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Thematische Bibliographien / Phosphorylation

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Zeitschriftenartikel
Dissertationen
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Auswahl der wissenschaftlichen Literatur zum Thema „Phosphorylation“

Autor: Grafiati

Veröffentlicht am 4. Juni 2021

Zuletzt aktualisiert am 25. Juli 2025

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Zeitschriftenartikel zum Thema "Phosphorylation"

1

Hizli, Asli A., Yong Chi, Jherek Swanger, et al. "Phosphorylation of Eukaryotic Elongation Factor 2 (eEF2) by Cyclin A–Cyclin-Dependent Kinase 2 Regulates Its Inhibition by eEF2 Kinase." Molecular and Cellular Biology 33, no. 3 (2012): 596–604. http://dx.doi.org/10.1128/mcb.01270-12.

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ABSTRACTProtein synthesis is highly regulated via both initiation and elongation. One mechanism that inhibits elongation is phosphorylation of eukaryotic elongation factor 2 (eEF2) on threonine 56 (T56) by eEF2 kinase (eEF2K). T56 phosphorylation inactivates eEF2 and is the only known normal eEF2 functional modification. In contrast, eEF2K undergoes extensive regulatory phosphorylations that allow diverse pathways to impact elongation. We describe a new mode of eEF2 regulation and show that its phosphorylation by cyclin A–cyclin-dependent kinase 2 (CDK2) on a novel site, serine 595 (S595), dir

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Coulonval, Katia, Hugues Kooken, and Pierre P. Roger. "Coupling of T161 and T14 phosphorylations protects cyclin B–CDK1 from premature activation." Molecular Biology of the Cell 22, no. 21 (2011): 3971–85. http://dx.doi.org/10.1091/mbc.e11-02-0136.

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Mitosis is triggered by the abrupt dephosphorylation of inhibitory Y15 and T14 residues of cyclin B1–bound cyclin-dependent kinase (CDK)1 that is also phosphorylated at T161 in its activation loop. The sequence of events leading to the accumulation of fully phosphorylated cyclin B1–CDK1 complexes remains unclear. Two-dimensional gel electrophoresis allowed us to determine whether T14, Y15, and T161 phosphorylations occur on same CDK1 molecules and to characterize the physiological occurrence of their seven phosphorylation combinations. Intriguingly, in cyclin B1–CDK1, the activating T161 phosp

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ADAMS, Ryan A., Xinran LIU, David S. WILLIAMS, and Alexandra C. NEWTON. "Differential spatial and temporal phosphorylation of the visual receptor, rhodopsin, at two primary phosphorylation sites in mice exposed to light." Biochemical Journal 374, no. 2 (2003): 537–43. http://dx.doi.org/10.1042/bj20030408.

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Phosphorylation of rhodopsin critically controls the visual transduction cascade by uncoupling it from the G-protein transducin. The kinase primarily responsible for this phosphorylation is rhodopsin kinase, a substrate-regulated kinase that phosphorylates light-activated rhodopsin. Protein kinase C has been implicated in controlling the phosphorylation of both light-activated and dark-adapted rhodopsin. Two of the major rhodopsin phosphorylation sites in vivo, Ser334 and Ser338, are effective protein kinase C phosphorylation sites in vitro, while the latter is preferentially phosphorylated by

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Vanoosthuyse, Vincent, and Kevin G. Hardwick. "The Complexity of Bub1 Regulation: Phosphorylation, Phosphorylation, Phosphorylation." Cell Cycle 2, no. 2 (2003): 118–19. http://dx.doi.org/10.4161/cc.2.2.343.

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Sluzala, Zachary B., Yang Shan, Lynda Elghazi, et al. "Novel mTORC2/HSPB4 Interaction: Role and Regulation of HSPB4 T148 Phosphorylation." Cells 13, no. 23 (2024): 2000. https://doi.org/10.3390/cells13232000.

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HSPB4 and HSPB5 (α-crystallins) have shown increasing promise as neuroprotective agents, demonstrating several anti-apoptotic and protective roles in disorders such as multiple sclerosis and diabetic retinopathy. HSPs are highly regulated by post-translational modification, including deamidation, glycosylation, and phosphorylation. Among them, T148 phosphorylation has been shown to regulate the structural and functional characteristics of HSPB4 and underlie, in part, its neuroprotective capacity. We recently demonstrated that this phosphorylation is reduced in retinal tissues from patients wit

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Pant, Harish C., and Veeranna. "Neurofilament phosphorylation." Biochemistry and Cell Biology 73, no. 9-10 (1995): 575–92. http://dx.doi.org/10.1139/o95-063.

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Neurofilament proteins (NFPs) are highly phosphorylated molecules in the axonal compartment of the adult nervous system. The phosphorylation of NFP is considered an important determinant of filament caliber, plasticity, and stability. This process reflects the function of NFs during the lifetime of a neuron from differentiation in the embryo through long-term activity in the adult until aging and environmental insult leads to pathology and ultimately death. NF function is modulated by phosphorylation–dephosphorylation in each of these diverse neuronal states. In this review, we have summarized

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Carty, DJ, DL Freas, and AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets." Blood 70, no. 2 (1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.511.

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Abstract We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 mumol/L and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was less than 1 second; 20-K phosphorylation was increased greater than 200% and 47-K phosphorylation was increased 50%. The ADP sensitivity of 20-K phosphorylation was greater than that of 47-K phosphorylation (

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Carty, DJ, DL Freas, and AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets." Blood 70, no. 2 (1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.bloodjournal702511.

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We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 mumol/L and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was less than 1 second; 20-K phosphorylation was increased greater than 200% and 47-K phosphorylation was increased 50%. The ADP sensitivity of 20-K phosphorylation was greater than that of 47-K phosphorylation (P less th

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Bhattacharyya, Sumit, Alip Borthakur, Arivarasu N. Anbazhagan, Shivani Katyal, Pradeep K. Dudeja та Joanne K. Tobacman. "Specific effects of BCL10 Serine mutations on phosphorylations in canonical and noncanonical pathways of NF-κB activation following carrageenan". American Journal of Physiology-Gastrointestinal and Liver Physiology 301, № 3 (2011): G475—G486. http://dx.doi.org/10.1152/ajpgi.00071.2011.

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To determine the impact of B cell leukemia/lymphoma (BCL) 10 on the phosphorylation of crucial mediators in NF-κB-mediated inflammatory pathways, human colonic epithelial cells were exposed to carrageenan (CGN), a sulfated polysaccharide commonly used as a food additive and known to induce NF-κB nuclear translocation by both canonical and noncanonical pathways. Phosphorylations of intermediates in inflammatory cascades, including NF-κB-inducing kinase (NIK) at Thr559, transforming growth factor-β-activating kinase (TAK) 1 at Thr184, Thr187, and Ser192, and inhibitory factor κBα (IκBα) at Ser32

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Langlais, Paul, Zhengping Yi, and Lawrence J. Mandarino. "The Identification of Raptor as a Substrate for p44/42 MAPK." Endocrinology 152, no. 4 (2011): 1264–73. http://dx.doi.org/10.1210/en.2010-1271.

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Abstract The adaptor protein raptor is the functional identifier for mammalian target of rapamycin (mTOR) complex 1 (mTORC1), acting to target mTOR to specific substrates for phosphorylation and regulation. Using HPLC-electrospray ionization tandem mass spectrometry, we confirmed the phosphorylation of raptor at Ser696, Thr706, Ser721, Ser722, Ser855, Ser859, Ser863, Thr865, Ser877, Ser881, Ser883, and Ser884 and identified Tyr692, Ser699, Thr700, Ser704, Ser854, Ser857, Ser882, Ser886, Ser887, and Thr889 as new, previously unidentified raptor phosphorylation sites. Treatment of cells with ins

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Dissertationen zum Thema "Phosphorylation"

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Hirose, Masayuki. "Phosphorylation and recruitment of Syk by ITAM-based phosphorylation of tamalin." Kyoto University, 2004. http://hdl.handle.net/2433/145291.

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Napper, Scott. "Phosphorylation sites of HPr." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0020/NQ43518.pdf.

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Craig, Timothy James. "Phosphorylation of exocytotic proteins." Thesis, University of Liverpool, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.406719.

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Ackerley, Steven. "Neurofilament transport and phosphorylation." Thesis, King's College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.289881.

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Cleverly, Karen Elizabeth. "Investigation of neurofilament phosphorylation." Thesis, King's College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267652.

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Chaubey, Mark. "Phosphorylation of endocytic proteins." Thesis, University of Cambridge, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615671.

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Thurston, Barbara. "Protein Phosphorylation in Archaea." Diss., Virginia Tech, 1997. http://hdl.handle.net/10919/30617.

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Protein phosphorylation constitutes an important mechanism for cellular regulation in both Eucarya and Bacteria. All living organisms evolved from a common progenitor; this implies that protein phosphorylation as a means of regulation also exists in Archaea. Previously, in the sulfur-dependent archaeon Sulfolobus solfataricus a gene was cloned encoding a protein-serine/threonine phosphatase that was similar to eucaryal protein-serine/threonine phosphatases type 1, 2A, and 2B. To identify protein phosphatases in other archaeons, oligonucleotides encoding conserved regions of eucaryal

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Martins, Filipa de Sá. "Abeta dependent tau phosphorylation." Master's thesis, Universidade de Aveiro, 2011. http://hdl.handle.net/10773/7647.

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Mestrado em Biomedicina Molecular<br>Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by the presence of two histopathological hallmarks: the extracellular amyloid plaques (APs) composed of beta-amyloid protein (Abeta) and intracellular neurofibrillary tangles (NFTs), containing hyperphosphorylated tau protein. Therefore, Abeta and tau are important molecules associated with AD and evidence suggests that Abeta may initiate the hyperphosphorylation of tau, which by disrupting neuronal network leads to the process of neurodegeneration. In the present study, using rat primar

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Rardin, Matthew James. "Reversible phosphorylation in mitochondria." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p3331484.

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Thesis (Ph. D.)--University of California, San Diego, 2008.<br>Title from first page of PDF file (viewed Dec. 16, 2008). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.

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Wang, Huachun. "Protein phosphorylation regulation in Arabidopsis." Diss., Columbia, Mo. : University of Missouri-Columbia, 2006. http://hdl.handle.net/10355/5896.

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Thesis (Ph. D.)--University of Missouri-Columbia, 2006.<br>The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file (viewed on July 18, 2008) Vita. Includes bibliographical references.

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Bücher zum Thema "Phosphorylation"

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Eyers, Claire E., ed. Histidine Phosphorylation. Springer US, 2020. http://dx.doi.org/10.1007/978-1-4939-9884-5.

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1936-, Marks Friedrich, ed. Protein phosphorylation. VCH, 1996.

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1945-, Moudgil V. K., ed. Receptor phosphorylation. CRC Press, 1989.

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M, Sefton Bartholomew, and Hunter Tony 1943-, eds. Protein phosphorylation. Academic Press, 1998.

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Kadenbach, Bernhard, ed. Mitochondrial Oxidative Phosphorylation. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3573-0.

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6

Doerig, Christian, Gerald Späth, and Martin Wiese, eds. Protein Phosphorylation in Parasites. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527675401.

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R, Shewry P., Halford N. G, and Hooley Richard, eds. Protein phosphorylation in plants. Clarendon Press, 1996.

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1946-, Kemp Bruce E., ed. Peptides and protein phosphorylation. CRC Press, 1990.

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Turner, Andrew Michael. Protein phosphorylation in "Rhodomicrobium vannielii". typescript, 1987.

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Heilmeyer, L. M. G., ed. Signal Transduction and Protein Phosphorylation. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4757-0166-1.

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Buchteile zum Thema "Phosphorylation"

1

Frank, J. Howard, J. Howard Frank, Michael C. Thomas, et al. "Phosphorylation." In Encyclopedia of Entomology. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6359-6_2918.

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Jones, Simon. "Phosphorylation." In Biotechnology. Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620913.ch4.

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Veenstra, Timothy D. "Phosphorylation." In Proteomics for Biological Discovery. John Wiley & Sons, Inc., 2019. http://dx.doi.org/10.1002/9781119081661.ch11.

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Baker, Julien S., Fergal Grace, Lon Kilgore, et al. "Phosphorylation." In Encyclopedia of Exercise Medicine in Health and Disease. Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2867.

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Gooch, Jan W. "Phosphorylation." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14487.

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Ellis, Jonathan J., and Boštjan Kobe. "Protein Phosphorylation." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_184.

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Nichols, R. Jeremy. "LRRK2 Phosphorylation." In Advances in Neurobiology. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-49969-7_3.

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Bizzarri, Bruno Mattia. "Prebiotic Phosphorylation." In Encyclopedia of Astrobiology. Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_5457.

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Bizzarri, Bruno Mattia. "Prebiotic Phosphorylation." In Encyclopedia of Astrobiology. Springer Berlin Heidelberg, 2022. http://dx.doi.org/10.1007/978-3-642-27833-4_5457-1.

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Baak, Marleen A., Bernard Gutin, Kim A. Krawczewski Carhuatanta, et al. "Oxidative Phosphorylation." In Encyclopedia of Exercise Medicine in Health and Disease. Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2816.

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Konferenzberichte zum Thema "Phosphorylation"

1

Dong, Yi, Min Zhang, Lang Wu, and Qiuxin Wu. "Imbalanced Phosphorylation Site Prediction Based on Federated Learning." In 2024 5th International Conference on Computer Engineering and Intelligent Control (ICCEIC). IEEE, 2024. https://doi.org/10.1109/icceic64099.2024.10775983.

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2

Gear, LR A., D. Freas, and J. D. Carty. "EARLY (< 5 SEC) PHOSPHORYLATIONS OF PLATELET PROTEINS FOLLOWING ACTIVATION BY ADP AND ADRENALIN, SEPARATELY AND IN COMBINATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643640.

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Understanding the earliest events (< 1 sec) in signal transduction of platelets is important, since there is evicenee that “shape change,” aggregation and secretion can all begin within this period. We have employed a guenched-flow approach to study these early events and found that thrombin can induce rapid phosphorylation of myosin light-chain kinase (20K) and a 47K protein (Blood, 67, 1738, 1986). To investigate the role of rapid phosphorylations in platelet activation, we have studied the influence of adrenalin and ADP during early (0.3 to 5 sec) stimulation. Aggregation in washed human

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Daniel, J. L., and M. Rigmaiden. "Evidence for Ca2+-independent phosphorylation of human platelet myosin." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644527.

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Phosphorylation of platelet myosin is thought to be required for activation of the contractile events occurring during platelet activation. At present the only known mechanism for Onitiating myosin phosphorylation is through a Ca2+-calmodulin-dependent activation of myosin light chain kinase. However, our previous studies using the fluorescent Ca2+-indicator quin2 indicated that both platelet shape change and myosin phosphorylation could be induced in an EGTA-containing media in the absence of a measurable change in cytosolic free Ca2+ concentration (Hallam, Daniel, Kendrick-Jones & Rink.

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Ayati, Marzieh, Danica Wiredja, Daniela Schlatzer, Goutham Narla, Mark R. Chance, and Mehmet Koyuturk. "MoBaS on Phosphorylation Data." In BCB '16: ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics. ACM, 2016. http://dx.doi.org/10.1145/2975167.2995267.

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Khaybrakhmanova, Elvira A., Stanislav V. Kozyrev, Tatyana V. Tyumkina, and Irina Yu Ponedel’kina. "Phosphorylation of Hyaluronic Acid." In International Electronic Conference on Synthetic Organic Chemistry. MDPI, 2022. http://dx.doi.org/10.3390/ecsoc-26-13535.

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Shvetsova, Anastasiia, Michele Fiore, Peter Strazewski, and Isabelle Daniel. "Phosphorylation of prebiotic precursors." In Goldschmidt2021. European Association of Geochemistry, 2021. http://dx.doi.org/10.7185/gold2021.6016.

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Enouf, J., R. Bredoux, A. Giraud, N. Bourdeau, and S. Levy-Toledano. "POSSIBLE RELATIONSHIP BETWEEN THE 23-kDa PHOSPHOPROTEIN AND THE IP3 -INDUCED Ca2+RELEASE IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644516.

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The regulation of Ca2+ concentration in human platelets involves intracellular membranes i.e. dense tubular system (DTS). Agonist-induced platelet activation generates inositol 1,4,5 trisphosphate (IP3) which is responsible for Ca2+ mobilization from DTS. However, its mechanism of action is still unknown. cAMP has been shown to regulate Ca2+ transport by isolated membrane vesicles. This effect was correlated with the phosphorylation of a 23 kDa protein. We investigated whether this phosphorylation could play a role in the mechanism of IP3-induced Ca release.We isolated a membrane fraction enri

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Cheng, Qiong, Mitsunori Ogihara, and Vineet Gupta. "Inferring conflict-sensitive phosphorylation dynamics." In the 2nd ACM Conference. ACM Press, 2011. http://dx.doi.org/10.1145/2147805.2147864.

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Krejčová, Romana, Květoslava Horská, Ivan Votruba, and Antonín Holý. "Phosphorylation of enantiomers of HPMPG." In XIth Symposium on Chemistry of Nucleic Acid Components. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199902286.

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Huzoor-Akbar, H., and Khursheed Anwer. "EVIDENCE THAT ABNORMAL PLATELET AGGREGATION IN SPONTANEOUSLY HYPERTENSIVE RATS IS LINKED WITH PHOSPHOINOSITIDES TURNOVER AND PHOSPHORYLATION OF 47,000 DALTON PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643810.

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We have shown earlier that abnormal platelet aggregation in spontaneously hypertensive rats (SHR) is not caused by prostaglandins (Thromb. Res. 41, 555-566, 1986). In this study platelets from SHR and normotensive (Wistar Kyoto, WKY) rats were used to examine the role of phosphoinositides (Pins) and protein phosphorylation in increased platelet activation in hypertension. Thrombin (0.05 U/ml) induced rapid hydrolysis of phosphatidylinositol-4,5-bis-phosphate (PIP2), phosphatidyl-inositol-4-phosphate (PIP), and phosphatidylinositol (PI) in (32p)-pO4 labeled platelets. However, significantly gre

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Berichte der Organisationen zum Thema "Phosphorylation"

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JOHN C WALKER. SYMPOSIUM ON PLANT PROTEIN PHOSPHORYLATION. Office of Scientific and Technical Information (OSTI), 2011. http://dx.doi.org/10.2172/1028190.

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Granot, David, Richard Amasino, and Avner Silber. Mutual effects of hexose phosphorylation enzymes and phosphorous on plant development. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7587223.bard.

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Research objectives 1) Analyze the combined effects of hexose phosphorylation and P level in tomato and Arabidopsis plants 2) Analyze the combined effects of hexose phosphorylation and P level in pho1 and pho2 Arabidopsis mutants 3) Clone and analyze the PHO2 gene 4) Select Arabidopsis mutants resistant to high and low P 5) Analyze the Arabidopsis mutants and clone the corresponding genes 6) Survey wild tomato species for growth characteristics at various P levels Background to the topic Hexose phosphorylating enzymes, the first enzymes of sugar metabolism, regulate key processes in plants suc

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Davisson, Vincent J., Anthony Pedley, Qingshou Chen, Matthew Bartolowits, and Raymond Fatig. Targeting PCNA Phosphorylation in Breast Cancer. Defense Technical Information Center, 2012. http://dx.doi.org/10.21236/ada586048.

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Davisson, Vincent J., Anthony Pedley, Qingshou Chen, Matthew Bartolowits, and Raymond Fatig. Targeting PCNA Phosphorylation in Breast Cancer. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada586063.

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Davisson, Vincent J., Anthony Pedley, Qingshou Chen, and Matthew Bartolowits. Targeting PCNA Phosphorylation in Breast Cancer. Defense Technical Information Center, 2011. http://dx.doi.org/10.21236/ada554228.

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Karen S. Browning. Protein Synthesis Initiation Factors: Phosphorylation and Regulation. Office of Scientific and Technical Information (OSTI), 2009. http://dx.doi.org/10.2172/956983.

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Dickman, Martin B., and Oded Yarden. Role of Phosphorylation in Fungal Spore Germination. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568761.bard.

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Spore germination is a common and fundamental event in fungal development and in many instances an essential phase of fungal infection and dissemination. Spore germination is also critical for hyperparasites to function as biocontrol agents as well as in fermentation proceses. Our common objective is to understand the mechanisms which regulated spore germination and identify factors involved in pathogenicity related prepenetration development. Our approach is to exploit the overall similarity among filamentous fungi using both a plant pathogen (Colletotricum trifolii) and a model system that i

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Greengard, P. Role of Protein Phosphorylation in Regulation of Bioreactivity. Defense Technical Information Center, 1985. http://dx.doi.org/10.21236/ada158875.

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Vasquez, Fancisca. Regulation of the Tumor Suppressor Protein PTEN by Phosphorylation. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada398955.

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Vazquez, Francisca. Regulation of the Tumor Suppressor Protein PTEN by Phosphorylation. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada392383.

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