Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha (Q27622027)

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scientific article

Language	Label	Description	Also known as
English	Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha	scientific article

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scholarly article

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

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author name string

E Conti

1

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J Kuriyan

2

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publication date

15 March 2000

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8

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3

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329-38

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Transport of proteins and RNAs in and out of the nucleus

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Nucleocytoplasmic transport: the soluble phase

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Karyopherins and kissing cousins

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Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope

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A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding

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Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes

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Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope

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Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins

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

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Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences

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7 January 2021

based on heuristic

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Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes

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7 January 2021

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

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Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor

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A polypeptide domain that specifies migration of nucleoplasmin into the nucleus

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Nuclear targeting sequences--a consensus?

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A short amino acid sequence able to specify nuclear location

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Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen.

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Extensive mutagenesis of the nuclear location signal of simian virus 40 large-T antigen

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The nucleoplasmin nuclear location sequence is larger and more complex than that of SV-40 large T antigen

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Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence

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Identification of the human c-myc protein nuclear translocation signal

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Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids

1 reference

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based on heuristic

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

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2800%2900107-6

7 January 2021

based on heuristic

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A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus

1 reference

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7 January 2021

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

1 reference

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Nuclear import: a tale of two sites

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The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5.

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Sequence requirements for synthetic peptide-mediated translocation to the nucleus

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

1 reference

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Determination of the functional domain organization of the importin alpha nuclear import factor

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Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1

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The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal

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

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10.1016/S0969-2126(00)00107-6

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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