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| ADP |
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| CHEBI:16761 |
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| A purine ribonucleoside 5'-diphosphate having adenine as the nucleobase. |
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This entity has been manually annotated by the ChEBI Team.
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CHEBI:40553, CHEBI:13222, CHEBI:2342, CHEBI:22244
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| No supplier information found for this compound. |
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Molfile
XML
SDF
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more structures >>
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call loadScript javascripts\jsmol\core\package.js call loadScript javascripts\jsmol\core\core.z.js -- required by ClazzNode call loadScript javascripts\jsmol\J\awtjs2d\WebOutputChannel.js
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InChI=1S/C10H15N5O10P2/c11- 8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1 |
| XTWYTFMLZFPYCI-KQYNXXCUSA-N |
| Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
fundamental metabolite
Any metabolite produced by all living cells.
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
(via nucleoside 5'-diphosphate )
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View more via ChEBI Ontology
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adenosine 5'-(trihydrogen diphosphate)
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5'-adenylphosphoric acid
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ChemIDplus
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Adenosine 5'-diphosphate
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KEGG COMPOUND
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ADENOSINE-5'-DIPHOSPHATE
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PDBeChem
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ADP
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KEGG COMPOUND
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H3adp
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IUPAC
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ADP
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PDBeChem
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C00008
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KEGG COMPOUND
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C00019353
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KNApSAcK
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DB03431
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DrugBank
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G11113
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KEGG GLYCAN
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MOL000173
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COMe
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| View more database links |
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20398-34-9
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CAS Registry Number
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KEGG COMPOUND
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58-64-0
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CAS Registry Number
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ChemIDplus
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67722
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Reaxys Registry Number
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Reaxys
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88452
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Gmelin Registry Number
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Gmelin
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Chapman J, Soloveichick L, Shavit S, Shoenfeld Y, Korczyn AD (2005)
Antiphospholipid antibodies bind ATP: a putative mechanism for the pathogenesis of neuronal dysfunction.
Clinical & developmental immunology 12, 175-180 [PubMed:16295522]
[show Abstract]
Antiphospholipid antibodies (aPL) generated in experimental animals cross-react with ATP. We therefore examined the possibility that aPL IgG from human subjects bind to ATP by affinity column and an enzyme linked immunosorbent assay (ELISA). Sera with high levels of aPL IgG were collected from 12 patients with the antiphospholipid syndrome (APS). IgG fractions from 10 of 12 APS patients contained aPL that could be affinity-bound to an ATP column and completely eluted with NaCl 0.5 M. A significant (> 50%) inhibition of aPL IgG binding by ATP 5 mM was found in the majority. Similar inhibition was obtained with ADP but not with AMP or cAMP. All the affinity purified anti-ATP antibodies also bound beta2-glycoprotein-I (beta2-GPI, also known as apolipoprotein H) suggesting that, similar to most pathogenic aPL, their binding depends on this serum cofactor. We further investigated this possibility and found that the binding of beta2-GPI to the ATP column was similar to that of aPL IgG in that most was reversed by NaCl 0.5 M. Furthermore, addition of beta2-GPI to aPL IgG significantly increased the amount of aPL binding to an ATP column. We conclude that aPL IgG bind ATP, probably through beta32-GPI. This binding could interfere with the normal extracellular function of ATP and similar neurotransmitters. |
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