Results 171 to 180 of about 5,815 (206)
The Role of SARS-CoV-2 Nucleocapsid Protein in Host Inflammation. [PDF]
Cao Y, Wang Y, Huang D, Tan YJ.
europepmc +1 more source
TDP-43: unveiling the hidden key to cellular fate decisions. [PDF]
Liu B +10 more
europepmc +1 more source
Phytophthora capsici carries and differentially expresses genes for the RNA interference pathway. [PDF]
Sevillano-Serrano J +5 more
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The balance between nuclear import and export of NLRC5 regulates MHC class I transactivation. [PDF]
Zhu B +4 more
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Karyopherin abnormalities in neurodegenerative proteinopathies [PDF]
Neurodegenerative proteinopathies are characterized by progressive cell loss that is preceded by the mislocalization and aberrant accumulation of proteins prone to aggregation.
Terouz Pasha +2 more
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Nuclear import by karyopherin-βs: Recognition and inhibition
Proteins in the karyopherin-β family mediate the majority of macromolecular transport between the nucleus and the cytoplasm. Eleven of the 19 known human karyopherin-βs and 10 of the 14S.
Yuh Min Chook
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Karyopherin-mediated nucleocytoplasmic transport
Nature Reviews Molecular Cell Biology, 2022Efficient and regulated nucleocytoplasmic trafficking of macromolecules to the correct subcellular compartment is critical for proper functions of the eukaryotic cell. The majority of the macromolecular traffic across the nuclear pores is mediated by the Karyopherin-β (or Kap) family of nuclear transport receptors.
Casey E. Wing +2 more
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The Karyopherin proteins, Crm1 and Karyopherin β1, are overexpressed in cervical cancer and are critical for cancer cell survival and proliferation [PDF]
AbstractThe Karyopherin proteins are involved in nucleo‐cytoplasmic trafficking and are critical for protein and RNA subcellular localization. Recent studies suggest they are important in nuclear envelope component assembly, mitosis and replication. Since these are all critical cellular functions, alterations in the expression of the Karyopherins may ...
Pauline J Van Der Watt +2 more
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International audienceHere, we describe the crystal structures of two distinct isoforms of ligand-free human karyopherin RanBP5 and investigate its global propensity to interact with influenza A virus polymerase.
Christopher Swale +2 more
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Background: Karyopherin α (importin α) is an adaptor molecule that recognizes proteins containing nuclear localization signals (NLSs). The prototypical NLS that is able to bind to karyopherin α is that of the SV40 T antigen, and consists of a short ...
Elena Conti, John Kuriyan
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