PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
17761174-2	2007	Using recombinant proteins, we show that Arabidopsis plastidial MSRB1 and MSRB2, which differ regarding the number of presumed redox-active cysteines, possess specific reductants.	Cysteine	140-149	methionine sulfoxide reductase B 1	Arabidopsis thaliana	64-69
21882992-9	2012	Biochemical analyses demonstrated that H(2)O(2) treatment actually converts several MSRB1-interacting proteins into MSRB substrates.	Hydrogen Peroxide	39-47	methionine sulfoxide reductase B 1	Arabidopsis thaliana	84-89
20236937-8	2010	Protein electrophoresis analyses coupled to mass spectrometry revealed that CDSP32 forms a heterodimeric complex with MSRB1 via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction.	Sulfenic Acids	145-158	methionine sulfoxide reductase B 1	Arabidopsis thaliana	118-123
20236937-8	2010	Protein electrophoresis analyses coupled to mass spectrometry revealed that CDSP32 forms a heterodimeric complex with MSRB1 via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction.	Sulfenic Acids	145-158	methionine sulfoxide reductase B 1	Arabidopsis thaliana	169-174
20236937-8	2010	Protein electrophoresis analyses coupled to mass spectrometry revealed that CDSP32 forms a heterodimeric complex with MSRB1 via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction.	Cysteine	185-188	methionine sulfoxide reductase B 1	Arabidopsis thaliana	118-123
20236937-8	2010	Protein electrophoresis analyses coupled to mass spectrometry revealed that CDSP32 forms a heterodimeric complex with MSRB1 via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction.	Cysteine	185-188	methionine sulfoxide reductase B 1	Arabidopsis thaliana	169-174
20236937-9	2010	MSR activity assays using variable CDSP32 amounts revealed that MSRB1 reduction proceeds with a 1:1 stoichiometry, and redox titrations indicated that CDSP32 and MSRB1 possess midpoints potentials of -337 and -328 mV at pH 7.9, respectively, indicating that regeneration of MSRB1 activity by the Trx through sulfenic acid reduction is thermodynamically feasible in physiological conditions.	Sulfenic Acids	308-321	methionine sulfoxide reductase B 1	Arabidopsis thaliana	162-167
20236937-9	2010	MSR activity assays using variable CDSP32 amounts revealed that MSRB1 reduction proceeds with a 1:1 stoichiometry, and redox titrations indicated that CDSP32 and MSRB1 possess midpoints potentials of -337 and -328 mV at pH 7.9, respectively, indicating that regeneration of MSRB1 activity by the Trx through sulfenic acid reduction is thermodynamically feasible in physiological conditions.	Sulfenic Acids	308-321	methionine sulfoxide reductase B 1	Arabidopsis thaliana	162-167
19457862-7	2009	Regarding 1-Cys MSRB1, oxidation of the enzyme after substrate reduction leads to the formation of a stable sulfenic acid on the catalytic Cys, which is subsequently glutathionylated.	1-cys	10-15	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
19457862-7	2009	Regarding 1-Cys MSRB1, oxidation of the enzyme after substrate reduction leads to the formation of a stable sulfenic acid on the catalytic Cys, which is subsequently glutathionylated.	Sulfenic Acids	108-121	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
19457862-7	2009	Regarding 1-Cys MSRB1, oxidation of the enzyme after substrate reduction leads to the formation of a stable sulfenic acid on the catalytic Cys, which is subsequently glutathionylated.	Cysteine	12-15	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
19457862-8	2009	The deglutathionylation of MSRB1 is achieved by both mono- and dithiol glutaredoxins and involves only their N-terminal conserved catalytic Cys.	Cysteine	140-143	methionine sulfoxide reductase B 1	Arabidopsis thaliana	27-32
15923321-10	2005	This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction.	Cysteine	100-103	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
15923321-10	2005	This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction.	Disulfides	223-232	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
15923321-10	2005	This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction.	Cysteine	68-76	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
15923321-10	2005	This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction.	Cysteine	78-81	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
15923321-10	2005	This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction.	Cysteine	100-103	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21