The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein
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The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Improving the chances of successful protein structure determination with a random forest classifierBiotinylation, a post-translational modification controlled by the rate of protein-protein association.Selectivity in post-translational biotin addition to five human carboxylases.A novel molecular mechanism to explain biotin-unresponsive holocarboxylase synthetase deficiency.
P2860
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein
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2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The N-terminal domain of human ...... ion with the substrate protein
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The N-terminal domain of human ...... ion with the substrate protein
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The N-terminal domain of human ...... ion with the substrate protein
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The N-terminal domain of human ...... ion with the substrate protein
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The N-terminal domain of human ...... ion with the substrate protein
@ast
The N-terminal domain of human ...... ion with the substrate protein
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The N-terminal domain of human ...... ion with the substrate protein
@en-gb
The N-terminal domain of human ...... ion with the substrate protein
@nl
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The N-terminal domain of human ...... ion with the substrate protein
@ast
The N-terminal domain of human ...... ion with the substrate protein
@en
The N-terminal domain of human ...... ion with the substrate protein
@en-gb
The N-terminal domain of human ...... ion with the substrate protein
@nl
P2860
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The N-terminal domain of human ...... ion with the substrate protein
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P2093
Chung-Kyung Lee
Young Ho Jeon
P2860
P304
P356
10.1016/J.FEBSLET.2009.12.059
P407
P577
2010-02-19T00:00:00Z