Site-directed fluorescence labeling of intrinsically disordered region of human transcription factor YY1: The inhibitory effect of zinc ions
Author:
Affiliation:
1. Department of Physical Biochemistry, Faculty of Biochemistry, Biophysics, and Biotechnology; Jagiellonian University; Kraków Poland
Funder
National Science Center Poland
Polish Ministry of Science and Higher Education
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Reference27 articles.
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3. Effect of sucrose on chemically and thermally induced unfolding of domain-I of human serum albumin: solvation dynamics and fluorescence anisotropy study;Yadav;Biophys Chem,2016
4. Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically disordered proteins;Schuler;Ann Rev Biophys,2016
5. General strategy for site-specific double labeling of globular proteins for kinetic FRET studies;Ratner;Bioconjug Chem
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1. Zinc controls operator affinity of human transcription factor YY1 by mediating dimerization via its N-terminal region;Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms;2023-03
2. Liver immune and lipid metabolism disorders in mice induced by triphenyl phosphate with or without high fructose and high fat diet;Chemosphere;2022-12
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