The interaction of schizophrenia-related proteins DISC1 and NDEL1, in light of the newly identified domain structure of DISC1.

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The interaction of schizophrenia-related proteins DISC1 and NDEL1, in light of the newly identified domain structure of DISC1.

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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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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

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2017年學術文章

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The interaction of schizophren ...... ied domain structure of DISC1.

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The interaction of schizophren ...... ied domain structure of DISC1.

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The interaction of schizophren ...... ied domain structure of DISC1.

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The interaction of schizophren ...... ied domain structure of DISC1.

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The interaction of schizophren ...... ied domain structure of DISC1.

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The interaction of schizophren ...... ied domain structure of DISC1.

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The interaction of schizophren ...... fied domain structure of DISC1

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P2093

Nicholas J. Bradshaw

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DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation

DISC1-NDEL1/NUDEL protein interaction, an essential component for neurite outgrowth, is modulated by genetic variations of DISC1

Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase activity by disrupted-in-schizophrenia 1

Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders

Oligomer assembly of the C-terminal DISC1 domain (640-854) is controlled by self-association motifs and disease-associated polymorphism S704C

Insolubility of disrupted-in-schizophrenia 1 disrupts oligomer-dependent interactions with nuclear distribution element 1 and is associated with sporadic mental disease

Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase

Mutually exclusive cytoplasmic dynein regulation by NudE-Lis1 and dynactin.

Molecular characterization of disrupted in schizophrenia-1 risk variant S704C reveals the formation of altered oligomeric assembly.

The mitosis and neurodevelopment proteins NDE1 and NDEL1 form dimers, tetramers, and polymers with a folded back structure in solution.

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scholarly article

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10.1080/19420889.2017.1335375

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2017-06-02T00:00:00Z

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schizophrenia

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5595412

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