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Paper Details

Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex.
Mol Cell Proteomics
54
2014
ALPS, ALPS motifs, ArfGAP1, Nup133, Saccharomyces cerevisiae, Saccharomyces cerevisiae (Sc) Nup133, Sc, ScNup133, ScNup133(, Vanderwaltozyma polyspora, Vanderwaltozyma polyspora (Vp) Nup133 residues, VpNup133, coatomer, eukaryotes, full-, nucleoporin Nup133, nucleoporins
Active Transport, Cell Nucleus, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Evolution, Molecular, Kluyveromyces, Models, Molecular, Mutation, Nuclear Envelope, Nuclear Pore, Nuclear Pore Complex Proteins, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid
Author NameAffiliation
Seung Joong KimDepartment of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California San Francisco
Javier Fernandez-MartinezThe Rockefeller University
Subbiah ParthasarathyAlbert Einstein College of Medicine
Anne Martel
Tsutomu Matsui
Hiro Tsuruta
Thomas M Weiss
Thomas M Weiss
Yi ShiThe Rockefeller University
Ane Markina-I??arrairaegui
Jeffrey B BonannoAlbert Einstein College of Medicine
J Michael Sauder
J Michael Sauder
Stephen K Burley||||Center for Integrative Proteomics Research, the State University of New Jersey
Brian T ChaitThe Rockefeller University
Brian T ChaitThe Rockefeller University
Steven C AlmoAlbert Einstein College of Medicine
Michael P RoutThe Rockefeller University
Michael P RoutThe Rockefeller University
Andrej Sali (CM4AI)Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California San Francisco
Andrej Sali (CM4AI)Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California San Francisco
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