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n2:pmcid: PMC0
bibo:doi: 10.3389%2Ffpls.2016.00152
n7:contains: _:vb49145028 _:vb49145041 _:vb49145011 _:vb49144970 _:vb49144980

Subject Item: _:vb49144970
rdf:type: n7:Section
dc:title: introduction
n7:contains: _:vb49144972 _:vb49144973 _:vb49144974 _:vb49144975 _:vb49144971 _:vb49144976 _:vb49144977 _:vb49144978 _:vb49144979

Subject Item: _:vb49144971
rdf:type: n2:Context
rdf:value: NO is involved in signaling pathways that are related to fundamental processes in plant biology such as growth and development (Beligni and Lamattina, >>2000<<; Pagnussat et al., 2002), senescence (Begara-Morales et al., 2013) and response to abiotic (Corpas et al., 2011; Siddiqui et al., 2011) or biotic stress (Delledonne et al., 1998; Durner et al., 1998; Feechan et al., 2005).
n2:mentions: n3:10664127

Subject Item: _:vb49144972
rdf:type: n2:Context
rdf:value: NO is involved in signaling pathways that are related to fundamental processes in plant biology such as growth and development (Beligni and Lamattina, 2000; Pagnussat et al., >>2002<<), senescence (Begara-Morales et al., 2013) and response to abiotic (Corpas et al., 2011; Siddiqui et al., 2011) or biotic stress (Delledonne et al., 1998; Durner et al., 1998; Feechan et al., 2005).
n2:mentions: n3:12114551

Subject Item: _:vb49144973
rdf:type: n2:Context
rdf:value: NO is involved in signaling pathways that are related to fundamental processes in plant biology such as growth and development (Beligni and Lamattina, 2000; Pagnussat et al., 2002), senescence (Begara-Morales et al., >>2013<<) and response to abiotic (Corpas et al., 2011; Siddiqui et al., 2011) or biotic stress (Delledonne et al., 1998; Durner et al., 1998; Feechan et al., 2005).
n2:mentions: n3:23362300

Subject Item: _:vb49144974
rdf:type: n2:Context
rdf:value: pathways that are related to fundamental processes in plant biology such as growth and development (Beligni and Lamattina, 2000; Pagnussat et al., 2002), senescence (Begara-Morales et al., 2013) and response to abiotic (Corpas et al., >>2011<<; Siddiqui et al., 2011) or biotic stress (Delledonne et al., 1998; Durner et al., 1998; Feechan et al., 2005).
n2:mentions: n3:21893257

Subject Item: _:vb49144975
rdf:type: n2:Context
rdf:value: to fundamental processes in plant biology such as growth and development (Beligni and Lamattina, 2000; Pagnussat et al., 2002), senescence (Begara-Morales et al., 2013) and response to abiotic (Corpas et al., 2011; Siddiqui et al., >>2011<<) or biotic stress (Delledonne et al., 1998; Durner et al., 1998; Feechan et al., 2005).
n2:mentions: n3:20827494

Subject Item: _:vb49144976
rdf:type: n2:Context
rdf:value: such as growth and development (Beligni and Lamattina, 2000; Pagnussat et al., 2002), senescence (Begara-Morales et al., 2013) and response to abiotic (Corpas et al., 2011; Siddiqui et al., 2011) or biotic stress (Delledonne et al., >>1998<<; Durner et al., 1998; Feechan et al., 2005).
n2:mentions: n3:9707120

Subject Item: _:vb49144977
rdf:type: n2:Context
rdf:value: development (Beligni and Lamattina, 2000; Pagnussat et al., 2002), senescence (Begara-Morales et al., 2013) and response to abiotic (Corpas et al., 2011; Siddiqui et al., 2011) or biotic stress (Delledonne et al., 1998; Durner et al., >>1998<<; Feechan et al., 2005).
n2:mentions: n3:9707647

Subject Item: _:vb49144978
rdf:type: n2:Context
rdf:value: Lamattina, 2000; Pagnussat et al., 2002), senescence (Begara-Morales et al., 2013) and response to abiotic (Corpas et al., 2011; Siddiqui et al., 2011) or biotic stress (Delledonne et al., 1998; Durner et al., 1998; Feechan et al., >>2005<<). Generally, the rise in NO levels in response to stress conditions is accompanied by another group of molecules called reactive oxygen species (ROS), some of which, particularly H2O2, are also involved in multiple signaling pathways
n2:mentions: n3:15911759

Subject Item: _:vb49144979
rdf:type: n2:Context
rdf:value: rise in NO levels in response to stress conditions is accompanied by another group of molecules called reactive oxygen species (ROS), some of which, particularly H2O2, are also involved in multiple signaling pathways (Neill et al., >>2002<<). This mini-review will explore recent findings concerning the modulation of the main antioxidant enzymes by NO, especially the enzymatic components of Asa-GSH cycle, with particular attention to the molecular mechanism underpinning this
n2:mentions: n3:11997372

Subject Item: _:vb49144980
rdf:type: n7:Section
dc:title: nitric oxide-mediated post-translational modifications: nitration and s-nitrosylation
n7:contains: _:vb49145008 _:vb49145009 _:vb49145010 _:vb49144996 _:vb49144997 _:vb49144998 _:vb49144999 _:vb49144992 _:vb49144993 _:vb49144994 _:vb49144995 _:vb49145004 _:vb49145005 _:vb49145006 _:vb49145007 _:vb49145000 _:vb49145001 _:vb49145002 _:vb49145003 _:vb49144981 _:vb49144982 _:vb49144983 _:vb49144988 _:vb49144989 _:vb49144990 _:vb49144991 _:vb49144984 _:vb49144985 _:vb49144986 _:vb49144987

Subject Item: _:vb49144981
rdf:type: n2:Context
rdf:value: Nitric oxide mainly transmits its action via post-translational modifications, such as S-nitrosylation and tyrosine nitration, which can regulate the function of the target proteins (Astier and Lindermayr, >>2012<<). These NO-PTMs may be involved in cell signaling under physiological and stress conditions (Corpas et al., 2015).
n2:mentions: n3:23203119

Subject Item: _:vb49144982
rdf:type: n2:Context
rdf:value: nitration, which is mediated mainly by peroxynitrite (ONOO-), consists of the addition of NO2 radicals to one of the two equivalent ortho-carbons of the aromatic ring of tyrosine residues leading to 3-nitrotyrosine (Gow et al., >>2004<<; Radi, 2004).
n2:mentions: n3:15246980

Subject Item: _:vb49144983
rdf:type: n2:Context
rdf:value: which is mediated mainly by peroxynitrite (ONOO-), consists of the addition of NO2 radicals to one of the two equivalent ortho-carbons of the aromatic ring of tyrosine residues leading to 3-nitrotyrosine (Gow et al., 2004; Radi, >>2004<<). This modification converts the tyrosine into a negatively charged residue and causes a marked shift in the hydroxyl group’s pKa (Turko and Murad, 2002; Abello et al., 2009) which can affect the target proteins resulting in a gain, loss
n2:mentions: n3:15020765

Subject Item: _:vb49144984
rdf:type: n2:Context
rdf:value: This modification converts the tyrosine into a negatively charged residue and causes a marked shift in the hydroxyl group’s pKa (Turko and Murad, >>2002<<; Abello et al., 2009) which can affect the target proteins resulting in a gain, loss or no change in the protein’s function (Souza et al., 2008; Radi, 2013).
n2:mentions: n3:12429871

Subject Item: _:vb49144985
rdf:type: n2:Context
rdf:value: This modification converts the tyrosine into a negatively charged residue and causes a marked shift in the hydroxyl group’s pKa (Turko and Murad, 2002; Abello et al., >>2009<<) which can affect the target proteins resulting in a gain, loss or no change in the protein’s function (Souza et al., 2008; Radi, 2013).
n2:mentions: n3:19415921

Subject Item: _:vb49144986
rdf:type: n2:Context
rdf:value: charged residue and causes a marked shift in the hydroxyl group’s pKa (Turko and Murad, 2002; Abello et al., 2009) which can affect the target proteins resulting in a gain, loss or no change in the protein’s function (Souza et al., >>2008<<; Radi, 2013).
n2:mentions: n3:18460345

Subject Item: _:vb49144987
rdf:type: n2:Context
rdf:value: and causes a marked shift in the hydroxyl group’s pKa (Turko and Murad, 2002; Abello et al., 2009) which can affect the target proteins resulting in a gain, loss or no change in the protein’s function (Souza et al., 2008; Radi, >>2013<<). Although tyrosine nitration has been traditionally considered as an irreversible mechanism and a nitrosative stress marker, the existence of tyrosine denitrase activity that reduces 3-nitrotyrosine in mammalian cells (Görg et al., 2007;
n2:mentions: n3:23157446

Subject Item: _:vb49144988
rdf:type: n2:Context
rdf:value: Although tyrosine nitration has been traditionally considered as an irreversible mechanism and a nitrosative stress marker, the existence of tyrosine denitrase activity that reduces 3-nitrotyrosine in mammalian cells (Görg et al., >>2007<<; Deeb et al., 2013) pointing toward a role of tyrosine nitration in NO-mediated signaling processes in these cells.
n2:mentions: n3:17174954

Subject Item: _:vb49144989
rdf:type: n2:Context
rdf:value: nitration has been traditionally considered as an irreversible mechanism and a nitrosative stress marker, the existence of tyrosine denitrase activity that reduces 3-nitrotyrosine in mammalian cells (Görg et al., 2007; Deeb et al., >>2013<<) pointing toward a role of tyrosine nitration in NO-mediated signaling processes in these cells.
n2:mentions: n3:23792683

Subject Item: _:vb49144990
rdf:type: n2:Context
rdf:value: S-nitrosylation consists of the addition of a NO group to a cysteine thiol leading to S-nitrosothiols (SNOs) and consequently can also alter the function of a broad variety of proteins (Hess et al., >>2005<<; Astier et al., 2011). S-nitrosoglutathione (GSNO), formed by S-nitrosylation of the antioxidant GSH, is the major low-molecular-weight S-nitrosothiol.
n2:mentions: n3:15688001

Subject Item: _:vb49144991
rdf:type: n2:Context
rdf:value: It is considered to be a NO reservoir in cells (Gaston et al., >>1993<<; Durner et al., 1999; Leitner et al., 2009) that due to its phloem mobility is involved in signaling mechanisms.
n2:mentions: n3:8248198

Subject Item: _:vb49144992
rdf:type: n2:Context
rdf:value: It is considered to be a NO reservoir in cells (Gaston et al., 1993; Durner et al., >>1999<<; Leitner et al., 2009) that due to its phloem mobility is involved in signaling mechanisms.
n2:mentions: n3:10588683

Subject Item: _:vb49144993
rdf:type: n2:Context
rdf:value: It is considered to be a NO reservoir in cells (Gaston et al., 1993; Durner et al., 1999; Leitner et al., >>2009<<) that due to its phloem mobility is involved in signaling mechanisms.
n2:mentions: n3:19608448

Subject Item: _:vb49144994
rdf:type: n2:Context
rdf:value: Furthermore, GSNO can mediate transnitrosylation reactions in which a new S-nitrosothiol is generated by transferring its NO group to a new cysteine thiol group (Hess et al., >>2005<<).
n2:mentions: n3:15688001

Subject Item: _:vb49144995
rdf:type: n2:Context
rdf:value: S-nitrosylation is a reversible mechanism since SNO can be specifically and enzymatically broken down by thioredoxins (Benhar et al., >>2008<<; Kneeshaw et al., 2014), in addition to the non-enzymatic decomposition by antioxidants such as ascorbate or glutathione.
n2:mentions: n3:18497292

Subject Item: _:vb49144996
rdf:type: n2:Context
rdf:value: S-nitrosylation is a reversible mechanism since SNO can be specifically and enzymatically broken down by thioredoxins (Benhar et al., 2008; Kneeshaw et al., >>2014<<), in addition to the non-enzymatic decomposition by antioxidants such as ascorbate or glutathione.
n2:mentions: n3:25201412

Subject Item: _:vb49144997
rdf:type: n2:Context
rdf:value: Furthermore, S-nitrosoglutathione reductase (GSNOR) decomposes GSNO and indirectly controls SNO levels (Liu et al., >>2001<<; Feechan et al., 2005).
n2:mentions: n3:11260719

Subject Item: _:vb49144998
rdf:type: n2:Context
rdf:value: Furthermore, S-nitrosoglutathione reductase (GSNOR) decomposes GSNO and indirectly controls SNO levels (Liu et al., 2001; Feechan et al., >>2005<<).
n2:mentions: n3:15911759

Subject Item: _:vb49144999
rdf:type: n2:Context
rdf:value: In recent years, mounting evidence has shown that SNOs are fundamental players in NO-signaling pathways in plant biology (Belenghi et al., >>2007<<; Romero-Puertas et al., 2007, 2008; Lindermayr and Durner, 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007;
n2:mentions: n3:17110382

Subject Item: _:vb49145000
rdf:type: n2:Context
rdf:value: In recent years, mounting evidence has shown that SNOs are fundamental players in NO-signaling pathways in plant biology (Belenghi et al., 2007; Romero-Puertas et al., >>2007<<, 2008; Lindermayr and Durner, 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et
n2:mentions: n3:18165327

Subject Item: _:vb49145001
rdf:type: n2:Context
rdf:value: In recent years, mounting evidence has shown that SNOs are fundamental players in NO-signaling pathways in plant biology (Belenghi et al., 2007; Romero-Puertas et al., 2007, >>2008<<; Lindermayr and Durner, 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al.,
n2:mentions: n3:18297659

Subject Item: _:vb49145002
rdf:type: n2:Context
rdf:value: In recent years, mounting evidence has shown that SNOs are fundamental players in NO-signaling pathways in plant biology (Belenghi et al., 2007; Romero-Puertas et al., 2007, 2008; Lindermayr and Durner, >>2009<<; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a,
n2:mentions: n3:19619680

Subject Item: _:vb49145003
rdf:type: n2:Context
rdf:value: years, mounting evidence has shown that SNOs are fundamental players in NO-signaling pathways in plant biology (Belenghi et al., 2007; Romero-Puertas et al., 2007, 2008; Lindermayr and Durner, 2009; Astier et al., 2011; Hu et al., >>2015<<), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:25699590

Subject Item: _:vb49145004
rdf:type: n2:Context
rdf:value: biology (Belenghi et al., 2007; Romero-Puertas et al., 2007, 2008; Lindermayr and Durner, 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., >>2005<<; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:15911759

Subject Item: _:vb49145005
rdf:type: n2:Context
rdf:value: 2007; Romero-Puertas et al., 2007, 2008; Lindermayr and Durner, 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., >>2007<<; Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:17277089

Subject Item: _:vb49145006
rdf:type: n2:Context
rdf:value: et al., 2007, 2008; Lindermayr and Durner, 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., >>2007<<; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:17240373

Subject Item: _:vb49145007
rdf:type: n2:Context
rdf:value: and Durner, 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al., >>2008<<; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:18801763

Subject Item: _:vb49145008
rdf:type: n2:Context
rdf:value: 2009; Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:19112080

Subject Item: _:vb49145009
rdf:type: n2:Context
rdf:value: Astier et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b). Due to its importance, increased efforts have been made to identify the processes that could be regulated by SNOs and subsequently hundreds of proteins that undergo S-nitrosylation under physiological or adverse conditions have been
n2:mentions: n3:21172815

Subject Item: _:vb49145010
rdf:type: n2:Context
rdf:value: et al., 2011; Hu et al., 2015), with an important role in plant immunity and plant response to abiotic stresses (Feechan et al., 2005; Rusterucci et al., 2007; Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b). Due to its importance, increased efforts have been made to identify the processes that could be regulated by SNOs and subsequently hundreds of proteins that undergo S-nitrosylation under physiological or adverse conditions have been
n2:mentions: n3:21676000

Subject Item: _:vb49145011
rdf:type: n7:Section
dc:title: s-nitrosylation controls onoo- levels via regulation of prxii e
n7:contains: _:vb49145016 _:vb49145017 _:vb49145018 _:vb49145019 _:vb49145020 _:vb49145021 _:vb49145022 _:vb49145023 _:vb49145012 _:vb49145013 _:vb49145014 _:vb49145015 _:vb49145024 _:vb49145025 _:vb49145026 _:vb49145027

Subject Item: _:vb49145012
rdf:type: n2:Context
rdf:value: Peroxiredoxins (Prx) are thiol based peroxidases that can be involved in multiple functions in addition to its role in detoxifying H2O2 (for review see Bhatt and Tripathi, >>2011<<). Some Prxs have been identified to be regulated by NO-PTMs in animals and plants.
n2:mentions: n3:21777667

Subject Item: _:vb49145013
rdf:type: n2:Context
rdf:value: In mammals, S-nitrosylation inhibits the enzymatic activity of neuronal Prx2 (Fang et al., >>2007<<) and Prx1 (Engelman et al., 2013) whereas the peroxidase activity of Prx2 from mammalian erythrocytes was induced after tyrosine nitration (Randall et al., 2014).
n2:mentions: n3:18003920

Subject Item: _:vb49145014
rdf:type: n2:Context
rdf:value: In mammals, S-nitrosylation inhibits the enzymatic activity of neuronal Prx2 (Fang et al., 2007) and Prx1 (Engelman et al., >>2013<<) whereas the peroxidase activity of Prx2 from mammalian erythrocytes was induced after tyrosine nitration (Randall et al., 2014).
n2:mentions: n3:23479738

Subject Item: _:vb49145015
rdf:type: n2:Context
rdf:value: inhibits the enzymatic activity of neuronal Prx2 (Fang et al., 2007) and Prx1 (Engelman et al., 2013) whereas the peroxidase activity of Prx2 from mammalian erythrocytes was induced after tyrosine nitration (Randall et al., >>2014<<). In plants, S-nitrosylation inhibits the peroxidase activity of PrxII E (Romero-Puertas et al., 2007) and PrxII F (Camejo et al., 2015).
n2:mentions: n3:24719319

Subject Item: _:vb49145016
rdf:type: n2:Context
rdf:value: In plants, S-nitrosylation inhibits the peroxidase activity of PrxII E (Romero-Puertas et al., >>2007<<) and PrxII F (Camejo et al., 2015).
n2:mentions: n3:18165327

Subject Item: _:vb49145017
rdf:type: n2:Context
rdf:value: In plants, S-nitrosylation inhibits the peroxidase activity of PrxII E (Romero-Puertas et al., 2007) and PrxII F (Camejo et al., >>2015<<). Interestingly, some members of Prx family posses ONOO- reductase activity (Bryk et al., 2000; Romero-Puertas et al., 2007; Pedrajas et al., 2010) and therefore could protect against ONOO--mediated oxidative and nitrosative stresses. In
n2:mentions: n3:25682994

Subject Item: _:vb49145018
rdf:type: n2:Context
rdf:value: Interestingly, some members of Prx family posses ONOO- reductase activity (Bryk et al., >>2000<<; Romero-Puertas et al., 2007; Pedrajas et al., 2010) and therefore could protect against ONOO--mediated oxidative and nitrosative stresses.
n2:mentions: n3:11001062

Subject Item: _:vb49145019
rdf:type: n2:Context
rdf:value: Interestingly, some members of Prx family posses ONOO- reductase activity (Bryk et al., 2000; Romero-Puertas et al., >>2007<<; Pedrajas et al., 2010) and therefore could protect against ONOO--mediated oxidative and nitrosative stresses.
n2:mentions: n3:18165327

Subject Item: _:vb49145020
rdf:type: n2:Context
rdf:value: Interestingly, some members of Prx family posses ONOO- reductase activity (Bryk et al., 2000; Romero-Puertas et al., 2007; Pedrajas et al., >>2010<<) and therefore could protect against ONOO--mediated oxidative and nitrosative stresses.
n2:mentions: n3:20547232

Subject Item: _:vb49145021
rdf:type: n2:Context
rdf:value: In plants, PrxII E is S-nitrosylated during hypersensitive response (Romero-Puertas et al., >>2008<<) and this modification inhibits its peroxynitrite reductase activity promoting tyrosine nitration (Romero-Puertas et al., 2007).
n2:mentions: n3:18297659

Subject Item: _:vb49145022
rdf:type: n2:Context
rdf:value: In plants, PrxII E is S-nitrosylated during hypersensitive response (Romero-Puertas et al., 2008) and this modification inhibits its peroxynitrite reductase activity promoting tyrosine nitration (Romero-Puertas et al., >>2007<<). Therefore, S-nitrosylation emerges as a key mechanism in ONOO- homeostasis, regulating endogenous level of ONOO- and tyrosine nitration via control of PrxII E (Romero-Puertas et al., 2007). Changes in ONOO- levels and/or tyrosine
n2:mentions: n3:18165327

Subject Item: _:vb49145023
rdf:type: n2:Context
rdf:value: Therefore, S-nitrosylation emerges as a key mechanism in ONOO- homeostasis, regulating endogenous level of ONOO- and tyrosine nitration via control of PrxII E (Romero-Puertas et al., >>2007<<). Changes in ONOO- levels and/or tyrosine nitration have been related to several abiotic/biotic stresses (Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b). Consequently, understanding if S-nitrosylation of PrxII
n2:mentions: n3:18165327

Subject Item: _:vb49145024
rdf:type: n2:Context
rdf:value: Changes in ONOO- levels and/or tyrosine nitration have been related to several abiotic/biotic stresses (Valderrama et al., >>2007<<; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:17240373

Subject Item: _:vb49145025
rdf:type: n2:Context
rdf:value: Changes in ONOO- levels and/or tyrosine nitration have been related to several abiotic/biotic stresses (Valderrama et al., 2007; Corpas et al., >>2008<<; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:18801763

Subject Item: _:vb49145026
rdf:type: n2:Context
rdf:value: Changes in ONOO- levels and/or tyrosine nitration have been related to several abiotic/biotic stresses (Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b).
n2:mentions: n3:19112080

Subject Item: _:vb49145027
rdf:type: n2:Context
rdf:value: Changes in ONOO- levels and/or tyrosine nitration have been related to several abiotic/biotic stresses (Valderrama et al., 2007; Corpas et al., 2008; Chaki et al., 2009a, 2011a,b). Consequently, understanding if S-nitrosylation of PrxII E could be involved in plant response to these stress conditions is a good issue to be addressed in the future.
n2:mentions: n3:21676000 n3:21172815

Subject Item: _:vb49145028
rdf:type: n7:Section
dc:title: nitric oxide interactions with catalase and superoxide dismutases
n7:contains: _:vb49145040 _:vb49145029 _:vb49145030 _:vb49145031 _:vb49145036 _:vb49145037 _:vb49145038 _:vb49145039 _:vb49145032 _:vb49145033 _:vb49145034 _:vb49145035

Subject Item: _:vb49145029
rdf:type: n2:Context
rdf:value: Superoxide dismutase (SOD) is a group of metalloenzymes that catalyze the disproportionation of superoxide radicals into H2O2 (Fridovich, >>1986<<; Halliwell and Gutteridge, 2000). SODs are classified into three main types containing Mn, Fe, or Cu plus Zn as prosthetic metals and they are present in all cell compartments (Parker et al., 1984; Zelko et al., 2002).
n2:mentions: n3:3010872

Subject Item: _:vb49145030
rdf:type: n2:Context
rdf:value: In eukaryotic cells from different organisms, it has been demonstrated that Mn-, Fe-, and CuZn-SODs undergo inactivation by peroxynitrite-mediated nitration (Demicheli et al., >>2007<<; Martinez et al., 2014) and SOD activity is increased after GSNO treatment (Sehrawat et al., 2013).
n2:mentions: n3:17395009

Subject Item: _:vb49145031
rdf:type: n2:Context
rdf:value: In eukaryotic cells from different organisms, it has been demonstrated that Mn-, Fe-, and CuZn-SODs undergo inactivation by peroxynitrite-mediated nitration (Demicheli et al., 2007; Martinez et al., >>2014<<) and SOD activity is increased after GSNO treatment (Sehrawat et al., 2013).
n2:mentions: n3:24616096

Subject Item: _:vb49145032
rdf:type: n2:Context
rdf:value: Thus, whereas S-nitrosylation did not affect SOD activities, nitration inhibited Mn-SOD1, Fe-SOD3, and CuZn-SOD3 activity to different degrees but affected no other SOD isozymes (Holzmeister et al., >>2015<<).
n2:mentions: n3:25428993

Subject Item: _:vb49145033
rdf:type: n2:Context
rdf:value: On the other hand, catalase, which is a peroxisomal key enzyme that regulates H2O2 levels (Chance et al., >>1979<<; Kirkman and Gaetani, 1984), was one of the first antioxidant enzymes to be analyzed in vitro to check how its activity can be modulated by NO donors (Clark et al., 2000).
n2:mentions: n3:37532

Subject Item: _:vb49145034
rdf:type: n2:Context
rdf:value: On the other hand, catalase, which is a peroxisomal key enzyme that regulates H2O2 levels (Chance et al., 1979; Kirkman and Gaetani, >>1984<<), was one of the first antioxidant enzymes to be analyzed in vitro to check how its activity can be modulated by NO donors (Clark et al., 2000).
n2:mentions: n3:6589599

Subject Item: _:vb49145035
rdf:type: n2:Context
rdf:value: key enzyme that regulates H2O2 levels (Chance et al., 1979; Kirkman and Gaetani, 1984), was one of the first antioxidant enzymes to be analyzed in vitro to check how its activity can be modulated by NO donors (Clark et al., >>2000<<). At present, it is known that plant catalase can be nitrated and S-nitrosylated in vitro, both of which inhibit its activity (Clark et al., 2000; Ortega-Galisteo et al., 2012), although, according to the literature available, the
n2:mentions: n3:11106031

Subject Item: _:vb49145036
rdf:type: n2:Context
rdf:value: At present, it is known that plant catalase can be nitrated and S-nitrosylated in vitro, both of which inhibit its activity (Clark et al., >>2000<<; Ortega-Galisteo et al., 2012), although, according to the literature available, the specific target residues have not yet been identified.
n2:mentions: n3:11106031

Subject Item: _:vb49145037
rdf:type: n2:Context
rdf:value: At present, it is known that plant catalase can be nitrated and S-nitrosylated in vitro, both of which inhibit its activity (Clark et al., 2000; Ortega-Galisteo et al., >>2012<<), although, according to the literature available, the specific target residues have not yet been identified.
n2:mentions: n3:22213812

Subject Item: _:vb49145038
rdf:type: n2:Context
rdf:value: that catalase undergoes increasing nitration during pepper fruit maturation, decreasing its activity as consequence of potential tyrosine nitration as corroborated after treatment with SIN-1 (a peroxynitrite donor; Chaki et al., >>2015<<). This inhibition could imply a lower capacity for removing H2O2 and therefore is well correlated with the increase of the oxidative metabolism observed during this physiological process (Martí et al., 2011; Chaki et al., 2015).
n2:mentions: n3:25814060

Subject Item: _:vb49145039
rdf:type: n2:Context
rdf:value: This inhibition could imply a lower capacity for removing H2O2 and therefore is well correlated with the increase of the oxidative metabolism observed during this physiological process (Martí et al., >>2011<<; Chaki et al., 2015).
n2:mentions: n3:21792678

Subject Item: _:vb49145040
rdf:type: n2:Context
rdf:value: This inhibition could imply a lower capacity for removing H2O2 and therefore is well correlated with the increase of the oxidative metabolism observed during this physiological process (Martí et al., 2011; Chaki et al., >>2015<<).
n2:mentions: n3:25814060

Subject Item: _:vb49145041
rdf:type: n7:Section
dc:title: ascorbate-glutathione cycle and nitric oxide-ptms
n7:contains: _:vb49145088 _:vb49145089 _:vb49145090 _:vb49145091 _:vb49145092 _:vb49145093 _:vb49145094 _:vb49145095 _:vb49145096 _:vb49145097 _:vb49145098 _:vb49145099 _:vb49145100 _:vb49145101 _:vb49145102 _:vb49145103 _:vb49145104 _:vb49145105 _:vb49145056 _:vb49145057 _:vb49145058 _:vb49145059 _:vb49145060 _:vb49145061 _:vb49145062 _:vb49145063 _:vb49145064 _:vb49145065 _:vb49145066 _:vb49145067 _:vb49145068 _:vb49145069 _:vb49145070 _:vb49145071 _:vb49145072 _:vb49145073 _:vb49145074 _:vb49145075 _:vb49145076 _:vb49145077 _:vb49145078 _:vb49145079 _:vb49145080 _:vb49145081 _:vb49145082 _:vb49145083 _:vb49145084 _:vb49145085 _:vb49145086 _:vb49145087 _:vb49145042 _:vb49145043 _:vb49145044 _:vb49145045 _:vb49145046 _:vb49145047 _:vb49145048 _:vb49145049 _:vb49145050 _:vb49145051 _:vb49145052 _:vb49145053 _:vb49145054 _:vb49145055

Subject Item: _:vb49145042
rdf:type: n2:Context
rdf:value: Ascorbate-glutathione cycle is a pivotal antioxidant system involved in the regulation of H2O2 levels (Asada, 1992; Noctor and Foyer, >>1998<<; Shigeoka et al., 2002) under development and unfavorable conditions in plant cells.
n2:mentions: n3:15012235

Subject Item: _:vb49145043
rdf:type: n2:Context
rdf:value: Ascorbate-glutathione cycle is a pivotal antioxidant system involved in the regulation of H2O2 levels (Asada, 1992; Noctor and Foyer, 1998; Shigeoka et al., >>2002<<) under development and unfavorable conditions in plant cells. The cycle is composed of the enzymes APX, MDAR, DHAR, and GR plus the non-enzymatic antioxidants ascorbate and glutathione (GSH).
n2:mentions: n3:11997377

Subject Item: _:vb49145044
rdf:type: n2:Context
rdf:value: ProteinNO-PTMEffectsTargetPlant speciesReferenceAscorbate peroxidase (APX)Tyrosine nitrationDecreased activityTyr235(1)Pisum sativumBegara-Morales et al., >>2014<<S-nitrosylationIncreased activityCys32(1)(2)(3)Arabidopsis thaliana,Begara-Morales et al., 2014;Pisum sativumYang et al., 2015Monodehydro-ascorbate reductase (MDAR)Tyrosine nitrationDecreased activityTyr345(1)Pisum sativumBegara-Morales et
n2:mentions: n3:24288182

Subject Item: _:vb49145045
rdf:type: n2:Context
rdf:value: speciesReferenceAscorbate peroxidase (APX)Tyrosine nitrationDecreased activityTyr235(1)Pisum sativumBegara-Morales et al., 2014S-nitrosylationIncreased activityCys32(1)(2)(3)Arabidopsis thaliana,Begara-Morales et al., >>2014<<;Pisum sativumYang et al., 2015Monodehydro-ascorbate reductase (MDAR)Tyrosine nitrationDecreased activityTyr345(1)Pisum sativumBegara-Morales et al., 2015S-nitrosylationDecreased activityCys68(3)Pisum sativumBegara-Morales et al.,
n2:mentions: n3:24288182

Subject Item: _:vb49145046
rdf:type: n2:Context
rdf:value: peroxidase (APX)Tyrosine nitrationDecreased activityTyr235(1)Pisum sativumBegara-Morales et al., 2014S-nitrosylationIncreased activityCys32(1)(2)(3)Arabidopsis thaliana,Begara-Morales et al., 2014;Pisum sativumYang et al., >>2015<<Monodehydro-ascorbate reductase (MDAR)Tyrosine nitrationDecreased activityTyr345(1)Pisum sativumBegara-Morales et al., 2015S-nitrosylationDecreased activityCys68(3)Pisum sativumBegara-Morales et al., 2015Dehydro-ascorbate reductase
n2:mentions: n3:25667317

Subject Item: _:vb49145047
rdf:type: n2:Context
rdf:value: activityCys32(1)(2)(3)Arabidopsis thaliana,Begara-Morales et al., 2014;Pisum sativumYang et al., 2015Monodehydro-ascorbate reductase (MDAR)Tyrosine nitrationDecreased activityTyr345(1)Pisum sativumBegara-Morales et al., >>2015<<S-nitrosylationDecreased activityCys68(3)Pisum sativumBegara-Morales et al., 2015Dehydro-ascorbate reductase (DHAR)Tyrosine nitrationN.D.N.D.N.D.Fares et al., 2011; Kato et al., 2013; Puyaubert et al., 2014S-nitrosylationDecreased
n2:mentions: n3:26116026

Subject Item: _:vb49145048
rdf:type: n2:Context
rdf:value: 2014;Pisum sativumYang et al., 2015Monodehydro-ascorbate reductase (MDAR)Tyrosine nitrationDecreased activityTyr345(1)Pisum sativumBegara-Morales et al., 2015S-nitrosylationDecreased activityCys68(3)Pisum sativumBegara-Morales et al., >>2015<<Dehydro-ascorbate reductase (DHAR)Tyrosine nitrationN.D.N.D.N.D.Fares et al., 2011; Kato et al., 2013; Puyaubert et al., 2014S-nitrosylationDecreased activityCys20(1)(2),Arabidopsis thaliana;Cys147(1)(2)Solanum tuberosumGlutathione
n2:mentions: n3:26116026

Subject Item: _:vb49145049
rdf:type: n2:Context
rdf:value: nitrationDecreased activityTyr345(1)Pisum sativumBegara-Morales et al., 2015S-nitrosylationDecreased activityCys68(3)Pisum sativumBegara-Morales et al., 2015Dehydro-ascorbate reductase (DHAR)Tyrosine nitrationN.D.N.D.N.D.Fares et al., >>2011<<; Kato et al., 2013; Puyaubert et al., 2014S-nitrosylationDecreased activityCys20(1)(2),Arabidopsis thaliana;Cys147(1)(2)Solanum tuberosumGlutathione reductase (GR)Tyrosine nitrationNo effectN.D.Pisum sativumBegara-Morales et al.,
n2:mentions: n3:22115780

Subject Item: _:vb49145050
rdf:type: n2:Context
rdf:value: activityTyr345(1)Pisum sativumBegara-Morales et al., 2015S-nitrosylationDecreased activityCys68(3)Pisum sativumBegara-Morales et al., 2015Dehydro-ascorbate reductase (DHAR)Tyrosine nitrationN.D.N.D.N.D.Fares et al., 2011; Kato et al., >>2013<<; Puyaubert et al., 2014S-nitrosylationDecreased activityCys20(1)(2),Arabidopsis thaliana;Cys147(1)(2)Solanum tuberosumGlutathione reductase (GR)Tyrosine nitrationNo effectN.D.Pisum sativumBegara-Morales et al.,
n2:mentions: n3:22924747

Subject Item: _:vb49145051
rdf:type: n2:Context
rdf:value: et al., 2015S-nitrosylationDecreased activityCys68(3)Pisum sativumBegara-Morales et al., 2015Dehydro-ascorbate reductase (DHAR)Tyrosine nitrationN.D.N.D.N.D.Fares et al., 2011; Kato et al., 2013; Puyaubert et al., >>2014<<S-nitrosylationDecreased activityCys20(1)(2),Arabidopsis thaliana;Cys147(1)(2)Solanum tuberosumGlutathione reductase (GR)Tyrosine nitrationNo effectN.D.Pisum sativumBegara-Morales et al., 2015S-nitrosylationNitration and S-nitrosylation
n2:mentions: n3:24388526

Subject Item: _:vb49145052
rdf:type: n2:Context
rdf:value: 2011; Kato et al., 2013; Puyaubert et al., 2014S-nitrosylationDecreased activityCys20(1)(2),Arabidopsis thaliana;Cys147(1)(2)Solanum tuberosumGlutathione reductase (GR)Tyrosine nitrationNo effectN.D.Pisum sativumBegara-Morales et al., >>2015<<S-nitrosylationNitration and S-nitrosylation targets have been identified by different technological approaches:
n2:mentions: n3:26116026

Subject Item: _:vb49145053
rdf:type: n2:Context
rdf:value: Proteomic approaches have identified all enzymes of the Asa-GSH cycle as potential nitrated proteins (Chaki et al., 2009b; Lin et al., 2012; Tanou et al., 2012).
n2:mentions: n3:19717529

Subject Item: _:vb49145054
rdf:type: n2:Context
rdf:value: Proteomic approaches have identified all enzymes of the Asa-GSH cycle as potential nitrated proteins (Chaki et al., 2009b; Lin et al., >>2012<<; Tanou et al., 2012).
n2:mentions: n3:22106097

Subject Item: _:vb49145055
rdf:type: n2:Context
rdf:value: Proteomic approaches have identified all enzymes of the Asa-GSH cycle as potential nitrated proteins (Chaki et al., 2009b; Lin et al., 2012; Tanou et al., >>2012<<). However, information related to the specific impact of this modification on the structure of these target proteins and the role of the tyrosine target of nitration is necessary in order to understand the cross-talk between NO and ROS in
n2:mentions: n3:22780834

Subject Item: _:vb49145056
rdf:type: n2:Context
rdf:value: the tyrosine target(s) of nitration and its (their) potential role within the mechanistic activity of the Asa-GSH cycle enzymes, showing that this NO-PTM could compromise the Asa-GSH cycle functioning (Begara-Morales et al., >>2014<<, 2015). Pea cytosolic APX is inactivated by ONOO- as consequence of tyrosine nitration (Begara-Morales et al., 2014) and as result the detoxification of H2O2 by Asa-GSH cycle could be compromised (Figure 1).
n2:mentions: n3:24288182

Subject Item: _:vb49145057
rdf:type: n2:Context
rdf:value: the tyrosine target(s) of nitration and its (their) potential role within the mechanistic activity of the Asa-GSH cycle enzymes, showing that this NO-PTM could compromise the Asa-GSH cycle functioning (Begara-Morales et al., 2014, >>2015<<). Pea cytosolic APX is inactivated by ONOO- as consequence of tyrosine nitration (Begara-Morales et al., 2014) and as result the detoxification of H2O2 by Asa-GSH cycle could be compromised (Figure 1).
n2:mentions: n3:26116026

Subject Item: _:vb49145058
rdf:type: n2:Context
rdf:value: Pea cytosolic APX is inactivated by ONOO- as consequence of tyrosine nitration (Begara-Morales et al., >>2014<<) and as result the detoxification of H2O2 by Asa-GSH cycle could be compromised (Figure 1).
n2:mentions: n3:24288182

Subject Item: _:vb49145059
rdf:type: n2:Context
rdf:value: and in silico approaches identified the Tyr235 as the most reliable target responsible for APX inactivation, since this residue is located just at 3.6 Å from the heme group at the bottom of the catalytic pocket (Patterson and Poulos, >>1995<<; Jespersen et al., 1997; Mandelman et al., 1998; Begara-Morales et al., 2014). Consequently, Tyr235 nitration may disrupt heme-group properties and result in a loss of activity (Begara-Morales et al., 2014).
n2:mentions: n3:7703247

Subject Item: _:vb49145060
rdf:type: n2:Context
rdf:value: identified the Tyr235 as the most reliable target responsible for APX inactivation, since this residue is located just at 3.6 Å from the heme group at the bottom of the catalytic pocket (Patterson and Poulos, 1995; Jespersen et al., >>1997<<; Mandelman et al., 1998; Begara-Morales et al., 2014). Consequently, Tyr235 nitration may disrupt heme-group properties and result in a loss of activity (Begara-Morales et al., 2014).
n2:mentions: n3:9291097

Subject Item: _:vb49145061
rdf:type: n2:Context
rdf:value: as the most reliable target responsible for APX inactivation, since this residue is located just at 3.6 Å from the heme group at the bottom of the catalytic pocket (Patterson and Poulos, 1995; Jespersen et al., 1997; Mandelman et al., >>1998<<; Begara-Morales et al., 2014). Consequently, Tyr235 nitration may disrupt heme-group properties and result in a loss of activity (Begara-Morales et al., 2014).
n2:mentions: n3:9860877

Subject Item: _:vb49145062
rdf:type: n2:Context
rdf:value: for APX inactivation, since this residue is located just at 3.6 Å from the heme group at the bottom of the catalytic pocket (Patterson and Poulos, 1995; Jespersen et al., 1997; Mandelman et al., 1998; Begara-Morales et al., >>2014<<). Consequently, Tyr235 nitration may disrupt heme-group properties and result in a loss of activity (Begara-Morales et al., 2014).
n2:mentions: n3:24288182

Subject Item: _:vb49145063
rdf:type: n2:Context
rdf:value: Consequently, Tyr235 nitration may disrupt heme-group properties and result in a loss of activity (Begara-Morales et al., >>2014<<).
n2:mentions: n3:24288182

Subject Item: _:vb49145064
rdf:type: n2:Context
rdf:value: In this case, ONOO- mediates nitration of recombinant pea MDAR at Tyr213, Tyr292, and Tyr345, causing an inhibition of the enzymatic activity (Begara-Morales et al., >>2015<<), and therefore may disrupt the regeneration of ascorbate and compromise the functioning of the Asa-GSH cycle.
n2:mentions: n3:26116026

Subject Item: _:vb49145065
rdf:type: n2:Context
rdf:value: tyrosine is located just at 3.3 Å from His313, which is involved in NADP binding, suggesting that the nitration of this tyrosine could alter the positioning of the cofactor, thereby decreasing protein activity (Begara-Morales et al., >>2015<<). DHAR is the other enzyme involved in the regeneration of ascorbate, but, although DHAR has been reported to be nitrated (Tanou et al., 2012) and its activity modulated by NO (see Groβ et al., 2013), no information is available on the
n2:mentions: n3:26116026

Subject Item: _:vb49145066
rdf:type: n2:Context
rdf:value: DHAR is the other enzyme involved in the regeneration of ascorbate, but, although DHAR has been reported to be nitrated (Tanou et al., >>2012<<) and its activity modulated by NO (see Groβ et al., 2013), no information is available on the tyrosine(s) involved in this modification and the impact on the protein structure.
n2:mentions: n3:22780834

Subject Item: _:vb49145067
rdf:type: n2:Context
rdf:value: Glutathione reductase has also been identified as tyrosine nitration target (Chaki et al., 2009b). In animals, peroxynitrite inhibits human and bovine GR activity by nitration of Tyr106 and Tyr114 which are located close to the GSSG binding zone (Francescutti et al., 1996; Savvides et al., 2002).
n2:mentions: n3:19717529

Subject Item: _:vb49145068
rdf:type: n2:Context
rdf:value: In animals, peroxynitrite inhibits human and bovine GR activity by nitration of Tyr106 and Tyr114 which are located close to the GSSG binding zone (Francescutti et al., >>1996<<; Savvides et al., 2002).
n2:mentions: n3:9005440

Subject Item: _:vb49145069
rdf:type: n2:Context
rdf:value: In animals, peroxynitrite inhibits human and bovine GR activity by nitration of Tyr106 and Tyr114 which are located close to the GSSG binding zone (Francescutti et al., 1996; Savvides et al., >>2002<<). However, very recently and in contrast to animals, it has been strikingly shown that chloroplastic and cytosolic pea GR activities are not affected by peroxynitrite-mediated tyrosine nitration (Begara-Morales et al., 2015). This
n2:mentions: n3:11705998

Subject Item: _:vb49145070
rdf:type: n2:Context
rdf:value: However, very recently and in contrast to animals, it has been strikingly shown that chloroplastic and cytosolic pea GR activities are not affected by peroxynitrite-mediated tyrosine nitration (Begara-Morales et al., >>2015<<). This behavior is unusual in higher plants, where the main effect of tyrosine nitration on target proteins is usually a loss of function (Astier and Lindermayr, 2012; Begara-Morales et al., 2013; Chaki et al., 2013; Corpas et al., 2013).
n2:mentions: n3:26116026

Subject Item: _:vb49145071
rdf:type: n2:Context
rdf:value: This behavior is unusual in higher plants, where the main effect of tyrosine nitration on target proteins is usually a loss of function (Astier and Lindermayr, >>2012<<; Begara-Morales et al., 2013; Chaki et al., 2013; Corpas et al., 2013).
n2:mentions: n3:23203119

Subject Item: _:vb49145072
rdf:type: n2:Context
rdf:value: This behavior is unusual in higher plants, where the main effect of tyrosine nitration on target proteins is usually a loss of function (Astier and Lindermayr, 2012; Begara-Morales et al., >>2013<<; Chaki et al., 2013; Corpas et al., 2013).
n2:mentions: n3:23362300

Subject Item: _:vb49145073
rdf:type: n2:Context
rdf:value: This behavior is unusual in higher plants, where the main effect of tyrosine nitration on target proteins is usually a loss of function (Astier and Lindermayr, 2012; Begara-Morales et al., 2013; Chaki et al., >>2013<<; Corpas et al., 2013).
n2:mentions: n3:23266784

Subject Item: _:vb49145074
rdf:type: n2:Context
rdf:value: This behavior is unusual in higher plants, where the main effect of tyrosine nitration on target proteins is usually a loss of function (Astier and Lindermayr, 2012; Begara-Morales et al., 2013; Chaki et al., 2013; Corpas et al., >>2013<<).
n2:mentions: n3:23860243

Subject Item: _:vb49145075
rdf:type: n2:Context
rdf:value: For instance, NO regulates many enzymes involved in ROS/RNS generation/scavenging such as GSNOR (Frungillo et al., 2014), NADPH oxidase (Yun et al., >>2011<<), catalase (Ortega-Galisteo et al., 2012), and peroxiredoxinII E (Romero-Puertas et al., 2007) and II F (Camejo et al., 2015).
n2:mentions: n3:21964330

Subject Item: _:vb49145076
rdf:type: n2:Context
rdf:value: For instance, NO regulates many enzymes involved in ROS/RNS generation/scavenging such as GSNOR (Frungillo et al., 2014), NADPH oxidase (Yun et al., 2011), catalase (Ortega-Galisteo et al., >>2012<<), and peroxiredoxinII E (Romero-Puertas et al., 2007) and II F (Camejo et al., 2015).
n2:mentions: n3:22213812

Subject Item: _:vb49145077
rdf:type: n2:Context
rdf:value: NO regulates many enzymes involved in ROS/RNS generation/scavenging such as GSNOR (Frungillo et al., 2014), NADPH oxidase (Yun et al., 2011), catalase (Ortega-Galisteo et al., 2012), and peroxiredoxinII E (Romero-Puertas et al., >>2007<<) and II F (Camejo et al., 2015).
n2:mentions: n3:18165327

Subject Item: _:vb49145078
rdf:type: n2:Context
rdf:value: involved in ROS/RNS generation/scavenging such as GSNOR (Frungillo et al., 2014), NADPH oxidase (Yun et al., 2011), catalase (Ortega-Galisteo et al., 2012), and peroxiredoxinII E (Romero-Puertas et al., 2007) and II F (Camejo et al., >>2015<<). S-nitrosylation appears to be critical to GSNO and ONOO- homeostasis as this NO-PTM inhibits GSNOR and PrxII E activities (Romero-Puertas et al., 2007; Frungillo et al., 2014) that decompose GSNO and ONOO-, respectively.
n2:mentions: n3:25682994

Subject Item: _:vb49145079
rdf:type: n2:Context
rdf:value: S-nitrosylation appears to be critical to GSNO and ONOO- homeostasis as this NO-PTM inhibits GSNOR and PrxII E activities (Romero-Puertas et al., >>2007<<; Frungillo et al., 2014) that decompose GSNO and ONOO-, respectively.
n2:mentions: n3:18165327

Subject Item: _:vb49145080
rdf:type: n2:Context
rdf:value: A connection has also been observed between NO and ROS pathway under different physiological and stress conditions (Corpas et al., >>2011<<; Groβ et al., 2013; Procházková et al., 2014).
n2:mentions: n3:21893257

Subject Item: _:vb49145081
rdf:type: n2:Context
rdf:value: Furthermore, all components of Asa-GSH cycle have been reported to be S-nitrosylated (Lin et al., >>2012<<; Tanou et al., 2012) with a different effect on protein activity (Kato et al., 2013; Begara-Morales et al., 2014, 2015).
n2:mentions: n3:22106097

Subject Item: _:vb49145082
rdf:type: n2:Context
rdf:value: Furthermore, all components of Asa-GSH cycle have been reported to be S-nitrosylated (Lin et al., 2012; Tanou et al., >>2012<<) with a different effect on protein activity (Kato et al., 2013; Begara-Morales et al., 2014, 2015).
n2:mentions: n3:22780834

Subject Item: _:vb49145083
rdf:type: n2:Context
rdf:value: Furthermore, all components of Asa-GSH cycle have been reported to be S-nitrosylated (Lin et al., 2012; Tanou et al., 2012) with a different effect on protein activity (Kato et al., >>2013<<; Begara-Morales et al., 2014, 2015).
n2:mentions: n3:22924747

Subject Item: _:vb49145084
rdf:type: n2:Context
rdf:value: Furthermore, all components of Asa-GSH cycle have been reported to be S-nitrosylated (Lin et al., 2012; Tanou et al., 2012) with a different effect on protein activity (Kato et al., 2013; Begara-Morales et al., >>2014<<, 2015).
n2:mentions: n3:24288182

Subject Item: _:vb49145085
rdf:type: n2:Context
rdf:value: Furthermore, all components of Asa-GSH cycle have been reported to be S-nitrosylated (Lin et al., 2012; Tanou et al., 2012) with a different effect on protein activity (Kato et al., 2013; Begara-Morales et al., 2014, >>2015<<).
n2:mentions: n3:26116026

Subject Item: _:vb49145086
rdf:type: n2:Context
rdf:value: Dehydroascorbate reductase has been identified as S-nitrosylation target at Cys20 under no-stress conditions in Arabidopsis, and this Cys20 is not over-nitrosylated under salinity or cold stress (Fares et al., >>2011<<; Puyaubert et al., 2014). Recently, it has been reported that S-nitrosylation at Cys20 and Cys147 negatively regulates the enzymatic activity of DHAR in potato plants (Kato et al., 2013).
n2:mentions: n3:22115780

Subject Item: _:vb49145087
rdf:type: n2:Context
rdf:value: Dehydroascorbate reductase has been identified as S-nitrosylation target at Cys20 under no-stress conditions in Arabidopsis, and this Cys20 is not over-nitrosylated under salinity or cold stress (Fares et al., 2011; Puyaubert et al., >>2014<<). Recently, it has been reported that S-nitrosylation at Cys20 and Cys147 negatively regulates the enzymatic activity of DHAR in potato plants (Kato et al., 2013).
n2:mentions: n3:24388526

Subject Item: _:vb49145088
rdf:type: n2:Context
rdf:value: Recently, it has been reported that S-nitrosylation at Cys20 and Cys147 negatively regulates the enzymatic activity of DHAR in potato plants (Kato et al., >>2013<<). Furthermore, peroxisomal recombinant pea MDAR, which has only two cysteines (Cys197 and Cys68) is also inhibited by S-nitrosylation (Begara-Morales et al., 2015). The authors suggest using in silico and evolutionary analysis that Cys68
n2:mentions: n3:22924747

Subject Item: _:vb49145089
rdf:type: n2:Context
rdf:value: Furthermore, peroxisomal recombinant pea MDAR, which has only two cysteines (Cys197 and Cys68) is also inhibited by S-nitrosylation (Begara-Morales et al., >>2015<<). The authors suggest using in silico and evolutionary analysis that Cys68 could be the most reliable residue responsible for the loss of activity following GSNO treatment. However, future experiments such as site-directed mutagenesis
n2:mentions: n3:26116026

Subject Item: _:vb49145090
rdf:type: n2:Context
rdf:value: In any case, it is clear that peroxisomal pea MDAR is S-nitrosylated by GSNO, as corroborated by the biotin-switch method, and as result the protein activity is inhibited (Begara-Morales et al., >>2015<<). The inhibition of DHAR and MDAR by S-nitrosylation (Figure 1) could compromise ascorbate regeneration and therefore the functioning of the cycle. Notably, in the same work it is shown that chloroplastic and cytosolic pea GR are also
n2:mentions: n3:26116026

Subject Item: _:vb49145091
rdf:type: n2:Context
rdf:value: In mammal cells GSNO treatment for 1h does not affect GR, although an inhibitory effect is produced after longer exposures to GSNO (Beltrán et al., >>2000<<). In addition, human GR is inhibited by GSNO as consequence of S-nitrosylation of two catalytic Cys, Cys63 and/or Cys58 (Becker et al., 1995; Francescutti et al., 1996). These results suggest a different regulation of pea and mammalian GR
n2:mentions: n3:10696095

Subject Item: _:vb49145092
rdf:type: n2:Context
rdf:value: In addition, human GR is inhibited by GSNO as consequence of S-nitrosylation of two catalytic Cys, Cys63 and/or Cys58 (Becker et al., >>1995<<; Francescutti et al., 1996).
n2:mentions: n3:8536691

Subject Item: _:vb49145093
rdf:type: n2:Context
rdf:value: In addition, human GR is inhibited by GSNO as consequence of S-nitrosylation of two catalytic Cys, Cys63 and/or Cys58 (Becker et al., 1995; Francescutti et al., >>1996<<). These results suggest a different regulation of pea and mammalian GR since that pea GR activity could be unaffected by any NO-PTMs under a nitro-oxidative stress situation (Begara-Morales et al., 2015) in an attempt to maintain GSH
n2:mentions: n3:9005440

Subject Item: _:vb49145094
rdf:type: n2:Context
rdf:value: These results suggest a different regulation of pea and mammalian GR since that pea GR activity could be unaffected by any NO-PTMs under a nitro-oxidative stress situation (Begara-Morales et al., >>2015<<) in an attempt to maintain GSH levels and consequently the cellular redox state.
n2:mentions: n3:26116026

Subject Item: _:vb49145095
rdf:type: n2:Context
rdf:value: APX S-nitrosylation could have an essential role in physiological and stress conditions via regulation of APX activity (Correa-Aragunde et al., >>2013<<; de Pinto et al., 2013; Begara-Morales et al., 2014), highlighting that APX can constitute a critical interface in the relationship between NO and H2O2 metabolism (Lindermayr and Durner, 2015).
n2:mentions: n3:23918967

Subject Item: _:vb49145096
rdf:type: n2:Context
rdf:value: APX S-nitrosylation could have an essential role in physiological and stress conditions via regulation of APX activity (Correa-Aragunde et al., 2013; de Pinto et al., >>2013<<; Begara-Morales et al., 2014), highlighting that APX can constitute a critical interface in the relationship between NO and H2O2 metabolism (Lindermayr and Durner, 2015).
n2:mentions: n3:24158396

Subject Item: _:vb49145097
rdf:type: n2:Context
rdf:value: APX S-nitrosylation could have an essential role in physiological and stress conditions via regulation of APX activity (Correa-Aragunde et al., 2013; de Pinto et al., 2013; Begara-Morales et al., >>2014<<), highlighting that APX can constitute a critical interface in the relationship between NO and H2O2 metabolism (Lindermayr and Durner, 2015).
n2:mentions: n3:24288182

Subject Item: _:vb49145098
rdf:type: n2:Context
rdf:value: of APX activity (Correa-Aragunde et al., 2013; de Pinto et al., 2013; Begara-Morales et al., 2014), highlighting that APX can constitute a critical interface in the relationship between NO and H2O2 metabolism (Lindermayr and Durner, >>2015<<). It has been suggested that Arabidopsis APX S-nitrosylation/denitrosylation mediated by auxins could be involved in the determination of root architecture (Correa-Aragunde et al., 2013, 2015).
n2:mentions: n3:25819986

Subject Item: _:vb49145099
rdf:type: n2:Context
rdf:value: It has been suggested that Arabidopsis APX S-nitrosylation/denitrosylation mediated by auxins could be involved in the determination of root architecture (Correa-Aragunde et al., >>2013<<, 2015). In this situation, APX1 is S-nitrosylated in vivo and auxins-mediated denitrosylation decreased the protein activity, an effect corroborated by the treatment of APX1 recombinant protein with CysNO (Correa-Aragunde et al., 2013).
n2:mentions: n3:23918967

Subject Item: _:vb49145100
rdf:type: n2:Context
rdf:value: It has been suggested that Arabidopsis APX S-nitrosylation/denitrosylation mediated by auxins could be involved in the determination of root architecture (Correa-Aragunde et al., 2013, >>2015<<). In this situation, APX1 is S-nitrosylated in vivo and auxins-mediated denitrosylation decreased the protein activity, an effect corroborated by the treatment of APX1 recombinant protein with CysNO (Correa-Aragunde et al., 2013). In
n2:mentions: n3:26229066

Subject Item: _:vb49145101
rdf:type: n2:Context
rdf:value: In this situation, APX1 is S-nitrosylated in vivo and auxins-mediated denitrosylation decreased the protein activity, an effect corroborated by the treatment of APX1 recombinant protein with CysNO (Correa-Aragunde et al., >>2013<<). In contrast, de Pinto et al. (2013) reported that APX S-nitrosylation mediated by GSNO inhibits protein activity in tobacco plants and that this change could be related to programmed cell death (PCD). By in silico analysis, in the
n2:mentions: n3:23918967

Subject Item: _:vb49145102
rdf:type: n2:Context
rdf:value: In contrast, de Pinto et al. (>>2013<<) reported that APX S-nitrosylation mediated by GSNO inhibits protein activity in tobacco plants and that this change could be related to programmed cell death (PCD).
n2:mentions: n3:24158396

Subject Item: _:vb49145103
rdf:type: n2:Context
rdf:value: However, Clark et al. (>>2000<<) reported that the inactivation of tobacco APX activity by GSNO could be due to the formation of an iron-nitrosyl complex between NO and the heme group’s iron atom.
n2:mentions: n3:11106031

Subject Item: _:vb49145104
rdf:type: n2:Context
rdf:value: Another study described an increase in S-nitrosylation of pea APX as a protective mechanism in response to salinity stress (Begara-Morales et al., >>2014<<). In this case, the cytosolic pea APX activity is stimulated by S-nitrosylation in vitro and in vivo.
n2:mentions: n3:24288182

Subject Item: _:vb49145105
rdf:type: n2:Context
rdf:value: This finding has been recently corroborated by Yang et al. (>>2015<<), who showed using proteomic and mutagenesis approaches that S-nitrosylation at Cys32 positively regulates APX1 activity in Arabidopsis.
n2:mentions: n3:25667317

Subject Item: _:vb599925061
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 7
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Subject Item: _:vb599925062
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 4
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Subject Item: _:vb599925063
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 4
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 4
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 4
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 4
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Subject Item: _:vb599925067
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 4
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Subject Item: _:vb599925068
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925069
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925070
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925071
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925072
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925073
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925074
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925075
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925076
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925077
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925078
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925079
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925080
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925081
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925082
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925083
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
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Subject Item: _:vb599925084
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:18701673

Subject Item: _:vb599925085
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:29304482

Subject Item: _:vb599925086
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:22106097

Subject Item: _:vb599925087
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:23157446

Subject Item: _:vb599925088
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:30703499

Subject Item: _:vb599925089
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:11260719

Subject Item: _:vb599925090
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:27895655

Subject Item: _:vb599925091
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 3
n2:hasRelevantPaperId: n3:25428993

Subject Item: _:vb599925092
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
n2:hasRelevantPaperId: n3:24158396

Subject Item: _:vb599925093
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925094
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
n2:hasRelevantPaperId: n3:26363958

Subject Item: _:vb599925095
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925096
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925097
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925098
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n2:RelevantScore: 2
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Subject Item: _:vb599925099
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
n2:hasRelevantPaperId: n3:15987996

Subject Item: _:vb599925101
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
n2:hasRelevantPaperId: n3:20827494

Subject Item: _:vb599925102
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
n2:hasRelevantPaperId: n3:12114551

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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925105
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925106
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925107
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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n2:RelevantScore: 2
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Subject Item: _:vb599925110
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925111
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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rdf:type: n2:RelevantBibliographicResource
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n2:RelevantScore: 2
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n2:RelevantScore: 2
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n2:RelevantScore: 2
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n2:RelevantScore: 2
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n2:RelevantScore: 2
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
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Subject Item: _:vb599925121
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 2
n2:hasRelevantPaperId: n3:23861399

Subject Item: _:vb599925122
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n2:RelevantScore: 2
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