ArticleiScience2026
Structural dissection of CD38 antigen engagement by CAR binders and rational affinity tuning.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chimeric antigen receptor (CAR) T cell therapy uses synthetic receptors to direct T cells to target and lyse cancer cells. CD38 is a multifunctional ectoenzyme involved in immunomodulation and a therapeutic target in hematological malignancies. Here, we report structural and functional characterization of two CD38-targeting binders, RP02 and 028, revealing distinct mechanisms of epitope engagement and enzymatic inhibition. Crystal structures demonstrate that RP02 binds the N-lobe of CD38 via VH-mediated interactions, while 028 spans both N- and C-lobes, inducing allosteric inhibition. Alanine scanning identified critical residues for affinity tuning. Functional assays showed 028 potently inhibits CD38's cyclase activity, whereas RP02 has minimal effect, correlating with 028's occlusion of the catalytic pocket via η6 loop-mediated dimerization. Further, CAR-T cells engineered with affinity-attenuated 028
Indexed as
Identifiers
What OpenQuestion holds
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.