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PMID |
Sentence |
1 |
20305679
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A variation in NOS1AP gene is associated with repaglinide efficacy on insulin resistance in type 2 diabetes of Chinese.
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2 |
23018631
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These genes belong to three major classes: genes involved in drug metabolism and transporters that influence pharmacokinetics (including the cytochrome P450 [CYP] superfamily, the organic anion transporting polypeptide [OATP] family, and the polyspecific organic cation transporter [OCT] family); genes encoding drug targets and receptors (including peroxisome proliferator-activated receptor gamma [PPARG], the adenosine triphosphate [ATP]-sensitive potassium channel [K(ATP)], and incretin receptors); and genes involved in the causal pathway of T2DM that are able to modify the effects of drugs (including adipokines, transcription factor 7-like 2 (T cell specific, HMG-box) [TCF7L2], insulin receptor substrate 1 [IRS1], nitric oxide synthase 1 (neuronal) adaptor protein [NOS1AP], and solute carrier family 30 (zinc transporter), member 8 [SLC30A8]).
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3 |
23018631
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In addition to these three major classes, we also review the available evidence on novel genes (CDK5 regulatory subunit associated protein 1-like 1 [CDKAL1], insulin-like growth factor 2 mRNA binding protein 2 [IGF2BP2], potassium voltage-gated channel, KQT-like subfamily, member 1 [KCNQ1], paired box 4 [PAX4] and neuronal differentiation 1 [NEUROD1] transcription factors, ataxia telangiectasia mutated [ATM], and serine racemase [SRR]) that have recently been proposed as possible modulators of therapeutic response in subjects with T2DM.
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4 |
23658158
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The nNOS-p38MAPK pathway is mediated by NOS1AP during neuronal death.
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5 |
23658158
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Excitotoxic stimulus induces recruitment of NOS1AP to nNOS in rat cortical neuron culture.
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6 |
23658158
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Excitotoxic activation of p38MAPK and subsequent neuronal death are reduced by competing with the nNOS:NOS1AP interaction and by knockdown with NOS1AP-targeting siRNAs.
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7 |
23658158
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We designed a cell-permeable peptide that competes for the unique PDZ domain of nNOS that interacts with NOS1AP.
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8 |
23658158
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This peptide inhibits NMDA-induced recruitment of NOS1AP to nNOS and in vivo in rat, doubles surviving tissue in a severe model of neonatal hypoxia-ischemia, a major cause of neonatal death and pediatric disability.
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9 |
23658158
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The highly unusual sequence specificity of the nNOS:NOS1AP interaction and involvement in excitotoxic signaling may provide future opportunities for generation of neuroprotectants with high specificity.
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10 |
23658158
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The nNOS-p38MAPK pathway is mediated by NOS1AP during neuronal death.
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11 |
23658158
|
Excitotoxic stimulus induces recruitment of NOS1AP to nNOS in rat cortical neuron culture.
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12 |
23658158
|
Excitotoxic activation of p38MAPK and subsequent neuronal death are reduced by competing with the nNOS:NOS1AP interaction and by knockdown with NOS1AP-targeting siRNAs.
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13 |
23658158
|
We designed a cell-permeable peptide that competes for the unique PDZ domain of nNOS that interacts with NOS1AP.
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14 |
23658158
|
This peptide inhibits NMDA-induced recruitment of NOS1AP to nNOS and in vivo in rat, doubles surviving tissue in a severe model of neonatal hypoxia-ischemia, a major cause of neonatal death and pediatric disability.
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15 |
23658158
|
The highly unusual sequence specificity of the nNOS:NOS1AP interaction and involvement in excitotoxic signaling may provide future opportunities for generation of neuroprotectants with high specificity.
|
16 |
23658158
|
The nNOS-p38MAPK pathway is mediated by NOS1AP during neuronal death.
|
17 |
23658158
|
Excitotoxic stimulus induces recruitment of NOS1AP to nNOS in rat cortical neuron culture.
|
18 |
23658158
|
Excitotoxic activation of p38MAPK and subsequent neuronal death are reduced by competing with the nNOS:NOS1AP interaction and by knockdown with NOS1AP-targeting siRNAs.
|
19 |
23658158
|
We designed a cell-permeable peptide that competes for the unique PDZ domain of nNOS that interacts with NOS1AP.
|
20 |
23658158
|
This peptide inhibits NMDA-induced recruitment of NOS1AP to nNOS and in vivo in rat, doubles surviving tissue in a severe model of neonatal hypoxia-ischemia, a major cause of neonatal death and pediatric disability.
|
21 |
23658158
|
The highly unusual sequence specificity of the nNOS:NOS1AP interaction and involvement in excitotoxic signaling may provide future opportunities for generation of neuroprotectants with high specificity.
|
22 |
23658158
|
The nNOS-p38MAPK pathway is mediated by NOS1AP during neuronal death.
|
23 |
23658158
|
Excitotoxic stimulus induces recruitment of NOS1AP to nNOS in rat cortical neuron culture.
|
24 |
23658158
|
Excitotoxic activation of p38MAPK and subsequent neuronal death are reduced by competing with the nNOS:NOS1AP interaction and by knockdown with NOS1AP-targeting siRNAs.
|
25 |
23658158
|
We designed a cell-permeable peptide that competes for the unique PDZ domain of nNOS that interacts with NOS1AP.
|
26 |
23658158
|
This peptide inhibits NMDA-induced recruitment of NOS1AP to nNOS and in vivo in rat, doubles surviving tissue in a severe model of neonatal hypoxia-ischemia, a major cause of neonatal death and pediatric disability.
|
27 |
23658158
|
The highly unusual sequence specificity of the nNOS:NOS1AP interaction and involvement in excitotoxic signaling may provide future opportunities for generation of neuroprotectants with high specificity.
|
28 |
23658158
|
The nNOS-p38MAPK pathway is mediated by NOS1AP during neuronal death.
|
29 |
23658158
|
Excitotoxic stimulus induces recruitment of NOS1AP to nNOS in rat cortical neuron culture.
|
30 |
23658158
|
Excitotoxic activation of p38MAPK and subsequent neuronal death are reduced by competing with the nNOS:NOS1AP interaction and by knockdown with NOS1AP-targeting siRNAs.
|
31 |
23658158
|
We designed a cell-permeable peptide that competes for the unique PDZ domain of nNOS that interacts with NOS1AP.
|
32 |
23658158
|
This peptide inhibits NMDA-induced recruitment of NOS1AP to nNOS and in vivo in rat, doubles surviving tissue in a severe model of neonatal hypoxia-ischemia, a major cause of neonatal death and pediatric disability.
|
33 |
23658158
|
The highly unusual sequence specificity of the nNOS:NOS1AP interaction and involvement in excitotoxic signaling may provide future opportunities for generation of neuroprotectants with high specificity.
|
34 |
23658158
|
The nNOS-p38MAPK pathway is mediated by NOS1AP during neuronal death.
|
35 |
23658158
|
Excitotoxic stimulus induces recruitment of NOS1AP to nNOS in rat cortical neuron culture.
|
36 |
23658158
|
Excitotoxic activation of p38MAPK and subsequent neuronal death are reduced by competing with the nNOS:NOS1AP interaction and by knockdown with NOS1AP-targeting siRNAs.
|
37 |
23658158
|
We designed a cell-permeable peptide that competes for the unique PDZ domain of nNOS that interacts with NOS1AP.
|
38 |
23658158
|
This peptide inhibits NMDA-induced recruitment of NOS1AP to nNOS and in vivo in rat, doubles surviving tissue in a severe model of neonatal hypoxia-ischemia, a major cause of neonatal death and pediatric disability.
|
39 |
23658158
|
The highly unusual sequence specificity of the nNOS:NOS1AP interaction and involvement in excitotoxic signaling may provide future opportunities for generation of neuroprotectants with high specificity.
|