ArticleActa crystallographica. Section D, Structural biology2019
Antibody fragments structurally enable a drug-discovery campaign on the cancer target Mcl-1.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed.
- 50 Years of Antibody Numbering Schemes: A Statistical and Structural Evaluation Reveals Key Differences and Limitations.Antibodies (Basel, Switzerland) · 2024Article
- The structure of the neurotoxin palytoxin determined by MicroED.bioRxiv : the preprint server for biology · 2023Article
- Structural basis of the specificity and interaction mechanism of Bmf binding to pro-survival Bcl-2 family proteins.Computational and structural biotechnology journal · 2023Article
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Authors and funding
10 authors.
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Abstract
Apoptosis is a crucial process by which multicellular organisms control tissue growth, removal and inflammation. Disruption of the normal apoptotic function is often observed in cancer, where cell death is avoided by the overexpression of anti-apoptotic proteins of the Bcl-2 (B-cell lymphoma 2) family, including Mcl-1 (myeloid cell leukaemia 1). This makes Mcl-1 a potential target for drug therapy, through which normal apoptosis may be restored by inhibiting the protective function of Mcl-1. Here, the discovery and biophysical properties of an anti-Mcl-1 antibody fragment are described and the utility of both the scFv and Fab are demonstrated in generating an Mcl-1 crystal system amenable to iterative structure-guided drug design.
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