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Gail Johnson Lab

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Publications

    1. Olesen MA
    2. Villavicencio-Tejo F
    3. Johnson GVW
    4. Porter GA
    5. Quintanilla RA
    Cyclophilin D (CypD) ablation prevents neurodegenerative and cognitive damage induced by caspase-3 cleaved tau.; Free radical biology & medicine. 2025 Feb 27.
    1. Lin H
    2. Ramanan S
    3. Kaplan S
    4. King DH
    5. Bunn D
    6. Johnson GV
    One BAG doesn't fit all: the differences and similarities of BAG family members in mediating CNS homeostasis.; Biological psychiatry. 2025 Jan 08.
    1. Isei MO
    2. Crockett M
    3. Chen E
    4. Rodwell-Bullock J
    5. Carroll T
    6. Girardi PA
    7. Nehrke K
    8. Johnson GVW
    Tau phosphorylation suppresses oxidative stress-induced mitophagy via FKBP8 receptor modulation.; PloS one; Vol 20(1), pp. e0307358. 2025 Jan 03.
    1. Delgado T
    2. Emerson J
    3. Hong M
    4. Keillor JW
    5. Johnson GVW
    Pharmacological Inhibition of Astrocytic Transglutaminase 2 Facilitates the Expression of a Neurosupportive Astrocyte Reactive Phenotype in Association with Increased Histone Acetylation.; Biomolecules; Vol 14(12). 2024 Dec 13.
    1. Ganguly U
    2. Carroll T
    3. Nehrke K
    4. Johnson GVW
    Mitochondrial Quality Control in Alzheimer's Disease: Insights from Caenorhabditis elegans Models.; Antioxidants (Basel, Switzerland); Vol 13(11). 2024 Nov 01.
    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
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    232. Camougrand N
    233. Campanella M
    234. Campbell GR
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    237. Candau R
    238. Caniggia I
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    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
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    253. Carra S
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    330. Chiang HL
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    343. Choi EJ
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    354. Chu CT
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    358. Chung T
    359. Chung YL
    360. Chwae YJ
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    370. Clarke R
    371. Clementi E
    372. Cleyrat C
    373. Cnop M
    374. Coccia EM
    375. Cocco T
    376. Codogno P
    377. Coers J
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    380. Coletto L
    381. Coll NS
    382. Colucci-Guyon E
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    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
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    403. Couve E
    404. Covey LR
    405. Cowart LA
    406. Cox JS
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    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
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    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
    501. Distler JH
    502. Diwan A
    503. Djavaheri-Mergny M
    504. Dmytruk K
    505. Dobson RC
    506. Doetsch V
    507. Dokladny K
    508. Dokudovskaya S
    509. Donadelli M
    510. Dong XC
    511. Dong X
    512. Dong Z
    513. Donohue TM
    514. Doran KS
    515. D'Orazi G
    516. Dorn GW
    517. Dosenko V
    518. Dridi S
    519. Drucker L
    520. Du J
    521. Du LL
    522. Du L
    523. du Toit A
    524. Dua P
    525. Duan L
    526. Duann P
    527. Dubey VK
    528. Duchen MR
    529. Duchosal MA
    530. Duez H
    531. Dugail I
    532. Dumit VI
    533. Duncan MC
    534. Dunlop EA
    535. Dunn WA
    536. Dupont N
    537. Dupuis L
    538. Durán RV
    539. Durcan TM
    540. Duvezin-Caubet S
    541. Duvvuri U
    542. Eapen V
    543. Ebrahimi-Fakhari D
    544. Echard A
    545. Eckhart L
    546. Edelstein CL
    547. Edinger AL
    548. Eichinger L
    549. Eisenberg T
    550. Eisenberg-Lerner A
    551. Eissa NT
    552. El-Deiry WS
    553. El-Khoury V
    554. Elazar Z
    555. Eldar-Finkelman H
    556. Elliott CJ
    557. Emanuele E
    558. Emmenegger U
    559. Engedal N
    560. Engelbrecht AM
    561. Engelender S
    562. Enserink JM
    563. Erdmann R
    564. Erenpreisa J
    565. Eri R
    566. Eriksen JL
    567. Erman A
    568. Escalante R
    569. Eskelinen EL
    570. Espert L
    571. Esteban-Martínez L
    572. Evans TJ
    573. Fabri M
    574. Fabrias G
    575. Fabrizi C
    576. Facchiano A
    577. Færgeman NJ
    578. Faggioni A
    579. Fairlie WD
    580. Fan C
    581. Fan D
    582. Fan J
    583. Fang S
    584. Fanto M
    585. Fanzani A
    586. Farkas T
    587. Faure M
    588. Favier FB
    589. Fearnhead H
    590. Federici M
    591. Fei E
    592. Felizardo TC
    593. Feng H
    594. Feng Y
    595. Feng Y
    596. Ferguson TA
    597. Fernández ÁF
    598. Fernandez-Barrena MG
    599. Fernandez-Checa JC
    600. Fernández-López A
    601. Fernandez-Zapico ME
    602. Feron O
    603. Ferraro E
    604. Ferreira-Halder CV
    605. Fesus L
    606. Feuer R
    607. Fiesel FC
    608. Filippi-Chiela EC
    609. Filomeni G
    610. Fimia GM
    611. Fingert JH
    612. Finkbeiner S
    613. Finkel T
    614. Fiorito F
    615. Fisher PB
    616. Flajolet M
    617. Flamigni F
    618. Florey O
    619. Florio S
    620. Floto RA
    621. Folini M
    622. Follo C
    623. Fon EA
    624. Fornai F
    625. Fortunato F
    626. Fraldi A
    627. Franco R
    628. Francois A
    629. François A
    630. Frankel LB
    631. Fraser ID
    632. Frey N
    633. Freyssenet DG
    634. Frezza C
    635. Friedman SL
    636. Frigo DE
    637. Fu D
    638. Fuentes JM
    639. Fueyo J
    640. Fujitani Y
    641. Fujiwara Y
    642. Fujiya M
    643. Fukuda M
    644. Fulda S
    645. Fusco C
    646. Gabryel B
    647. Gaestel M
    648. Gailly P
    649. Gajewska M
    650. Galadari S
    651. Galili G
    652. Galindo I
    653. Galindo MF
    654. Galliciotti G
    655. Galluzzi L
    656. Galluzzi L
    657. Galy V
    658. Gammoh N
    659. Gandy S
    660. Ganesan AK
    661. Ganesan S
    662. Ganley IG
    663. Gannagé M
    664. Gao FB
    665. Gao F
    666. Gao JX
    667. García Nannig L
    668. García Véscovi E
    669. Garcia-Macía M
    670. Garcia-Ruiz C
    671. Garg AD
    672. Garg PK
    673. Gargini R
    674. Gassen NC
    675. Gatica D
    676. Gatti E
    677. Gavard J
    678. Gavathiotis E
    679. Ge L
    680. Ge P
    681. Ge S
    682. Gean PW
    683. Gelmetti V
    684. Genazzani AA
    685. Geng J
    686. Genschik P
    687. Gerner L
    688. Gestwicki JE
    689. Gewirtz DA
    690. Ghavami S
    691. Ghigo E
    692. Ghosh D
    693. Giammarioli AM
    694. Giampieri F
    695. Giampietri C
    696. Giatromanolaki A
    697. Gibbings DJ
    698. Gibellini L
    699. Gibson SB
    700. Ginet V
    701. Giordano A
    702. Giorgini F
    703. Giovannetti E
    704. Girardin SE
    705. Gispert S
    706. Giuliano S
    707. Gladson CL
    708. Glavic A
    709. Gleave M
    710. Godefroy N
    711. Gogal RM
    712. Gokulan K
    713. Goldman GH
    714. Goletti D
    715. Goligorsky MS
    716. Gomes AV
    717. Gomes LC
    718. Gomez H
    719. Gomez-Manzano C
    720. Gómez-Sánchez R
    721. Gonçalves DA
    722. Goncu E
    723. Gong Q
    724. Gongora C
    725. Gonzalez CB
    726. Gonzalez-Alegre P
    727. Gonzalez-Cabo P
    728. González-Polo RA
    729. Goping IS
    730. Gorbea C
    731. Gorbunov NV
    732. Goring DR
    733. Gorman AM
    734. Gorski SM
    735. Goruppi S
    736. Goto-Yamada S
    737. Gotor C
    738. Gottlieb RA
    739. Gozes I
    740. Gozuacik D
    741. Graba Y
    742. Graef M
    743. Granato GE
    744. Grant GD
    745. Grant S
    746. Gravina GL
    747. Green DR
    748. Greenhough A
    749. Greenwood MT
    750. Grimaldi B
    751. Gros F
    752. Grose C
    753. Groulx JF
    754. Gruber F
    755. Grumati P
    756. Grune T
    757. Guan JL
    758. Guan KL
    759. Guerra B
    760. Guillen C
    761. Gulshan K
    762. Gunst J
    763. Guo C
    764. Guo L
    765. Guo M
    766. Guo W
    767. Guo XG
    768. Gust AA
    769. Gustafsson ÅB
    770. Gutierrez E
    771. Gutierrez MG
    772. Gwak HS
    773. Haas A
    774. Haber JE
    775. Hadano S
    776. Hagedorn M
    777. Hahn DR
    778. Halayko AJ
    779. Hamacher-Brady A
    780. Hamada K
    781. Hamai A
    782. Hamann A
    783. Hamasaki M
    784. Hamer I
    785. Hamid Q
    786. Hammond EM
    787. Han F
    788. Han W
    789. Handa JT
    790. Hanover JA
    791. Hansen M
    792. Harada M
    793. Harhaji-Trajkovic L
    794. Harper JW
    795. Harrath AH
    796. Harris AL
    797. Harris J
    798. Hasler U
    799. Hasselblatt P
    800. Hasui K
    801. Hawley RG
    802. Hawley TS
    803. He C
    804. He CY
    805. He F
    806. He G
    807. He RR
    808. He XH
    809. He YW
    810. He YY
    811. Heath JK
    812. Hébert MJ
    813. Heinzen RA
    814. Helgason GV
    815. Hensel M
    816. Henske EP
    817. Her C
    818. Herman PK
    819. Hernández A
    820. Hernandez C
    821. Hernández-Tiedra S
    822. Hetz C
    823. Hiesinger PR
    824. Higaki K
    825. Hilfiker S
    826. Hill BG
    827. Hill JA
    828. Hill WD
    829. Hino K
    830. Hofius D
    831. Hofman P
    832. Höglinger GU
    833. Höhfeld J
    834. Holz MK
    835. Hong Y
    836. Hood DA
    837. Hoozemans JJ
    838. Hoppe T
    839. Hsu C
    840. Hsu CY
    841. Hsu LC
    842. Hu D
    843. Hu G
    844. Hu HM
    845. Hu H
    846. Hu MC
    847. Hu YC
    848. Hu ZW
    849. Hua F
    850. Hua Y
    851. Huang C
    852. Huang HL
    853. Huang KH
    854. Huang KY
    855. Huang S
    856. Huang S
    857. Huang WP
    858. Huang YR
    859. Huang Y
    860. Huang Y
    861. Huber TB
    862. Huebbe P
    863. Huh WK
    864. Hulmi JJ
    865. Hur GM
    866. Hurley JH
    867. Husak Z
    868. Hussain SN
    869. Hussain S
    870. Hwang JJ
    871. Hwang S
    872. Hwang TI
    873. Ichihara A
    874. Imai Y
    875. Imbriano C
    876. Inomata M
    877. Into T
    878. Iovane V
    879. Iovanna JL
    880. Iozzo RV
    881. Ip NY
    882. Irazoqui JE
    883. Iribarren P
    884. Isaka Y
    885. Isakovic AJ
    886. Ischiropoulos H
    887. Isenberg JS
    888. Ishaq M
    889. Ishida H
    890. Ishii I
    891. Ishmael JE
    892. Isidoro C
    893. Isobe K
    894. Isono E
    895. Issazadeh-Navikas S
    896. Itahana K
    897. Itakura E
    898. Ivanov AI
    899. Iyer AK
    900. Izquierdo JM
    901. Izumi Y
    902. Izzo V
    903. Jäättelä M
    904. Jaber N
    905. Jackson DJ
    906. Jackson WT
    907. Jacob TG
    908. Jacques TS
    909. Jagannath C
    910. Jain A
    911. Jana NR
    912. Jang BK
    913. Jani A
    914. Janji B
    915. Jannig PR
    916. Jansson PJ
    917. Jean S
    918. Jendrach M
    919. Jeon JH
    920. Jessen N
    921. Jeung EB
    922. Jia K
    923. Jia L
    924. Jiang H
    925. Jiang H
    926. Jiang L
    927. Jiang T
    928. Jiang X
    929. Jiang X
    930. Jiang X
    931. Jiang Y
    932. Jiang Y
    933. Jiménez A
    934. Jin C
    935. Jin H
    936. Jin L
    937. Jin M
    938. Jin S
    939. Jinwal UK
    940. Jo EK
    941. Johansen T
    942. Johnson DE
    943. Johnson GV
    944. Johnson JD
    945. Jonasch E
    946. Jones C
    947. Joosten LA
    948. Jordan J
    949. Joseph AM
    950. Joseph B
    951. Joubert AM
    952. Ju D
    953. Ju J
    954. Juan HF
    955. Juenemann K
    956. Juhász G
    957. Jung HS
    958. Jung JU
    959. Jung YK
    960. Jungbluth H
    961. Justice MJ
    962. Jutten B
    963. Kaakoush NO
    964. Kaarniranta K
    965. Kaasik A
    966. Kabuta T
    967. Kaeffer B
    968. Kågedal K
    969. Kahana A
    970. Kajimura S
    971. Kakhlon O
    972. Kalia M
    973. Kalvakolanu DV
    974. Kamada Y
    975. Kambas K
    976. Kaminskyy VO
    977. Kampinga HH
    978. Kandouz M
    979. Kang C
    980. Kang R
    981. Kang TC
    982. Kanki T
    983. Kanneganti TD
    984. Kanno H
    985. Kanthasamy AG
    986. Kantorow M
    987. Kaparakis-Liaskos M
    988. Kapuy O
    989. Karantza V
    990. Karim MR
    991. Karmakar P
    992. Kaser A
    993. Kaushik S
    994. Kawula T
    995. Kaynar AM
    996. Ke PY
    997. Ke ZJ
    998. Kehrl JH
    999. Keller KE
    1000. Kemper JK
    1001. Kenworthy AK
    1002. Kepp O
    1003. Kern A
    1004. Kesari S
    1005. Kessel D
    1006. Ketteler R
    1007. Kettelhut Ido C
    1008. Khambu B
    1009. Khan MM
    1010. Khandelwal VK
    1011. Khare S
    1012. Kiang JG
    1013. Kiger AA
    1014. Kihara A
    1015. Kim AL
    1016. Kim CH
    1017. Kim DR
    1018. Kim DH
    1019. Kim EK
    1020. Kim HY
    1021. Kim HR
    1022. Kim JS
    1023. Kim JH
    1024. Kim JC
    1025. Kim JH
    1026. Kim KW
    1027. Kim MD
    1028. Kim MM
    1029. Kim PK
    1030. Kim SW
    1031. Kim SY
    1032. Kim YS
    1033. Kim Y
    1034. Kimchi A
    1035. Kimmelman AC
    1036. Kimura T
    1037. King JS
    1038. Kirkegaard K
    1039. Kirkin V
    1040. Kirshenbaum LA
    1041. Kishi S
    1042. Kitajima Y
    1043. Kitamoto K
    1044. Kitaoka Y
    1045. Kitazato K
    1046. Kley RA
    1047. Klimecki WT
    1048. Klinkenberg M
    1049. Klucken J
    1050. Knævelsrud H
    1051. Knecht E
    1052. Knuppertz L
    1053. Ko JL
    1054. Kobayashi S
    1055. Koch JC
    1056. Koechlin-Ramonatxo C
    1057. Koenig U
    1058. Koh YH
    1059. Köhler K
    1060. Kohlwein SD
    1061. Koike M
    1062. Komatsu M
    1063. Kominami E
    1064. Kong D
    1065. Kong HJ
    1066. Konstantakou EG
    1067. Kopp BT
    1068. Korcsmaros T
    1069. Korhonen L
    1070. Korolchuk VI
    1071. Koshkina NV
    1072. Kou Y
    1073. Koukourakis MI
    1074. Koumenis C
    1075. Kovács AL
    1076. Kovács T
    1077. Kovacs WJ
    1078. Koya D
    1079. Kraft C
    1080. Krainc D
    1081. Kramer H
    1082. Kravic-Stevovic T
    1083. Krek W
    1084. Kretz-Remy C
    1085. Krick R
    1086. Krishnamurthy M
    1087. Kriston-Vizi J
    1088. Kroemer G
    1089. Kruer MC
    1090. Kruger R
    1091. Ktistakis NT
    1092. Kuchitsu K
    1093. Kuhn C
    1094. Kumar AP
    1095. Kumar A
    1096. Kumar A
    1097. Kumar D
    1098. Kumar D
    1099. Kumar R
    1100. Kumar S
    1101. Kundu M
    1102. Kung HJ
    1103. Kuno A
    1104. Kuo SH
    1105. Kuret J
    1106. Kurz T
    1107. Kwok T
    1108. Kwon TK
    1109. Kwon YT
    1110. Kyrmizi I
    1111. La Spada AR
    1112. Lafont F
    1113. Lahm T
    1114. Lakkaraju A
    1115. Lam T
    1116. Lamark T
    1117. Lancel S
    1118. Landowski TH
    1119. Lane DJ
    1120. Lane JD
    1121. Lanzi C
    1122. Lapaquette P
    1123. Lapierre LR
    1124. Laporte J
    1125. Laukkarinen J
    1126. Laurie GW
    1127. Lavandero S
    1128. Lavie L
    1129. LaVoie MJ
    1130. Law BY
    1131. Law HK
    1132. Law KB
    1133. Layfield R
    1134. Lazo PA
    1135. Le Cam L
    1136. Le Roch KG
    1137. Le Stunff H
    1138. Leardkamolkarn V
    1139. Lecuit M
    1140. Lee BH
    1141. Lee CH
    1142. Lee EF
    1143. Lee GM
    1144. Lee HJ
    1145. Lee H
    1146. Lee JK
    1147. Lee J
    1148. Lee JH
    1149. Lee JH
    1150. Lee M
    1151. Lee MS
    1152. Lee PJ
    1153. Lee SW
    1154. Lee SJ
    1155. Lee SJ
    1156. Lee SY
    1157. Lee SH
    1158. Lee SS
    1159. Lee SJ
    1160. Lee S
    1161. Lee YR
    1162. Lee YJ
    1163. Lee YH
    1164. Leeuwenburgh C
    1165. Lefort S
    1166. Legouis R
    1167. Lei J
    1168. Lei QY
    1169. Leib DA
    1170. Leibowitz G
    1171. Lekli I
    1172. Lemaire SD
    1173. Lemasters JJ
    1174. Lemberg MK
    1175. Lemoine A
    1176. Leng S
    1177. Lenz G
    1178. Lenzi P
    1179. Lerman LO
    1180. Lettieri Barbato D
    1181. Leu JI
    1182. Leung HY
    1183. Levine B
    1184. Lewis PA
    1185. Lezoualc'h F
    1186. Li C
    1187. Li F
    1188. Li FJ
    1189. Li J
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    1191. Li L
    1192. Li M
    1193. Li M
    1194. Li Q
    1195. Li R
    1196. Li S
    1197. Li W
    1198. Li W
    1199. Li X
    1200. Li Y
    1201. Lian J
    1202. Liang C
    1203. Liang Q
    1204. Liao Y
    1205. Liberal J
    1206. Liberski PP
    1207. Lie P
    1208. Lieberman AP
    1209. Lim HJ
    1210. Lim KL
    1211. Lim K
    1212. Lima RT
    1213. Lin CS
    1214. Lin CF
    1215. Lin F
    1216. Lin F
    1217. Lin FC
    1218. Lin K
    1219. Lin KH
    1220. Lin PH
    1221. Lin T
    1222. Lin WW
    1223. Lin YS
    1224. Lin Y
    1225. Linden R
    1226. Lindholm D
    1227. Lindqvist LM
    1228. Lingor P
    1229. Linkermann A
    1230. Liotta LA
    1231. Lipinski MM
    1232. Lira VA
    1233. Lisanti MP
    1234. Liton PB
    1235. Liu B
    1236. Liu C
    1237. Liu CF
    1238. Liu F
    1239. Liu HJ
    1240. Liu J
    1241. Liu JJ
    1242. Liu JL
    1243. Liu K
    1244. Liu L
    1245. Liu L
    1246. Liu Q
    1247. Liu RY
    1248. Liu S
    1249. Liu S
    1250. Liu W
    1251. Liu XD
    1252. Liu X
    1253. Liu XH
    1254. Liu X
    1255. Liu X
    1256. Liu X
    1257. Liu Y
    1258. Liu Y
    1259. Liu Z
    1260. Liu Z
    1261. Liuzzi JP
    1262. Lizard G
    1263. Ljujic M
    1264. Lodhi IJ
    1265. Logue SE
    1266. Lokeshwar BL
    1267. Long YC
    1268. Lonial S
    1269. Loos B
    1270. López-Otín C
    1271. López-Vicario C
    1272. Lorente M
    1273. Lorenzi PL
    1274. Lõrincz P
    1275. Los M
    1276. Lotze MT
    1277. Lovat PE
    1278. Lu B
    1279. Lu B
    1280. Lu J
    1281. Lu Q
    1282. Lu SM
    1283. Lu S
    1284. Lu Y
    1285. Luciano F
    1286. Luckhart S
    1287. Lucocq JM
    1288. Ludovico P
    1289. Lugea A
    1290. Lukacs NW
    1291. Lum JJ
    1292. Lund AH
    1293. Luo H
    1294. Luo J
    1295. Luo S
    1296. Luparello C
    1297. Lyons T
    1298. Ma J
    1299. Ma Y
    1300. Ma Y
    1301. Ma Z
    1302. Machado J
    1303. Machado-Santelli GM
    1304. Macian F
    1305. MacIntosh GC
    1306. MacKeigan JP
    1307. Macleod KF
    1308. MacMicking JD
    1309. MacMillan-Crow LA
    1310. Madeo F
    1311. Madesh M
    1312. Madrigal-Matute J
    1313. Maeda A
    1314. Maeda T
    1315. Maegawa G
    1316. Maellaro E
    1317. Maes H
    1318. Magariños M
    1319. Maiese K
    1320. Maiti TK
    1321. Maiuri L
    1322. Maiuri MC
    1323. Maki CG
    1324. Malli R
    1325. Malorni W
    1326. Maloyan A
    1327. Mami-Chouaib F
    1328. Man N
    1329. Mancias JD
    1330. Mandelkow EM
    1331. Mandell MA
    1332. Manfredi AA
    1333. Manié SN
    1334. Manzoni C
    1335. Mao K
    1336. Mao Z
    1337. Mao ZW
    1338. Marambaud P
    1339. Marconi AM
    1340. Marelja Z
    1341. Marfe G
    1342. Margeta M
    1343. Margittai E
    1344. Mari M
    1345. Mariani FV
    1346. Marin C
    1347. Marinelli S
    1348. Mariño G
    1349. Markovic I
    1350. Marquez R
    1351. Martelli AM
    1352. Martens S
    1353. Martin KR
    1354. Martin SJ
    1355. Martin S
    1356. Martin-Acebes MA
    1357. Martín-Sanz P
    1358. Martinand-Mari C
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    Evaluation of refolding conditions for a human recombinant fusion cytokine protein, promegapoietin-1a.; Biotechnology and applied biochemistry; Vol 49(Pt 1). 2008 Jan.
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    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.