Surachai Supattapone - Publications

Affiliations: 
Biochemistry Dartmouth College, Hanover, NH, United States 
Area:
Biochemistry

92 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2021 Chidawanyika T, Chakrabarti R, Beauchemin KS, Higgs HN, Supattapone S. SEC24A facilitates colocalization and calcium flux between endoplasmic reticulum and mitochondria. Journal of Cell Science. PMID 33622772 DOI: 10.1242/jcs.249276  1
2020 Burke CM, Mark KMK, Walsh DJ, Noble GP, Steele AD, Diack AB, Manson JC, Watts JC, Supattapone S. Identification of a homology-independent linchpin domain controlling mouse and bank vole prion protein conversion. Plos Pathogens. 16: e1008875. PMID 32898162 DOI: 10.1371/journal.ppat.1008875  1
2020 Chidawanyika T, Mark KMK, Supattapone S. A Genome-Wide CRISPR/Cas9 Screen Reveals that Riboflavin Regulates Hydrogen Peroxide Entry into HAP1 Cells. Mbio. 11. PMID 32788383 DOI: 10.1128/mBio.01704-20  1
2020 Burke CM, Mark KMK, Kun J, Beauchemin KS, Supattapone S. Emergence of prions selectively resistant to combination drug therapy. Plos Pathogens. 16: e1008581. PMID 32421750 DOI: 10.1371/journal.ppat.1008581  0.48
2020 Burke CM, Walsh DJ, Mark KMK, Deleault NR, Nishina KA, Agrimi U, Di Bari MA, Supattapone S. Cofactor and glycosylation preferences for In Vitro prion conversion are predominantly determined by strain conformation. Plos Pathogens. 16: e1008495. PMID 32294141 DOI: 10.1371/journal.ppat.1008495  1
2019 Gunther EC, Smith LM, Kostylev MA, Cox TO, Kaufman AC, Lee S, Folta-Stogniew E, Maynard GD, Um JW, Stagi M, Heiss JK, Stoner A, Noble GP, Takahashi H, Haas LT, ... ... Supattapone S, et al. Rescue of Transgenic Alzheimer's Pathophysiology by Polymeric Cellular Prion Protein Antagonists. Cell Reports. 26: 1368. PMID 30699361 DOI: 10.1016/j.celrep.2019.01.064  1
2019 Gunther EC, Smith LM, Kostylev MA, Cox TO, Kaufman AC, Lee S, Folta-Stogniew E, Maynard GD, Um JW, Stagi M, Heiss JK, Stoner A, Noble GP, Takahashi H, Haas LT, ... ... Supattapone S, et al. Rescue of Transgenic Alzheimer's Pathophysiology by Polymeric Cellular Prion Protein Antagonists. Cell Reports. 26: 145-158.e8. PMID 30605671 DOI: 10.1016/j.celrep.2018.12.021  1
2018 Chidawanyika T, Sergison E, Cole M, Mark K, Supattapone S. SEC24A identified as an essential mediator of thapsigargin-induced cell death in a genome-wide CRISPR/Cas9 screen. Cell Death Discovery. 4: 115. PMID 30588337 DOI: 10.1038/s41420-018-0135-5  1
2018 Zhao Y, Zurawel AA, Jenkins NP, Duennwald ML, Cheng C, Kettenbach AN, Supattapone S. Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species. Scientific Reports. 8: 9554. PMID 29934597 DOI: 10.1038/s41598-018-27900-5  1
2016 Zurawel AA, Kabeche R, DiGregorio SE, Deng L, Menon KM, Opalko H, Duennwald ML, Moseley JB, Supattapone S. CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins. Mbio. 7. PMID 27677791 DOI: 10.1128/mBio.01367-16  1
2016 Noble GP, Dolph PJ, Supattapone S. Interallelic Transcriptional Enhancement as an In Vivo Measure of Transvection in Drosophila melanogaster. G3 (Bethesda, Md.). PMID 27489208 DOI: 10.1534/g3.116.032300  1
2015 Noble GP, Supattapone S. Dissociation of recombinant prion autocatalysis from infectivity. Prion. 9: 405-11. PMID 26645356 DOI: 10.1080/19336896.2015.1123843  1
2015 Supattapone S. Expanding the prion disease repertoire. Proceedings of the National Academy of Sciences of the United States of America. 112: 11748-9. PMID 26330608 DOI: 10.1073/pnas.1515143112  1
2015 Noble GP, Wang DW, Walsh DJ, Barone JR, Miller MB, Nishina KA, Li S, Supattapone S. A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers. Plos Pathogens. 11: e1005017. PMID 26125623 DOI: 10.1371/journal.ppat.1005017  1
2015 Noble GP, Walsh DJ, Miller MB, Jackson WS, Supattapone S. Requirements for mutant and wild-type prion protein misfolding in vitro. Biochemistry. 54: 1180-7. PMID 25584902 DOI: 10.1021/bi501495j  1
2014 Supattapone S. Synthesis of high titer infectious prions with cofactor molecules. The Journal of Biological Chemistry. 289: 19850-4. PMID 24860097 DOI: 10.1074/jbc.R113.511329  1
2014 Supattapone S. Elucidating the role of cofactors in mammalian prion propagation. Prion. 8: 100-5. PMID 24365977 DOI: 10.4161/pri.27501  1
2014 Zurawel AA, Walsh DJ, Fortier SM, Chidawanyika T, Sengupta S, Zilm K, Supattapone S. Prion nucleation site unmasked by transient interaction with phospholipid cofactor. Biochemistry. 53: 68-76. PMID 24328062 DOI: 10.1021/bi4014825  1
2013 Miller MB, Wang DW, Wang F, Noble GP, Ma J, Woods VL, Li S, Supattapone S. Cofactor molecules induce structural transformation during infectious prion formation. Structure (London, England : 1993). 21: 2061-8. PMID 24120764 DOI: 10.1016/j.str.2013.08.025  1
2013 Supattapone S, Miller MB. Cofactor involvement in prion propagation Prions and Diseases. 1: 93-105. DOI: 10.1007/978-1-4614-5305-5_7  1
2013 Kaufman AC, Strittmatter SM. Role of cellular prion protein in the amyloid-β oligomer Pathophysiology of alzheimer’s disease Prions and Diseases: Volume 1, Physiology and Pathophysiology. 35-48. DOI: 10.1007/978-1-4614-5305-5  0.6
2012 Supattapone S. Phosphatidylethanolamine as a prion cofactor: potential implications for disease pathogenesis. Prion. 6: 417-9. PMID 22895101 DOI: 10.4161/pri.21826  1
2012 Turnbaugh JA, Unterberger U, Saá P, Massignan T, Fluharty BR, Bowman FP, Miller MB, Supattapone S, Biasini E, Harris DA. The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc). The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 8817-30. PMID 22745483 DOI: 10.1523/JNEUROSCI.1103-12.2012  1
2012 Deleault NR, Walsh DJ, Piro JR, Wang F, Wang X, Ma J, Rees JR, Supattapone S. Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions. Proceedings of the National Academy of Sciences of the United States of America. 109: E1938-46. PMID 22711839 DOI: 10.1073/pnas.1206999109  1
2012 Deleault NR, Piro JR, Walsh DJ, Wang F, Ma J, Geoghegan JC, Supattapone S. Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids. Proceedings of the National Academy of Sciences of the United States of America. 109: 8546-51. PMID 22586108 DOI: 10.1073/pnas.1204498109  1
2012 Walsh DJ, Noble GP, Piro JR, Supattapone S. Non-reducing alkaline solubilization and rapid on-column refolding of recombinant prion protein. Preparative Biochemistry & Biotechnology. 42: 77-86. PMID 22239709 DOI: 10.1080/10826068.2011.564256  1
2011 Miller MB, Geoghegan JC, Supattapone S. Dissociation of infectivity from seeding ability in prions with alternate docking mechanism. Plos Pathogens. 7: e1002128. PMID 21779169 DOI: 10.1371/journal.ppat.1002128  1
2011 Piro JR, Wang F, Walsh DJ, Rees JR, Ma J, Supattapone S. Seeding specificity and ultrastructural characteristics of infectious recombinant prions. Biochemistry. 50: 7111-6. PMID 21776987 DOI: 10.1021/bi200786p  1
2011 Piro JR, Supattapone S. Photodegradation illuminates the role of polyanions in prion infectivity. Prion. 5: 49-51. PMID 21646861 DOI: 10.4161/pri.5.2.16155  1
2011 Piro JR, Harris BT, Supattapone S. In situ photodegradation of incorporated polyanion does not alter prion infectivity. Plos Pathogens. 7: e1002001. PMID 21304885 DOI: 10.1371/journal.ppat.1002001  1
2011 Miller MB, Supattapone S. Superparamagnetic nanoparticle capture of prions for amplification. Journal of Virology. 85: 2813-7. PMID 21228242 DOI: 10.1128/JVI.02451-10  1
2010 Deleault NR, Kascsak R, Geoghegan JC, Supattapone S. Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry. 49: 3928-34. PMID 20377181 DOI: 10.1021/bi100370b  1
2010 Supattapone S. Biochemistry. What makes a prion infectious? Science (New York, N.Y.). 327: 1091-2. PMID 20185716 DOI: 10.1126/science.1187790  1
2009 Supattapone S, Piro JR, Rees JR. Complex polyamines: unique prion disaggregating compounds. Cns & Neurological Disorders Drug Targets. 8: 323-8. PMID 19702574  1
2009 Geoghegan JC, Miller MB, Kwak AH, Harris BT, Supattapone S. Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor. Plos Pathogens. 5: e1000535. PMID 19649330 DOI: 10.1371/journal.ppat.1000535  1
2009 Piro JR, Harris BT, Nishina K, Soto C, Morales R, Rees JR, Supattapone S. Prion protein glycosylation is not required for strain-specific neurotropism. Journal of Virology. 83: 5321-8. PMID 19297485 DOI: 10.1128/JVI.02502-08  1
2008 Deleault AM, Deleault NR, Harris BT, Rees JR, Supattapone S. The effects of prion protein proteolysis and disaggregation on the strain properties of hamster scrapie. The Journal of General Virology. 89: 2642-50. PMID 18796735 DOI: 10.1099/vir.0.2008/002303-0  1
2008 Supattapone S, Deleault NR, Rees JR. Amplification of purified prions in vitro. Methods in Molecular Biology (Clifton, N.J.). 459: 117-30. PMID 18576152 DOI: 10.1007/978-1-59745-234-2_9  1
2008 Tribouillard-Tanvier D, Dos Reis S, Gug F, Voisset C, Béringue V, Sabate R, Kikovska E, Talarek N, Bach S, Huang C, Desban N, Saupe SJ, Supattapone S, Thuret JY, Chédin S, et al. Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs. Plos One. 3: e2174. PMID 18478094 DOI: 10.1371/journal.pone.0002174  1
2008 Deleault NR, Harris BT, Rees JR, Supattapone S. Formation of native prions from minimal components in vitro (Proceedings of the National Academy of Sciences of the United States of America (2007) 104, 23 (9741-9746) DOI: 10.1073/pnas.0702662104) Proceedings of the National Academy of Sciences of the United States of America. 105: 12636. DOI: 10.1073/pnas.0807173105  1
2008 Supattapone S, Rees JR. Transmissible spongiform encephalopathies Neurotropic Viral Infections. 251-262. DOI: 10.1017/CBO9780511541728.017  1
2008 Gavin BA, Dolph MJ, Deleault NR, Geoghegan JC, Khurana V, Feany MB, Dolph PJ, Supattapone S. Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann-Straussler-Scheinker syndrome (Journal of Neuroscience (November 29, 2006) (12408-12414)) Journal of Neuroscience. 28: 1P.  1
2007 Geoghegan JC, Valdes PA, Orem NR, Deleault NR, Williamson RA, Harris BT, Supattapone S. Selective incorporation of polyanionic molecules into hamster prions. The Journal of Biological Chemistry. 282: 36341-53. PMID 17940287 DOI: 10.1074/jbc.M704447200  1
2007 Kurt TD, Perrott MR, Wilusz CJ, Wilusz J, Supattapone S, Telling GC, Zabel MD, Hoover EA. Efficient in vitro amplification of chronic wasting disease PrPRES. Journal of Virology. 81: 9605-8. PMID 17553879 DOI: 10.1128/JVI.00635-07  1
2007 Deleault NR, Harris BT, Rees JR, Supattapone S. Formation of native prions from minimal components in vitro. Proceedings of the National Academy of Sciences of the United States of America. 104: 9741-6. PMID 17535913 DOI: 10.1073/pnas.0702662104  1
2007 Nishina KA, Supattapone S. Immunodetection of glycophosphatidylinositol-anchored proteins following treatment with phospholipase C. Analytical Biochemistry. 363: 318-20. PMID 17321480 DOI: 10.1016/j.ab.2007.01.032  1
2007 Giles K, Supattapone S, Peretz D, Glidden DV, Baron H, Prusiner SB. Disinfection of prions Acs Symposium Series. 967: 52-74.  1
2006 Gavin BA, Dolph MJ, Deleault NR, Geoghegan JC, Khurana V, Feany MB, Dolph PJ, Supattapone S. Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann-Sträussler-Scheinker syndrome. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 26: 12408-14. PMID 17135402 DOI: 10.1523/JNEUROSCI.3372-06.2006  1
2006 Nishina KA, Deleault NR, Mahal SP, Baskakov I, Luhrs T, Riek R, Supattapone S. The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry. 45: 14129-39. PMID 17115708 DOI: 10.1021/bi061526k  1
2006 Supattapone S, Rees JR. Which criteria best support the diagnosis of VV1 sporadic Creutzfeldt-Jakob disease? Nature Clinical Practice. Neurology. 2: 296-7. PMID 16932568 DOI: 10.1038/ncpneuro0192  1
2006 Saupe SJ, Supattapone S. What makes a good prion? Conference on Prion Biology. Embo Reports. 7: 254-8. PMID 16485026 DOI: 10.1038/sj.embor.7400642  1
2006 Supattapone S, Geoghegan JC, Rees JR. On the horizon: a blood test for prions. Trends in Microbiology. 14: 149-51. PMID 16483780 DOI: 10.1016/j.tim.2006.02.001  1
2006 Orem NR, Geoghegan JC, Deleault NR, Kascsak R, Supattapone S. Copper (II) ions potently inhibit purified PrPres amplification. Journal of Neurochemistry. 96: 1409-15. PMID 16417569 DOI: 10.1111/j.1471-4159.2006.03650.x  1
2006 Peretz D, Supattapone S, Giles K, Vergara J, Freyman Y, Lessard P, Safar JG, Glidden DV, McCulloch C, Nguyen HO, Scott M, Dearmond SJ, Prusiner SB. Inactivation of prions by acidic sodium dodecyl sulfate. Journal of Virology. 80: 322-31. PMID 16352557 DOI: 10.1128/JVI.80.1.322-331.2006  1
2005 Deleault NR, Geoghegan JC, Nishina K, Kascsak R, Williamson RA, Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. The Journal of Biological Chemistry. 280: 26873-9. PMID 15917229 DOI: 10.1074/jbc.M503973200  1
2004 Nishina K, Jenks S, Supattapone S. Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity. The Journal of Biological Chemistry. 279: 40788-94. PMID 15262998 DOI: 10.1074/jbc.M406548200  1
2004 Supattapone S. Prion protein conversion in vitro. Journal of Molecular Medicine (Berlin, Germany). 82: 348-56. PMID 15014886 DOI: 10.1007/s00109-004-0534-3  1
2004 Nishina K, Deleault NR, Lucassen RW, Supattapone S. In vitro prion protein conversion in detergent-solubilized membranes. Biochemistry. 43: 2613-21. PMID 14992599 DOI: 10.1021/bi035889l  1
2003 Deleault NR, Lucassen RW, Supattapone S. RNA molecules stimulate prion protein conversion. Nature. 425: 717-20. PMID 14562104 DOI: 10.1038/nature01979  1
2003 Deleault NR, Dolph PJ, Feany MB, Cook ME, Nishina K, Harris DA, Supattapone S. Post-transcriptional suppression of pathogenic prion protein expression in Drosophila neurons. Journal of Neurochemistry. 85: 1614-23. PMID 12787080 DOI: 10.1046/j.1471-4159.2003.01819.x  1
2003 Lucassen R, Nishina K, Supattapone S. In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups. Biochemistry. 42: 4127-35. PMID 12680767 DOI: 10.1021/bi027218d  1
2002 Supattapone S, Nishina K, Rees JR. Pharmacological approaches to prion research. Biochemical Pharmacology. 63: 1383-8. PMID 11996878 DOI: 10.1016/S0006-2952(02)00874-2  1
2002 Wille H, Michelitsch MD, Guenebaut V, Supattapone S, Serban A, Cohen FE, Agard DA, Prusiner SB. Structural studies of the scrapie prion protein by electron crystallography. Proceedings of the National Academy of Sciences of the United States of America. 99: 3563-8. PMID 11891310 DOI: 10.1073/pnas.052703499  1
2001 Supattapone S, Bouzamondo E, Ball HL, Wille H, Nguyen HO, Cohen FE, DeArmond SJ, Prusiner SB, Scott M. A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice. Molecular and Cellular Biology. 21: 2608-16. PMID 11259607 DOI: 10.1128/MCB.21.7.2608-2616.2001  1
2001 Supattapone S, Wille H, Uyechi L, Safar J, Tremblay P, Szoka FC, Cohen FE, Prusiner SB, Scott MR. Branched polyamines cure prion-infected neuroblastoma cells. Journal of Virology. 75: 3453-61. PMID 11238871 DOI: 10.1128/JVI.75.7.3453-3461.2001  1
2001 Supattapone S, Muramoto T, Legname G, Mehlhorn I, Cohen FE, DeArmond SJ, Prusiner SB, Scott MR. Identification of two prion protein regions that modify scrapie incubation time. Journal of Virology. 75: 1408-13. PMID 11152514 DOI: 10.1128/JVI.75.3.1408-1413.2001  1
2000 Scott MR, Supattapone S, Nguyen HO, DeArmond SJ, Prusiner SB. Transgenic models of prion disease. Archives of Virology. Supplementum. 113-24. PMID 11214913  1
2000 Supattapone S, Nguyen HO, Muramoto T, Cohen FE, DeArmond SJ, Prusiner SB, Scott M. Affinity-tagged miniprion derivatives spontaneously adopt protease-resistant conformations. Journal of Virology. 74: 11928-34. PMID 11090193 DOI: 10.1128/JVI.74.24.11928-11934.2000  1
1999 Supattapone S, Nguyen HO, Cohen FE, Prusiner SB, Scott MR. Elimination of prions by branched polyamines and implications for therapeutics. Proceedings of the National Academy of Sciences of the United States of America. 96: 14529-34. PMID 10588739 DOI: 10.1073/pnas.96.25.14529  1
1999 Supattapone S, Bosque P, Muramoto T, Wille H, Aagaard C, Peretz D, Nguyen HO, Heinrich C, Torchia M, Safar J, Cohen FE, DeArmond SJ, Prusiner SB, Scott M. Prion protein of 106 residues creates an artifical transmission barrier for prion replication in transgenic mice. Cell. 96: 869-78. PMID 10102274  1
1991 Supattapone S, Ashley CC. Endothelin Opens Potassium Channels in Glial Cells. The European Journal of Neuroscience. 3: 349-355. PMID 12106193  1
1991 Supattapone S, Ashley CC. Endothelin increases rubidium uptake through calcium-activated potassium channels in C6 glioma cells. Annals of the New York Academy of Sciences. 633: 597-8. PMID 1789589  1
1990 Mourey RJ, Verma A, Supattapone S, Snyder SH. Purification and characterization of the inositol 1,4,5- trisphosphate receptor protein from rat vas deferens. The Biochemical Journal. 272: 383-9. PMID 2176461 DOI: 10.1042/BJ2720383  1
1990 Satoh T, Ross CA, Villa A, Supattapone S, Pozzan T, Snyder SH, Meldolesi J. The inositol 1,4,5,-trisphosphate receptor in cerebellar Purkinje cells: quantitative immunogold labeling reveals concentration in an ER subcompartment. The Journal of Cell Biology. 111: 615-24. PMID 2166053 DOI: 10.1083/jcb.111.2.615  1
1990 Theibert AB, Supattapone S, Ferris CD, Danoff SK, Evans RK, Snyder SH. Solubilization and separation of inositol 1,3,4,5-tetrakisphosphate- and inositol 1,4,5-trisphosphate-binding proteins and metabolizing enzymes in rat brain. The Biochemical Journal. 267: 441-5. PMID 2159282 DOI: 10.1042/BJ2670441  1
1990 Supattapone S, Simpson AW, Ashley CC. Endothelin causes a free calcium rise in rat astrocytes. Advances in Second Messenger and Phosphoprotein Research. 24: 429-33. PMID 2119649  1
1990 Verma A, Ross CA, Verma D, Supattapone S, Snyder SH. Rat brain endoplasmic reticulum calcium pools are anatomically and functionally segregated. Cell Regulation. 1: 781-90. PMID 1966012 DOI: 10.1091/MBC.1.10.781  1
1989 Supattapone S, Simpson AW, Ashley CC. Free calcium rise and mitogenesis in glial cells caused by endothelin. Biochemical and Biophysical Research Communications. 165: 1115-22. PMID 2692560 DOI: 10.1016/0006-291X(89)92718-6  1
1989 Ferris CD, Huganir RL, Supattapone S, Snyder SH. Purified inositol 1,4,5-trisphosphate receptor mediates calcium flux in reconstituted lipid vesicles. Nature. 342: 87-9. PMID 2554143 DOI: 10.1038/342087a0  1
1989 Snyder SH, Supattapone S. Isolation and functional characterization of an inositol trisphosphate receptor from brain Cell Calcium. 10: 337-342. PMID 2548727 DOI: 10.1016/0143-4160(89)90059-6  1
1989 Blackstone CD, Supattapone S, Snyder SH. Inositolphospholipid-linked glutamate receptors mediate cerebellar parallel-fiber-Purkinje-cell synaptic transmission Proceedings of the National Academy of Sciences of the United States of America. 86: 4316-4320. PMID 2542969 DOI: 10.1073/PNAS.86.11.4316  1
1989 Ross CA, Meldolesi J, Milner TA, Satoh T, Supattapone S, Snyder SH. Inositol 1,4,5-trisphosphate receptor localized to endoplasmic reticulum in cerebellar Purkinje neurons. Nature. 339: 468-70. PMID 2542801 DOI: 10.1038/339468a0  1
1988 Supattapone S, Strittmatter SM, Fricker LD, Snyder SH. Characterization of a neutral, divalent cation-sensitive endopeptidase: a possible role in neuropeptide processing. Brain Research. 427: 173-81. PMID 3382941 DOI: 10.1016/0169-328X(88)90063-0  1
1988 Danoff SK, Supattapone S, Snyder SH. Characterization of a membrane protein from brain mediating the inhibition of inositol 1,4,5-trisphosphate receptor binding by calcium Biochemical Journal. 254: 701-705. PMID 2848495 DOI: 10.1042/BJ2540701  1
1988 Supattapone S, Danoff SK, Theibert A, Joseph SK, Steiner J, Snyder SH. Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium Proceedings of the National Academy of Sciences of the United States of America. 85: 8747-8750. PMID 2847175 DOI: 10.1073/PNAS.85.22.8747  1
1988 Snyder SH, Supattapone S, Danoff S, Worley PF, Baraban JM. The inositol trisphosphate receptor: a potpourri of second-messenger regulation. Cellular and Molecular Neurobiology. 8: 1-5. PMID 2841024 DOI: 10.1007/BF00712905  1
1988 Supattapone S, Worley PF, Baraban JM, Snyder SH. Solubilization, purification, and characterization of an inositol trisphosphate receptor. The Journal of Biological Chemistry. 263: 1530-4. PMID 2826483  1
1987 Costa E, Mocchetti I, Supattapone S, Snyder SH. Opioid peptide biosynthesis: Enzymatic selectivity and regulation mechanisms Faseb Journal. 1: 16-21. PMID 3111927 DOI: 10.1096/fasebj.1.1.3111927  1
1987 Worley PF, Baraban JM, Supattapone S, Wilson VS, Snyder SH. Characterization of inositol trisphosphate receptor binding in brain. Regulation by pH and calcium. The Journal of Biological Chemistry. 262: 12132-6. PMID 3040730  1
1987 Theibert AB, Supattapone S, Worley PF, Baraban JM, Meek JL, Snyder SH. Demonstration of inositol 1,3,4,5-tetrakisphosphate receptor binding. Biochemical and Biophysical Research Communications. 148: 1283-9. PMID 2825681 DOI: 10.1016/S0006-291X(87)80272-3  1
1984 Supattapone S, Fricker LD, Snyder SH. Purification and Characterization of a Membrane‐Bound Enkephalin‐Forming Carboxypeptidase, “Enkephalin Convertase” Journal of Neurochemistry. 42: 1017-1023. PMID 6421996 DOI: 10.1111/j.1471-4159.1984.tb12705.x  1
1982 Fricker LD, Supattapone S, Snyder SH. Enkephalin convertase: A specific enkephalin synthesizing carboxypeptidase in adrenal chromaffin granules, brain, and pituitary gland Life Sciences. 31: 1841-1844. PMID 6818411 DOI: 10.1016/0024-3205(82)90224-7  1
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