ReviewThe Journal of biological chemistry2026
Decoding the glycan shield: Immune recognition and response to the HIV-1 envelope trimer.
Review in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The HIV-1 envelope glycoprotein (Env) is essential for viral entry and infection of host cells. Composed of a trimer of the gp120-gp41 heterodimeric glycoproteins, the Env trimer is the primary target for neutralizing antibodies. Extensive research over the past 40 years has focused on developing advanced immunogens, specifically recombinant, native-like Env trimers and structure-guided, germline-targeting constructs, to elicit protective antibody responses. The Env trimer is encased by up to 90 N-linked glycosylation sites, whose occupancy effectively shields the underlying protein from immune surveillance. While it is well established that glycosylation of HIV-1 gp120 affects antibody responses in infected individuals and that many broadly neutralizing antibodies depend on glycan-specific epitopes, the capacity of Env-derived glycopeptides to act as unconventional CD4
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.