Publications

• 1. Sweeney N
  2. Kim TY
  3. Morrison CT
  4. Li L
  5. Acosta D
  6. Liang J
  7. Datla NV
  8. Fitzgerald JA
  9. Huang H
  10. Liu X
  11. Tan GH
  12. Wu M
  13. Karelina K
  14. Bray CE
  15. Weil ZM
  16. Scharre DW
  17. Serrano GE
  18. Saito T
  19. Saido TC
  20. Beach TG
  21. Kokiko-Cochran ON
  22. Godbout JP
  23. Johnson GVW
  24. Fu H
  Neuronal BAG3 attenuates tau hyperphosphorylation, synaptic dysfunction, and cognitive deficits induced by traumatic brain injury via the regulation of autophagy-lysosome pathway.; Acta neuropathologica; Vol 148(1), pp. 52. 2024 Oct 11.
• 1. Isei MO
  2. Crockett M
  3. Chen E
  4. Rodwell-Bullock J
  5. Caroll T
  6. Girardi PA
  7. Nehrke K
  8. Johnson GV
  Tau phosphorylation suppresses oxidative stress-induced mitophagy via FKBP8 receptor modulation.; bioRxiv : the preprint server for biology. 2024 Jul 09.
• 1. Emerson J
  2. Delgado T
  3. Hong M
  4. Keillor JW
  5. Johnson GV
  Stabilizing transglutaminase 2 in the open conformation results in reactive astrocytes being more neurosupportive.; bioRxiv : the preprint server for biology. 2024 Apr 19.
• 1. Olesen MA
  2. Pradenas E
  3. Villavicencio-Tejo F
  4. Porter GA
  5. Johnson GVW
  6. Quintanilla RA
  Mitochondria-tau association promotes cognitive decline and hippocampal bioenergetic deficits during the aging.; Free radical biology & medicine. 2024 Mar 27.
• 1. Koren SA
  2. Ahmed Selim N
  3. De la Rosa L
  4. Horn J
  5. Farooqi MA
  6. Wei AY
  7. Müller-Eigner A
  8. Emerson J
  9. Johnson GVW
  10. Wojtovich AP
  All-optical spatiotemporal mapping of ROS dynamics across mitochondrial microdomains in situ.; Nature communications; Vol 14(1), pp. 6036. 2023 Sep 27.
• 1. Pérez MJ
  2. Ibarra-García-Padilla R
  3. Tang M
  4. Porter GA
  5. Johnson GVW
  6. Quintanilla RA
  Caspase-3 cleaved tau impairs mitochondrial function through the opening of the mitochondrial permeability transition pore.; Biochimica et biophysica acta. Molecular basis of disease. 2023 Sep 27.
• 1. Emerson J
  2. Delgado T
  3. Girardi P
  4. Johnson GVW
  Deletion of Transglutaminase 2 from Mouse Astrocytes Significantly Improves Their Ability to Promote Neurite Outgrowth on an Inhibitory Matrix.; International journal of molecular sciences; Vol 24(7). 2023 Mar 23.
• 1. Isei MO
  2. Girardi PA
  3. Rodwell-Bullock J
  4. Nehrke K
  5. Johnson GV
  Site-specific phosphorylation of tau impacts mitochondrial biology and response to stressors.; bioRxiv : the preprint server for biology. 2023 Feb 19.
• 1. Lin H
  2. Sandkuhler S
  3. Dunlea C
  4. King DH
  5. Johnson GVW
  BAG3 regulates the specificity of the recognition of specific MAPT species by NBR1 and SQSTM1.; bioRxiv : the preprint server for biology. 2023 Feb 09.
• 1. Emerson J
  2. Delgado T
  3. Girardi P
  4. Johnson GV
  Deletion of transglutaminase 2 from astrocytes significantly improves their ability to promote neurite outgrowth on an inhibitory matrix.; bioRxiv : the preprint server for biology. 2023 Feb 06.
• 1. Lin H
  2. Sandkuhler S
  3. Dunlea C
  4. Rodwell-Bullock J
  5. King DH
  6. Johnson GVW
  BAG3 regulates the specificity of the recognition of specific MAPT species by NBR1 and SQSTM1.; Autophagy. 2023 Jan 30.
• 1. Koren SA
  2. Ahmed Selim N
  3. De la Rosa L
  4. Horn J
  5. Farooqi MA
  6. Wei AY
  7. Müller-Eigner A
  8. Emerson J
  9. Johnson GVW
  10. Wojtovich AP
  Author Correction: All-optical spatiotemporal mapping of ROS dynamics across mitochondrial microdomains in situ.; Nature communications; Vol 14(1), pp. 8230. 2023 Jan 12.
• 1. Isei MO
  2. Girardi PA
  3. Rodwell-Bullock J
  4. Nehrke K
  5. Johnson GVW
  Site-specific phosphorylation of tau impacts mitochondrial function and response to stressors.; Journal of neurochemistry. 2023 Jan 03.
• 1. Guha S
  2. Cheng A
  3. Carroll T
  4. King D
  5. Koren SA
  6. Swords S
  7. Nehrke K
  8. Johnson GVW
  Selective Disruption of Drp1-Independent Mitophagy and Mitolysosome Trafficking by an Alzheimer's Disease Relevant Tau Modification in a Novel C. elegans Model.; Genetics. 2022 Aug 02.
• 1. Lin H
  2. Deaton CA
  3. Johnson GVW
  Commentary: BAG3 as a mediator of endosome function and tau clearance.; Neuroscience. 2022 May 09.
• 1. Lin H
  2. Tang M
  3. Ji C
  4. Girardi P
  5. Cvetojevic G
  6. Chen D
  7. Koren SA
  8. Johnson GVW
  BAG3 Regulation of RAB35 Mediates the Endosomal Sorting Complexes Required for Transport/Endolysosome Pathway and Tau Clearance.; Biological psychiatry. 2021 Nov 10.
• 1. Elahi A
  2. Emerson J
  3. Rudlong J
  4. Keillor JW
  5. Salois G
  6. Visca A
  7. Girardi P
  8. Johnson GVW
  9. Pröschel C
  Deletion or Inhibition of Astrocytic Transglutaminase 2 Promotes Functional Recovery after Spinal Cord Injury.; Cells; Vol 10(11). 2021 Oct 29.
• 1. Carroll T
  2. Guha S
  3. Nehrke K
  4. Johnson GVW
  Tau Post-Translational Modifications: Potentiators of Selective Vulnerability in Sporadic Alzheimer's Disease.; Biology; Vol 10(10). 2021 Oct 15.
• 1. Keillor JW
  2. Johnson GVW
  Transglutaminase 2 as a therapeutic target for neurological conditions.; Expert opinion on therapeutic targets. 2021 Oct 05.
• 1. Lin H
  2. Koren SA
  3. Cvetojevic G
  4. Girardi P
  5. Johnson GVW
  The role of BAG3 in health and disease: A "Magic BAG of Tricks".; Journal of cellular biochemistry. 2021 May 14.
• 1. Guha S
  2. Fischer S
  3. Cheng A
  4. Johnson GVW
  5. Nehrke K
  A T231E Mutant that Mimics Pathologic Phosphorylation of Tau in Alzheimer's disease Causes Activation of the Mitochondrial Unfolded Protein Response in C. elegans touch neurons.; microPublication biology; Vol 2020. 2020 Sep 09.
• 1. Guha S
  2. Johnson GVW
  3. Nehrke K
  The Crosstalk Between Pathological Tau Phosphorylation and Mitochondrial Dysfunction as a Key to Understanding and Treating Alzheimer's Disease.; Molecular neurobiology. 2020 Aug 26.
• 1. Guha S
  2. Fischer S
  3. Johnson GVW
  4. Nehrke K
  Tauopathy-associated tau modifications selectively impact neurodegeneration and mitophagy in a novel C. elegans single-copy transgenic model.; Molecular neurodegeneration; Vol 15(1). 2020 Jan 09.
• 1. Deaton CA
  2. Johnson GVW
  Presenilin 1 Regulates Membrane Homeostatic Pathways that are Dysregulated in Alzheimer's Disease.; Journal of Alzheimer's disease : JAD; Vol 77(3). 2020.
• 1. Rudlong J
  2. Cheng A
  3. Johnson GVW
  The role of transglutaminase 2 in mediating glial cell function and pathophysiology in the central nervous system.; Analytical biochemistry. 2019 Dec 19.
• 1. Ji C
  2. Tang M
  3. Zeidler C
  4. Höhfeld J
  5. Johnson GV
  BAG3 and SYNPO (synaptopodin) facilitate phospho-MAPT/Tau degradation via autophagy in neuronal processes.; Autophagy. 2019 Feb 11.
• 1. Liu C
  2. Luo R
  3. Wang W
  4. Peng Z
  5. Johnson GVW
  6. Kellems RE
  7. Xia Y
  Tissue transglutaminase-mediated AT1 receptor sensitization underlies pro-inflammatory cytokine LIGHT-induced hypertension.; American journal of hypertension. 2019 Feb 02.
• 1. Fu H
  2. Possenti A
  3. Freer R
  4. Nakano Y
  5. Villegas NCH
  6. Tang M
  7. Cauhy PVM
  8. Lassus BA
  9. Chen S
  10. Fowler SL
  11. Figueroa HY
  12. Huey ED
  13. Johnson GVW
  14. Vendruscolo M
  15. Duff KE
  A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology.; Nature neuroscience; Vol 22(1). 2019 Jan.
• 1. Tang M
  2. Harrison J
  3. Deaton CA
  4. Johnson GVW
  Tau Clearance Mechanisms.; Advances in experimental medicine and biology; Vol 1184. 2019.
• 1. Tapia-Rojas C
  2. Cabezas-Opazo F
  3. Deaton CA
  4. Vergara EH
  5. Johnson GVW
  6. Quintanilla RA
  It's all about tau.; Progress in neurobiology. 2018 Dec 31.
• 1. Ji C
  2. Tang M
  3. Harrison J
  4. Paciorkowski A
  5. Johnson GV
  Nuclear transglutaminase 2 directly regulates expression of cathepsin S in rat cortical neurons.; The European journal of neuroscience. 2018 Sep 21.
• 1. Quinn BR
  2. Yunes-Medina L
  3. Johnson GVW
  Transglutaminase 2: Friend or foe? The discordant role in neurons and astrocytes.; Journal of neuroscience research; Vol 96(7). 2018 Jul.
• 1. Monteagudo A
  2. Feola J
  3. Natola H
  4. Ji C
  5. Pröschel C
  6. Johnson GVW
  Depletion of astrocytic transglutaminase 2 improves injury outcomes.; Molecular and cellular neurosciences. 2018 Jun 30.
• 1. Yunes-Medina L
  2. Paciorkowski A
  3. Nuzbrokh Y
  4. Johnson GVW
  Depletion of transglutaminase 2 in neurons alters expression of extracellular matrix and signal transduction genes and compromises cell viability.; Molecular and cellular neurosciences; Vol 86. 2018 Jan.
• 1. Tang M
  2. Ji C
  3. Pallo S
  4. Rahman I
  5. Johnson GVW
  Nrf2 mediates the expression of BAG3 and autophagy cargo adaptor proteins and tau clearance in an age-dependent manner.; Neurobiology of aging; Vol 63. 2017 Dec 09.
• 1. Yunes-Medina L
  2. Feola J
  3. Johnson GVW
  Subcellular localization patterns of transglutaminase 2 in astrocytes and neurons are differentially altered by hypoxia.; Neuroreport. 2017 Sep 27.
• 1. Feola J
  2. Barton A
  3. Akbar A
  4. Keillor J
  5. Johnson GVW
  Transglutaminase 2 Modulation of NF-κB Signaling in Astrocytes is Independent of its Ability to Mediate Astrocytic Viability in Ischemic Injury.; Brain research. 2017 May 15.
• 1. Gundemir S
  2. Monteagudo A
  3. Akbar A
  4. Keillor JW
  5. Johnson GVW
  The complex role of transglutaminase 2 in glioblastoma proliferation.; Neuro-oncology; Vol 19(2). 2017 Feb 01.
• 1. Monteagudo A
  2. Ji C
  3. Akbar A
  4. Keillor JW
  5. Johnson GVW
  Inhibition or ablation of transglutaminase 2 impairs astrocyte migration.; Biochemical and biophysical research communications; Vol 482(4). 2017 Jan 22.
• 1. Ji C
  2. Tang M
  3. Johnson GVW
  Assessing the degradation of tau in primary neurons: The role of autophagy.; Methods in cell biology; Vol 141. 2017.
• 1. Lin CH
  2. Chen J
  3. Zhang Z
  4. Johnson GV
  5. Cooper AJ
  6. Feola J
  7. Bank A
  8. Shein J
  9. Ruotsalainen HJ
  10. Pihlajaniemi TA
  11. Goligorsky MS
  Endostatin and transglutaminase 2 are involved in fibrosis of the aging kidney.; Kidney international; Vol 89(6). 2016 Jun.
• 1. Kim S
  2. Choi KJ
  3. Cho SJ
  4. Yun SM
  5. Jeon JP
  6. Koh YH
  7. Song J
  8. Johnson GV
  9. Jo C
  Fisetin stimulates autophagic degradation of phosphorylated tau via the activation of TFEB and Nrf2 transcription factors.; Scientific reports; Vol 6. 2016 Apr 26.
• 1. Pallo SP
  2. DiMaio J
  3. Cook A
  4. Nilsson B
  5. Johnson GVW
  Mechanisms of tau and Aβ-induced excitotoxicity.; Brain research; Vol 1634. 2016 Mar 01.
• 1. Chesser AS
  2. Ganeshan V
  3. Yang J
  4. Johnson GV
  Epigallocatechin-3-gallate enhances clearance of phosphorylated tau in primary neurons.; Nutritional neuroscience; Vol 19(1). 2016.
• 1. Klionsky DJ
  2. Abdelmohsen K
  3. Abe A
  4. Abedin MJ
  5. Abeliovich H
  6. Acevedo Arozena A
  7. Adachi H
  8. Adams CM
  9. Adams PD
  10. Adeli K
  11. Adhihetty PJ
  12. Adler SG
  13. Agam G
  14. Agarwal R
  15. Aghi MK
  16. Agnello M
  17. Agostinis P
  18. Aguilar PV
  19. Aguirre-Ghiso J
  20. Airoldi EM
  21. Ait-Si-Ali S
  22. Akematsu T
  23. Akporiaye ET
  24. Al-Rubeai M
  25. Albaiceta GM
  26. Albanese C
  27. Albani D
  28. Albert ML
  29. Aldudo J
  30. Algül H
  31. Alirezaei M
  32. Alloza I
  33. Almasan A
  34. Almonte-Beceril M
  35. Alnemri ES
  36. Alonso C
  37. Altan-Bonnet N
  38. Altieri DC
  39. Alvarez S
  40. Alvarez-Erviti L
  41. Alves S
  42. Amadoro G
  43. Amano A
  44. Amantini C
  45. Ambrosio S
  46. Amelio I
  47. Amer AO
  48. Amessou M
  49. Amon A
  50. An Z
  51. Anania FA
  52. Andersen SU
  53. Andley UP
  54. Andreadi CK
  55. Andrieu-Abadie N
  56. Anel A
  57. Ann DK
  58. Anoopkumar-Dukie S
  59. Antonioli M
  60. Aoki H
  61. Apostolova N
  62. Aquila S
  63. Aquilano K
  64. Araki K
  65. Arama E
  66. Aranda A
  67. Araya J
  68. Arcaro A
  69. Arias E
  70. Arimoto H
  71. Ariosa AR
  72. Armstrong JL
  73. Arnould T
  74. Arsov I
  75. Asanuma K
  76. Askanas V
  77. Asselin E
  78. Atarashi R
  79. Atherton SS
  80. Atkin JD
  81. Attardi LD
  82. Auberger P
  83. Auburger G
  84. Aurelian L
  85. Autelli R
  86. Avagliano L
  87. Avantaggiati ML
  88. Avrahami L
  89. Awale S
  90. Azad N
  91. Bachetti T
  92. Backer JM
  93. Bae DH
  94. Bae JS
  95. Bae ON
  96. Bae SH
  97. Baehrecke EH
  98. Baek SH
  99. Baghdiguian S
  100. Bagniewska-Zadworna A
  101. Bai H
  102. Bai J
  103. Bai XY
  104. Bailly Y
  105. Balaji KN
  106. Balduini W
  107. Ballabio A
  108. Balzan R
  109. Banerjee R
  110. Bánhegyi G
  111. Bao H
  112. Barbeau B
  113. Barrachina MD
  114. Barreiro E
  115. Bartel B
  116. Bartolomé A
  117. Bassham DC
  118. Bassi MT
  119. Bast RC
  120. Basu A
  121. Batista MT
  122. Batoko H
  123. Battino M
  124. Bauckman K
  125. Baumgarner BL
  126. Bayer KU
  127. Beale R
  128. Beaulieu JF
  129. Beck GR
  130. Becker C
  131. Beckham JD
  132. Bédard PA
  133. Bednarski PJ
  134. Begley TJ
  135. Behl C
  136. Behrends C
  137. Behrens GM
  138. Behrns KE
  139. Bejarano E
  140. Belaid A
  141. Belleudi F
  142. Bénard G
  143. Berchem G
  144. Bergamaschi D
  145. Bergami M
  146. Berkhout B
  147. Berliocchi L
  148. Bernard A
  149. Bernard M
  150. Bernassola F
  151. Bertolotti A
  152. Bess AS
  153. Besteiro S
  154. Bettuzzi S
  155. Bhalla S
  156. Bhattacharyya S
  157. Bhutia SK
  158. Biagosch C
  159. Bianchi MW
  160. Biard-Piechaczyk M
  161. Billes V
  162. Bincoletto C
  163. Bingol B
  164. Bird SW
  165. Bitoun M
  166. Bjedov I
  167. Blackstone C
  168. Blanc L
  169. Blanco GA
  170. Blomhoff HK
  171. Boada-Romero E
  172. Böckler S
  173. Boes M
  174. Boesze-Battaglia K
  175. Boise LH
  176. Bolino A
  177. Boman A
  178. Bonaldo P
  179. Bordi M
  180. Bosch J
  181. Botana LM
  182. Botti J
  183. Bou G
  184. Bouché M
  185. Bouchecareilh M
  186. Boucher MJ
  187. Boulton ME
  188. Bouret SG
  189. Boya P
  190. Boyer-Guittaut M
  191. Bozhkov PV
  192. Brady N
  193. Braga VM
  194. Brancolini C
  195. Braus GH
  196. Bravo-San Pedro JM
  197. Brennan LA
  198. Bresnick EH
  199. Brest P
  200. Bridges D
  201. Bringer MA
  202. Brini M
  203. Brito GC
  204. Brodin B
  205. Brookes PS
  206. Brown EJ
  207. Brown K
  208. Broxmeyer HE
  209. Bruhat A
  210. Brum PC
  211. Brumell JH
  212. Brunetti-Pierri N
  213. Bryson-Richardson RJ
  214. Buch S
  215. Buchan AM
  216. Budak H
  217. Bulavin DV
  218. Bultman SJ
  219. Bultynck G
  220. Bumbasirevic V
  221. Burelle Y
  222. Burke RE
  223. Burmeister M
  224. Bütikofer P
  225. Caberlotto L
  226. Cadwell K
  227. Cahova M
  228. Cai D
  229. Cai J
  230. Cai Q
  231. Calatayud S
  232. Camougrand N
  233. Campanella M
  234. Campbell GR
  235. Campbell M
  236. Campello S
  237. Candau R
  238. Caniggia I
  239. Cantoni L
  240. Cao L
  241. Caplan AB
  242. Caraglia M
  243. Cardinali C
  244. Cardoso SM
  245. Carew JS
  246. Carleton LA
  247. Carlin CR
  248. Carloni S
  249. Carlsson SR
  250. Carmona-Gutierrez D
  251. Carneiro LA
  252. Carnevali O
  253. Carra S
  254. Carrier A
  255. Carroll B
  256. Casas C
  257. Casas J
  258. Cassinelli G
  259. Castets P
  260. Castro-Obregon S
  261. Cavallini G
  262. Ceccherini I
  263. Cecconi F
  264. Cederbaum AI
  265. Ceña V
  266. Cenci S
  267. Cerella C
  268. Cervia D
  269. Cetrullo S
  270. Chaachouay H
  271. Chae HJ
  272. Chagin AS
  273. Chai CY
  274. Chakrabarti G
  275. Chamilos G
  276. Chan EY
  277. Chan MT
  278. Chandra D
  279. Chandra P
  280. Chang CP
  281. Chang RC
  282. Chang TY
  283. Chatham JC
  284. Chatterjee S
  285. Chauhan S
  286. Che Y
  287. Cheetham ME
  288. Cheluvappa R
  289. Chen CJ
  290. Chen G
  291. Chen GC
  292. Chen G
  293. Chen H
  294. Chen JW
  295. Chen JK
  296. Chen M
  297. Chen M
  298. Chen P
  299. Chen Q
  300. Chen Q
  301. Chen SD
  302. Chen S
  303. Chen SS
  304. Chen W
  305. Chen WJ
  306. Chen WQ
  307. Chen W
  308. Chen X
  309. Chen YH
  310. Chen YG
  311. Chen Y
  312. Chen Y
  313. Chen Y
  314. Chen YJ
  315. Chen YQ
  316. Chen Y
  317. Chen Z
  318. Chen Z
  319. Cheng A
  320. Cheng CH
  321. Cheng H
  322. Cheong H
  323. Cherry S
  324. Chesney J
  325. Cheung CH
  326. Chevet E
  327. Chi HC
  328. Chi SG
  329. Chiacchiera F
  330. Chiang HL
  331. Chiarelli R
  332. Chiariello M
  333. Chieppa M
  334. Chin LS
  335. Chiong M
  336. Chiu GN
  337. Cho DH
  338. Cho SG
  339. Cho WC
  340. Cho YY
  341. Cho YS
  342. Choi AM
  343. Choi EJ
  344. Choi EK
  345. Choi J
  346. Choi ME
  347. Choi SI
  348. Chou TF
  349. Chouaib S
  350. Choubey D
  351. Choubey V
  352. Chow KC
  353. Chowdhury K
  354. Chu CT
  355. Chuang TH
  356. Chun T
  357. Chung H
  358. Chung T
  359. Chung YL
  360. Chwae YJ
  361. Cianfanelli V
  362. Ciarcia R
  363. Ciechomska IA
  364. Ciriolo MR
  365. Cirone M
  366. Claerhout S
  367. Clague MJ
  368. Clària J
  369. Clarke PG
  370. Clarke R
  371. Clementi E
  372. Cleyrat C
  373. Cnop M
  374. Coccia EM
  375. Cocco T
  376. Codogno P
  377. Coers J
  378. Cohen EE
  379. Colecchia D
  380. Coletto L
  381. Coll NS
  382. Colucci-Guyon E
  383. Comincini S
  384. Condello M
  385. Cook KL
  386. Coombs GH
  387. Cooper CD
  388. Cooper JM
  389. Coppens I
  390. Corasaniti MT
  391. Corazzari M
  392. Corbalan R
  393. Corcelle-Termeau E
  394. Cordero MD
  395. Corral-Ramos C
  396. Corti O
  397. Cossarizza A
  398. Costelli P
  399. Costes S
  400. Cotman SL
  401. Coto-Montes A
  402. Cottet S
  403. Couve E
  404. Covey LR
  405. Cowart LA
  406. Cox JS
  407. Coxon FP
  408. Coyne CB
  409. Cragg MS
  410. Craven RJ
  411. Crepaldi T
  412. Crespo JL
  413. Criollo A
  414. Crippa V
  415. Cruz MT
  416. Cuervo AM
  417. Cuezva JM
  418. Cui T
  419. Cutillas PR
  420. Czaja MJ
  421. Czyzyk-Krzeska MF
  422. Dagda RK
  423. Dahmen U
  424. Dai C
  425. Dai W
  426. Dai Y
  427. Dalby KN
  428. Dalla Valle L
  429. Dalmasso G
  430. D'Amelio M
  431. Damme M
  432. Darfeuille-Michaud A
  433. Dargemont C
  434. Darley-Usmar VM
  435. Dasarathy S
  436. Dasgupta B
  437. Dash S
  438. Dass CR
  439. Davey HM
  440. Davids LM
  441. Dávila D
  442. Davis RJ
  443. Dawson TM
  444. Dawson VL
  445. Daza P
  446. de Belleroche J
  447. de Figueiredo P
  448. de Figueiredo RC
  449. de la Fuente J
  450. De Martino L
  451. De Matteis A
  452. De Meyer GR
  453. De Milito A
  454. De Santi M
  455. de Souza W
  456. De Tata V
  457. De Zio D
  458. Debnath J
  459. Dechant R
  460. Decuypere JP
  461. Deegan S
  462. Dehay B
  463. Del Bello B
  464. Del Re DP
  465. Delage-Mourroux R
  466. Delbridge LM
  467. Deldicque L
  468. Delorme-Axford E
  469. Deng Y
  470. Dengjel J
  471. Denizot M
  472. Dent P
  473. Der CJ
  474. Deretic V
  475. Derrien B
  476. Deutsch E
  477. Devarenne TP
  478. Devenish RJ
  479. Di Bartolomeo S
  480. Di Daniele N
  481. Di Domenico F
  482. Di Nardo A
  483. Di Paola S
  484. Di Pietro A
  485. Di Renzo L
  486. DiAntonio A
  487. Díaz-Araya G
  488. Díaz-Laviada I
  489. Diaz-Meco MT
  490. Diaz-Nido J
  491. Dickey CA
  492. Dickson RC
  493. Diederich M
  494. Digard P
  495. Dikic I
  496. Dinesh-Kumar SP
  497. Ding C
  498. Ding WX
  499. Ding Z
  500. Dini L
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  3. Johnson GV
  4. Gustafson ME
  5. Ho SV
  Use of cyclohexanedimethanol as a nonflammable organic solvent for industrial scale reversed phase chromatography.; Journal of chromatography. A; Vol 1202(1). 2008 Aug 15.
• 1. Ding H
  2. Johnson GV
  The last tangle of tau.; Journal of Alzheimer's disease : JAD; Vol 14(4). 2008 Aug.
• 1. Filiano AJ
  2. Bailey CD
  3. Tucholski J
  4. Gundemir S
  5. Johnson GV
  Transglutaminase 2 protects against ischemic insult, interacts with HIF1beta, and attenuates HIF1 signaling.; FASEB journal : official publication of the Federation of American Societies for Experimental Biology; Vol 22(8). 2008 Aug.
• 1. Ding H
  2. Johnson GV
  New application of beta-galactosidase complementation to monitor tau self-association.; Journal of neurochemistry; Vol 106(4). 2008 Aug.
• 1. Boyle DM
  2. Johnson GV
  3. Heeren RA
  4. Shell RE
  5. Banerjee A
  6. Gustafson ME
  Evaluation of refolding conditions for a human recombinant fusion cytokine protein, promegapoietin-1a.; Biotechnology and applied biochemistry; Vol 49(Pt 1). 2008 Jan.
• 1. Chun W
  2. Waldo GS
  3. 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; Vol 103(6). 2007 Dec.
• 1. Mookherjee P
  2. Quintanilla R
  3. Roh MS
  4. Zmijewska AA
  5. Jope RS
  6. Johnson GV
  Mitochondrial-targeted active Akt protects SH-SY5Y neuroblastoma cells from staurosporine-induced apoptotic cell death.; Journal of cellular biochemistry; Vol 102(1). 2007 Sep 01.
• 1. Chun W
  2. 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; Vol 282(32). 2007 Aug 10.
• 1. Ruan Q
  2. Quintanilla RA
  3. Johnson GV
  Type 2 transglutaminase differentially modulates striatal cell death in the presence of wild type or mutant huntingtin.; Journal of neurochemistry; Vol 102(1). 2007 Jul.
• 1. Hunter JM
  2. Lesort M
  3. Johnson GV
  Ubiquitin-proteasome system alterations in a striatal cell model of Huntington's disease.; Journal of neuroscience research; Vol 85(8). 2007 Jun.
• 1. Johnson GV
  2. Barton LL
  Inhibition of iron deficiency stress response in cucumber by rare earth elements.; Plant physiology and biochemistry : PPB; Vol 45(5). 2007 May.