The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes (original) (raw)

The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins

Iain Mattaj

2001

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Nucleoporin domain topology is linked to the transport status of the nuclear pore complex

Katharine Ullman, Sara Paulillo

Journal of molecular biology, 2005

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Structural and Functional Studies of Nup107/Nup133 Interaction and Its Implications for the Architecture of the Nuclear Pore Complex

Thomas Schwartz

Molecular Cell, 2008

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The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly

Karsten Weis

The Journal of Cell Biology, 2009

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Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors

Pramod Kumar

eLife, 2013

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Nup192p Is a Conserved Nucleoporin with a Preferential Location at the Inner Site of the Nuclear Membrane

Buket Kosova

Journal of Biological Chemistry, 1999

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Disruption of the FG nucleoporin NUP98 causes selective changes in nuclear pore complex stoichiometry and function

Xiaosheng Wu

Proceedings of the National Academy of Sciences, 2001

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Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold

Panagiotis Kastritis

The Journal of cell biology, 2015

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Domain topology of nucleoporin Nup98 within the nuclear pore complex

Birthe Fahrenkrog

Journal of Structural Biology, 2012

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Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p

Roger Wepf

The Journal of Cell Biology, 1996

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Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex

Michael Rout

Molecular & cellular proteomics : MCP, 2014

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Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex

Joachim Koeser, Ueli Aebi

Journal of Structural Biology, 2002

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The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex

Aurelian Radu

Cell, 1995

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Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex

Michael Rout

Structure, 2013

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Dynamics and diverse functions of nuclear pore complex proteins

Birthe Fahrenkrog

Nucleus, 2012

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Nup53 is required for nuclear envelope and nuclear pore complex assembly

Melpomeni Platani

2008

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RNA Association Defines a Functionally Conserved Domain in the Nuclear Pore Protein Nup153

Chelle Dimaano

Journal of Biological …, 2001

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Nup98 Localizes to Both Nuclear and Cytoplasmic Sides of the Nuclear Pore and Binds to Two Distinct Nucleoporin Subcomplexes

Brian Ribbeck

Molecular Biology of The Cell, 2003

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Nuclear pore complex—a coat specifically tailored for the nuclear envelope

Karsten Weis

Current Opinion in Cell Biology, 2011

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The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex

Michael Rout

The Journal of Cell Biology, 1996

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The Conserved Transmembrane Nucleoporin NDC1 Is Required for Nuclear Pore Complex Assembly in Vertebrate Cells

Stephan Guttinger

Molecular Cell, 2006

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Characterization of the membrane-coating Nup84 complex Paradigm for the nuclear pore complex structure

Erik Debler

2010

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The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function

Karsten Weis, W. Z Cande

The Journal of Cell Biology, 2006

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Assembly and Preferential Localization of Nup116p on the Cytoplasmic Face of the Nuclear Pore Complex by Interaction with Nup82p

Elena Kiseleva

Molecular and Cellular Biology, 2000

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The Nuclear Pore Complex as a Transport Machine

Michael Rout

Journal of Biological Chemistry, 2001

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The nuclear pore complex and nuclear transport

Michael Rout

Cold Spring Harbor perspectives in biology, 2010

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Integrative Structure and Functional Anatomy of a Nuclear Pore Complex

Michael Rout

Microscopy and Microanalysis, 2018

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