Publications by authors named "Anne E van Vlimmeren"
The rapid identification of protein-protein interactions has been significantly enabled by mass spectrometry (MS) proteomics-based methods, including affinity purification-MS, crosslinking-MS, and proximity-labeling proteomics. While these methods can reveal networks of interacting proteins, they cannot reveal how specific protein-protein interactions alter protein function or cell signaling. For instance, when two proteins interact, there can be emergent signaling processes driven purely by the individual activities of those proteins being co-localized.
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- Scientists studied an enzyme called SHP2, which is made up of different parts that can control how it works.
- They found that SHP2 can be turned on by certain proteins sticking to it, but it can also be turned off by changes in its structure or mutations.
- The researchers used experiments and simulations to learn more about how SHP2 changes shape to do its job, and they discovered new parts of the enzyme that help control its activity.
The rapid identification of protein-protein interactions has been significantly enabled by mass spectrometry (MS) proteomics-based methods, including affinity purification-MS, crosslinking-MS, and proximity-labeling proteomics. While these methods can reveal networks of interacting proteins, they cannot reveal how specific protein-protein interactions alter protein function or cell signaling. For instance, when two proteins interact, there can be emergent signaling processes driven purely by the individual activities of those proteins being co-localized.
View Article and Find Full Text PDFMutations in the tyrosine phosphatase Src homology-2 domain-containing protein tyrosine phosphatase-2 (SHP2) are associated with a variety of human diseases. Most mutations in SHP2 increase its basal catalytic activity by disrupting autoinhibitory interactions between its phosphatase domain and N-terminal SH2 (phosphotyrosine recognition) domain. By contrast, some disease-associated mutations located in the ligand-binding pockets of the N- or C-terminal SH2 domains do not increase basal activity and likely exert their pathogenicity through alternative mechanisms.
View Article and Find Full Text PDFMutations in the tyrosine phosphatase SHP2 are associated with a variety of human diseases. Most mutations in SHP2 increase its basal catalytic activity by disrupting auto-inhibitory interactions between its phosphatase domain and N-terminal SH2 (phosphotyrosine recognition) domain. By contrast, some disease-associated mutations located in the ligand-binding pockets of the N- or C-terminal SH2 domains do not increase basal activity and likely exert their pathogenicity through alternative mechanisms.
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- Protein phosphorylation is a major biological process, with over 90,000 phosphorylation sites identified and linked to various human diseases.
- Researchers analyzed the substrate specificity of 303 Ser/Thr kinases in humans, revealing a diverse range of preferences and the role of negative selectivity in their activity.
- The findings provide insights into cellular signaling pathways, identify kinases responsible for phosphorylation events, and enhance our understanding of biological processes affected by various stimuli.