Source:http://linkedlifedata.com/resource/pubmed/id/20807953
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
137
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pubmed:dateCreated |
2010-9-2
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pubmed:abstractText |
Controlled production of reactive oxygen species leads to reversible oxidation of protein tyrosine phosphatases (PTPs) and has emerged as an important tier of regulation over phosphorylation-dependent signal transduction. We present a modified cysteinyl-labeling assay that detects reversible oxidation of members of each of the different PTP subclasses. Here, we describe the methods for enriching reversibly oxidized PTPs from complex protein extracts, illustrating the procedure in IMR90 fibroblasts.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1937-9145
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
pl2
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pubmed:meshHeading |
pubmed-meshheading:20807953-Animals,
pubmed-meshheading:20807953-Humans,
pubmed-meshheading:20807953-Oxidation-Reduction,
pubmed-meshheading:20807953-Phosphorylation,
pubmed-meshheading:20807953-Protein Tyrosine Phosphatases,
pubmed-meshheading:20807953-Reactive Oxygen Species,
pubmed-meshheading:20807953-Signal Transduction
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pubmed:year |
2010
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pubmed:articleTitle |
Targeting the reversibly oxidized protein tyrosine phosphatase superfamily.
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pubmed:affiliation |
Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, N.I.H., Extramural
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