Michael J Root
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Explore the profile of Michael J Root including associated specialties, affiliations and a list of published articles.
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21
Citations
473
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Recent Articles
1.
Schapiro H, Khasnis M, Ahn K, Karagiaridi A, Hayden S, Cilento M, et al.
PLoS Pathog
. 2022 May;
18(5):e1010531.
PMID: 35584191
Glycoprotein Env of human immunodeficiency virus type 1 (HIV-1) mediates viral entry through membrane fusion. Composed of gp120 and gp41 subunits arranged as a trimer-of-heterodimers, Env adopts a metastable, highly...
2.
Zhang S, Holmes A, Dick A, Rashad A, Enriquez Rodriguez L, Canziani G, et al.
Retrovirology
. 2021 Oct;
18(1):31.
PMID: 34627310
Background: We previously developed drug-like peptide triazoles (PTs) that target HIV-1 Envelope (Env) gp120, potently inhibit viral entry, and irreversibly inactivate virions. Here, we investigated potential mechanisms of viral escape...
3.
Smith A, Weinstock M, Siglin A, Whitby F, Francis J, Hill C, et al.
Retrovirology
. 2019 Oct;
16(1):28.
PMID: 31640718
Background: PIE12-trimer is a highly potent D-peptide HIV-1 entry inhibitor that broadly targets group M isolates. It specifically binds the three identical conserved hydrophobic pockets at the base of the...
4.
Ahn K, Root M
J Biol Chem
. 2017 Jul;
292(40):16498-16510.
PMID: 28696261
The homotrimeric HIV-1 envelope glycoprotein (Env) undergoes receptor-triggered structural changes that mediate viral entry through membrane fusion. This process is inhibited by chemokine receptor antagonists (CoRAs) that block Env-receptor interactions...
5.
Khasnis M, Halkidis K, Bhardwaj A, Root M
PLoS Pathog
. 2016 Dec;
12(12):e1006098.
PMID: 27992602
Structural rearrangements of HIV-1 glycoprotein Env promote viral entry through membrane fusion. Env is a symmetric homotrimer with each protomer composed of surface subunit gp120 and transmembrane subunit gp41. Cellular...
6.
Leslie G, Wang J, Richardson M, Haggarty B, Hua K, Duong J, et al.
PLoS Pathog
. 2016 Nov;
12(11):e1005983.
PMID: 27855210
HIV-1 entry can be inhibited by soluble peptides from the gp41 heptad repeat-2 (HR2) domain that interfere with formation of the 6-helix bundle during fusion. Inhibition has also been seen...
7.
Danial M, Stauffer A, Wurm F, Root M, Klok H
Bioconjug Chem
. 2016 Oct;
28(3):701-712.
PMID: 27737540
A popular strategy for overcoming the limited plasma half-life of peptide heptad repeat 2 (HR2) fusion inhibitors against HIV-1 is conjugation with biocompatible polymers such as poly(ethylene glycol) (PEG). However,...
8.
Danial M, Root M, Klok H
Biomacromolecules
. 2012 Mar;
13(5):1438-47.
PMID: 22455441
This report describes the synthesis and properties of a series of polyvalent side chain peptide-synthetic polymer conjugates designed to block the CD4 binding site on gp120 and inhibit HIV-1 entry...
9.
Pumroy R, Nardozzi J, Hart D, Root M, Cingolani G
J Biol Chem
. 2011 Dec;
287(3):2022-31.
PMID: 22130666
The human genome encodes six isoforms of importin α that show greater than 60% sequence similarity and remarkable substrate specificity. The isoform importin α5 can bind phosphorylated cargos such as...
10.
Welch B, Francis J, Redman J, Paul S, Weinstock M, Reeves J, et al.
J Virol
. 2010 Aug;
84(21):11235-44.
PMID: 20719956
The HIV gp41 N-trimer pocket region is an ideal viral target because it is extracellular, highly conserved, and essential for viral entry. Here, we report on the design of a...