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MafG controls the hypoxic response of cells by accumulating HIF‐1α in the nuclei
Author(s) -
Ueda Koji,
Xu Jing,
Morimoto Haruka,
Kawabe Atsumi,
Imaoka Susumu
Publication year - 2008
Publication title -
febs letters
Language(s) - Slovak
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.05.040
Subject(s) - gene knockdown , microbiology and biotechnology , nucleolus , chromosomal translocation , chemistry , biology , cytoplasm , biochemistry , gene
MINT‐6550898:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by two hybrid (MI:0018) MINT‐6550966:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 alpha (uniprotkb:P07900) by surface plasmon resonance (MI:0107) MINT‐6550948:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFK (uniprotkb:A5PLQ5) by surface plasmon resonance (MI:0107) MINT‐6550925:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by surface plasmon resonance (MI:0107) MINT‐6550912:MAFG (uniprotkb:Q9BRP3) and HIF1A (uniprotkb:Q16665) physically interact (MI:0218) by fluorescence microscopy (MI:0416) MINT‐6550980:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 beta (uniprotkb:P08238) by surface plasmon resonance (MI:0107)

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