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Attenuated mismatch negativity in patients with first-episode antipsychotic-naive schizophrenia using a source-resolved method.

08:00 EDT 12th March 2019 | BioPortfolio

Summary of "Attenuated mismatch negativity in patients with first-episode antipsychotic-naive schizophrenia using a source-resolved method."

Mismatch negativity (MMN) is a measure of pre-attentive auditory information processing related to change detection. Traditional scalp-level EEG methods consistently find attenuated MMN in patients with chronic but not first-episode schizophrenia. In the current paper, we use a source-resolved method to assess MMN and hypothesize that more subtle changes can be identified with this analysis method.

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This article was published in the following journal.

Name: NeuroImage. Clinical
ISSN: 2213-1582
Pages: 101760

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Medical and Biotech [MESH] Definitions

Eukaryotic homolog of the bacterial MutL DNA MISMATCH REPAIR protein. It heterodimerizes with MISMATCH REPAIR ENDONUCLEASE PMS2 to form MutL alpha, which is recruited to DNA mismatch sites by the MUTS DNA MISMATCH-BINDING PROTEIN. Mutations in the human MLH1 gene are associated with COLORECTAL NEOPLASMS, HEREDITARY NONPOLYPOSIS.

A MutL protein and component of the DNA MISMATCH REPAIR system. Its ENDONUCLEASE activity introduces SINGLE-STRAND DNA BREAKS which create entry points for EXO1 exonuclease to remove the strand containing the mismatch. It may also function in DNA DAMAGE signaling.

An episode of MYOCARDIAL ISCHEMIA that generally lasts longer than a transient anginal episode but that does not usually result in MYOCARDIAL INFARCTION.

A methyl-directed mismatch DNA REPAIR protein that has weak ATPASE activity. MutS was originally described in ESCHERICHIA COLI.

DNA repair proteins that include the bacterial MutS DNA mismatch-binding protein and its eukaryotic homologs that function in DNA MISMATCH REPAIR and recombination of DNA during MEIOSIS. MutS has a conserved mismatch recognition domain characterized by GxFxE, or similar AMINO ACID MOTIFS that also occur in eukaryotic homologs such as MSH1, MSH6, and MSH8. All MutS proteins also contain a highly-conserved ATP-binding domain and most have weak ATPase activity.

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