Structure-function mapping of a heptameric module in the nuclear pore complex. - Test2 - elhamkhani - TriplyDB

Structure-function mapping of a heptameric module in the nuclear pore complex.

Structure-function mapping of a heptameric module in the nuclear pore complex.

http://www.wikidata.org/entity/Q27933557

about

Three-dimensional structures of membrane proteins from genomic sequencing Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics Enriching the pore: splendid complexity from humble origins Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Molecular architecture and function of the SEA complex, a modulator of the TORC1 pathway.Molecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complex Protein structure prediction from sequence variation Assembly and Molecular Architecture of the Phosphoinositide 3-Kinase p85α Homodimer.Structural characterization by cross-linking reveals the detailed architecture of a coatomer-related heptameric module from the nuclear pore complex.Revealing Higher Order Protein Structure Using Mass Spectrometry.Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.Extensive libraries of gene truncation variants generated by in vitro transposition.Method for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes.Macromolecular transport between the nucleus and the cytoplasm: Advances in mechanism and emerging links to disease.Systems cell biology.A robust pipeline for rapid production of versatile nanobody repertoires.A pipeline for determining protein-protein interactions and proximities in the cellular milieu Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex Molecular architecture of the yeast Mediator complex.Evidence for the robustness of protein complexes to inter-species hybridization.Determining protein complex structures based on a Bayesian model of in vivo Förster resonance energy transfer (FRET) data Atomic structure of the Y complex of the nuclear pore.Affinity proteomics to study endogenous protein complexes: pointers, pitfalls, preferences and perspectives.Interactome Mapping Reveals the Evolutionary History of the Nuclear Pore Complex.High Sensitivity Crosslink Detection Coupled With Integrative Structure Modeling in the Mass Spec Studio.Structural systems biology and multiscale signaling models.Conserved spatial organization of FG domains in the nuclear pore complex.A Robust Workflow for Native Mass Spectrometric Analysis of Affinity-Isolated Endogenous Protein Assemblies.A strategy for dissecting the architectures of native macromolecular assemblies Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions.Functional insights from studies on the structure of the nuclear pore and coat protein complexes.Dissecting the NUP107 complex: multiple components and even more functions.Toward understanding the structure of the vertebrate nuclear pore complex The nuclear pore complex core scaffold and permeability barrier: variations of a common theme.Comparative interactomics provides evidence for functional specialization of the nuclear pore complex.Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging.Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform.Structure of Complement C3(H2O) Revealed By Quantitative Cross-Linking/Mass Spectrometry And Modeling.

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P2860

Structure-function mapping of a heptameric module in the nuclear pore complex.

http://www.wikidata.org/entity/Q27933557

description

2012 nî lūn-bûn

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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2012 թվականի փետրվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Structure-function mapping of a heptameric module in the nuclear pore complex.

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Structure-function mapping of a heptameric module in the nuclear pore complex.

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Structure-function mapping of a heptameric module in the nuclear pore complex.

@nl

type

label

Structure-function mapping of a heptameric module in the nuclear pore complex.

@ast

Structure-function mapping of a heptameric module in the nuclear pore complex.

@en

Structure-function mapping of a heptameric module in the nuclear pore complex.

@nl

prefLabel

Structure-function mapping of a heptameric module in the nuclear pore complex.

@ast

Structure-function mapping of a heptameric module in the nuclear pore complex.

@en

Structure-function mapping of a heptameric module in the nuclear pore complex.

@nl

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Journal of Cell Biology

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Structure-function mapping of a heptameric module in the nuclear pore complex

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P2093

Andrej Sali

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Brian T Chait

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David L Stokes

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Javier Velazquez-Muriel

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Jeremy Phillips

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Josef D Franke

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Matthew D Sekedat

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Rosemary Williams

http://www.w3.org/2001/XMLSchema#string

Ruben Diaz-Avalos

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P2860

An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells

Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.

The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis

Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket

Architecture of a coat for the nuclear pore membrane

Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3

Structural basis for cargo regulation of COPII coat assembly.

Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex

ModBase, a database of annotated comparative protein structure models, and associated resources

The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly

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419-434

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scholarly article

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1351945

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10.1083/JCB.201109008

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4

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196

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Javier Fernandez-Martinez

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2012-02-13T00:00:00Z

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221830061

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22331846

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3283990

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