Results 181 to 190 of about 16,651 (218)
The Importin β Binding Domain Modulates the Avidity of Importin β for the Nuclear Pore Complex [PDF]
Journal of Biological Chemistry, 2010 Importin beta mediates active passage of cellular substrates through the nuclear pore complex (NPC). Adaptors such as importin alpha and snurportin associate with importin beta via an importin beta binding (IBB) domain. The intrinsic structural flexibility of importin beta allows its concerted interactions with IBB domains, phenylalanine-glycine ...
Anshul Bhardwaj +2 more
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Trends in Cell Biology, 1995
The accumulation of karyophilic proteins in the nucleus requires cytoplasmic factors. Cell-free systems that reconstitute nuclear protein import have been used to identify several of these factors and to define the biochemical requirements for the import process.
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The accumulation of karyophilic proteins in the nucleus requires cytoplasmic factors. Cell-free systems that reconstitute nuclear protein import have been used to identify several of these factors and to define the biochemical requirements for the import process.
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Importins: Diverse roles in male fertility
Seminars in Cell & Developmental Biology, 2022Regulated nucleocytoplasmic transport is central to the changes in gene expression that underpin cellular development and homeostasis, including in the testis, and proteins in the importin family are the predominant facilitators of cargo transport through the nuclear envelope.
Benedict Nathaniel +3 more
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2002
Importins are nuclear transport receptors of the karyopherin superfamily. They recognize nuclear proteins that are synthesized in the cytoplasm and translocate them to the nucleus (Mattaj and Englmeier 1998; Weis 1998; Gorlich and Kutay 1999; Nakielny and Dreyfuss 1999).
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Importins are nuclear transport receptors of the karyopherin superfamily. They recognize nuclear proteins that are synthesized in the cytoplasm and translocate them to the nucleus (Mattaj and Englmeier 1998; Weis 1998; Gorlich and Kutay 1999; Nakielny and Dreyfuss 1999).
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Science's STKE, 2001
The small guanosine triphosphatase Ran is involved in transport of proteins into the nucleus and has been recognized more recently as a regulator of formation of the mitotic spindle. Wiese et al. show that Ran uses the same binding partner, importin-β, to control microtubule formation that it uses to promote protein
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The small guanosine triphosphatase Ran is involved in transport of proteins into the nucleus and has been recognized more recently as a regulator of formation of the mitotic spindle. Wiese et al. show that Ran uses the same binding partner, importin-β, to control microtubule formation that it uses to promote protein
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Importin-mediated nuclear transport in neurons
Current Opinion in Neurobiology, 2006The polarized morphology of neurons poses a particular challenge to intracellular signal transduction. Local signals generated at distal sites must be retrogradely transported to the nucleus to produce persistent changes in neuronal function. Such communication of signals between distal neuronal compartments and the nucleus occurs during axon guidance,
Klara Olofsdotter, Otis +2 more
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Importins and exportins as therapeutic targets in cancer
Pharmacology & Therapeutics, 2016The nuclear transport proteins, importins and exportins (karyopherin-β proteins), may play an important role in cancer by transporting key mediators of oncogenesis across the nuclear membrane in cancer cells. During nucleocytoplasmic transport of tumor suppressor proteins and cell cycle regulators during the processing of these proteins, aberrant ...
Amit, Mahipal, Mokenge, Malafa
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The Interaction Between Importin‐α and Nup153 Promotes Importin‐α/β‐Mediated Nuclear Import
Traffic, 2012AbstractNuclear transport is mediated by transport factors, including the importin β family members. The directionality of nuclear transport is governed by the asymmetrical distribution of the small GTPase Ran. Of note, importin α/β‐mediated import of classical nuclear localization signal (cNLS) – containing cargo is more efficient than other Ran ...
Yutaka, Ogawa +3 more
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Structure of importin-beta bound to the IBB domain of importin-alpha.
Nature, 1999Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-alpha and importin-beta (also called karyopherin-alpha and -beta). The formation of this heterodimer involves the importin-beta-binding (IBB) domain of importin-alpha, a highly basic amino-terminal region of roughly 40 amino-acid ...
G, Cingolani +3 more
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Structures of Importins and Exportins
2018The karyopherin-β (Kap) family of nuclear transport receptors mediates the majority of nuclear-cytoplasmic transport of macromolecules, especially that of proteins. Kaps include importins that transport cargos into the nucleus, exportins that transport cargos out of the nucleus, and bidirectional Kaps that transport one set of cargos into the nucleus ...
Jordan Baumhardt, Yuh Min Chook
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