ArticleMethods in molecular biology (Clifton, N.J.)2012
Assignment of backbone resonances in a eukaryotic protein kinase - ERK2 as a representative example.
Article in Methods in molecular biology (Clifton, N.J.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Dynamics-Driven Allostery in Protein Kinases.Trends in biochemical sciences · 2015Review
- Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Scientific reports · 2015Article
- Molecular basis of MAP kinase regulation.Protein science : a publication of the Protein Society · 2013Review
- Structural and functional characterization of the recombinant death domain from death-associated protein kinase.PloS one · 2013Article
- Docking interactions of hematopoietic tyrosine phosphatase with MAP kinases ERK2 and p38α.Biochemistry · 2012Article
- Solution NMR insights into docking interactions involving inactive ERK2.Biochemistry · 2011Article
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Authors and funding
3 authors.
Funding
Abstract
A first step toward the analysis of the structure, dynamics, and interactions of proteins by NMR is obtaining an acceptable level of resonance assignments. This process is nontrivial in most eukaryotic kinases given their size and suboptimal behavior in solution. Using inactive ERK2 as a representative example, we describe the procedures we utilized to achieve a significant degree of completeness of backbone resonance assignment.
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