Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19 (Q27653722)

5

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Susanne A Kassube

object named as

Susanne A Kassube

2

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Erik W. Debler

object named as

Erik W Debler

3

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author name string

Johanna Napetschnig

1

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Richard W Wong

4

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André Hoelz

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

3 March 2009

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published in

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volume

106

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issue

9

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page(s)

3089-94

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cites work

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Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding

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Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN

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Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II

20 March 2017

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Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii

20 March 2017

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Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase

20 March 2017

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The yeast nuclear pore complex: composition, architecture, and transport mechanism

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Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p

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The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm

20 March 2017

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The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA

20 March 2017

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Refinement of macromolecular structures by the maximum-likelihood method

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export

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Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export

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The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore

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Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export

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7 April 2017

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The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events

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The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim.

21 January 2018

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Peering through the Pore

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21 January 2018

Identifiers

DOI

10.1073/PNAS.0813267106

1 reference

release_y66hnlmovramnacgujtfo2mfqe

0 references

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/y66hnlmovramnacgujtfo2mfqe

mapped directly with Wikidata item

24 November 2022

based on heuristic

3391106

1 reference

1 reference

1 reference