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Human importin alpha 3 and its N-terminal truncated form, without the importin-beta-binding domain, are oligomeric species with a low conformational stability in solution

Academic Article
Publication Date:
2020
abstract:
Background: Eukaryotic cells have a continuous transit of macromolecules between the cytoplasm and the nucleus. Several carrier proteins are involved in this transport. One of them is importin alpha, which must form a complex with importin beta to accomplish its function, by domain-swapping its 60-residue-long N terminus. There are several human isoforms of importin alpha; among them, importin alpha 3 has a particularly high flexibility.
Iris type:
01.01 Articolo in rivista
Keywords:
Circular dichroism; Fluorescence; Importins; Protein-stability; Self-association
List of contributors:
Rizzuti, Bruno
Authors of the University:
RIZZUTI BRUNO
Handle:
https://iris.cnr.it/handle/20.500.14243/382718
Published in:
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Journal
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