Cleave to leave: structural insights into the dynamic organization of the nuclear pore complex.
A detailed understanding of the fine structure of the nuclear pore complex has remained elusive. Now, studies on a small protein domain have shed light on the dynamic organization of this massive assembly.
Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10021, USA.
Svetlana
S
Dokudovskaya
Liesbeth M
LM
Veenhoff
Michael P
MP
Rout
D017398:Alternative Splicing; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism; D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational
D028861:Nuclear Pore Complex Proteins; D010446:Peptide Fragments; C119239:nuclear pore complex protein 96; C093350:nuclear pore complex protein 98; D010450:Endopeptidases