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1.
Epilepsy Res ; 200: 107311, 2024 Feb.
Article in English | MEDLINE | ID: mdl-38286108

ABSTRACT

Epileptic nystagmus (EN) is a subtle seizure semiology, most commonly seen in seizures originating in the posterior cortical regions. EN is broadly categorized into type I and type II. Type I EN consists of contralateral repetitive saccadic eye movements alternating with post-saccadic slow drifts with an overall contralateral deviation. Type II EN is characterized by ipsilateral slow drift alternating with contralateral corrective saccades. In this article, we report a method to perform oculographic analysis of eye movements using EEG only. We used this method to classify the type of EN in three patients with parieto-occipital seizures. In all three patients, the ictal EEG demonstrated repetitive saccadic eye movements, directed contralateral to the seizure onset zone. With prolonged time constant, we were able to identify this eye movement pattern as EN with distinct slow and fast phases. We were able to further characterize the type of EN as type I and type II. In all three patients, the direction of EN (direction of fast phase or saccades) was contralateral to the seizure onset zone. EN can be easily missed on video-electroencephalography (vEEG) recordings because of various reasons. Our study demonstrates a systematic method of eye movement analysis on EEG, which can be used to not only identify EN as seizure semiology but also classify it, without requiring additional electrodes.


Subject(s)
Epilepsy , Nystagmus, Pathologic , Humans , Epilepsy/diagnosis , Epilepsy/complications , Nystagmus, Pathologic/diagnosis , Nystagmus, Pathologic/etiology , Seizures/complications , Electroencephalography/adverse effects , Video Recording
3.
J Neuroimmunol ; 353: 577521, 2021 04 15.
Article in English | MEDLINE | ID: mdl-33607505

ABSTRACT

BACKGROUND: Serious neurological complications of SARS-CoV-2 are increasingly being recognized. CASE: We report a novel case of HHV6 myelitis with parainfectious MOG-IgG in the setting of COVID-19-induced lymphopenia and hypogammaglobulinemia. The patient experienced complete neurological recovery with gancyclovir, high dose corticosteroids, and plasma exchange. To our knowledge, this is the first case of HHV6 reactivation in the central nervous system in the setting of COVID19 infection and the first case of MOG-IgG myelitis in the setting of SARS-CoV-2 and HHV6 coinfection. CONCLUSION: Patients with neurological manifestations in the setting of COVID19-related immunodeficiency should be tested for opportunistic infections including HHV6. Viral infection is a known trigger for MOG-IgG and therefore this antibody should be checked in patients with SARS-CoV-2 associated demyelination.


Subject(s)
COVID-19/complications , Coinfection/complications , Lymphopenia/virology , Myelitis, Transverse/virology , Roseolovirus Infections/immunology , Anti-Inflammatory Agents/therapeutic use , Antiviral Agents/therapeutic use , Autoantibodies/immunology , Autoantigens/immunology , COVID-19/immunology , Coinfection/immunology , Ganciclovir/therapeutic use , Herpesvirus 6, Human , Humans , Male , Methylprednisolone/therapeutic use , Middle Aged , Myelitis, Transverse/immunology , Myelitis, Transverse/therapy , Plasma Exchange/methods , Roseolovirus Infections/drug therapy , SARS-CoV-2 , Virus Activation/immunology
4.
J Inorg Biochem ; 141: 152-160, 2014 Dec.
Article in English | MEDLINE | ID: mdl-25265377

ABSTRACT

Mercury(II) metallation of Pseudomonas aeruginosa azurin has been characterized structurally and biochemically. The X-ray crystal structure at 1.5Å of mercury(II) metallated azurin confirms the coordination of mercury at the copper binding active site and a second surface site. These findings are further validated by NMR, Matrix-assisted laser desorption/ionization spectrometry (MALDI), and UV-visible spectroscopic methods indicating copper displacement from the wild-type protein. Bioinformatic analysis has identified homologous human protein domains computationally, and compared them to the structure of azurin, providing a model for human mercury interactions. Study of the mercury-azurin adduct, in combination with other known examples of protein-heavy metal interactions, could provide further insight into the chemical mechanisms of toxicological interactions, leading toward a global understanding of the biological speciation of toxic heavy metals.


Subject(s)
Azurin/chemistry , Ceruloplasmin/chemistry , Copper/chemistry , Factor VIII/chemistry , Mercury/chemistry , Amino Acid Sequence , Azurin/genetics , Azurin/metabolism , Binding Sites , Cations, Divalent , Ceruloplasmin/genetics , Ceruloplasmin/metabolism , Copper/metabolism , Crystallography, X-Ray , Escherichia coli/chemistry , Escherichia coli/genetics , Factor VIII/genetics , Factor VIII/metabolism , Gene Expression , Humans , Mercury/metabolism , Models, Molecular , Molecular Sequence Data , Protein Binding , Protein Structure, Tertiary , Pseudomonas aeruginosa/chemistry , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sequence Alignment , Structural Homology, Protein
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