Taylor Arhar
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Explore the profile of Taylor Arhar including associated specialties, affiliations and a list of published articles.
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10
Citations
278
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Recent Articles
1.
Johnson O, Nadel C, Carroll E, Arhar T, Gestwicki J
J Biol Chem
. 2022 Feb;
298(3):101697.
PMID: 35148989
Chaperones of the heat shock protein 70 (Hsp70) family engage in protein-protein interactions with many cochaperones. One "hotspot" for cochaperone binding is the EEVD motif, found at the extreme C ...
2.
Arhar T, Shkedi A, Nadel C, Gestwicki J
J Biol Chem
. 2021 Oct;
297(5):101282.
PMID: 34624315
The major classes of molecular chaperones have highly variable sequences, sizes, and shapes, yet they all bind to unfolded proteins, limit their aggregation, and assist in their folding. Despite the...
3.
Abrams J, Arhar T, Mok S, Taylor I, Kampmann M, Gestwicki J
Cell Stress Chaperones
. 2021 Feb;
26(2):443-452.
PMID: 33547632
Prion protein (PrP) adopts either a helical conformation (PrP) or an alternative, beta sheet-rich, misfolded conformation (PrP). The PrP form has the ability to "infect" PrP and force it into...
4.
Newberry R, Arhar T, Costello J, Hartoularos G, Maxwell A, Naing Z, et al.
ACS Chem Biol
. 2020 Aug;
15(8):2137-2153.
PMID: 32786289
Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific proteins remains largely uncharacterized, in part due to the challenge of probing protein...
5.
Sohn P, Huang C, Yan R, Fan L, Tracy T, Camargo C, et al.
Neuron
. 2019 Sep;
104(3):458-470.e5.
PMID: 31542321
Dysregulation of neuronal excitability underlies the pathogenesis of tauopathies, including frontotemporal dementia (FTD) with tau inclusions. A majority of FTD-causing tau mutations are located in the microtubule-binding domain, but how...
6.
Mavor D, Barlow K, Asarnow D, Birman Y, Britain D, Chen W, et al.
Biol Open
. 2018 Jul;
7(7).
PMID: 30037883
Although the primary protein sequence of ubiquitin (Ub) is extremely stable over evolutionary time, it is highly tolerant to mutation during selection experiments performed in the laboratory. We have proposed...
7.
Mapping interactions with the chaperone network reveals factors that protect against tau aggregation
Mok S, Condello C, Freilich R, Gillies A, Arhar T, Oroz J, et al.
Nat Struct Mol Biol
. 2018 May;
25(5):384-393.
PMID: 29728653
A network of molecular chaperones is known to bind proteins ('clients') and balance their folding, function and turnover. However, it is often unclear which chaperones are critical for selective recognition...
8.
Freilich R, Arhar T, Abrams J, Gestwicki J
Acc Chem Res
. 2018 Apr;
51(4):940-949.
PMID: 29613769
Molecular chaperones play a central role in protein homeostasis (a.k.a. proteostasis) by balancing protein folding, quality control, and turnover. To perform these diverse tasks, chaperones need the malleability to bind...
9.
Mirheydari M, Rathnayake S, Frederick H, Arhar T, Mann E, Cocklin S, et al.
J Lipid Res
. 2016 Jun;
57(8):1465-76.
PMID: 27256689
Lipid droplets (LDs) are organelles that contribute to various cellular functions that are vital for life. Aside from acting as a neutral lipid storage depot, they are also involved in...
10.
Kao P, Green E, Pereira C, Ekimura S, Juarez D, Whyte T, et al.
J Funct Foods
. 2016 Feb;
12:450-457.
PMID: 26893614
The aggregation of the 37-amino acid polypeptide islet amyloid polypeptide (IAPP, amylin), as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of...