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Toward the atomic structure of the nuclear pore complex: when top down meets bottom up
by
Glavy, Joseph S
, Hoelz, André
, Beck, Martin
in
631/535/1258/1260
/ 631/535/1266
/ 631/80/389/2029
/ Analysis
/ Biochemistry
/ Biological Microscopy
/ Cell nuclei
/ Crystals
/ Gene Expression
/ Humans
/ Life Sciences
/ Membrane Biology
/ Models, Molecular
/ Molecular biology
/ Molecular Chaperones - chemistry
/ Molecular Chaperones - genetics
/ Molecular Chaperones - metabolism
/ Molecular structure
/ Nuclear Pore - genetics
/ Nuclear Pore - metabolism
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ perspective
/ Protein Isoforms - chemistry
/ Protein Isoforms - genetics
/ Protein Isoforms - metabolism
/ Protein Multimerization
/ Protein Structure
/ Protein Structure, Secondary
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae - ultrastructure
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Structural models
/ Structure
/ X-ray crystallography
2016
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Toward the atomic structure of the nuclear pore complex: when top down meets bottom up
by
Glavy, Joseph S
, Hoelz, André
, Beck, Martin
in
631/535/1258/1260
/ 631/535/1266
/ 631/80/389/2029
/ Analysis
/ Biochemistry
/ Biological Microscopy
/ Cell nuclei
/ Crystals
/ Gene Expression
/ Humans
/ Life Sciences
/ Membrane Biology
/ Models, Molecular
/ Molecular biology
/ Molecular Chaperones - chemistry
/ Molecular Chaperones - genetics
/ Molecular Chaperones - metabolism
/ Molecular structure
/ Nuclear Pore - genetics
/ Nuclear Pore - metabolism
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ perspective
/ Protein Isoforms - chemistry
/ Protein Isoforms - genetics
/ Protein Isoforms - metabolism
/ Protein Multimerization
/ Protein Structure
/ Protein Structure, Secondary
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae - ultrastructure
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Structural models
/ Structure
/ X-ray crystallography
2016
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Toward the atomic structure of the nuclear pore complex: when top down meets bottom up
by
Glavy, Joseph S
, Hoelz, André
, Beck, Martin
in
631/535/1258/1260
/ 631/535/1266
/ 631/80/389/2029
/ Analysis
/ Biochemistry
/ Biological Microscopy
/ Cell nuclei
/ Crystals
/ Gene Expression
/ Humans
/ Life Sciences
/ Membrane Biology
/ Models, Molecular
/ Molecular biology
/ Molecular Chaperones - chemistry
/ Molecular Chaperones - genetics
/ Molecular Chaperones - metabolism
/ Molecular structure
/ Nuclear Pore - genetics
/ Nuclear Pore - metabolism
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ perspective
/ Protein Isoforms - chemistry
/ Protein Isoforms - genetics
/ Protein Isoforms - metabolism
/ Protein Multimerization
/ Protein Structure
/ Protein Structure, Secondary
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae - ultrastructure
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Structural models
/ Structure
/ X-ray crystallography
2016
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Toward the atomic structure of the nuclear pore complex: when top down meets bottom up
Journal Article
Toward the atomic structure of the nuclear pore complex: when top down meets bottom up
2016
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Overview
This Perspective discusses how two complementary approaches, bottom-up
in vitro
and top-down
in situ
structural biology, have now converged to generate the first predictive structural models of the nuclear pore scaffold.
Elucidating the structure of the nuclear pore complex (NPC) is a prerequisite for understanding the molecular mechanism of nucleocytoplasmic transport. However, owing to its sheer size and flexibility, the NPC is unapproachable by classical structure determination techniques and requires a joint effort of complementary methods. Whereas bottom-up approaches rely on biochemical interaction studies and crystal-structure determination of NPC components, top-down approaches attempt to determine the structure of the intact NPC
in situ
. Recently, both approaches have converged, thereby bridging the resolution gap from the higher-order scaffold structure to near-atomic resolution and opening the door for structure-guided experimental interrogations of NPC function.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Analysis
/ Crystals
/ Humans
/ Molecular Chaperones - chemistry
/ Molecular Chaperones - genetics
/ Molecular Chaperones - metabolism
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ Protein Isoforms - chemistry
/ Protein Isoforms - metabolism
/ Protein Structure, Secondary
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae - ultrastructure
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
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