Biophysical characterization of interactions involving importin-alpha during nuclear import (Q27633151)

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9 November 2019

title

Biophysical characterization of interactions involving importin-alpha during nuclear import (English)

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9 November 2019

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9 November 2019

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9 November 2019

Catimel B

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9 November 2019

Teh T

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9 November 2019

Jans DA

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9 November 2019

Howlett GJ

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9 November 2019

Nice EC

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9 November 2019

Kobe B

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9 November 2019

language of work or name

English

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publication date

11 July 2001

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Journal of Biological Chemistry

9 November 2019

published in

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volume

276

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issue

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page(s)

34189-34198

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Nuclear targeting sequences--a consensus?

9 November 2019

cites work

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Nuclear targeting of proteins: how many different signals?

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Nuclear targeting signal recognition: a key control point in nuclear transport?

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Gatekeepers of the nucleus

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Nucleocytoplasmic protein traffic and its significance to cell function

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The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence

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A repeating amino acid motif shared by proteins with diverse cellular roles

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Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha

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Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha

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Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha

21 January 2018

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Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha

21 January 2018

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Active site-directed protein regulation

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Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins

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The protein kinase CK2 site (Ser111/112) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin

21 January 2018

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The cAMP-dependent protein kinase site (Ser312) enhances dorsal nuclear import through facilitating nuclear localization sequence/importin interaction

21 January 2018

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Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis

21 January 2018

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RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import

21 January 2018

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Purification and characterization of a novel restricted antigen expressed by normal and transformed human colonic epithelium.

21 January 2018

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Synthesis, conformational studies and biological activity of N(alpha)-mono-biotinylated rat relaxin.

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Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

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Structure of importin-beta bound to the IBB domain of importin-alpha

21 January 2018

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The nuclear pore‐targeting complex binds to nuclear pores after association with a karyophile

21 January 2018

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Isolation of a protein that is essential for the first step of nuclear protein import

21 January 2018

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Evidence for distinct substrate specificities of importin alpha family members in nuclear protein import

21 January 2018

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Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R.

21 January 2018

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Efficiency of importin alpha/beta-mediated nuclear localization sequence recognition and nuclear import. Differential role of NTF2.

21 January 2018

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Dissection of a nuclear localization signal

21 January 2018

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A novel class of RanGTP binding proteins

21 January 2018

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Structural view of the Ran-Importin beta interaction at 2.3 A resolution

21 January 2018

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The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport

21 January 2018

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Nuclear import factors importin α and importin β undergo mutually induced conformational changes upon association

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Identifiers

DOI

10.1074/JBC.M103531200

2 references

Consolidated OpenCitations Corpus – April 2017

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9 November 2019

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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