| D011971 |
Receptors, Immunologic |
Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behavior of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere. |
Immunologic Receptors,Immunologic Receptor,Immunological Receptors,Receptor, Immunologic,Receptors, Immunological |
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| D002352 |
Carrier Proteins |
Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. |
Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier |
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| D003598 |
Cytoskeletal Proteins |
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible. |
Proteins, Cytoskeletal |
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| D004268 |
DNA-Binding Proteins |
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. |
DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D000071198 |
Pyrin |
A tripartite motif protein that consists of an N-terminal pyrin domain, a central coiled-coil region and B-box type ZINC FINGER, and C-terminal regions that mediate homotrimerization and interactions with other proteins (the B30.2/SPRY DOMAIN). It is expressed primarily by mature GRANULOCYTES and associates with the cytoskeleton in the perinuclear area as well as AUTOPHAGOSOMES, where it co-ordinates the assembly of AUTOPHAGY-RELATED PROTEINS and degradation of INFLAMMASOME components. It functions in INNATE IMMUNITY and INFLAMMATION; mutations in the Pyrin protein (MEFV) gene are associated with FAMILIAL MEDITERRANEAN FEVER. |
MEFV Protein,Marenostrin,Mediterranean Fever Protein,TRIM20 Protein |
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| D000071199 |
NLR Family, Pyrin Domain-Containing 3 Protein |
An NLR protein that contains an N-terminal PYRIN DOMAIN and ATP-binding site and 9 C-terminal LEUCINE-rich repeats; it is expressed primarily by MACROPHAGES. It is a core component of the INFLAMMASOME and directs its assembly in response to pathogen infection and damage-associated stimuli. Mutations in the NLRP3 gene are associated with FAMILIAL COLD AUTOINFLAMMATORY SYNDROME. |
Cold Autoinflammatory Syndrome 1 Protein,NACHT, LRR and PYD Domains-Containing Protein 3,NLRP3 Protein,NACHT, LRR and PYD Domains Containing Protein 3,NLR Family, Pyrin Domain Containing 3 Protein |
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| D000071457 |
DEAD Box Protein 58 |
A DEAD-box RNA helicase that contains an N-terminal DEATH-LIKE DOMAIN, AAA+ ATPase domain, and C-terminal RNA HELICASE activity. It functions as an innate immune receptor through its recognition of viral nucleic acids. It also induces the expression of INTERFERON TYPE I and proinflammatory CYTOKINES. Its ligands include: 5'-triphosphorylated SINGLE-STRANDED RNA, DOUBLE-STRANDED RNA (dsRNA), and short dsRNA (less than 1 kb in length). |
DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 58,Probable ATP-Dependent RNA Helicase DDX58,RIG-I-like Receptor 1,Probable ATP Dependent RNA Helicase DDX58,RIG I like Receptor 1 |
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| D012328 |
RNA Viruses |
Viruses whose genetic material is RNA. |
RNA Rodent Viruses,RNA Rodent Virus,RNA Virus,Rodent Virus, RNA,Rodent Viruses, RNA,Virus, RNA,Virus, RNA Rodent,Viruses, RNA,Viruses, RNA Rodent |
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| D012330 |
RNA, Double-Stranded |
RNA consisting of two strands as opposed to the more prevalent single-stranded RNA. Most of the double-stranded segments are formed from transcription of DNA by intramolecular base-pairing of inverted complementary sequences separated by a single-stranded loop. Some double-stranded segments of RNA are normal in all organisms. |
Double-Stranded RNA,Double Stranded RNA,RNA, Double Stranded |
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