adenosine diphosphate ribose

{{chembox

| Verifiedfields = changed

| Watchedfields = changed

| verifiedrevid = 457804269

| ImageFile=ADP ribose.svg

| ImageFile1=ADP-ribose 3D.png

| ImageFile2=Three-dimensional model of ADP ribose.png

| ImageSize=250px

| ImageSize2=250px

| IUPACName=

| OtherNames=ADP ribose
ADPR
Adenosine 5'-diphosphoribose

|Section1={{Chembox Identifiers

| CASNo_Ref = {{cascite|changed|??}}

| CASNo=20762-30-5

| UNII_Ref = {{fdacite|correct|FDA}}

| UNII = XV3S4KV26E

| ChEMBL_Ref = {{ebicite|changed|EBI}}

| ChEMBL = 1161865

| MeSHName=Adenosine+Diphosphate+Ribose

| PubChem = 439200

| ChemSpiderID_Ref = {{chemspidercite|changed|chemspider}}

| ChemSpiderID = 388340

| SMILES = O=P(O[C@H]1O[C@H]([C@H](O)[C@@H]1O)CO)(O)OP(=O)(OC[C@H]4O[C@@H](n3c2ncnc(N)c2nc3)[C@H](O)[C@@H]4O)O

| InChI = 1/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(24)9(23)6(31-14)2-30-35(26,27)34-36(28,29)33-15-11(25)8(22)5(1-21)32-15/h3-6,8-11,14-15,21-25H,1-2H2,(H4,16,17,18,26,27,28,29)/p+1/t5-,6+,8-,9+,10+,11-,14+,15+/m0/s1

| InChIKey = YNCNQNWXUFCWJS-LKOYDKQFBH

| StdInChI_Ref = {{stdinchicite|changed|chemspider}}

| StdInChI = 1S/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(24)9(23)6(31-14)2-30-35(26,27)34-36(28,29)33-15-11(25)8(22)5(1-21)32-15/h3-6,8-11,14-15,21-25H,1-2H2,(H4,16,17,18,26,27,28,29)/p+1/t5-,6+,8-,9+,10+,11-,14+,15+/m0/s1

| StdInChIKey_Ref = {{stdinchicite|changed|chemspider}}

| StdInChIKey = YNCNQNWXUFCWJS-DKMYFHGXSA-O

}}

|Section2={{Chembox Properties

| C=15 | H=23 | N=5 | O=14 | P=2

| MolarMass=559.316 g/mol

| Appearance=

| Density=

| MeltingPt=

| BoilingPt=

| Solubility=

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|Section3={{Chembox Hazards

| MainHazards=

| FlashPt=

| AutoignitionPt =

}}

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Adenosine diphosphate ribose (ADPR) is an ester molecule formed into chains by the enzyme poly ADP ribose polymerase.{{cite journal | vauthors = Braidy N, Berg J, Clement J, Sachdev P | title = Role of Nicotinamide Adenine Dinucleotide and Related Precursors as Therapeutic Targets for Age-Related Degenerative Diseases: Rationale, Biochemistry, Pharmacokinetics, and Outcomes | journal = Antioxidants & Redox Signaling | volume = 10 | issue = 2 | pages = 251–294 | date=2019 | doi = 10.1089/ars.2017.7269 | pmc =6277084 | pmid = 29634344}} ADPR is created from cyclic ADP-ribose (cADPR) by the CD38 enzyme using nicotinamide adenine dinucleotide (NAD⁺) as a cofactor.

ADPR binds to and activates the TRPM2 ion channel.{{cite journal |vauthors =Fonfria E, Marshall IC, Benham CD |title=TRPM2 channel opening in response to oxidative stress is dependent on activation of poly(ADP-ribose) polymerase |journal=Br. J. Pharmacol. |volume=143 |issue=1 |pages=186–92 |date=September 2004|pmid=15302683 |pmc=1575275 |doi=10.1038/sj.bjp.0705914 |display-authors=etal}} ADPR is the most potent agonist of the TRPM2 channel.{{cite journal | vauthors = Yu P, Cai X, Liang Y, Yang W | title = Roles of NAD + and Its Metabolites Regulated Calcium Channels in Cancer | journal = Molecules | volume = 25 | issue = 20 | pages = 4826 | date=2019 | doi = 10.3390/molecules25204826 | pmc =7587972 | pmid = 33092205 | doi-access = free }} cADPR also binds to TPRM2, and the action of both molecules is synergistic, with both molecules enhancing the action of the other molecule in activating the TRPM2 channel.{{cite journal | author = Lee HC | title = Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling | journal = Science China Life Sciences | volume = 54 | issue = 8 | pages = 699–711 | date=2011 | doi = 10.1007/s11427-011-4197-3 | pmid = 21786193| s2cid = 24286381 | doi-access = free }} Researchers are not sure how the Adenosine diphosphate reacts with the TRPM2 channel, but the ribose sugar may play a role in activating the TRPM2 ion channel.{{cite journal | doi = 10.1021/acs.joc.9b00338 | title = Synthesis of Terminal Ribose Analogues of Adenosine 5′-Diphosphate Ribose as Probes for the Transient Receptor Potential Cation Channel TRPM2 | date = 2019 | last1 = Baszczyňski | first1 = Ondřej | last2 = Watt | first2 = Joanna M. | last3 = Rozewitz | first3 = Monika D. | last4 = Guse | first4 = Andreas H. | last5 = Fliegert | first5 = Ralf | last6 = Potter | first6 = Barry V. L. | journal = The Journal of Organic Chemistry | volume = 84 | issue = 10 | pages = 6143–6157 | pmid = 30978018 | pmc = 6528165 }}

Researchers believe that co-targeting DNA-dependent protein kinase and poly(adenosine diphosphate-ribose) polymerase-1 does not promote apoptosis or mitotic catastrophe of cancer cells after radiation.{{Cite journal |last1=Azad |first1=Arun |last2=Bukczynska |first2=Patricia |last3=Jackson |first3=Susan |last4=Haput |first4=Ygal |last5=Cullinane |first5=Carleen |last6=McArthur |first6=Grant A. |last7=Solomon |first7=Benjamin |date=2014-02-01 |title=Co-targeting Deoxyribonucleic Acid–Dependent Protein Kinase and Poly(Adenosine Diphosphate-Ribose) Polymerase-1 Promotes Accelerated Senescence of Irradiated Cancer Cells |url=https://www.sciencedirect.com/science/article/abs/pii/S0360301613033026 |journal= International Journal of Radiation Oncology, Biology and Physics |volume=88 |issue=2 |pages=385–394 |doi=10.1016/j.ijrobp.2013.10.043 |pmid=24411611 |issn=0360-3016 |via=Elsevier Science Direct|url-access=subscription }}