Publications by authors named "Emily Byrd"

Introduction: The COVID-19 pandemic resulted in the rapid expansion of telemedicine, including in specialties traditionally dependent on physical exams, such as pediatric surgery. Trends in its utilization as in-person visits resumed are not well understood, nor is its effect on mitigating disparities related to social determinants of health (SDOH). We hypothesize that telemedicine utilization increased after the pandemic and has remained higher compared to pre-pandemic levels.

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Deposits of aggregated TAR DNA-binding protein 43 (TDP-43) in the brain are associated with several neurodegenerative diseases. It is well established that binding of RNA/DNA to TDP-43 can prevent TDP-43 aggregation, but an understanding of the structure(s) and conformational dynamics of TDP-43, and TDP-43-RNA complexes, is lacking, including knowledge of how the solution environment modulates these properties. Here, we address this challenge using hydrogen-deuterium exchange-mass spectrometry.

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Oligomeric species populated during α-synuclein aggregation are considered key drivers of neurodegeneration in Parkinson's disease. However, the development of oligomer-targeting therapeutics is constrained by our limited knowledge of their structure and the molecular determinants driving their conversion to fibrils. Phenol-soluble modulin α3 (PSMα3) is a nanomolar peptide binder of α-synuclein oligomers that inhibits aggregation by blocking oligomer-to-fibril conversion.

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Αlpha-synuclein (αS) is an intrinsically disordered protein which exhibits a high degree of conformational heterogeneity. , αS experiences various environments which cause adaptation of its structural ensemble. Divalent metal ions are prominent in synaptic terminals where αS is located and are thought to bind to the αS C-terminal region.

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Alpha-synuclein (αSyn) is a protein involved in neurodegenerative disorders including Parkinson's disease. Amyloid formation of αSyn can be modulated by the 'P1 region' (residues 36-42). Here, mutational studies of P1 reveal that Y39A and S42A extend the lag-phase of αSyn amyloid formation in vitro and rescue amyloid-associated cytotoxicity in C.

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Alphaviruses are small enveloped RNA viruses that bud from the host cell plasma membrane. Alphavirus particles have a highly organized structure, with a nucleocapsid core containing the RNA genome surrounded by the capsid protein, and a viral envelope containing 80 spikes, each a trimer of heterodimers of the E1 and E2 glycoproteins. The capsid protein and envelope proteins are both arranged in organized lattices that are linked via the interaction of the E2 cytoplasmic tail/endodomain with the capsid protein.

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Alphaviruses are members of a group of small enveloped RNA viruses that includes important human pathogens such as Chikungunya virus and the equine encephalitis viruses. The virus membrane is covered by a lattice composed of 80 spikes, each a trimer of heterodimers of the E2 and E1 transmembrane proteins. During virus endocytic entry, the E1 glycoprotein mediates the low-pH-dependent fusion of the virus membrane with the endosome membrane, thus initiating virus infection.

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Objectives: Our objectives were (1) to determine demographic characteristics of intimate partner violence (IPV) victims and perpetrators, as reported by victims in a Victim Assistance Unit where police are called to the scene for IPV, and (2) to compare the relative risk of methamphetamine, cocaine, and alcohol use in perpetrators vs victims of IPV, as reported by victims.

Methods: Data from a Victim Assistance Unit intake statistics for the months of January to November 2006 were accessed. For this system in a city of approximately 500,000 population, with a large Hispanic population, police call for an onsite advocate intervention (trained social worker) at their own discretion for the victim and for children involved.

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