William D Tolbert
Overview
Explore the profile of William D Tolbert including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
59
Citations
1033
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Benlarbi M, Richard J, Clemente T, Bourassa C, Tolbert W, Gottumukkala S, et al.
medRxiv
. 2025 Mar;
PMID: 40061344
While antiretroviral therapy efficiently suppresses viral replication, inflammation and immune dysfunction persist in some people living with HIV-1 (PLWH). Soluble gp120 (sgp120) has been detected in PLWH plasma and its...
2.
Lee D, Niu L, Ding S, Zhu H, Tolbert W, Medjahed H, et al.
ACS Med Chem Lett
. 2024 Nov;
15(11):1961-1969.
PMID: 39563795
The ability of the HIV-1 accessory proteins Nef and Vpu to decrease CD4 protects infected cells from antibody-dependent cellular cytotoxicity (ADCC) by limiting the exposure of vulnerable epitopes to envelope...
3.
Richard J, Grunst M, Niu L, Diaz-Salinas M, Tolbert W, Marchitto L, et al.
bioRxiv
. 2024 Sep;
PMID: 39253431
HIV-1 envelope glycoproteins (Env) from primary HIV-1 isolates typically adopt a pretriggered "closed" conformation that resists to CD4-induced (CD4i) non-neutralizing antibodies (nnAbs) mediating antibody-dependent cellular cytotoxicity (ADCC). CD4-mimetic compounds (CD4mcs)...
4.
Marchitto L, Richard J, Prevost J, Tauzin A, Yang D, Chiu T, et al.
J Virol
. 2024 Sep;
98(10):e0101624.
PMID: 39248460
The majority of naturally elicited antibodies against the HIV-1 envelope glycoproteins (Env) are non-neutralizing (nnAbs) because they are unable to recognize the Env trimer in its native "closed" conformation. Nevertheless,...
5.
Tauzin A, Marchitto L, Belanger E, Benlarbi M, Beaudoin-Bussieres G, Prevost J, et al.
J Virol
. 2024 Sep;
98(10):e0096024.
PMID: 39230306
Importance: There are several reasons that make it difficult to target the HIV reservoir. One of them is the capacity of infected cells to prevent the recognition of HIV-1 envelope...
6.
Marchitto L, Richard J, Prevost J, Tauzin A, Yang D, Chiu T, et al.
bioRxiv
. 2024 Jun;
PMID: 38895270
The majority of naturally-elicited antibodies against the HIV-1 envelope glycoproteins (Env) are non-neutralizing (nnAbs), because they are unable to recognize the Env timer in its native "closed" conformation. Nevertheless, it...
7.
Tauzin A, Marchitto L, Belanger E, Benlarbi M, Beaudoin-Bussieres G, Prevost J, et al.
medRxiv
. 2024 Jun;
PMID: 38883797
CD4-mimetics (CD4mcs) are small molecule compounds that mimic the interaction of the CD4 receptor with HIV-1 envelope glycoproteins (Env). Env from primary viruses normally samples a "closed" conformation which occludes...
8.
Conley H, He M, Easterhoff D, Kirshner H, Cocklin S, Meyer J, et al.
Front Immunol
. 2024 Jan;
14:1306292.
PMID: 38264644
Fcγ receptors (FcγRs) are membrane-bound glycoproteins that bind to the fragment crystallizable (Fc) constant regions of IgG antibodies. Interactions between IgG immune complexes and FcγRs can initiate signal transduction that...
9.
Benlarbi M, Richard J, Bourassa C, Tolbert W, Chartrand-Lefebvre C, Gendron-Lepage G, et al.
J Infect Dis
. 2023 Nov;
229(3):763-774.
PMID: 38035854
Background: Chronic inflammation persists in some people living with human immunodeficiency virus (HIV) during antiretroviral therapy and is associated with premature aging. The glycoprotein 120 (gp120) subunit of HIV-1 envelope...
10.
Prevost J, Chen Y, Zhou F, Tolbert W, Gasser R, Medjahed H, et al.
Nat Commun
. 2023 Oct;
14(1):6710.
PMID: 37872202
The HIV-1 entry inhibitor temsavir prevents the viral receptor CD4 (cluster of differentiation 4) from interacting with the envelope glycoprotein (Env) and blocks its conformational changes. To do this, temsavir...