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Andrew Umstead

Explore the profile of Andrew Umstead including associated specialties, affiliations and a list of published articles. Areas
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Articles 11
Citations 51
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Recent Articles
1.
Soliman A, Umstead A, Lamp J, Vega I
Front Neurosci . 2024 May; 18:1373410. PMID: 38765673
Tauopathies are characterized by the abnormal buildup of tau protein, with early oligomeric forms associated with neurodegeneration and the later neurofibrillary tangles possibly conferring neuroprotection. The molecular mechanisms governing the...
2.
Vega I, Umstead A
Methods Mol Biol . 2022 Oct; 2551:253-267. PMID: 36310208
Liquid-liquid phase separation (LLPS) is a reversible biological process that contributes to the formation of critical concentration of proteins, forming membraneless compartments that are physiologically and pathologically relevant. Several proteins...
3.
Patterson J, Cole-Strauss A, Kuhn N, Mercier C, Kochmanski J, Gerlach J, et al.
J Vis Exp . 2022 Jul; (184). PMID: 35815999
Identification and isolation of contagious individuals along with quarantine of close contacts, is critical for slowing the spread of COVID-19. Large-scale testing in a surveillance or screening capacity for asymptomatic...
4.
Patterson J, Hirst W, Howe J, Russell C, Cole-Strauss A, Kemp C, et al.
NPJ Parkinsons Dis . 2022 May; 8(1):61. PMID: 35610264
β2-adrenoreceptor (β2AR) agonists have been associated with a decreased risk of developing Parkinson's disease (PD) and are hypothesized to decrease expression of both alpha-synuclein mRNA (Snca) and protein (α-syn). Effects...
5.
Soliman A, Umstead A, Grabinski T, Kanaan N, Lee A, Ryan J, et al.
J Neurochem . 2021 Sep; 159(6):992-1007. PMID: 34543436
EFhd2 is a conserved calcium-binding protein that is highly expressed in the central nervous system. We have shown that EFhd2 interacts with tau protein, a key pathological hallmark in Alzheimer's...
6.
Umstead A, Soliman A, Lamp J, Vega I
Anal Biochem . 2020 Oct; 611:113999. PMID: 33098768
E. coli is a common host for generating human recombinant proteins in in vitro studies that seek to understand the biochemical and structural properties of proteins and in drug discovery....
7.
Vega I, Umstead A, Kanaan N
Front Neurosci . 2019 Aug; 13:845. PMID: 31456657
The transition of tau proteins from its soluble physiological conformation to the pathological aggregate forms found in Alzheimer's disease and related dementias, is poorly understood. Therefore, understanding the process that...
8.
Umstead A, Vega I
J Alzheimers Dis . 2019 Mar; 68(2):511-516. PMID: 30814358
The accumulation of tau protein aggregates is a pathological hallmark in Alzheimer's disease (AD) and other neurodegenerative diseases. However, the identity of the toxic tau conformation that propagates and induces...
9.
Vega I, Sutter A, Parks L, Umstead A, Ivanova M
Front Neurosci . 2018 Dec; 12:879. PMID: 30559642
Aggregation of the protein tau is a pathological hallmark of Alzheimer's disease (AD) and related disorders. However, the molecular mechanisms that lead to tau protein aggregation are still unclear. Previously,...
10.
Cornett E, Dickson B, Krajewski K, Spellmon N, Umstead A, Vaughan R, et al.
Sci Adv . 2018 Dec; 4(11):eaav2623. PMID: 30498785
Lysine methylation is a key regulator of histone protein function. Beyond histones, few connections have been made to the enzymes responsible for the deposition of these posttranslational modifications. Here, we...