Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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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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Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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P1476

Mechanism of midline defect-causing mutation P151L in MID1 revealed.

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Linda K Nicholson

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Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22

Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A

Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4.

The anti-diabetic drug metformin reduces BACE1 protein level by interfering with the MID1 complex

MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation

NMR studies of the C-terminus of alpha4 reveal possible mechanism of its interaction with MID1 and protein phosphatase 2A

Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination

Mib-Jag1-Notch signalling regulates patterning and structural roles of the notochord by controlling cell-fate decisions.

In the right place at the right time: visualizing and understanding mRNA localization.

E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration

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2167-2169

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scholarly article

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10.1111/FEBS.14149

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English

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284

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2017-07-01T00:00:00Z

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28714291

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