Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism

By Alexandr P. Kornev, N. Haste, Susan S. Taylor, L. T. Ten Eyck. Proceedings of the National Academy of Sciences of the United States of America, 2006

751 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7afd7a34edc6668fe6f3aa476262e522ea42f4ed

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. R. Roskoski
2. Alexandr P. Kornev
3. Susan S. Taylor

In Molecular Biology

1. R. Roskoski
2. Alexandr P. Kornev
3. Susan S. Taylor

Citations in the corpus

• The ErbB/HER family of protein-tyrosine kinases and cancer. (2014, background): “The quinazoline ring of gefitinib is oriented with its N-1 in the back of the ATP-binding pocket of the Leu858Arg mutant where it accepts a hydrogen bond from the main chain NH amide of Met793 (residue numbers including the signal peptide) (Fig.”
• Protein Kinases: Evolution of Dynamic Regulatory Proteins (2010, methodology): “Local Spatial Pattern (LSP) alignment was developed as a method to rapidly compare any two structures and identify spatially conserved residues (Box 2) [11, 12].”
• ERK1/2 MAP kinases: structure, function, and regulation. (2012, background): “The R-spine binds to the F-helix by hydrophobic bonds as do the catalytic loop, the P + 1 loop, the activation lip, and the HI loop [64].”