Structural basis for leucine-rich nuclear export signal recognition by CRM1

By Xiuhua Dong, A. Biswas, Katherine E. Süel, L. Jackson, R. Martinez, H. Gu, Yuh Min Chook. Nature, 2009

207 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/cae498dab2fe26a1d167806bdddba640cb6b5a17

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In Molecular Biology

1. G. Cingolani
2. Kaylen Lott

Citations in the corpus

• The Importin β Binding Domain as a Master Regulator of Nucleocytoplasmic Transport (2010, background): “1–17) contains an NES partially responsible for the interaction between snurportin and CRM1. sIBB amino acids 1–17 bind to a hydrophobic groove on CRM1 with the first N-terminal 10 amino acids folding into an α helix [56,104] (Fig.”