Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.
about
Protein O-GlcNAcylation: emerging mechanisms and functions.Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcaseIncrease of enzyme activity through specific covalent modification with fragments.Enzymatic properties of β-N-acetylglucosaminidases.Nutrient-driven O-GlcNAc in proteostasis and neurodegeneration.Carb cutting works better with a partner.
P2860
Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
@zh-my
2017年学术文章
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2017年學術文章
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2017年學術文章
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2017年學術文章
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name
Structures of human O-GlcNAcas ...... ew substrate recognition mode.
@en
Structures of human O-GlcNAcas ...... ew substrate recognition mode.
@nl
type
label
Structures of human O-GlcNAcas ...... ew substrate recognition mode.
@en
Structures of human O-GlcNAcas ...... ew substrate recognition mode.
@nl
prefLabel
Structures of human O-GlcNAcas ...... ew substrate recognition mode.
@en
Structures of human O-GlcNAcas ...... ew substrate recognition mode.
@nl
P2093
P2860
P356
P1476
Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode
@en
P2093
P2860
P2888
P304
P356
10.1038/NSMB.3390
P50
P577
2017-03-20T00:00:00Z