Publications by authors named "E E Crooks"
Antibodies that target the gp120-gp41 interface of the HIV-1 envelope (Env) trimer comprise a commonly elicited category of broadly neutralizing antibodies (bNAbs). Here, we isolate and characterize VRC44, a bNAb lineage with up to 52% neutralization breadth. The cryoelectron microscopy (cryo-EM) structure of antibody VRC44.
View Article and Find Full Text PDFBackground: Disordered sleep and fatigue are common in the acute phase of stroke and can impede recovery.
Objective: A randomized parallel group placebo-controlled pilot study compared daily morning exposure to blue light or red light (placebo) for improving daytime sleepiness, fatigue, nocturnal sleep, and cognition in patients receiving inpatient rehabilitation for acute stroke.
Methods: 43 patients with disordered sleep secondary to first episode stroke (n = 34 ischemic, n = 9 hemorrhagic; aged 66.
Background: The integration of diversity, equity, and inclusion (DEI) concepts throughout the curriculum is imperative to the preparation of advanced-practice nurses to deliver person-centered care. This article describes the design and evaluation of one institution's faculty-developed DEI competencies for graduate nursing students.
Method: A task force of faculty and content experts utilized a modified Delphi approach in the development of DEI-focused competencies related to advanced-level nursing education.
Article Synopsis
- Broadly neutralizing antibodies (bNAbs) from HIV-1 infected donors show promise for vaccine development, particularly because they target specific glycan structures on HIV envelope proteins.
- Two methods for modifying the glycan structures of HIV envelope proteins are proposed: using the NGAF3 cocktail to reduce complex glycans and co-expressing certain enzymes (B4G and ST6) to promote desirable glycan types.
- Experimental results indicate that while B4G and ST6 modifications generally led to less complex glycan structures, they may alter antibody responses in vaccinations, with implications for future vaccine design strategies.
Cerebral amyloid angiopathy (CAA) is associated with the accumulation of fibrillar Aβ peptides upon and within the cerebral vasculature, which leads to loss of vascular integrity and contributes to disease progression in Alzheimer's disease (AD). We investigate the structure of human-derived Aβ40 fibrils obtained from patients diagnosed with sporadic or familial Dutch-type (E22Q) CAA. Using cryo-EM, two primary structures are identified containing elements that have not been observed in in vitro Aβ40 fibril structures.
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