2	the localizations of the immunoreactivities for SOD1 and Prx2/GPx1 Prx2 GPx1 were similar in the inclusions the co-aggregation of Prx2/GPx1 Prx2
14648077	GPX1	GPx1	2.2	were similar in the inclusions the co-aggregation of Prx2/GPx1 Prx2 GPx1 with SOD1 in neuronal LBHIs in mutant SOD1-related FALS patients
14648077	GPX1	GPx1	2.2	Based on the fact that Prx2/GPx1 Prx2 GPx1 directly regulates the redox system such co-aggregation of Prx2/GPx1 Prx2
14648077	GPX1	GPx1	2.2	directly regulates the redox system such co-aggregation of Prx2/GPx1 Prx2 GPx1 with SOD1 in neuronal LBHIs may lead to the breakdown
14648077	GPX1	GPx1	2.2	EC 1.11.1.9 a classical selenium-dependent isoform (also also assigned as GPx1 was first described as an enzyme that protects hemoglobin from
14648077	GPX1	GPx1	2.2	Among them GPx1 is considered as the major enzyme responsible for removing intracytoplasmic
14648077	GPX1	GPx1	2.2	Like Prx2 GPx1 needs glutathione reductase (GR) GR as a secondary enzyme as
14648077	GPX1	GPx1	2.2	Therefore Prx2 and GPx1 directly control the redox system
14648077	GPX1	GPx1	2.2	induce mutant and wild-type SOD1 as well as Prx2 and GPx1
14648077	GPX1	GPx1	2.2	Considering that Prx2 and GPx1 interact not only with wild-type SOD1 but also with mutant
14648077	GPX1	GPx1	2.2	but also with mutant SOD1 the interaction of Prx2/GPx1 Prx2 GPx1 with SOD1 has been suggested to contribute to mutant SOD1
14648077	GPX1	GPx1	2.2	suggested to contribute to mutant SOD1 aggregation toxicity Prx2/GPx1 Prx2 GPx1 possibly aggregate as LBHIs in SOD1-mutated motor neurons
14648077	GPX1	GPx1	2.2	Furthermore the aggregation of Prx2/GPx1 Prx2 GPx1 might affect the intracytoplasmic redox regulation and amplify mutant SOD1-mediated
14648077	GPX1	GPx1	2.2	clarify the biological significance of the interaction of Prx2/GPx1 Prx2 GPx1 (redox redox system with SOD1 in SOD1-mutated motor neurons in
14648077	GPX1	GPx1	2.2	Prx2 and analyzed the characteristic expressions of both Prx2 and GPx1 in neuronal LBHIs in SOD1-mutated motor neurons of humans and
14648077	GPX1	GPx1	2.2	concentration 1 _amp_micro;g/ml), _amp_micro g ml a polyclonal antibody to GPx1 diluted 1 2 000 in 1% bovine serum albumin-containing phosphate-buffered
14648077	GPX1	GPx1	2.2	B C Immunostaining for GPx1 ( B and Prx2 ( C
14648077	GPX1	GPx1	2.2	GPx1 and Prx2 immunoreactivities are found diffusely in the neuropil with
14648077	GPX1	GPx1	2.2	No counterstaining ( HE hematoxylin and eosin GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2
14648077	GPX1	GPx1	2.2	Fig 3 Detection of Prx2 and GPx1 in the normal motor neurons of the human spinal cord
14648077	GPX1	GPx1	2.2	B Immunostaining with the antibody against GPx1 showing GPx1-positive neurons
14648077	GPX1	GPx1-positive	1.9	B Immunostaining with the antibody against GPx1 showing GPx1-positive neurons
14648077	GPX1	GPx1	2.2	the normal motor neurons in the spinal cord co-express both GPx1 ( B and Prx2 ( C although their staining intensities
14648077	GPX1	GPx1	2.2	E GPx1 immunostaining of the neuronal cytoplasm and proximal dendrites is observed
14648077	GPX1	GPx1	2.2	B _amp_#x2013 F No counterstaining ( HE hematoxylin and eosin GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2
14648077	GPX1	GPx1	2.2	staining pattern similar to that for Prx2 was observed with GPx1 weak GPx1 immunoreactivity was diffusely seen in the neuropil in
14648077	GPX1	GPx1	2.2	similar to that for Prx2 was observed with GPx1 weak GPx1 immunoreactivity was diffusely seen in the neuropil in transverse sections
14648077	GPX1	GPx1	2.2	GPx1 immunostaining was observed in the cytoplasm with cell bodies and
14648077	GPX1	GPx1	2.2	The stainability and intensity of Prx2 and GPx1 in the normal anterior horn cells of the spinal cords
14648077	GPX1	GPx1	2.2	motor neurons in the spinal cords co-expressed both Prx2 and GPx1 (Fig Fig 3 A_amp_#x2013 C although the staining intensities of
14648077	GPX1	GPx1	2.2	With respect to the GPx1 immunostaining in the neuronal LBHIs similar stainability and immunolocalization to
14648077	GPX1	GPx1	2.2	The immunoreactivity for GPx1 in the FALS patients was similar to that in the
14648077	GPX1	GPx1	2.2	Like Prx2 the immunolocalization of GPx1 was similar to that of SOD1 in both diseases
14648077	GPX1	GPx1-immunoreactive	1.9	GPx1-immunoreactive products in many core and halo-type inclusions were mainly localized
14648077	GPX1	GPx1	2.2	B Immunostaining for GPx1 immunoreactivity is located in the SOD1-positive portion of the LBHI
14648077	GPX1	GPx1	2.2	Co-localization of the three proteins SOD1 GPx1 and Prx2 in the LBHI is evident
14648077	GPX1	GPx1	2.2	Immunostaining for SOD1 ( D GPx1 ( E and Prx2 ( F
14648077	GPX1	GPx1	2.2	Similar stainability and immunolocalization of SOD1 GPx1 and Prx2 in the LBHI are observed ( LBHI Lewy
14648077	GPX1	GPx1	2.2	inclusion FALS familial amyotrophic lateral sclerosis SOD1 superoxide dismutase 1 GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2
14648077	GPX1	GPx1	2.2	Immunostaining for SOD1 ( A GPx1 ( B and Prx2 ( C
14648077	GPX1	GPx1	2.2	Immunostaining for SOD1 ( D GPx1 ( E and Prx2 ( F
14648077	GPX1	GPx1	2.2	Immunostaining GPx1 ( E and Prx2 ( F are observed in only
14648077	GPX1	GPx1	2.2	inclusion FALS familial amyotrophic lateral sclerosis SOD1 superoxide dismutase 1 GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2
14648077	GPX1	GPx1	2.2	H46R mutation immunostained with antibodies against SOD1 ( A and GPx1 ( B
14648077	GPX1	GPx1	2.2	LBHIs in the neuropil are positive for both SOD1 and GPx1 ( arrows ( SOD1 superoxide dismutase1 LBHI Lewy body-like hyaline
14648077	GPX1	GPx1	2.2	arrows ( SOD1 superoxide dismutase1 LBHI Lewy body-like hyaline inclusion GPx1 glutathione peroxidase1
14648077	GPX1	GPx1	2.2	Noticeably the co-localization of the three proteins SOD1 Prx2 and GPx1 in neuronal LBHIs in SOD1-mutated FALS patients and transgenic rats
14648077	GPX1	GPx1	2.2	three proteins differed Prx2 (Fig Fig 5 D F and GPx1 (Fig Fig 5 D E immunostaining was observed in only
14648077	GPX1	GPx1	2.2	Discussion Under normal physiological conditions Prx2 and GPx1 immunoreactivities in the spinal cord anterior horns in humans and
14648077	GPX1	GPx1	2.2	Considering that endogenous Prx2 and GPx1 within the neuronal cytoplasm are extremely effective regulators of the
14648077	GPX1	GPx1	2.2	of the normal spinal motor neurons co-expressed both Prx2 and GPx1 confirms that these motor neurons maintain themselves using the intracellular
14648077	GPX1	GPx1	2.2	these motor neurons maintain themselves using the intracellular Prx2/GPx1 Prx2 GPx1 system that is the redox system
14648077	GPX1	GPx1	2.2	Intense co-expression of SOD1 Prx2 and GPx1 in neuronal LBHIs in both diseases was evident
14648077	GPX1	GPx1	2.2	mutant wild-type SOD1 as an antioxidant system and Prx2/GPx1 Prx2 GPx1 as a redox system
14648077	GPX1	GPx1	2.2	this in vivo milieu where mutant SOD1 exists Prx2 and GPx1 would aberrantly interact with the mutant SOD1 which is assumed
14648077	GPX1	GPx1	2.2	that there are neuronal LBHIs positive for SOD1 Prx2 and GPx1 in the milieu where mutant SOD1 exists but no LBHIs
14648077	GPX1	GPx1	2.2	conditions our study demonstrates an aberrant interaction of Prx2/GPx1 Prx2 GPx1 with mutant SOD1 the aggregation of which results in neuronal
14648077	GPX1	GPx1	2.2	In addition intra-inclusional co-aggregation of Prx2/GPx1 Prx2 GPx1 with mutant SOD1 causes the intracytoplasmic reduction of Prx2/GPx1, Prx2
14648077	GPX1	GPx1	2.2	with mutant SOD1 causes the intracytoplasmic reduction of Prx2/GPx1, Prx2 GPx1 thereby reducing the availability of the redox system
14648077	GPX1	GPx1	2.2	the aberrant interaction of cytotoxic mutant SOD1 with Prx2/GPx1 Prx2 GPx1 directly regulating a redox system our finding leads us to
14648077	GPX1	GPx1	2.2	us to speculate that not only co-aggregation of Prx2/GPx1 Prx2 GPx1 and SOD1 into LBHIs but also intracytoplasmic reduction of Prx2/GPx1
14648077	GPX1	GPx1	2.2	SOD1 into LBHIs but also intracytoplasmic reduction of Prx2/GPx1 Prx2 GPx1 in both diseases may partly contribute to the breakdown of
14648077	GPX1	GPx1	2.2	to be determined whether this aberrant interaction of Prx2/GPx1 Prx2 GPx1 with mutant SOD1 is a direct or an indirect effect
14648077	GPX1	GPx1	2.2	pathogenesis of SOD1-mutated FALS disease itself or whether Prx2 and GPx1 play a primary or a secondary role to mutant SOD1
14648077	GPX1	GPx1	2.2	emphasize that the aberrant interaction and co-aggregation of Prx2/GPx1 Prx2 GPx1 and SOD1 (probably probably Prx2/GPx1 Prx2 GPx1 and mutant SOD1
14648077	GPX1	GPx1	2.2	of Prx2/GPx1 Prx2 GPx1 and SOD1 (probably probably Prx2/GPx1 Prx2 GPx1 and mutant SOD1 in FALS patients with SOD1 gene mutations
10643818	cellular glutathione peroxidase	cellular glutathione peroxidase	1.0	furthermore around 10% of cellular glutathione peroxidase are mitochondrial and there prevent oxidative damage by hydrogen peroxide.
14648077	glutathione peroxidase 1	glutathione peroxidase1	1.0	otect themselves from these ross the cells have developed both an antioxidant system containing superoxide dismutase 1 sod1 and a redox system including peroxiredoxin2 prx2 thioredoxin peroxidase and glutathione peroxidase1 gpx1 : sod1 converts superoxide radicals into hydrogen peroxide h 2 o 2 and h 2 o 2 is then converted into harmless water h 2 o and oxygen o 2 by prx2 and gpx1 that directly regulate the redox system
14648077	glutathione peroxidase 1	glutathione peroxidase 1	1.0	keywords peroxiredoxin 2 glutathione peroxidase 1 redox system superoxide dismutase 1 familial amyotrophic lateral sclerosis
14648077	glutathione peroxidase 1	glutathione peroxidase1	1.0	no counterstaining he hematoxylin and eosin gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .
14648077	glutathione peroxidase 1	glutathione peroxidase1	1.0	b _amp_#x2013; f no counterstaining he hematoxylin and eosin gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .
14648077	glutathione peroxidase 1	glutathione peroxidase1	1.0	r stainability and immunolocalization of sod1 gpx1 and prx2 in the lbhi are observed lbhi lewy body like hyaline inclusion fals familial amyotrophic lateral sclerosis sod1 superoxide dismutase 1 gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .
14648077	glutathione peroxidase 1	glutathione peroxidase1	1.0	onal immunolocalizations of these three proteins differ from each other in this lbhi lbhi lewy body like hyaline inclusion fals familial amyotrophic lateral sclerosis sod1 superoxide dismutase 1 gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .
14648077	glutathione peroxidase 1	glutathione peroxidase1	1.0	round lbhis in the neuropil are positive for both sod1 and gpx1 arrows sod1 superoxide dismutase1 lbhi lewy body like hyaline inclusion gpx1 glutathione peroxidase1 .