Abstract
The precise contribution of endoplasmic reticulum (ER) chaperone protein disulfide isomerase (PDI) variants in human amyotrophic lateral sclerosis (ALS) patients to the pathogenesis of ALS remained unclear. In the present study, Woehlbier et al (2016) demonstrated that these PDI variants are capable of altering motor neuron morphology, impairing the expression of synaptic proteins, and compromising neuromuscular junction (NMJ) integrity.
Publication types
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Comment
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Research Support, Non-U.S. Gov't
MeSH terms
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Amyotrophic Lateral Sclerosis / genetics
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Amyotrophic Lateral Sclerosis / metabolism*
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Amyotrophic Lateral Sclerosis / pathology
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Endoplasmic Reticulum / metabolism
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Endoplasmic Reticulum Stress / physiology*
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Humans
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Procollagen-Proline Dioxygenase / genetics
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Procollagen-Proline Dioxygenase / metabolism
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Protein Disulfide-Isomerases / genetics
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Protein Disulfide-Isomerases / metabolism
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Proteostasis Deficiencies / metabolism
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Proteostasis Deficiencies / pathology
Substances
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Procollagen-Proline Dioxygenase
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P4HB protein, human
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Protein Disulfide-Isomerases
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PDIA3 protein, human