Comparative Analysis of the Tyr-Kinases CapB1 and CapB2 Fused to Their Cognate Modulators CapA1 and...
Comparative Analysis of the Tyr-Kinases CapB1 and CapB2 Fused to Their Cognate Modulators CapA1 and CapA2 from Staphylococcus aureus
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United States: Public Library of Science
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English
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United States: Public Library of Science
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A particular class of tyrosine-kinases sharing no structural similarity with eukaryotic tyrosine-kinases has been evidenced in a large array of bacterial species. These bacterial tyrosine-kinases are able to autophosphorylate on a C-terminal tyrosine-rich motif. Their autophosphorylation has been shown to play a crucial role in the biosynthesis or...
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Comparative Analysis of the Tyr-Kinases CapB1 and CapB2 Fused to Their Cognate Modulators CapA1 and CapA2 from Staphylococcus aureus
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TN_cdi_plos_journals_1441432696
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1441432696
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ISSN
1932-6203
E-ISSN
1932-6203
DOI
10.1371/journal.pone.0075958