ArticleImmunology1993
Structure and homology of human C1q receptor (collectin receptor).
Article in Immunology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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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.
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
30 citing papers in PubMed, 111 citations in OpenAlex.
- Calreticulin-From the Endoplasmic Reticulum to the Plasma Membrane-Adventures of a Wandering Protein.Cancers · 2025Review
- The therapeutic mavericks: Potent immunomodulating chaperones capable of treating human diseases.Journal of cellular and molecular medicine · 2023Review
- Membrane Bound CRT Fragment Accelerates Tumor Growth of Melanoma B16 Cell In Vivo through Promoting M2 Polarization via TLR4.Journal of immunology research · 2022Article
- Molecular and Cellular Interactions of Scavenger Receptor SR-F1 With Complement C1q Provide Insights Into Its Role in the Clearance of Apoptotic Cells.Frontiers in immunology · 2020Article
- Collectins: Innate Immune Pattern Recognition Molecules.Advances in experimental medicine and biology · 2020Review
- Complement Component C1q: Historical Perspective of a Functionally Versatile, and Structurally Unusual, Serum Protein.Frontiers in immunology · 2018Review
- C1q: A fresh look upon an old molecule.Molecular immunology · 2017Review
- Calreticulin: roles in cell-surface protein expression.Membranes · 2014Review
- Entamoeba histolytica cell surface calreticulin binds human c1q and functions in amebic phagocytosis of host cells.Infection and immunity · 2012Article
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- Ultraviolet-B recruits mannose-binding lectin into skin from non-cutaneous sources.The Journal of investigative dermatology · 2005Article
- The FK506 binding protein 13 kDa (FKBP13) interacts with the C-chain of complement C1q.BMC pharmacology · 2004Article
- C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells.The Journal of experimental medicine · 2001Article
- C1q receptors.Clinical and experimental immunology · 2000Review
- C1q-mediated chemotaxis by human neutrophils: involvement of gClqR and G-protein signalling mechanisms.The Biochemical journal · 1998Article
- Anti-C1q receptor/calreticulin autoantibodies in patients with systemic lupus erythematosus (SLE).Clinical and experimental immunology · 1998Article
- Release of calreticulin from neutrophils may alter C1q-mediated immune functions.The Biochemical journal · 1997Article
- Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.Molecular biology of the cell · 1995Article
- Identification of a gC1q-binding protein (gC1q-R) on the surface of human neutrophils. Subcellular localization and binding properties in comparison with the cC1q-R.The Journal of clinical investigation · 1995Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper we report partial amino acid sequence for C1q receptor (C1qR). The N-terminal amino acid sequence of isolated C1qR and the sequences of peptides obtained by V8/trypsin digestion show a high degree of similarity to the cDNA-derived amino acid sequence of a human protein which was initially reported as a component of RoSSA and subsequently as calreticulin. This sequence in turn shows homology with Onchocerca volvulus antigen (RAL-1) and B50 murine melanoma antigen. A component of approximately 53,000 MW, isolated from human spleen, was found to have identical mobility on SDS-PAGE to C1qR and identical N-terminal sequence, but a different overall charge. Human antibodies from Sjögren's syndrome patients did not recognize C1qR, but showed positive reaction with the purified 53,000 MW component from spleen. Rabbit antibodies against denatured C1qR, in contrast, recognized both C1qR and the purified 53,000 MW component. The 53,000 MW spleen component thus has an identical N-terminal sequence to calreticulin, and to the reported RoSSA component, and is recognized by antibodies in Sjögren's syndrome sera. The data obtained indicate that C1qR and the reported calreticulin/RoSSA component are similar but not identical molecules, which belong to the same protein superfamily.
Indexed as
Identifiers
8478019PMC1421832W97744267What 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.