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  2. RAGE (receptor) - Wikipedia

    en.wikipedia.org/wiki/RAGE_(receptor)

    Schematic of the relation between an immunoglobulin and RAGE Schematic of the RAGE gene and its products. RAGE (receptor for advanced glycation endproducts), also called AGER, is a 35 kilodalton transmembrane receptor [5] of the immunoglobulin super family which was first characterized in 1992 by Neeper et al. [6] Its name comes from its ability to bind advanced glycation endproducts (), which ...

  3. RAGE (gene) - Wikipedia

    en.wikipedia.org/wiki/RAGE_(gene)

    5891 26448 Ensembl ENSG00000080823 ENSMUSG00000056458 UniProt Q9UQ07 Q9WVS4 RefSeq (mRNA) NM_001272011 NM_014226 NM_001330234 NM_001353827 NM_001353828 NM_001353829 NM_001353830 NM_001353831 NM_001353832 NM_011973 RefSeq (protein) NP_001258940 NP_001317163 NP_055041 NP_001340756 NP_001340757 NP_001340758 NP_001340759 NP_001340760 NP_001340761 NP_036103 Location (UCSC) Chr 14: 102.22 – 102.31 ...

  4. Damage-associated molecular pattern - Wikipedia

    en.wikipedia.org/wiki/Damage-associated...

    Protein DAMPs include intracellular proteins, such as heat-shock proteins [11] or HMGB1, [12] and materials derived from the extracellular matrix that are generated following tissue injury, such as hyaluronan fragments. [13] Non-protein DAMPs include ATP, [14] [15] uric acid, [16] heparin sulfate and DNA. [17]

  5. Recombination-activating gene - Wikipedia

    en.wikipedia.org/wiki/Recombination-activating_gene

    As with many enzymes, RAG proteins are fairly large. For example, mouse RAG-1 contains 1040 amino acids and mouse RAG-2 contains 527 amino acids. The enzymatic activity of the RAG proteins is concentrated largely in a core region; Residues 384–1008 of RAG-1 and residues 1–387 of RAG-2 retain most of the DNA cleavage activity.

  6. HMGB1 - Wikipedia

    en.wikipedia.org/wiki/HMGB1

    HMGB1 has to interact with p53. [15] [16]HMGB1 is a nuclear protein that binds to DNA and acts as an architectural chromatin-binding factor. It can also be released from cells, in which extracellular form it can bind the inflammatory receptor RAGE (Receptor for Advanced Glycation End-products) and Toll-like receptors (TLRs).

  7. Toll-like receptor 9 - Wikipedia

    en.wikipedia.org/wiki/Toll-like_receptor_9

    54106 81897 Ensembl ENSG00000239732 ENSMUSG00000045322 UniProt Q9NR96 Q9EQU3 RefSeq (mRNA) NM_138688 NM_017442 NM_031178 RefSeq (protein) NP_059138 NP_112455 Location (UCSC) Chr 3: 52.22 – 52.23 Mb Chr 9: 106.1 – 106.1 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Toll-like receptor 9 is a protein that in humans is encoded by the TLR9 gene. TLR9 has also been designated as ...

  8. S100A12 - Wikipedia

    en.wikipedia.org/wiki/S100A12

    n/a Ensembl ENSG00000163221 n/a UniProt P80511 n/a RefSeq (mRNA) NM_005621 n/a RefSeq (protein) NP_005612 n/a Location (UCSC) Chr 1: 153.37 – 153.38 Mb n/a PubMed search n/a Wikidata View/Edit Human S100 calcium-binding protein A12 (S100A12) is a protein that in humans is encoded by the S100A12 gene. Human S100A12, also known as calgranulin C, was first described in 1995. The protein encoded ...

  9. Glycation - Wikipedia

    en.wikipedia.org/wiki/Glycation

    In contrast with glycation, glycosylation is the enzyme-mediated ATP-dependent attachment of sugars to a protein or lipid. [1] Glycosylation occurs at defined sites on the target molecule. It is a common form of post-translational modification of proteins and is required for the functioning of the mature protein.