Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
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Details on Person Structural and biophysical studies indicate that the adaptab...
| Class:Id | Summation:453172 |
|---|---|
| _displayName | Structural and biophysical studies indicate that the adaptab... |
| _timestamp | 2010-01-19 12:58:49 |
| created | [InstanceEdit:453180] Jupe, S, 2010-01-19 |
| literatureReference | [LiteratureReference:453191] Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130 [LiteratureReference:453202] Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling |
| text | Structural and biophysical studies indicate that the adaptability of the Syk tandem SH2 domains is made possible by relatively weak interactions between the two SH2 domains and the flexibility of interdomain A (Zhang et al. 2008). A large proportion of phosphorylated Syk is released into the cytosol. One factor that has been proposed for modulating the interactions of Syk with the receptor ITAM is the phosphorylation of Syk on Y130 (Keshvara et al. 1997). |
| (summation) | [Reaction:453183] p-Y348-SYK dissociates [Homo sapiens] |
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No pathways have been reviewed or authored by Structural and biophysical studies indicate that the adaptab... (453172)
