ArticleThe Journal of biological chemistry2014
Polymorphisms in the human inhibitory signal-regulatory protein α do not affect binding to its ligand CD47.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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Who cites it
31 citing papers in PubMed, 51 citations in OpenAlex.
- Engineering SIRPα conformational plasticity to reveal a cryptic pocket suitable for structure-based drug design.bioRxiv : the preprint server for biology · 2025Article
- Impact of SIRPα genotype combinations in recipients and donors on alloimmune response in liver transplantation.PNAS nexus · 2025Article
- Donor-recipient mismatch at theScience translational medicine · 2025Article
- The impact of curation errors in the PDBBind Database on machine learning predictions of protein-protein binding affinity.Database : the journal of biological databases and curation · 2025Article
- Development of small molecule drugs targeting immune checkpoints.Cancer biology & medicine · 2024Review
- Discovery and Preclinical Activity of BMS-986351, an Antibody to SIRPα That Enhances Macrophage-mediated Tumor Phagocytosis When Combined with Opsonizing Antibodies.Cancer research communications · 2024Article
- The Impact of Patterns in Linkage Disequilibrium and Sequencing Quality on the Imprint of Balancing Selection.Genome biology and evolution · 2024Article
- Binding Mechanism of CD47 with SIRPα Variants and Its Antibody: Elucidated by Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2023Article
- BYON4228 is a pan-allelic antagonistic SIRPα antibody that potentiates destruction of antibody-opsonized tumor cells and lacks binding to SIRPγ on T cells.Journal for immunotherapy of cancer · 2023Article
- Crystal Structure of Human CD47 in Complex with Engineered SIRPα.D1(N80A).Molecules (Basel, Switzerland) · 2022Article
- Blockade of CD47 enhances the antitumor effect of macrophages in renal cell carcinoma through trogocytosis.Scientific reports · 2022Article
- Targeting the CD47-SIRPα Innate Immune Checkpoint to Potentiate Antibody Therapy in Cancer by Neutrophils.Cancers · 2022Review
- Targeting CD47/SIRPα as a therapeutic strategy, where we are and where we are headed.Biomarker research · 2022Review
- Preclinical characterization of the novel anti-SIRPα antibody BR105 that targets the myeloid immune checkpoint.Journal for immunotherapy of cancer · 2022Article
- SIRPα Mismatch Is Associated With Relapse Protection and Chronic Graft-Versus-Host Disease After Related Hematopoietic Stem Cell Transplantation for Lymphoid Malignancies.Frontiers in immunology · 2022Article
- SIRPα-αCD123 fusion antibodies targeting CD123 in conjunction with CD47 blockade enhance the clearance of AML-initiating cells.Journal of hematology & oncology · 2021Article
- Mismatch in SIRPα, a regulatory protein in innate immunity, is associated with chronic GVHD in hematopoietic stem cell transplantation.Blood advances · 2021Article
- Structural analysis and binding sites of inhibitors targeting the CD47/SIRPα interaction in anticancer therapy.Computational and structural biotechnology journal · 2021Review
- Multivalent, Soluble Nano-Self Peptides Increase Phagocytosis of Antibody-Opsonized Targets while Suppressing "Self" Signaling.ACS nano · 2020Article
- The CD47-SIRPα Immune Checkpoint.Immunity · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
CD47 is a widely distributed membrane protein that interacts with signal-regulatory protein α (SIRPα), an inhibitory receptor on myeloid cells that gives a "don't-eat-me" signal. Manipulation of the interaction is of considerable interest in the immunotherapy of cancer and in xenotransplantation. The amino-terminal ligand binding domain of SIRPα is highly polymorphic in contrast to the single Ig-like domain of CD47. There is confusion as to whether the polymorphisms will affect ligand binding, but this is an important point for this interaction and other paired receptors being considered as targets for therapy. We show by x-ray crystallography that one human SIRPα allele differing in 13 amino acid residues has a very similar binding site and that several different alleles all bind CD47 with similar affinity as expected because the residues are mostly surface-exposed and distant from the binding site. A peptide from the binding site of CD47 has been reported to mimic the CD47 interaction with SIRPα, but we could find no binding. We discuss the possible pitfalls in determining the affinity of weak interactions and also speculate on how SIRPα polymorphisms may have been selected by pathogens and how this may also be true in other paired receptors such as the KIRs.
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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.