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CD33 (UniProt P20138) is confirmed as Siglec-3 (sialic acid-binding immunoglobulin-like lectin 3), a myeloid cell surface antigen and member of the immunoglobulin superfamily in Homo sapiens (vu2025structureofthe pages 1-3, laubli2022targetingthesiglec–sialic pages 1-1). The protein is also known as gp67 and belongs to the CD33-related Siglec family, which has evolved rapidly through gene duplication and exon shuffling (laubli2022targetingthesiglec–sialic pages 2-3). This identity matches the UniProt description, confirming we are researching the correct human gene.
CD33 is a type I single-pass transmembrane receptor characterized by a modular architecture consisting of extracellular immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic tail (vu2025structureofthe pages 1-3, yeh2026crystalstructureof pages 1-2). Among the Siglec family members, CD33 and Siglec-15 are the smallest, containing only one C-set immunoglobulin (IgC) domain in addition to the N-terminal V-set Ig domain (IgV) (vu2025structureofthe pages 1-3).
Recent structural studies have characterized the CD33 extracellular domain (residues 1-232) in detail (yeh2026crystalstructureof pages 2-4). The N-terminal IgV domain contains the sialoglycan-binding site and is encoded by exon 2, while the IgC domain adopts a C1-type fold characterized by the presence of a βD strand (vu2025structureofthe pages 3-4, vu2025structureofthe pages 4-6). Crystal structures reveal that the IgC domain can homodimerize through intermolecular β-strand pairing, specifically via parallel pairing of βC-βC strands and side-chain packing between βC-βD and βC-βF* strands, burying approximately 808 Ų of surface area (vu2025structureofthe pages 3-4). This dimerization mechanism appears unique to CD33 and Siglec-6 among the CD33-related Siglecs (vu2025structureofthe pages 4-6).
The transmembrane (TM) domain of CD33 consists of a 21-residue α-helix (Ala265-His285) that appears monomeric in standard lipid bilayers (vu2025structureofthe pages 4-6). The TM helix exhibits a characteristic "thin neck, thick belly" profile, with small side chains (Ala265, Gly266, Ala269, Ala272) in the extracellular leaflet and bulkier residues, including two phenylalanines (Phe279-Phe280), in the core (vu2025structureofthe pages 4-6). The cytoplasmic side features a cluster of positively charged residues (Arg286, Arg287, Lys288, Arg291) creating a distinctive positive patch (vu2025structureofthe pages 4-6).
The cytoplasmic tail of CD33 is dynamically unstructured and contains one immunoreceptor tyrosine-based inhibitory motif (ITIM) and one ITIM-like motif, which are essential for its inhibitory signaling function (vu2025structureofthe pages 3-4, vu2025structureofthe pages 1-3, k2026immunologicalandpathological pages 1-2).
CD33 functions as a lectin receptor that recognizes terminal sialic acids on cell-surface glycans rather than catalyzing enzymatic reactions (vu2025structureofthe pages 1-3, gonzalezgil2021siglecligands pages 1-3). The protein exhibits preference for α2,6-linked sialoglycans, though it can also recognize α2,3-linked structures (vu2025structureofthe pages 1-3, yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4). A specific high-affinity ligand has been identified as the sialylated sulfated trisaccharide Neu5Acα2-3[6SO3]Galβ1-4GlcNAc (vu2025structureofthe pages 1-3).
The sialic acid-binding site is centered on a conserved arginine residue (Arg119) that forms a salt bridge with the sialic acid carboxylate group (yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4). This interaction is further stabilized by an aromatic cluster comprising Phe21, His45, and Tyr127, and by the STKYSYK motif (residues 124-130), which collectively provide the structural basis for the receptor's glycan-binding specificity (yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4).
Physiological ligands for CD33 include keratan sulfate proteoglycans in the brain, which serve as endogenous binding partners in the central nervous system (vu2025structureofthe pages 1-3). Additionally, α2,6-biantennary sialoglycans on hepatitis B virus surface antigen (HBsAg) have been identified as pathogen-derived ligands that engage CD33 to suppress immune responses (yeh2026crystalstructureof pages 2-4).
CD33 is a cell-surface receptor localized to the plasma membrane, where it performs its glycan-recognition functions (vu2025structureofthe pages 1-3). Upon antibody-mediated cross-linking, CD33 can be redistributed to lipid raft domains in the membrane, suggesting that clustering contributes to receptor signaling (vu2025structureofthe pages 3-4, vu2025structureofthe pages 1-3).
CD33 is expressed on cells of the myeloid lineage, including myeloid progenitor cells, monocytes, macrophages, mast cells, dendritic cells, and brain microglia (vu2025structureofthe pages 1-3, gonzalezgil2021siglecligands pages 3-4, wissfeld2021deletionofalzheimers pages 1-2). In the brain, CD33 is prominently expressed on microglial cells, where it plays important roles in regulating innate immune responses to amyloid-β and other pathological stimuli (wissfeld2021deletionofalzheimers pages 1-2, griciuc2020genetherapyfor pages 1-2). The protein is also expressed on cells in hematological malignancies, particularly acute myeloid leukemia, where it serves as a lineage marker (vu2025structureofthe pages 1-3, gonzalezgil2021siglecligands pages 3-4).
CD33 functions as an inhibitory immune checkpoint receptor through a well-characterized ITIM-dependent signaling pathway (vu2025structureofthe pages 1-3, k2026immunologicalandpathological pages 1-2). Upon ligand engagement or appropriate receptor clustering, tyrosine residues within the ITIM and ITIM-like motifs become phosphorylated, creating docking sites for SH2 domain-containing protein tyrosine phosphatases (yeh2026crystalstructureof pages 2-4, k2026immunologicalandpathological pages 1-2).
The phosphorylated ITIM motifs recruit SHP-1 (encoded by PTPN6) and SHP-2 (encoded by PTPN11) phosphatases to the receptor complex (yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4, k2026immunologicalandpathological pages 1-2, beckers2024cd33andshp1ptpn6 pages 1-2). In human microglia and microglia-like cells, genetic studies have demonstrated genotype-dependent differences in CD33-SHP-1 interaction, with the Alzheimer's disease risk variant affecting this critical signaling partnership (beckers2024cd33andshp1ptpn6 pages 1-2). The recruited phosphatases dephosphorylate activating signaling molecules, thereby attenuating downstream pathways and suppressing cellular activation (k2026immunologicalandpathological pages 1-2).
CD33 signaling directly opposes immunoreceptor tyrosine-based activation motif (ITAM)/DAP12-associated pathways, including those mediated by TREM2 and other activating receptors (wissfeld2021deletionofalzheimers pages 1-2, k2026immunologicalandpathological pages 1-2). In microglia, deletion or functional disruption of CD33 leads to increased phosphorylation of spleen tyrosine kinase (SYK) and extracellular signal-regulated kinases 1 and 2 (ERK1/2), indicating relief from CD33-mediated inhibition (wissfeld2021deletionofalzheimers pages 1-2). This antagonistic relationship positions CD33 as a key negative regulator of myeloid cell activation and phagocytosis.
The primary biological function of CD33 is to serve as an inhibitory immune checkpoint that recognizes self-associated sialoglycans and dampens myeloid cell activation (vu2025structureofthe pages 1-3, laubli2022targetingthesiglec–sialic pages 1-1). By recognizing terminal sialic acids on self-glycans, CD33 contributes to immune self/non-self discrimination and prevents excessive immune activation (vu2025structureofthe pages 1-3, gonzalezgil2021siglecligands pages 1-3).
CD33 potently inhibits phagocytosis in myeloid cells, including microglia (wissfeld2021deletionofalzheimers pages 1-2, griciuc2020genetherapyfor pages 1-2). Loss of CD33 function or genetic knockout increases the phagocytosis of aggregated amyloid-β1-42 peptides, bacterial particles, and cellular debris (wissfeld2021deletionofalzheimers pages 1-2). This inhibitory effect on phagocytosis is mediated through the ITIM-dependent recruitment of phosphatases that counteract activating signals required for efficient phagocytosis.
Deletion of CD33 or knockdown of its signaling partner PTPN6/SHP-1 leads to constitutive activation of inflammation-related gene transcription pathways (wissfeld2021deletionofalzheimers pages 1-2). CD33 knockout human macrophages and microglia show increased transcript levels of pro-inflammatory cytokines including IL-1β, IL-8, and IL-10, along with upregulation of the AD-associated phosphatase INPP5D (wissfeld2021deletionofalzheimers pages 1-2). These findings demonstrate that CD33 normally suppresses inflammatory gene expression in myeloid cells.
Human CD33 undergoes alternative splicing to generate two major isoforms: the full-length CD33M containing all extracellular domains and the short isoform CD33m (also called CD33ΔE2), which lacks exon 2 and therefore the sialic acid-binding IgV domain (wissfeld2021deletionofalzheimers pages 1-2, beckers2024cd33andshp1ptpn6 pages 1-2). The relative expression of these isoforms has important functional and disease-relevant consequences.
The full-length CD33M isoform is generally inhibitory, suppressing microglial phagocytosis, migration, and proliferation while promoting cell adhesion (wissfeld2021deletionofalzheimers pages 1-2). In contrast, the short CD33m isoform exhibits gain-of-function properties, enhancing phagocytosis and proliferation while inhibiting cell adhesion (wissfeld2021deletionofalzheimers pages 1-2). Importantly, CD33m can increase phagocytosis of Aβ1-42 without the detrimental oxidative burst observed with complete CD33 knockout, suggesting a more balanced functional profile (wissfeld2021deletionofalzheimers pages 1-2).
CD33 is a validated genetic risk factor for late-onset Alzheimer's disease (wissfeld2021deletionofalzheimers pages 1-2, griciuc2020genetherapyfor pages 1-2, beckers2024cd33andshp1ptpn6 pages 1-2). The rs3865444C risk allele is associated with increased surface expression of full-length CD33 on myeloid cells, reduced phagocytosis of amyloid-β, and greater amyloid plaque accumulation in the brain (beckers2024cd33andshp1ptpn6 pages 1-2). Conversely, the protective haplotype involving the rs12459419T single nucleotide polymorphism promotes exon 2 skipping, leading to increased expression of the CD33m isoform and reduced AD risk (wissfeld2021deletionofalzheimers pages 1-2, beckers2024cd33andshp1ptpn6 pages 1-2).
CD33 is upregulated on microglial cells in post-mortem AD patient brains, and high levels of CD33 correlate positively with amyloid-β burden and plaque load (wissfeld2021deletionofalzheimers pages 1-2, griciuc2020genetherapyfor pages 1-2). Gene therapy approaches using adeno-associated virus (AAV) vectors encoding artificial microRNA targeting CD33 have shown promise in mouse models, reducing CD33 mRNA, soluble Aβ40 and Aβ42 levels, amyloid plaque burden, and neuroinflammatory markers when administered early in disease progression (griciuc2020genetherapyfor pages 1-2).
CD33 serves as a well-established lineage marker on myeloid leukemias and has been successfully exploited as a therapeutic target in acute myeloid leukemia (AML) (vu2025structureofthe pages 1-3, laubli2022targetingthesiglec–sialic pages 1-1, gonzalezgil2021siglecligands pages 3-4). Antibody-drug conjugates targeting CD33, such as gemtuzumab ozogamicin, deliver cytotoxic payloads specifically to CD33-expressing malignant cells, demonstrating the clinical utility of targeting this receptor in hematologic malignancies (laubli2022targetingthesiglec–sialic pages 1-1).
CD33 has been implicated as an inhibitory receptor exploited by chronic hepatitis B virus (HBV) infection (yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4). The α2,6-biantennary sialoglycans present on HBV surface antigen (HBsAg) engage CD33 on myeloid cells, triggering ITIM phosphorylation and SHP-1/2 recruitment, thereby dampening antiviral immune responses and promoting immune tolerance (yeh2026crystalstructureof pages 2-4). Monoclonal antibodies that block CD33-HBsAg interactions can restore immune function in this context (yeh2026crystalstructureof pages 2-4).
| Aspect | Key findings for human CD33 (SIGLEC3; UniProt P20138) | Evidence/Citation |
|---|---|---|
| Verified identity | CD33 is the human myeloid cell surface antigen also called Siglec-3, a member of the CD33-related Siglec family within the immunoglobulin superfamily; this matches the UniProt target description and distinguishes it from unrelated genes. | (vu2025structureofthe pages 1-3, laubli2022targetingthesiglec–sialic pages 2-3) |
| Protein class and overall architecture | Single-pass type I transmembrane receptor with an extracellular region containing 2 Ig-like domains, a transmembrane helix, and a cytoplasmic tail. The extracellular domains are an N-terminal V-set Ig domain for glycan recognition and one C-set/C2-set Ig-like domain contributing to structure and receptor organization. | (vu2025structureofthe pages 1-3, yeh2026crystalstructureof pages 1-2, k2026immunologicalandpathological pages 1-2) |
| Structural/domain details | CD33 is among the smallest Siglecs because it contains only one IgC domain after the IgV domain. Recent structural work supports an IgC1 homodimerization interface, a 21-residue mostly monomeric transmembrane helix, and a dynamically unstructured cytosolic domain. | (vu2025structureofthe pages 1-3, vu2025structureofthe pages 3-4, vu2025structureofthe pages 4-6) |
| Extracellular domain boundaries used experimentally | A recent structural study expressed human CD33 extracellular domain as residues 1-232, supporting the two-domain ectodomain organization used in biochemical and crystallographic analyses. | (yeh2026crystalstructureof pages 2-4) |
| Sialic acid-binding site | The glycan-binding site is centered on a conserved Arg119 that ligates the sialic acid carboxylate. Binding is further stabilized by an aromatic cluster including Phe21, His45, and Tyr127 and by the STKYSYK motif spanning residues 124-130. | (yeh2026crystalstructureof pages 1-2) |
| Glycan/substrate specificity | CD33 recognizes terminal sialic acids on sialoglycans rather than catalyzing a reaction. Siglecs in general discriminate among α2-3, α2-6, and α2-8 linkages and underlying glycan context; for CD33, available structural and functional evidence supports preference for α2-6-linked sialoglycans and also binding to the sulfated sialylated trisaccharide Neu5Acα2-3[6SO3]Galβ1-4GlcNAc. | (gonzalezgil2021siglecligands pages 1-3, vu2025structureofthe pages 1-3, yeh2026crystalstructureof pages 1-2) |
| Physiologic and disease-relevant ligands | Reported physiological ligands include keratan sulfate proteoglycans in the brain. In chronic hepatitis B work, α2,6-biantennary sialoglycans on HBsAg bind CD33 directly and trigger inhibitory signaling. | (vu2025structureofthe pages 1-3, yeh2026crystalstructureof pages 2-4) |
| Ligand-binding mode | CD33 recognizes self-associated sialoglycans as part of immune self/non-self discrimination. Multivalency and receptor clustering are likely important for productive signaling. | (vu2025structureofthe pages 1-3, laubli2022targetingthesiglec–sialic pages 1-1, gonzalezgil2021siglecligands pages 1-3) |
| Cellular localization | Cell-surface receptor on the plasma membrane of myeloid-lineage cells; antibody cross-linking can relocalize CD33 to lipid raft membrane domains. | (vu2025structureofthe pages 1-3, vu2025structureofthe pages 3-4) |
| Cell-type expression | Expressed on myeloid progenitors, monocytes, macrophages, mast cells, dendritic cells, and brain microglia; disease/atlas-style summaries also list leukemias and myelodysplastic syndromes among contexts where these expressing cells are clinically important. | (vu2025structureofthe pages 1-3, gonzalezgil2021siglecligands pages 3-4) |
| Cytoplasmic signaling motifs | CD33 contains one ITIM and one ITIM-like motif in its cytoplasmic tail; inhibitory Siglecs use these phosphotyrosine motifs to recruit phosphatases after receptor engagement. | (vu2025structureofthe pages 1-3, k2026immunologicalandpathological pages 1-2) |
| Proximal signaling mechanism | Upon ligand engagement or appropriate crosslinking, CD33 ITIM motifs become phosphorylated and recruit SHP-1 and/or SHP-2 phosphatases, attenuating activating pathways and suppressing cell activation. HBV-associated studies specifically describe ITIM phosphorylation followed by SHP-1/2 recruitment. | (yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4, k2026immunologicalandpathological pages 1-2) |
| SHP phosphatase coupling | Human AD-focused work emphasizes CD33-SHP-1/PTPN6 interaction, including genotype-dependent differences in microglia-like cells, while broader Siglec studies and HBV work support SHP-1 and SHP-2 recruitment capability. | (beckers2024cd33andshp1ptpn6 pages 1-2, yeh2026crystalstructureof pages 1-2, k2026immunologicalandpathological pages 1-2) |
| Relationship to activating pathways | CD33 functions as an inhibitory checkpoint that counterbalances ITAM/DAP12-SYK/MAPK-type activation pathways. In microglia, CD33 loss or signaling disruption increases SYK and ERK1/2 phosphorylation and enhances phagocytosis, consistent with antagonism of activating receptors such as TREM2-associated pathways. | (wissfeld2021deletionofalzheimers pages 1-2, k2026immunologicalandpathological pages 1-2) |
| Primary biological function | Immune inhibitory receptor that senses sialoglycans and dampens myeloid-cell activation. In the CNS, CD33 modulates microglial responses, including phagocytosis of amyloid-β and inflammatory output; in peripheral myeloid cells it contributes to inhibitory checkpoint control. | (vu2025structureofthe pages 1-3, wissfeld2021deletionofalzheimers pages 1-2, griciuc2020genetherapyfor pages 1-2) |
| Functional consequences of reduced CD33 signaling | CD33 knockout or exon-2-deleted CD33 expression in human macrophages/microglia increases inflammatory-pathway transcription, SYK and ERK1/2 phosphorylation, and phagocytosis of aggregated Aβ1-42 and bacterial particles; oxidative burst rises after knockout but not necessarily after the short isoform. | (wissfeld2021deletionofalzheimers pages 1-2) |
| Alzheimer’s disease genetics | CD33 is an AD susceptibility locus. The rs3865444C risk allele is associated with increased surface density/full-length CD33 on myeloid cells and reduced Aβ phagocytosis, while the protective haplotype involving rs12459419T favors exon 2 skipping and production of the short isoform lacking the canonical sialic acid-binding IgV domain. | (beckers2024cd33andshp1ptpn6 pages 1-2, wissfeld2021deletionofalzheimers pages 1-2) |
| AD isoforms and function | Full-length CD33M is generally inhibitory and associated with increased Aβ burden, whereas the short isoform CD33m/CD33ΔE2 is AD-protective and can enhance phagocytosis or plaque compaction despite lacking the canonical exon 2-encoded binding domain. | (wissfeld2021deletionofalzheimers pages 1-2) |
| Therapeutic relevance in AD | AAV-mediated knockdown of CD33 in APP/PS1 mice reduced CD33 mRNA, soluble Aβ40/Aβ42, plaque burden, and neuroinflammatory readouts, supporting CD33 as a therapeutic target for microglial reprogramming in AD. | (griciuc2020genetherapyfor pages 1-2) |
| Hematologic malignancy relevance | CD33 is a lineage marker on myeloid leukemias and a validated therapeutic target in acute myeloid leukemia; this clinical use reflects stable cell-surface expression on malignant myeloid cells rather than an enzymatic activity. | (vu2025structureofthe pages 1-3, laubli2022targetingthesiglec–sialic pages 1-1, gonzalezgil2021siglecligands pages 3-4) |
| Additional disease context | CD33 has also been implicated as an inhibitory receptor exploited by HBV, where viral HBsAg-associated α2,6 sialoglycans engage CD33 to promote immune tolerance in myeloid cells. | (yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4) |
Table: This table summarizes the verified identity, structure, ligand specificity, localization, signaling mechanism, core functions, and disease relevance of human CD33/Siglec-3. It is useful as a compact evidence map for functional annotation of the gene product.
CD33 (Siglec-3, UniProt P20138) is a myeloid cell surface receptor belonging to the sialic acid-binding immunoglobulin-like lectin family in humans. The protein functions as an inhibitory immune checkpoint that recognizes terminal sialic acids on self-glycans through its N-terminal V-set immunoglobulin domain, with binding specificity centered on a conserved Arg119 residue and preferential recognition of α2,6-linked sialoglycans (vu2025structureofthe pages 1-3, yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4). CD33 is expressed on myeloid lineage cells including monocytes, macrophages, and brain microglia, where it localizes to the cell surface and can redistribute to lipid raft domains upon clustering (vu2025structureofthe pages 3-4, vu2025structureofthe pages 1-3).
The primary signaling mechanism involves ITIM-mediated recruitment of SHP-1 and SHP-2 phosphatases, which dephosphorylate activating signaling molecules and suppress cellular responses (yeh2026crystalstructureof pages 1-2, yeh2026crystalstructureof pages 2-4, k2026immunologicalandpathological pages 1-2, beckers2024cd33andshp1ptpn6 pages 1-2). This inhibitory signaling opposes ITAM/DAP12-associated activation pathways such as TREM2, positioning CD33 as a key negative regulator of microglial phagocytosis and inflammatory responses (wissfeld2021deletionofalzheimers pages 1-2, k2026immunologicalandpathological pages 1-2). CD33 undergoes alternative splicing to produce functionally distinct isoforms, with the full-length CD33M being inhibitory and the exon 2-deleted CD33m isoform exhibiting gain-of-function properties including enhanced phagocytosis (wissfeld2021deletionofalzheimers pages 1-2).
CD33 plays critical roles in Alzheimer's disease pathogenesis, where genetic variants modulating isoform expression influence amyloid-β clearance and AD risk, and in acute myeloid leukemia, where it serves as a validated therapeutic target (wissfeld2021deletionofalzheimers pages 1-2, griciuc2020genetherapyfor pages 1-2, beckers2024cd33andshp1ptpn6 pages 1-2). Understanding CD33's structure, substrate specificity, signaling mechanisms, and disease associations provides a foundation for developing targeted immunotherapies in neurodegeneration and cancer.
References
(vu2025structureofthe pages 1-3): Han N. Vu, Alan J. Situ, Xuhang Dai, and Tobias S. Ulmer. Structure of the cd33 receptor and implications for the siglec family. Biochemistry, 64:1450-1462, Mar 2025. URL: https://doi.org/10.1021/acs.biochem.4c00864, doi:10.1021/acs.biochem.4c00864. This article has 6 citations and is from a peer-reviewed journal.
(laubli2022targetingthesiglec–sialic pages 1-1): Heinz Läubli, Sam C. Nalle, and Daniel Maslyar. Targeting the siglec–sialic acid immune axis in cancer: current and future approaches. Cancer Immunology Research, 10:1423-1432, Oct 2022. URL: https://doi.org/10.1158/2326-6066.cir-22-0366, doi:10.1158/2326-6066.cir-22-0366. This article has 114 citations and is from a domain leading peer-reviewed journal.
(laubli2022targetingthesiglec–sialic pages 2-3): Heinz Läubli, Sam C. Nalle, and Daniel Maslyar. Targeting the siglec–sialic acid immune axis in cancer: current and future approaches. Cancer Immunology Research, 10:1423-1432, Oct 2022. URL: https://doi.org/10.1158/2326-6066.cir-22-0366, doi:10.1158/2326-6066.cir-22-0366. This article has 114 citations and is from a domain leading peer-reviewed journal.
(yeh2026crystalstructureof pages 1-2): Yi-Hung Yeh, Min-Guan Lin, Pei-Shan Sung, Shie-Liang Hsieh, and Chwan-Deng Hsiao. Crystal structure of the cd33/fab-10c8 complex elucidates the mechanism of antibody antagonism in hbv-induced immunosuppression. Journal of Biomedical Science, May 2026. URL: https://doi.org/10.1186/s12929-026-01248-9, doi:10.1186/s12929-026-01248-9. This article has 0 citations and is from a domain leading peer-reviewed journal.
(yeh2026crystalstructureof pages 2-4): Yi-Hung Yeh, Min-Guan Lin, Pei-Shan Sung, Shie-Liang Hsieh, and Chwan-Deng Hsiao. Crystal structure of the cd33/fab-10c8 complex elucidates the mechanism of antibody antagonism in hbv-induced immunosuppression. Journal of Biomedical Science, May 2026. URL: https://doi.org/10.1186/s12929-026-01248-9, doi:10.1186/s12929-026-01248-9. This article has 0 citations and is from a domain leading peer-reviewed journal.
(vu2025structureofthe pages 3-4): Han N. Vu, Alan J. Situ, Xuhang Dai, and Tobias S. Ulmer. Structure of the cd33 receptor and implications for the siglec family. Biochemistry, 64:1450-1462, Mar 2025. URL: https://doi.org/10.1021/acs.biochem.4c00864, doi:10.1021/acs.biochem.4c00864. This article has 6 citations and is from a peer-reviewed journal.
(vu2025structureofthe pages 4-6): Han N. Vu, Alan J. Situ, Xuhang Dai, and Tobias S. Ulmer. Structure of the cd33 receptor and implications for the siglec family. Biochemistry, 64:1450-1462, Mar 2025. URL: https://doi.org/10.1021/acs.biochem.4c00864, doi:10.1021/acs.biochem.4c00864. This article has 6 citations and is from a peer-reviewed journal.
(k2026immunologicalandpathological pages 1-2): Lakshmi K and Vino Sundararajan. Immunological and pathological roles of siglecs: a molecular review. Frontiers in Immunology, May 2026. URL: https://doi.org/10.3389/fimmu.2026.1826359, doi:10.3389/fimmu.2026.1826359. This article has 0 citations and is from a peer-reviewed journal.
(gonzalezgil2021siglecligands pages 1-3): Anabel Gonzalez-Gil and Ronald L. Schnaar. Siglec ligands. Cells, 10:1260, May 2021. URL: https://doi.org/10.3390/cells10051260, doi:10.3390/cells10051260. This article has 131 citations.
(gonzalezgil2021siglecligands pages 3-4): Anabel Gonzalez-Gil and Ronald L. Schnaar. Siglec ligands. Cells, 10:1260, May 2021. URL: https://doi.org/10.3390/cells10051260, doi:10.3390/cells10051260. This article has 131 citations.
(wissfeld2021deletionofalzheimers pages 1-2): Jannis Wißfeld, Ichiro Nozaki, Mona Mathews, Tamara Raschka, Christian Ebeling, Veit Hornung, Oliver Brüstle, and Harald Neumann. Deletion of alzheimer's disease‐associated cd33 results in an inflammatory human microglia phenotype. Glia, 69:1393-1412, Feb 2021. URL: https://doi.org/10.1002/glia.23968, doi:10.1002/glia.23968. This article has 111 citations and is from a domain leading peer-reviewed journal.
(griciuc2020genetherapyfor pages 1-2): Ana Griciuc, Anthony N Federico, Jeyashree Natasan, Angela M Forte, Danielle McGinty, Huong Nguyen, Adrienn Volak, Stanley LeRoy, Sheetal Gandhi, Eli P Lerner, Eloise Hudry, Rudolph E Tanzi, and Casey A Maguire. Gene therapy for alzheimer's disease targeting cd33 reduces amyloid beta accumulation and neuroinflammation. Human molecular genetics, 29:2920-2935, Aug 2020. URL: https://doi.org/10.1093/hmg/ddaa179, doi:10.1093/hmg/ddaa179. This article has 151 citations and is from a domain leading peer-reviewed journal.
(beckers2024cd33andshp1ptpn6 pages 1-2): Lien Beckers, Mamunur Rashid, Annie J. Lee, Zena K. Chatila, Kirstin A. Tamucci, Ryan C. Talcoff, Jennifer L. Hall, David A. Bennett, Badri N. Vardarajan, and Elizabeth M. Bradshaw. Cd33 and shp-1/ptpn6 interaction in alzheimer’s disease. Genes, 15:1204, Sep 2024. URL: https://doi.org/10.3390/genes15091204, doi:10.3390/genes15091204. This article has 8 citations.