Solution NMR Study of the Interaction Between NTF2 and Nucleoporin FxFG Repeats (Q79160268)

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20 December 2019

title

Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats (English)

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20 December 2019

Solution NMR Study of the Interaction Between NTF2 and Nucleoporin FxFG Repeats (English)

1 reference

https://api.crossref.org/works/10.1016/J.JMB.2003.08.050

Nuclear Magnetic Resonance, Biomolecular

20 March 2024

main subject

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Repetitive Sequences, Amino Acid

20 March 2024

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20 March 2024

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20 March 2024

author name string

Jonathan Morrison

1

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20 December 2019

Ji-Chun Yang

2

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20 December 2019

Murray Stewart

3

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20 December 2019

David Neuhaus

4

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20 December 2019

language of work or name

English

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National Center for Biotechnology Information

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20 March 2024

publication date

1 October 2003

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20 December 2019

24 October 2003

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National Center for Biotechnology Information

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full work available at URL

20 March 2024

https://api.elsevier.com/content/article/PII:S0022283603010933?httpAccept=text/xml

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https://api.elsevier.com/content/article/PII:S0022283603010933?httpAccept=text/plain

20 March 2024

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Journal of Molecular Biology

20 March 2024

published in

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20 December 2019

volume

333

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20 December 2019

issue

3

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20 December 2019

page(s)

587-603

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Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle

20 December 2019

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GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta

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The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex

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Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62

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Separate binding sites on nuclear transport factor 2 (NTF2) for GDP-Ran and the phenylalanine-rich repeat regions of nucleoporins p62 and Nsp1p

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The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2)

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Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran

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20 December 2019

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