Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes.
about
Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity.A Novel Regulator of Activation-Induced Cytidine Deaminase/APOBECs in Immunity and Cancer: Schrödinger's CATalytic Pocket.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.The APOBEC Protein Family: United by Structure, Divergent in Function.Diversification of AID/APOBEC-like deaminases in metazoa: multiplicity of clades and widespread roles in immunity.
P2860
Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes.
description
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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年論文
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name
Zinc enhancement of cytidine d ...... in regulating APOBEC3 enzymes.
@en
type
label
Zinc enhancement of cytidine d ...... in regulating APOBEC3 enzymes.
@en
prefLabel
Zinc enhancement of cytidine d ...... in regulating APOBEC3 enzymes.
@en
P2860
P356
P1433
P1476
Zinc enhancement of cytidine d ...... in regulating APOBEC3 enzymes.
@en
P2093
Ailie Marx
Meytal Galilee
P2860
P2888
P356
10.1038/SREP18191
P407
P50
P577
2015-12-18T00:00:00Z
P5875
P6179
1015896949