The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
about
Computation and Functional Studies Provide a Model for the Structure of the Zinc Transporter hZIP4.Genome-wide identification, in silico characterization and expression analysis of ZIP-like genes from Trichomonas vaginalis in response to Zinc and Iron.Properties of Zip4 accumulation during zinc deficiency and its usefulness to evaluate zinc status: a study of the effects of zinc deficiency during lactation.
P2860
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
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2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
@ast
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
@en
type
label
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
@ast
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
@en
prefLabel
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
@ast
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
@en
P2093
P2860
P356
P1433
P1476
The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain
@en
P2093
Brian Doyon
Elizabeth M Bafaro
Robert E Dempski
Sagar Antala
Stephen P Dzul
Tuong-Vi Nguyen
P2860
P304
P356
10.1039/C5MT00066A
P577
2015-09-01T00:00:00Z