| Year |
Citation |
Score |
| 2023 |
Isei MO, Girardi PA, Rodwell-Bullock J, Nehrke K, Johnson GV. Site-specific phosphorylation of tau impacts mitochondrial biology and response to stressors. Biorxiv : the Preprint Server For Biology. PMID 36824940 DOI: 10.1101/2023.02.19.529131 |
0.461 |
|
| 2019 |
Ji C, Tang M, Zeidler C, Höhfeld J, Johnson GV. BAG3 and SYNPO (synaptopodin) facilitate phospho-MAPT/Tau degradation via autophagy in neuronal processes. Autophagy. PMID 30744518 DOI: 10.1080/15548627.2019.1580096 |
0.472 |
|
| 2016 |
Kim S, Choi KJ, Cho SJ, Yun SM, Jeon JP, Koh YH, Song J, Johnson GV, Jo C. Fisetin stimulates autophagic degradation of phosphorylated tau via the activation of TFEB and Nrf2 transcription factors. Scientific Reports. 6: 24933. PMID 27112200 DOI: 10.1038/srep24933 |
0.502 |
|
| 2015 |
Pallo SP, DiMaio J, Cook A, Nilsson B, Johnson GV. Mechanisms of tau and Aβ-induced excitotoxicity. Brain Research. PMID 26731336 DOI: 10.1016/J.Brainres.2015.12.048 |
0.418 |
|
| 2015 |
Chesser AS, Ganeshan V, Yang J, Johnson GV. Epigallocatechin-3-gallate enhances clearance of phosphorylated tau in primary neurons. Nutritional Neuroscience. PMID 26207957 DOI: 10.1179/1476830515Y.0000000038 |
0.526 |
|
| 2015 |
Pallo SP, Johnson GV. Tau facilitates Aβ-induced loss of mitochondrial membrane potential independent of cytosolic calcium fluxes in mouse cortical neurons. Neuroscience Letters. 597: 32-7. PMID 25888814 DOI: 10.1016/j.neulet.2015.04.021 |
0.462 |
|
| 2015 |
Zare-Shahabadi A, Masliah E, Johnson GV, Rezaei N. Autophagy in Alzheimer's disease. Reviews in the Neurosciences. PMID 25870960 DOI: 10.1515/Revneuro-2014-0076 |
0.402 |
|
| 2015 |
Lei Z, Brizzee C, Johnson GV. BAG3 facilitates the clearance of endogenous tau in primary neurons. Neurobiology of Aging. 36: 241-8. PMID 25212465 DOI: 10.1016/j.neurobiolaging.2014.08.012 |
0.31 |
|
| 2014 |
Kim S, Lee D, Song JC, Cho SJ, Yun SM, Koh YH, Song J, Johnson GV, Jo C. NDP52 associates with phosphorylated tau in brains of an Alzheimer disease mouse model. Biochemical and Biophysical Research Communications. 454: 196-201. PMID 25450380 DOI: 10.1016/j.bbrc.2014.10.066 |
0.5 |
|
| 2014 |
Quintanilla RA, von Bernhardi R, Godoy JA, Inestrosa NC, Johnson GV. Phosphorylated tau potentiates Aβ-induced mitochondrial damage in mature neurons. Neurobiology of Disease. 71: 260-9. PMID 25134729 DOI: 10.1016/j.nbd.2014.08.016 |
0.453 |
|
| 2014 |
Jo C, Gundemir S, Pritchard S, Jin YN, Rahman I, Johnson GV. Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52. Nature Communications. 5: 3496. PMID 24667209 DOI: 10.1038/Ncomms4496 |
0.493 |
|
| 2014 |
Cho C, Kim S, Cho S, Choi K, Yun S, Koh YH, Johnson G, Park SI. Sulforaphane Promotes The Degradation Of Phosphorylated Tau Via The Induction Of Autophagy Alzheimers & Dementia. 10. DOI: 10.1016/J.Jalz.2014.05.691 |
0.503 |
|
| 2014 |
Chesser A, Lei Z, Johnson GV. P1-005: SELECTIVELY ENHANCING PATHOLOGICAL FORMS OF TAU VIA THE AUTOPHAGY PATHWAY Alzheimer's & Dementia. 10: P306-P306. DOI: 10.1016/j.jalz.2014.05.240 |
0.318 |
|
| 2013 |
Chesser AS, Pritchard SM, Johnson GV. Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease. Frontiers in Neurology. 4: 122. PMID 24027553 DOI: 10.3389/fneur.2013.00122 |
0.508 |
|
| 2012 |
Jin YN, Chen PC, Watson JA, Walters BJ, Phillips SE, Green K, Schmidt R, Wilson JA, Johnson GV, Roberson ED, Dobrunz LE, Wilson SM. Usp14 deficiency increases tau phosphorylation without altering tau degradation or causing tau-dependent deficits. Plos One. 7: e47884. PMID 23144711 DOI: 10.1371/Journal.Pone.0047884 |
0.553 |
|
| 2012 |
Quintanilla RA, Dolan PJ, Jin YN, Johnson GV. Truncated tau and Aβ cooperatively impair mitochondria in primary neurons. Neurobiology of Aging. 33: 619.e25-35. PMID 21450370 DOI: 10.1016/J.Neurobiolaging.2011.02.007 |
0.695 |
|
| 2011 |
Dolan PJ, Jin YN, Hwang W, Johnson GV. Decreases in valosin-containing protein result in increased levels of tau phosphorylated at Ser262/356. Febs Letters. 585: 3424-9. PMID 21983102 DOI: 10.1016/J.Febslet.2011.09.032 |
0.724 |
|
| 2011 |
Pritchard SM, Dolan PJ, Vitkus A, Johnson GV. The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics. Journal of Cellular and Molecular Medicine. 15: 1621-35. PMID 21348938 DOI: 10.1111/J.1582-4934.2011.01273.X |
0.718 |
|
| 2011 |
Chun W, Waldo GS, Johnson GV. Split GFP complementation assay for quantitative measurement of tau aggregation in situ. Methods in Molecular Biology (Clifton, N.J.). 670: 109-23. PMID 20967587 DOI: 10.1007/978-1-60761-744-0_9 |
0.385 |
|
| 2010 |
Dolan PJ, Johnson GV. The role of tau kinases in Alzheimer's disease. Current Opinion in Drug Discovery & Development. 13: 595-603. PMID 20812151 |
0.723 |
|
| 2010 |
Dolan PJ, Johnson GV. A caspase cleaved form of tau is preferentially degraded through the autophagy pathway. The Journal of Biological Chemistry. 285: 21978-87. PMID 20466727 DOI: 10.1074/jbc.M110.110940 |
0.734 |
|
| 2010 |
Filiano AJ, Tucholski J, Dolan PJ, Colak G, Johnson GV. Transglutaminase 2 protects against ischemic stroke. Neurobiology of Disease. 39: 334-43. PMID 20451610 DOI: 10.1016/J.Nbd.2010.04.018 |
0.601 |
|
| 2009 |
Quintanilla RA, Matthews-Roberson TA, Dolan PJ, Johnson GV. Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: implications for the pathogenesis of Alzheimer disease. The Journal of Biological Chemistry. 284: 18754-66. PMID 19389700 DOI: 10.1074/Jbc.M808908200 |
0.68 |
|
| 2008 |
Matthews-Roberson TA, Quintanilla RA, Ding H, Johnson GV. Immortalized cortical neurons expressing caspase-cleaved tau are sensitized to endoplasmic reticulum stress induced cell death. Brain Research. 1234: 206-12. PMID 18718455 DOI: 10.1016/J.Brainres.2008.07.111 |
0.362 |
|
| 2008 |
Ding H, Johnson GV. The last tangle of tau. Journal of Alzheimer's Disease : Jad. 14: 441-7. PMID 18688096 DOI: 10.3233/Jad-2008-14413 |
0.447 |
|
| 2008 |
Ding H, Dolan PJ, Johnson GV. Histone deacetylase 6 interacts with the microtubule-associated protein tau. Journal of Neurochemistry. 106: 2119-30. PMID 18636984 DOI: 10.1111/J.1471-4159.2008.05564.X |
0.698 |
|
| 2008 |
Ding H, Johnson GV. New application of beta-galactosidase complementation to monitor tau self-association. Journal of Neurochemistry. 106: 1545-51. PMID 18498442 DOI: 10.1111/J.1471-4159.2008.05496.X |
0.375 |
|
| 2007 |
Chun W, Waldo GS, Johnson GV. Split GFP complementation assay: a novel approach to quantitatively measure aggregation of tau in situ: effects of GSK3beta activation and caspase 3 cleavage. Journal of Neurochemistry. 103: 2529-39. PMID 17908237 DOI: 10.1111/J.1471-4159.2007.04941.X |
0.357 |
|
| 2007 |
Chun W, Johnson GV. Activation of glycogen synthase kinase 3beta promotes the intermolecular association of tau. The use of fluorescence resonance energy transfer microscopy. The Journal of Biological Chemistry. 282: 23410-7. PMID 17565981 DOI: 10.1074/Jbc.M703706200 |
0.423 |
|
| 2007 |
Ruan Q, Johnson GV. Transglutaminase 2 in neurodegenerative disorders. Frontiers in Bioscience : a Journal and Virtual Library. 12: 891-904. PMID 17127346 DOI: 10.2741/2111 |
0.332 |
|
| 2007 |
Chun W, Johnson GV. The role of tau phosphorylation and cleavage in neuronal cell death. Frontiers in Bioscience : a Journal and Virtual Library. 12: 733-56. PMID 17127334 DOI: 10.2741/2097 |
0.533 |
|
| 2006 |
Mi K, Johnson GV. The role of tau phosphorylation in the pathogenesis of Alzheimer's disease. Current Alzheimer Research. 3: 449-63. PMID 17168644 DOI: 10.2174/156720506779025279 |
0.506 |
|
| 2006 |
Clodfelder-Miller BJ, Zmijewska AA, Johnson GV, Jope RS. Tau is hyperphosphorylated at multiple sites in mouse brain in vivo after streptozotocin-induced insulin deficiency. Diabetes. 55: 3320-5. PMID 17130475 DOI: 10.2337/Db06-0485 |
0.438 |
|
| 2006 |
Johnson GV. Tau phosphorylation and proteolysis: insights and perspectives. Journal of Alzheimer's Disease : Jad. 9: 243-50. PMID 16914862 |
0.415 |
|
| 2006 |
Ding H, Matthews TA, Johnson GV. Site-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation. The Journal of Biological Chemistry. 281: 19107-14. PMID 16687396 DOI: 10.1074/Jbc.M511697200 |
0.451 |
|
| 2006 |
Mi K, Dolan PJ, Johnson GV. The low density lipoprotein receptor-related protein 6 interacts with glycogen synthase kinase 3 and attenuates activity. The Journal of Biological Chemistry. 281: 4787-94. PMID 16365045 DOI: 10.1074/Jbc.M508657200 |
0.642 |
|
| 2005 |
Matthews TA, Johnson GV. 14-3-3Zeta does not increase GSK3beta-mediated tau phosphorylation in cell culture models. Neuroscience Letters. 384: 211-6. PMID 15963640 DOI: 10.1016/J.Neulet.2005.04.101 |
0.45 |
|
| 2005 |
Stoothoff WH, Johnson GV. Tau phosphorylation: physiological and pathological consequences. Biochimica Et Biophysica Acta. 1739: 280-97. PMID 15615646 DOI: 10.1016/J.Bbadis.2004.06.017 |
0.526 |
|
| 2005 |
Stoothoff WH, Cho JH, McDonald RP, Johnson GV. FRAT-2 preferentially increases glycogen synthase kinase 3 beta-mediated phosphorylation of primed sites, which results in enhanced tau phosphorylation. The Journal of Biological Chemistry. 280: 270-6. PMID 15522877 DOI: 10.1074/Jbc.M410061200 |
0.305 |
|
| 2004 |
Johnson GV, Stoothoff WH. Tau phosphorylation in neuronal cell function and dysfunction. Journal of Cell Science. 117: 5721-9. PMID 15537830 DOI: 10.1242/Jcs.01558 |
0.548 |
|
| 2004 |
Cho JH, Johnson GV. Glycogen synthase kinase 3 beta induces caspase-cleaved tau aggregation in situ. The Journal of Biological Chemistry. 279: 54716-23. PMID 15494420 DOI: 10.1074/jbc.M403364200 |
0.42 |
|
| 2004 |
Jope RS, Johnson GV. The glamour and gloom of glycogen synthase kinase-3. Trends in Biochemical Sciences. 29: 95-102. PMID 15102436 DOI: 10.1016/J.Tibs.2003.12.004 |
0.329 |
|
| 2004 |
Shelton SB, Krishnamurthy P, Johnson GV. Effects of cyclin-dependent kinase-5 activity on apoptosis and tau phosphorylation in immortalized mouse brain cortical cells. Journal of Neuroscience Research. 76: 110-20. PMID 15048935 DOI: 10.1002/Jnr.20051 |
0.433 |
|
| 2004 |
Shelton SB, Johnson GV. Cyclin-dependent kinase-5 in neurodegeneration. Journal of Neurochemistry. 88: 1313-26. PMID 15009631 DOI: 10.1111/J.1471-4159.2003.02328.X |
0.325 |
|
| 2004 |
Cho JH, Johnson GV. Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules. Journal of Neurochemistry. 88: 349-58. PMID 14690523 |
0.444 |
|
| 2004 |
Krishnamurthy PK, Johnson GV. Mutant (R406W) human tau is hyperphosphorylated and does not efficiently bind microtubules in a neuronal cortical cell model. The Journal of Biological Chemistry. 279: 7893-900. PMID 14660557 DOI: 10.1074/Jbc.M311203200 |
0.464 |
|
| 2004 |
Johnson GV, Jenkins SM. Tau protein in normal and Alzheimer's disease brain. Journal of Alzheimer's Disease : Jad. 1: 307-28. PMID 12214128 DOI: 10.3233/JAD-1999-14-511 |
0.484 |
|
| 2003 |
Cho JH, Johnson GV. Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding. The Journal of Biological Chemistry. 278: 187-93. PMID 12409305 DOI: 10.1074/jbc.M206236200 |
0.411 |
|
| 2002 |
Johnson GV, Bailey CD. Tau, where are we now? Journal of Alzheimer's Disease : Jad. 4: 375-98. PMID 12446970 |
0.508 |
|
| 2002 |
Stoothoff WH, Bailey CD, Mi K, Lin SC, Johnson GV. Axin negatively affects tau phosphorylation by glycogen synthase kinase 3beta. Journal of Neurochemistry. 83: 904-13. PMID 12421363 DOI: 10.1046/J.1471-4159.2002.01197.X |
0.389 |
|
| 2002 |
Lesort M, Chun W, Tucholski J, Johnson GV. Does tissue transglutaminase play a role in Huntington's disease? Neurochemistry International. 40: 37-52. PMID 11738471 DOI: 10.1046/J.1471-4159.81.S1.20_8.X |
0.303 |
|
| 2001 |
Mookherjee P, Johnson GV. Tau phosphorylation during apoptosis of human SH-SY5Y neuroblastoma cells. Brain Research. 921: 31-43. PMID 11720709 DOI: 10.1016/S0006-8993(01)03074-8 |
0.461 |
|
| 2001 |
Grierson AJ, Johnson GV, Miller CC. Three different human tau isoforms and rat neurofilament light, middle and heavy chain proteins are cellular substrates for transglutaminase. Neuroscience Letters. 298: 9-12. PMID 11154823 DOI: 10.1016/S0304-3940(00)01714-6 |
0.439 |
|
| 2000 |
Zhang J, Johnson GV. Tau protein is hyperphosphorylated in a site-specific manner in apoptotic neuronal PC12 cells. Journal of Neurochemistry. 75: 2346-57. PMID 11080186 DOI: 10.1046/j.1471-4159.2000.0752346.x |
0.497 |
|
| 1999 |
Johnson GV, Hartigan JA. Tau protein in normal and Alzheimer's disease brain: an update. Journal of Alzheimer's Disease : Jad. 1: 329-51. PMID 12214129 DOI: 10.3233/Jad-1999-14-512 |
0.502 |
|
| 1999 |
Davis PK, Johnson GV. The microtubule binding of Tau and high molecular weight Tau in apoptotic PC12 cells is impaired because of altered phosphorylation. The Journal of Biological Chemistry. 274: 35686-92. PMID 10585448 DOI: 10.1074/jbc.274.50.35686 |
0.377 |
|
| 1999 |
Hartigan JA, Johnson GV. Transient increases in intracellular calcium result in prolonged site-selective increases in Tau phosphorylation through a glycogen synthase kinase 3beta-dependent pathway. The Journal of Biological Chemistry. 274: 21395-401. PMID 10409701 DOI: 10.1074/Jbc.274.30.21395 |
0.301 |
|
| 1999 |
Hensley K, Floyd RA, Zheng NY, Nael R, Robinson KA, Nguyen X, Pye QN, Stewart CA, Geddes J, Markesbery WR, Patel E, Johnson GV, Bing G. p38 kinase is activated in the Alzheimer's disease brain. Journal of Neurochemistry. 72: 2053-8. PMID 10217284 DOI: 10.1046/J.1471-4159.1999.0722053.X |
0.407 |
|
| 1998 |
Xie HQ, Johnson GV. Calcineurin inhibition prevents calpain-mediated proteolysis of tau in differentiated PC12 cells. Journal of Neuroscience Research. 53: 153-64. PMID 9671972 DOI: 10.1002/(SICI)1097-4547(19980715)53:2<153::AID-JNR4>3.0.CO;2-6 |
0.442 |
|
| 1998 |
Xie H, Litersky JM, Hartigan JA, Jope RS, Johnson GV. The interrelationship between selective tau phosphorylation and microtubule association. Brain Research. 798: 173-83. PMID 9666118 DOI: 10.1016/S0006-8993(98)00407-7 |
0.437 |
|
| 1997 |
Xie H, Johnson GV. Ceramide selectively decreases tau levels in differentiated PC12 cells through modulation of calpain I. Journal of Neurochemistry. 69: 1020-30. PMID 9282924 DOI: 10.1046/j.1471-4159.1997.69031020.x |
0.324 |
|
| 1997 |
Johnson GV, Seubert P, Cox TM, Motter R, Brown JP, Galasko D. The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments. Journal of Neurochemistry. 68: 430-3. PMID 8978756 DOI: 10.1046/j.1471-4159.1997.68010430.x |
0.462 |
|
| 1997 |
Arnold CS, Johnson GV, Cole RN, Dong DL, Lee M, Hart GW. The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine. The Journal of Biological Chemistry. 271: 28741-4. PMID 8910513 DOI: 10.1074/Jbc.271.46.28741 |
0.371 |
|
| 1996 |
Litersky JM, Johnson GV, Jakes R, Goedert M, Lee M, Seubert P. Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356. The Biochemical Journal. 316: 655-60. PMID 8687413 DOI: 10.1042/Bj3160655 |
0.384 |
|
| 1996 |
Fleming LM, Weisgraber KH, Strittmatter WJ, Troncoso JC, Johnson GV. Differential binding of apolipoprotein E isoforms to tau and other cytoskeletal proteins. Experimental Neurology. 138: 252-60. PMID 8620924 DOI: 10.1006/Exnr.1996.0064 |
0.391 |
|
| 1995 |
Guttmann RP, Erickson AC, Johnson GV. Tau self-association: stabilization with a chemical cross-linker and modulation by phosphorylation and oxidation state. Journal of Neurochemistry. 64: 1209-15. PMID 7861153 DOI: 10.1046/j.1471-4159.1995.64031209.x |
0.447 |
|
| 1995 |
Seubert P, Mawal-Dewan M, Barbour R, Jakes R, Goedert M, Johnson GV, Litersky JM, Schenk D, Lieberburg I, Trojanowski JQ. Detection of phosphorylated Ser262 in fetal tau, adult tau, and paired helical filament tau. The Journal of Biological Chemistry. 270: 18917-22. PMID 7642549 DOI: 10.1074/Jbc.270.32.18917 |
0.451 |
|
| 1995 |
Fleming LM, Johnson GV. Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP. The Biochemical Journal. 41-7. PMID 7619080 DOI: 10.1042/bj3090041 |
0.377 |
|
| 1995 |
Litersky JM, Johnson GV. Phosphorylation of tau in situ: inhibition of calcium-dependent proteolysis. Journal of Neurochemistry. 65: 903-11. PMID 7616252 DOI: 10.1046/j.1471-4159.1995.65020903.x |
0.417 |
|
| 1993 |
Erickson AC, Johnson GV. Metal (Fe3+) affinity chromatography: differential adsorption of tau phosphoproteins. Journal of Neuroscience Methods. 46: 245-9. PMID 8483317 DOI: 10.1016/0165-0270(93)90073-Z |
0.44 |
|
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