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Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1
Qing Zhao, Xiu Bao Chang
Biochemistry and Molecular Biology
Research output
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Contribution to journal
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Article
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peer-review
24
Scopus citations
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Dive into the research topics of 'Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1'. Together they form a unique fingerprint.
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Medicine & Life Sciences
Aromatic Amino Acids
100%
Adenine
82%
ATP Binding Cassette Transporter, Subfamily B, Member 1
77%
Adenosine Triphosphate
54%
Mutation
39%
multidrug resistance-associated protein 1
21%
Leukotriene C4
19%
Cysteine
18%
ATP-Binding Cassette Transporters
17%
Histidine
11%
Cystic Fibrosis Transmembrane Conductance Regulator
6%
Chloride Channels
6%
Serine
4%
Nucleotides
4%
Proteins
3%
Chemical Compounds
Aromatic Amino Acid
81%
Adenine
64%
Mutation
59%
Resistance
44%
Leukotriene C4
40%
Cysteine Residue
36%
Protein
28%
Substitution Reaction
27%
Histidine
16%
Amino-Acid Residue
15%
Serine Residue
11%
Solute
7%