-
1
-
-
84856800302
-
Role of AMPK-mTORUlk1/2 in the regulation of autophagy: Cross talk, shortcuts, and feedbacks
-
Alers S, Loffler AS, Wesselborg S, Stork B. Role of AMPK-mTORUlk1/ 2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks. Mol Cell Biol 32: 2-11, 2012.
-
(2012)
Mol Cell Biol
, vol.32
, pp. 2-11
-
-
Alers, S.1
Loffler, A.S.2
Wesselborg, S.3
Stork, B.4
-
2
-
-
84891275812
-
Metformin modulates hyperglycaemia-induced endothelial senescence and apoptosis through SIRT1
-
Arunachalam G, Samuel SM, Marei I, Ding H, Triggle CR. Metformin modulates hyperglycaemia-induced endothelial senescence and apoptosis through SIRT1. Br J Pharmacol 171: 523-535, 2014.
-
(2014)
Br J Pharmacol
, vol.171
, pp. 523-535
-
-
Arunachalam, G.1
Samuel, S.M.2
Marei, I.3
Ding, H.4
Triggle, C.R.5
-
3
-
-
80455128548
-
Insulin resistance, hyperglycemia, and atherosclerosis
-
Bornfeldt KE, Tabas I. Insulin resistance, hyperglycemia, and atherosclerosis. Cell Metab 14: 575-585, 2011.
-
(2011)
Cell Metab
, vol.14
, pp. 575-585
-
-
Bornfeldt, K.E.1
Tabas, I.2
-
4
-
-
63549150420
-
Nicotinamide phosphoribosyltransferase imparts human endothelial cells with extended replicative lifespan and enhanced angiogenic capacity in a high glucose environment
-
Borradaile NM, Pickering JG. Nicotinamide phosphoribosyltransferase imparts human endothelial cells with extended replicative lifespan and enhanced angiogenic capacity in a high glucose environment. Aging Cell 8: 100-112, 2009.
-
(2009)
Aging Cell
, vol.8
, pp. 100-112
-
-
Borradaile, N.M.1
Pickering, J.G.2
-
5
-
-
79952836464
-
A lipidomic screen of palmitatetreated MIN6 beta-cells links sphingolipid metabolites with endoplasmic reticulum (ER) stress and impaired protein trafficking
-
Boslem E, MacIntosh G, Preston AM, Bartley C, Busch AK, Fuller M, Laybutt DR, Meikle PJ, Biden TJ. A lipidomic screen of palmitatetreated MIN6 beta-cells links sphingolipid metabolites with endoplasmic reticulum (ER) stress and impaired protein trafficking. Biochem J 435: 267-276, 2011.
-
(2011)
Biochem J
, vol.435
, pp. 267-276
-
-
Boslem, E.1
Macintosh, G.2
Preston, A.M.3
Bartley, C.4
Busch, A.K.5
Fuller, M.6
Laybutt, D.R.7
Meikle, P.J.8
Biden, T.J.9
-
6
-
-
19944434059
-
Inhibition of macroautophagy triggers apoptosis
-
Boya P, Gonzalez-Polo RA, Casares N, Perfettini JL, Dessen P, Larochette N, Metivier D, Meley D, Souquere S, Yoshimori T, Pierron G, Codogno P, Kroemer G. Inhibition of macroautophagy triggers apoptosis. Mol Cell Biol 25: 1025-1040, 2005.
-
(2005)
Mol Cell Biol
, vol.25
, pp. 1025-1040
-
-
Boya, P.1
Gonzalez-Polo, R.A.2
Casares, N.3
Perfettini, J.L.4
Dessen, P.5
Larochette, N.6
Metivier, D.7
Meley, D.8
Souquere, S.9
Yoshimori, T.10
Pierron, G.11
Codogno, P.12
Kroemer, G.13
-
7
-
-
0034948738
-
The autophagosomal-lysosomal compartment in programmed cell death
-
Bursch W. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ 8: 569-581, 2001.
-
(2001)
Cell Death Differ
, vol.8
, pp. 569-581
-
-
Bursch, W.1
-
8
-
-
20044386906
-
Palmitate-induced apoptosis in cultured bovine retinal pericytes: Roles of NAD(P)H oxidase, oxidant stress, and ceramide
-
Cacicedo JM, Benjachareowong S, Chou E, Ruderman NB, Ido Y. Palmitate-induced apoptosis in cultured bovine retinal pericytes: roles of NAD(P)H oxidase, oxidant stress, and ceramide. Diabetes 54: 1838-1845, 2005.
-
(2005)
Diabetes
, vol.54
, pp. 1838-1845
-
-
Cacicedo, J.M.1
Benjachareowong, S.2
Chou, E.3
Ruderman, N.B.4
Ido, Y.5
-
9
-
-
14344257169
-
AMPK inhibits fatty acid-induced increases in NF-kappaB transactivation in cultured human umbilical vein endothelial cells
-
Cacicedo JM, Yagihashi N, Keaney JF Jr, Ruderman NB, Ido Y. AMPK inhibits fatty acid-induced increases in NF-kappaB transactivation in cultured human umbilical vein endothelial cells. Biochem Biophys Res Commun 324: 1204-1209, 2004.
-
(2004)
Biochem Biophys Res Commun
, vol.324
, pp. 1204-1209
-
-
Cacicedo, J.M.1
Yagihashi, N.2
Keaney, J.F.3
Ruderman, N.B.4
Ido, Y.5
-
10
-
-
0017727138
-
A comparison of phenformin and metformin in the treatment of maturity onset diabetes
-
Cairns SA, Shalet S, Marshall AJ, Hartog M. A comparison of phenformin and metformin in the treatment of maturity onset diabetes. Diabete Metab 3: 183-188, 1977.
-
(1977)
Diabete Metab
, vol.3
, pp. 183-188
-
-
Cairns, S.A.1
Shalet, S.2
Marshall, A.J.3
Hartog, M.4
-
11
-
-
67349276169
-
AMPK regulates energy expenditure by modulating NAD_ metabolism and SIRT1 activity
-
Canto C, Gerhart-Hines Z, Feige JN, Lagouge M, Noriega L, Milne JC, Elliott PJ, Puigserver P, Auwerx J. AMPK regulates energy expenditure by modulating NAD_ metabolism and SIRT1 activity. Nature 458: 1056-1060, 2009.
-
(2009)
Nature
, vol.458
, pp. 1056-1060
-
-
Canto, C.1
Gerhart-Hines, Z.2
Feige, J.N.3
Lagouge, M.4
Noriega, L.5
Milne, J.C.6
Elliott, P.J.7
Puigserver, P.8
Auwerx, J.9
-
12
-
-
84862849835
-
Redox implications of AMPKmediated signal transduction beyond energetic clues
-
Cardaci S, Filomeni G, Ciriolo MR. Redox implications of AMPKmediated signal transduction beyond energetic clues. J Cell Sci 125: 2115-2125, 2012.
-
(2012)
J Cell Sci
, vol.125
, pp. 2115-2125
-
-
Cardaci, S.1
Filomeni, G.2
Ciriolo, M.R.3
-
13
-
-
84863499345
-
Regulation and function of uncoordinated-51 like kinase proteins
-
Chan EY. Regulation and function of uncoordinated-51 like kinase proteins. Antioxid Redox Signal 17: 775-785, 2012.
-
(2012)
Antioxid Redox Signal
, vol.17
, pp. 775-785
-
-
Chan, E.Y.1
-
14
-
-
21244442275
-
Acid ceramidase overexpression prevents the inhibitory effects of saturated fatty acids on insulin signaling
-
Chavez JA, Holland WL, Bar J, Sandhoff K, Summers SA. Acid ceramidase overexpression prevents the inhibitory effects of saturated fatty acids on insulin signaling. J Biol Chem 280: 20148-20153, 2005.
-
(2005)
J Biol Chem
, vol.280
, pp. 20148-20153
-
-
Chavez, J.A.1
Holland, W.L.2
Bar, J.3
Sandhoff, K.4
Summers, S.A.5
-
15
-
-
33845875499
-
Vascular lipotoxicity: Endothelial dysfunction via fatty-acid-induced reactive oxygen species overproduction in obese Zucker diabetic fatty rats
-
Chinen I, Shimabukuro M, Yamakawa K, Higa N, Matsuzaki T, Noguchi K, Ueda S, Sakanashi M, Takasu N. Vascular lipotoxicity: endothelial dysfunction via fatty-acid-induced reactive oxygen species overproduction in obese Zucker diabetic fatty rats. Endocrinology 148: 160-165, 2007.
-
(2007)
Endocrinology
, vol.148
, pp. 160-165
-
-
Chinen, I.1
Shimabukuro, M.2
Yamakawa, K.3
Higa, N.4
Matsuzaki, T.5
Noguchi, K.6
Ueda, S.7
Sakanashi, M.8
Takasu, N.9
-
16
-
-
33744514139
-
Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome
-
Cool B, Zinker B, Chiou W, Kifle L, Cao N, Perham M, Dickinson R, Adler A, Gagne G, Iyengar R, Zhao G, Marsh K, Kym P, Jung P, Camp HS, Frevert E. Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome. Cell Metab 3: 403-416, 2006.
-
(2006)
Cell Metab
, vol.3
, pp. 403-416
-
-
Cool, B.1
Zinker, B.2
Chiou, W.3
Kifle, L.4
Cao, N.5
Perham, M.6
Dickinson, R.7
Adler, A.8
Gagne, G.9
Iyengar, R.10
Zhao, G.11
Marsh, K.12
Kym, P.13
Jung, P.14
Camp, H.S.15
Frevert, E.16
-
18
-
-
77951174682
-
Downregulation of the longevity-associated protein sirtuin 1 in insulin resistance and metabolic syndrome: Potential biochemical mechanisms
-
de Kreutzenberg SV, Ceolotto G, Papparella I, Bortoluzzi A, Semplicini A, Dalla Man C, Cobelli C, Fadini GP, Avogaro A. Downregulation of the longevity-associated protein sirtuin 1 in insulin resistance and metabolic syndrome: potential biochemical mechanisms. Diabetes 59: 1006-1015, 2010.
-
(2010)
Diabetes
, vol.59
, pp. 1006-1015
-
-
De Kreutzenberg, S.V.1
Ceolotto, G.2
Papparella, I.3
Bortoluzzi, A.4
Semplicini, A.5
Dalla Man, C.6
Cobelli, C.7
Fadini, G.P.8
Avogaro, A.9
-
19
-
-
84862888230
-
Autophagy: An emerging immunological paradigm
-
Deretic V. Autophagy: an emerging immunological paradigm. J Immunol 189: 15-20, 2012.
-
(2012)
J Immunol
, vol.189
, pp. 15-20
-
-
Deretic, V.1
-
20
-
-
84922210546
-
Uncoupling AMPK from autophagy: A foe that hinders the beneficial effects of metformin treatment on metabolic syndrome-associated atherosclerosis?
-
December 10
-
Ding WX. Uncoupling AMPK from autophagy: a foe that hinders the beneficial effects of metformin treatment on metabolic syndrome-associated atherosclerosis? Focus on “Glucose and palmitate uncouple AMPK from autophagy in human aortic endothelial cells.” Am J Physiol Cell Physiol (December 10, 2014). doi:10.1152/ajpcell.00375.2014.
-
(2014)
Am J Physiol Cell Physiol
-
-
Ding, W.X.1
-
21
-
-
77953226963
-
Activation of AMP-activated protein kinase inhibits oxidized LDL-triggered endoplasmic reticulum stress in vivo
-
Dong Y, Zhang M, Wang S, Liang B, Zhao Z, Liu C, Wu M, Choi HC, Lyons TJ, Zou MH. Activation of AMP-activated protein kinase inhibits oxidized LDL-triggered endoplasmic reticulum stress in vivo. Diabetes 59: 1386-1396, 2010.
-
(2010)
Diabetes
, vol.59
, pp. 1386-1396
-
-
Dong, Y.1
Zhang, M.2
Wang, S.3
Liang, B.4
Zhao, Z.5
Liu, C.6
Wu, M.7
Choi, H.C.8
Lyons, T.J.9
Zou, M.H.10
-
22
-
-
79251587803
-
Phosphorylation of ULK1 (HATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
-
Egan DF, Shackelford DB, Mihaylova MM, Gelino S, Kohnz RA, Mair W, Vasquez DS, Joshi A, Gwinn DM, Taylor R, Asara JM, Fitzpatrick J, Dillin A, Viollet B, Kundu M, Hansen M, Shaw RJ. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 331: 456-461, 2011.
-
(2011)
Science
, vol.331
, pp. 456-461
-
-
Egan, D.F.1
Shackelford, D.B.2
Mihaylova, M.M.3
Gelino, S.4
Kohnz, R.A.5
Mair, W.6
Vasquez, D.S.7
Joshi, A.8
Gwinn, D.M.9
Taylor, R.10
Asara, J.M.11
Fitzpatrick, J.12
Dillin, A.13
Viollet, B.14
Kundu, M.15
Hansen, M.16
Shaw, R.J.17
-
23
-
-
84896405415
-
Propolis protects against high glucose-induced vascular endothelial dysfunction in isolated rat aorta
-
El-Awady MS, El-Agamy DS, Suddek GM, Nader MA. Propolis protects against high glucose-induced vascular endothelial dysfunction in isolated rat aorta. J Physiol Biochem 70: 247-254, 2014.
-
(2014)
J Physiol Biochem
, vol.70
, pp. 247-254
-
-
El-Awady, M.S.1
El-Agamy, D.S.2
Suddek, G.M.3
Nader, M.A.4
-
24
-
-
84874644987
-
Endothelial dysfunction in (Pre)diabetes: Characteristics, causative mechanisms and pathogenic role in type 2 diabetes
-
Eringa EC, Serne EH, Meijer RI, Schalkwijk CG, Houben AJ, Stehouwer CD, Smulders YM, van Hinsbergh VW. Endothelial dysfunction in (pre)diabetes: characteristics, causative mechanisms and pathogenic role in type 2 diabetes. Rev Endocr Metab Disord 14: 39-48, 2013.
-
(2013)
Rev Endocr Metab Disord
, vol.14
, pp. 39-48
-
-
Eringa, E.C.1
Serne, E.H.2
Meijer, R.I.3
Schalkwijk, C.G.4
Houben, A.J.5
Stehouwer, C.D.6
Smulders, Y.M.7
Van Hinsbergh, V.W.8
-
25
-
-
34548603259
-
Benefits and harms of antidiabetic agents in patients with diabetes and heart failure: Systematic review
-
Eurich DT, McAlister FA, Blackburn DF, Majumdar SR, Tsuyuki RT, Varney J, Johnson JA. Benefits and harms of antidiabetic agents in patients with diabetes and heart failure: systematic review. BMJ 335: 497, 2007.
-
(2007)
BMJ
, vol.335
-
-
Eurich, D.T.1
McAlister, F.A.2
Blackburn, D.F.3
Majumdar, S.R.4
Tsuyuki, R.T.5
Varney, J.6
Johnson, J.A.7
-
26
-
-
33646891970
-
Bax inhibition protects against free fatty acid-induced lysosomal permeabilization
-
Feldstein AE, Werneburg NW, Li Z, Bronk SF, Gores GJ. Bax inhibition protects against free fatty acid-induced lysosomal permeabilization. Am J Physiol Gastrointest Liver Physiol 290: G1339-G1346, 2006.
-
(2006)
Am J Physiol Gastrointest Liver Physiol
, vol.290
, pp. G1339-G1346
-
-
Feldstein, A.E.1
Werneburg, N.W.2
Li, Z.3
Bronk, S.F.4
Gores, G.J.5
-
27
-
-
0026455145
-
Glucose tolerance and the risk of cardiovascular disease: The Zutphen Study
-
Feskens EJ, Kromhout D. Glucose tolerance and the risk of cardiovascular disease: the Zutphen Study. J Clin Epidemiol 45: 1327-1334, 1992.
-
(1992)
J Clin Epidemiol
, vol.45
, pp. 1327-1334
-
-
Feskens, E.J.1
Kromhout, D.2
-
28
-
-
0000702611
-
The metabolism of albumin-bound C14-labeled unesterified fatty acids in normal human subjects
-
Fredrickson DS, Gordon RS, Ono K, Cherkes A. The metabolism of albumin-bound C14-labeled unesterified fatty acids in normal human subjects. J Clin Invest 37: 1504, 1958.
-
(1958)
J Clin Invest
, vol.37
-
-
Fredrickson, D.S.1
Gordon, R.S.2
Ono, K.3
Cherkes, A.4
-
29
-
-
84901062946
-
Impaired autophagic flux is associated with increased endoplasmic reticulum stress during the development of NAFLD
-
Gonzalez-Rodriguez A, Mayoral R, Agra N, Valdecantos MP, Pardo V, Miquilena-Colina ME, Vargas-Castrillon J, Lo Iacono O, Corazzari M, Fimia GM, Piacentini M, Muntane J, Bosca L, Garcia- Monzon C, Martin-Sanz P, Valverde AM. Impaired autophagic flux is associated with increased endoplasmic reticulum stress during the development of NAFLD. Cell Death Dis 5: e1179, 2014.
-
(2014)
Cell Death Dis
, vol.5
-
-
Gonzalez-Rodriguez, A.1
Mayoral, R.2
Agra, N.3
Valdecantos, M.P.4
Pardo, V.5
Miquilena-Colina, M.E.6
Vargas-Castrillon, J.7
Lo Iacono, O.8
Corazzari, M.9
Fimia, G.M.10
Piacentini, M.11
Muntane, J.12
Bosca, L.13
Garcia- Monzon, C.14
Martin-Sanz, P.15
Valverde, A.M.16
-
30
-
-
42949139481
-
AMPK phosphorylation of raptor mediates a metabolic checkpoint
-
Gwinn DM, Shackelford DB, Egan DF, Mihaylova MM, Mery A, Vasquez DS, Turk BE, Shaw RJ. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol Cell 30: 214-226, 2008.
-
(2008)
Mol Cell
, vol.30
, pp. 214-226
-
-
Gwinn, D.M.1
Shackelford, D.B.2
Egan, D.F.3
Mihaylova, M.M.4
Mery, A.5
Vasquez, D.S.6
Turk, B.E.7
Shaw, R.J.8
-
31
-
-
0033648637
-
Analysis of the role of the AMPactivated protein kinase in the response to cellular stress
-
Hardie DG, Salt IP, Davies SP. Analysis of the role of the AMPactivated protein kinase in the response to cellular stress. Methods Mol Biol 99: 63-74, 2000.
-
(2000)
Methods Mol Biol
, vol.99
, pp. 63-74
-
-
Hardie, D.G.1
Salt, I.P.2
Davies, S.P.3
-
32
-
-
78650691023
-
Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes
-
Hariharan N, Maejima Y, Nakae J, Paik J, Depinho RA, Sadoshima J. Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes. Circ Res 107: 1470-1482, 2010.
-
(2010)
Circ Res
, vol.107
, pp. 1470-1482
-
-
Hariharan, N.1
Maejima, Y.2
Nakae, J.3
Paik, J.4
Depinho, R.A.5
Sadoshima, J.6
-
33
-
-
0001330559
-
Turnover rate and oxidation of free fatty acids of blood plasma in man during exercise: Studies during continuous infusion of palmitate-1-C14
-
Havel RJ, Naimark A, Borchgrevink CF. Turnover rate and oxidation of free fatty acids of blood plasma in man during exercise: studies during continuous infusion of palmitate-1-C14. J Clin Invest 42: 1054-1063, 1963.
-
(1963)
J Clin Invest
, vol.42
, pp. 1054-1063
-
-
Havel, R.J.1
Naimark, A.2
Borchgrevink, C.F.3
-
34
-
-
0345107247
-
Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
-
Hawley SA, Boudeau J, Reid JL, Mustard KJ, Udd L, Makela TP, Alessi DR, Hardie DG. Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J Biol 2: 28, 2003.
-
(2003)
J Biol
, vol.2
-
-
Hawley, S.A.1
Boudeau, J.2
Reid, J.L.3
Mustard, K.J.4
Udd, L.5
Makela, T.P.6
Alessi, D.R.7
Hardie, D.G.8
-
35
-
-
84875450015
-
Dissociation of Bcl-2-Beclin1 complex by activated AMPK enhances cardiac autophagy and protects against cardiomyocyte apoptosis in diabetes
-
He C, Zhu H, Li H, Zou MH, Xie Z. Dissociation of Bcl-2-Beclin1 complex by activated AMPK enhances cardiac autophagy and protects against cardiomyocyte apoptosis in diabetes. Diabetes 62: 1270-1281, 2013.
-
(2013)
Diabetes
, vol.62
, pp. 1270-1281
-
-
He, C.1
Zhu, H.2
Li, H.3
Zou, M.H.4
Xie, Z.5
-
36
-
-
84872741363
-
Acute regulation of 5’-AMP-activated protein kinase by long-chain fatty acid, glucose and insulin in rat primary adipocytes
-
Hebbachi A, Saggerson D. Acute regulation of 5’-AMP-activated protein kinase by long-chain fatty acid, glucose and insulin in rat primary adipocytes. Biosci Rep 33: 71-82, 2012.
-
(2012)
Biosci Rep
, vol.33
, pp. 71-82
-
-
Hebbachi, A.1
Saggerson, D.2
-
37
-
-
0033840188
-
Palmitate-mediated alterations in the fatty acid metabolism of rat neonatal cardiac myocytes
-
Hickson-Bick DL, Buja LM, McMillin JB. Palmitate-mediated alterations in the fatty acid metabolism of rat neonatal cardiac myocytes. J Mol Cell Cardiol 32: 511-519, 2000.
-
(2000)
J Mol Cell Cardiol
, vol.32
, pp. 511-519
-
-
Hickson-Bick, D.L.1
Buja, L.M.2
McMillin, J.B.3
-
38
-
-
0023521261
-
3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors in the treatment of hypercholesterolemia
-
Hoeg JM, Brewer HB Jr. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors in the treatment of hypercholesterolemia. JAMA 258: 3532-3536, 1987.
-
(1987)
JAMA
, vol.258
, pp. 3532-3536
-
-
Hoeg, J.M.1
Brewer, H.B.2
-
39
-
-
78651260799
-
Receptor-mediated activation of ceramidase activity initiates the pleiotropic actions of adiponectin
-
Holland WL, Miller RA, Wang ZV, Sun K, Barth BM, Bui HH, Davis KE, Bikman BT, Halberg N, Rutkowski JM, Wade MR, Tenorio VM, Kuo MS, Brozinick JT, Zhang BB, Birnbaum MJ, Summers SA, Scherer PE. Receptor-mediated activation of ceramidase activity initiates the pleiotropic actions of adiponectin. Nat Med 17: 55-63, 2011.
-
(2011)
Nat Med
, vol.17
, pp. 55-63
-
-
Holland, W.L.1
Miller, R.A.2
Wang, Z.V.3
Sun, K.4
Barth, B.M.5
Bui, H.H.6
Davis, K.E.7
Bikman, B.T.8
Halberg, N.9
Rutkowski, J.M.10
Wade, M.R.11
Tenorio, V.M.12
Kuo, M.S.13
Brozinick, J.T.14
Zhang, B.B.15
Birnbaum, M.J.16
Summers, S.A.17
Scherer, P.E.18
-
40
-
-
50649112638
-
SIRT1regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase
-
Hou X, Xu S, Maitland-Toolan KA, Sato K, Jiang B, Ido Y, Lan F, Walsh K, Wierzbicki M, Verbeuren TJ, Cohen RA, Zang M. SIRT1regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase. J Biol Chem 283: 20015-20026, 2008.
-
(2008)
J Biol Chem
, vol.283
, pp. 20015-20026
-
-
Hou, X.1
Xu, S.2
Maitland-Toolan, K.A.3
Sato, K.4
Jiang, B.5
Ido, Y.6
Lan, F.7
Walsh, K.8
Wierzbicki, M.9
Verbeuren, T.J.10
Cohen, R.A.11
Zang, M.12
-
41
-
-
84896807067
-
Thioredoxin-interacting protein mediates dysfunction of tubular autophagy in diabetic kidneys through inhibiting autophagic flux
-
Huang C, Lin MZ, Cheng D, Braet F, Pollock CA, Chen XM. Thioredoxin-interacting protein mediates dysfunction of tubular autophagy in diabetic kidneys through inhibiting autophagic flux. Lab Invest 94: 309-320, 2014.
-
(2014)
Lab Invest
, vol.94
, pp. 309-320
-
-
Huang, C.1
Lin, M.Z.2
Cheng, D.3
Braet, F.4
Pollock, C.A.5
Chen, X.M.6
-
42
-
-
0036095269
-
Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: Inhibition by the AMP-activated protein kinase activation
-
Ido Y, Carling D, Ruderman N. Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: inhibition by the AMP-activated protein kinase activation. Diabetes 51: 159-167, 2002.
-
(2002)
Diabetes
, vol.51
, pp. 159-167
-
-
Ido, Y.1
Carling, D.2
Ruderman, N.3
-
43
-
-
0345167800
-
TSC2 mediates cellular energy response to control cell growth and survival
-
Inoki K, Zhu T, Guan KL. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115: 577-590, 2003.
-
(2003)
Cell
, vol.115
, pp. 577-590
-
-
Inoki, K.1
Zhu, T.2
Guan, K.L.3
-
44
-
-
84870880174
-
The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
-
Itakura E, Kishi-Itakura C, Mizushima N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 151: 1256-1269, 2012.
-
(2012)
Cell
, vol.151
, pp. 1256-1269
-
-
Itakura, E.1
Kishi-Itakura, C.2
Mizushima, N.3
-
45
-
-
77956467450
-
Metabolic memory: A vascular perspective
-
Jax TW. Metabolic memory: a vascular perspective. Cardiovasc Diabetol 9: 51, 2010.
-
(2010)
Cardiovasc Diabetol
, vol.9
-
-
Jax, T.W.1
-
46
-
-
79952355107
-
Selective autophagy mediated by autophagic adapter proteins
-
Johansen T, Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 7: 279-296, 2011.
-
(2011)
Autophagy
, vol.7
, pp. 279-296
-
-
Johansen, T.1
Lamark, T.2
-
47
-
-
84893500894
-
Molecular mechanism of autophagic membrane-scaffold assembly and disassembly
-
Kaufmann A, Beier V, Franquelim HG, Wollert T. Molecular mechanism of autophagic membrane-scaffold assembly and disassembly. Cell 156: 469-481, 2014.
-
(2014)
Cell
, vol.156
, pp. 469-481
-
-
Kaufmann, A.1
Beier, V.2
Franquelim, H.G.3
Wollert, T.4
-
48
-
-
20944436777
-
Free fatty acid impairment of nitric oxide production in endothelial cells is mediated by IKKbeta
-
Kim F, Tysseling KA, Rice J, Pham M, Haji L, Gallis BM, Baas AS, Paramsothy P, Giachelli CM, Corson MA, Raines EW. Free fatty acid impairment of nitric oxide production in endothelial cells is mediated by IKKbeta. Arterioscler Thromb Vasc Biol 25: 989-994, 2005.
-
(2005)
Arterioscler Thromb Vasc Biol
, vol.25
, pp. 989-994
-
-
Kim, F.1
Tysseling, K.A.2
Rice, J.3
Pham, M.4
Haji, L.5
Gallis, B.M.6
Baas, A.S.7
Paramsothy, P.8
Giachelli, C.M.9
Corson, M.A.10
Raines, E.W.11
-
49
-
-
79551598347
-
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
-
Kim J, Kundu M, Viollet B, Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 13: 132-141, 2011.
-
(2011)
Nat Cell Biol
, vol.13
, pp. 132-141
-
-
Kim, J.1
Kundu, M.2
Viollet, B.3
Guan, K.L.4
-
50
-
-
0024460580
-
Role of reversible phosphorylation of acetyl-CoA carboxylase in long-chain fatty acid synthesis
-
Kim KH, Lopez-Casillas F, Bai DH, Luo X, Pape ME. Role of reversible phosphorylation of acetyl-CoA carboxylase in long-chain fatty acid synthesis. FASEB J 3: 2250-2256, 1989.
-
(1989)
FASEB J
, vol.3
, pp. 2250-2256
-
-
Kim, K.H.1
Lopez-Casillas, F.2
Bai, D.H.3
Luo, X.4
Pape, M.E.5
-
51
-
-
84862295360
-
Guidelines for the use and interpretation of assays for monitoring autophagy
-
Klionsky DJ, Abdalla FC, Abeliovich H, Abraham RT, Acevedo- Arozena A, Adeli K, Agholme L, Agnello M, Agostinis P, Aguirre- Ghiso JA, Ahn HJ, Ait-Mohamed O, Ait-Si-Ali S, Akematsu T, Akira S, Al-Younes HM, Al-Zeer MA, Albert ML, Albin RL, Alegre-Abarrategui J, Aleo MF, Alirezaei M, Almasan A, Almonte-Becerril M, Amano A, Amaravadi R, Amarnath S, Amer AO, Andrieu-Abadie N, Anantharam V, Ann DK, Anoopkumar-Dukie S, Aoki H, Apostolova N, Arancia G, Aris JP, Asanuma K, Asare NY, Ashida H, Askanas V, Askew DS, Auberger P, Baba M, Backues SK, Baehrecke EH, Bahr BA, Bai XY, Bailly Y, Baiocchi R, Baldini G, Balduini W, Ballabio A, Bamber BA, Bampton ET, Banhegyi G, Bartholomew CR, Bassham DC, Bast RC, Jr, Batoko H, Bay BH, Beau I, Bechet DM, Begley TJ, Behl C, Behrends C, Bekri S, Bellaire B, Bendall LJ, Benetti L, Berliocchi L, Bernardi H, Bernassola F, Besteiro S, Bhatia-Kissova I, Bi X, Biard-Piechaczyk M, Blum JS, Boise LH, Bonaldo P, Boone DL, Bornhauser BC, Bortoluci KR, Bossis I, Bost F, Bourquin JP, Boya P, Boyer-Guittaut M, Bozhkov PV, Brady NR, Brancolini C, Brech A, Brenman JE, Brennand A, Bresnick EH, Brest P, Bridges D, Bristol ML, Brookes PS, Brown EJ, Brumell JH, Brunetti-Pierri N, Brunk UT, Bulman DE, Bultman SJ, Bultynck G, Burbulla LF, Bursch W, Butchar JP, Buzgariu W, Bydlowski SP, Cadwell K, Cahova M, Cai D, Cai J, Cai Q, Calabretta B, Calvo-Garrido J, Camougrand N, Campanella M, Campos-Salinas J, Candi E, Cao L, Caplan AB, Carding SR, Cardoso SM, Carew JS, Carlin CR, Carmignac V, Carneiro LA, Carra S, Caruso RA, Casari G, Casas C, Castino R, Cebollero E, Cecconi F, Celli J, Chaachouay H, Chae HJ, Chai CY, Chan DC, Chan EY, Chang RC, Che CM, Chen CC, Chen GC, Chen GQ, Chen M, Chen Q, Chen SS, Chen W, Chen X, Chen YG, Chen Y, Chen YJ, Chen Z, Cheng A, Cheng CH, Cheng Y, Cheong H, Cheong JH, Cherry S, Chess-Williams R, Cheung ZH, Chevet E, Chiang HL, Chiarelli R, Chiba T, Chin LS, Chiou SH, Chisari FV, Cho CH, Cho DH, Choi AM, Choi D, Choi KS, Choi ME, Chouaib S, Choubey D, Choubey V, Chu CT, Chuang TH, Chueh SH, Chun T, Chwae YJ, Chye ML, Ciarcia R, Ciriolo MR, Clague MJ, Clark RS, Clarke PG, Clarke R, Codogno P, Coller HA, Colombo MI, Comincini S, Condello M, Condorelli F, Cookson MR, Coombs GH, Coppens I, Corbalan R, Cossart P, Costelli P, Costes S, Coto-Montes A, Couve E, Coxon FP, Cregg JM, Crespo JL, Cronje MJ, Cuervo AM, Cullen JJ, Czaja MJ, D’Amelio M, Darfeuille-Michaud A, Davids LM, Davies FE, De Felici M, de Groot JF, de Haan CA, De Martino L, De Milito A, De Tata V, Debnath J, Degterev A, Dehay B, Delbridge LM, Demarchi F, Deng YZ, Dengjel J, Dent P, Denton D, Deretic V, Desai SD, Devenish RJ, Di Gioacchino M, Di Paolo G, Di Pietro C, Diaz- Araya G, Diaz-Laviada I, Diaz-Meco MT, Diaz-Nido J, Dikic I, Dinesh-Kumar SP, Ding WX, Distelhorst CW, Diwan A, Djavaheri- Mergny M, Dokudovskaya S, Dong Z, Dorsey FC, Dosenko V, Dowling JJ, Doxsey S, Dreux M, Drew ME, Duan Q, Duchosal MA, Duff K, Dugail I, Durbeej M, Duszenko M, Edelstein CL, Edinger AL, Egea G, Eichinger L, Eissa NT, Ekmekcioglu S, El-Deiry WS, Elazar Z, Elgendy M, Ellerby LM, Eng KE, Engelbrecht AM, Engelender S, Erenpreisa J, Escalante R, Esclatine A, Eskelinen EL, Espert L, Espina V, Fan H, Fan J, Fan QW, Fan Z, Fang S, Fang Y, Fanto M, Fanzani A, Farkas T, Farre JC, Faure M, Fechheimer M, Feng CG, Feng J, Feng Q, Feng Y, Fesus L, Feuer R, Figueiredo-Pereira ME, Fimia GM, Fingar DC, Finkbeiner S, Finkel T, Finley KD, Fiorito F, Fisher EA, Fisher PB, Flajolet M, Florez-McClure ML, Florio S, Fon EA, Fornai F, Fortunato F, Fotedar R, Fowler DH, Fox HS, Franco R, Frankel LB, Fransen M, Fuentes JM, Fueyo J, Fujii J, Fujisaki K, Fujita E, Fukuda M, Furukawa RH, Gaestel M, Gailly P, Gajewska M, Galliot B, Galy V, Ganesh S, Ganetzky B, Ganley IG, Gao FB, Gao GF, Gao J, Garcia L, Garcia-Manero G, Garcia-Marcos M, Garmyn M, Gartel AL, Gatti E, Gautel M, Gawriluk TR, Gegg ME, Geng J, Germain M, Gestwicki JE, Gewirtz DA, Ghavami S, Ghosh P, Giammarioli AM, Giatromanolaki AN, Gibson SB, Gilkerson RW, Ginger ML, Ginsberg HN, Golab J, Goligorsky MS, Golstein P, Gomez- Manzano C, Goncu E, Gongora C, Gonzalez CD, Gonzalez R, Gonzalez- Estevez C, Gonzalez-Polo RA, Gonzalez-Rey E, Gorbunov NV, Gorski S, Goruppi S, Gottlieb RA, Gozuacik D, Granato GE, Grant GD, Green KN, Gregorc A, Gros F, Grose C, Grunt TW, Gual P, Guan JL, Guan KL, Guichard SM, Gukovskaya AS, Gukovsky I, Gunst J, Gustafsson AB, Halayko AJ, Hale AN, Halonen SK, Hamasaki M, Han F, Han T, Hancock MK, Hansen M, Harada H, Harada M, Hardt SE, Harper JW, Harris AL, Harris J, Harris SD, Hashimoto M, Haspel JA, Hayashi S, Hazelhurst LA, He C, He YW, Hebert MJ, Heidenreich KA, Helfrich MH, Helgason GV, Henske EP, Herman B, Herman PK, Hetz C, Hilfiker S, Hill JA, Hocking LJ, Hofman P, Hofmann TG, Hohfeld J, Holyoake TL, Hong MH, Hood DA, Hotamisligil GS, Houwerzijl EJ, Hoyer-Hansen M, Hu B, Hu CA, Hu HM, Hua Y, Huang C, Huang J, Huang S, Huang WP, Huber TB, Huh WK, Hung TH, Hupp TR, Hur GM, Hurley JB, Hussain SN, Hussey PJ, Hwang JJ, Hwang S, Ichihara A, Ilkhanizadeh S, Inoki K, Into T, Iovane V, Iovanna JL, Ip NY, Isaka Y, Ishida H, Isidoro C, Isobe K, Iwasaki A, Izquierdo M, Izumi Y, Jaakkola PM, Jaattela M, Jackson GR, Jackson WT, Janji B, Jendrach M, Jeon JH, Jeung EB, Jiang H, Jiang JX, Jiang M, Jiang Q, Jiang X, Jimenez A, Jin M, Jin S, Joe CO, Johansen T, Johnson DE, Johnson GV, Jones NL, Joseph B, Joseph SK, Joubert AM, Juhasz G, Juillerat-Jeanneret L, Jung CH, Jung YK, Kaarniranta K, Kaasik A, Kabuta T, Kadowaki M, Kagedal K, Kamada Y, Kaminskyy VO, Kampinga HH, Kanamori H, Kang C, Kang KB, Kang KI, Kang R, Kang YA, Kanki T, Kanneganti TD, Kanno H, Kanthasamy AG, Kanthasamy A, Karantza V, Kaushal GP, Kaushik S, Kawazoe Y, Ke PY, Kehrl JH, Kelekar A, Kerkhoff C, Kessel DH, Khalil H, Kiel JA, Kiger AA, Kihara A, Kim DR, Kim DH, Kim EK, Kim HR, Kim JS, Kim JH, Kim JC, Kim JK, Kim PK, Kim SW, Kim YS, Kim Y, Kimchi A, Kimmelman AC, King JS, Kinsella TJ, Kirkin V, Kirshenbaum LA, Kitamoto K, Kitazato K, Klein L, Klimecki WT, Klucken J, Knecht E, Ko BC, Koch JC, Koga H, Koh JY, Koh YH, Koike M, Komatsu M, Kominami E, Kong HJ, Kong WJ, Korolchuk VI, Kotake Y, Koukourakis MI, Kouri Flores JB, Kovacs AL, Kraft C, Krainc D, Kramer H, Kretz-Remy C, Krichevsky AM, Kroemer G, Kruger R, Krut O, Ktistakis NT, Kuan CY, Kucharczyk R, Kumar A, Kumar R, Kumar S, Kundu M, Kung HJ, Kurz T, Kwon HJ, La Spada AR, Lafont F, Lamark T, Landry J, Lane JD, Lapaquette P, Laporte JF, Laszlo L, Lavandero S, Lavoie JN, Layfield R, Lazo PA, Le W, Le Cam L, Ledbetter DJ, Lee AJ, Lee BW, Lee GM, Lee J, Lee JH, Lee M, Lee MS, Lee SH, Leeuwenburgh C, Legembre P, Legouis R, Lehmann M, Lei HY, Lei QY, Leib DA, Leiro J, Lemasters JJ, Lemoine A, Lesniak MS, Lev D, Levenson VV, Levine B, Levy E, Li F, Li JL, Li L, Li S, Li W, Li XJ, Li YB, Li YP, Liang C, Liang Q, Liao YF, Liberski PP, Lieberman A, Lim HJ, Lim KL, Lim K, Lin CF, Lin FC, Lin J, Lin JD, Lin K, Lin WW, Lin WC, Lin YL, Linden R, Lingor P, Lippincott-Schwartz J, Lisanti MP, Liton PB, Liu B, Liu CF, Liu K, Liu L, Liu QA, Liu W, Liu YC, Liu Y, Lockshin RA, Lok CN, Lonial S, Loos B, Lopez-Berestein G, Lopez-Otin C, Lossi L, Lotze MT, Low P, Lu B, Lu Z, Luciano F, Lukacs NW, Lund AH, Lynch-Day MA, Ma Y, Macian F, MacKeigan JP, Macleod KF, Madeo F, Maiuri L, Maiuri MC, Malagoli D, Malicdan MC, Malorni W, Man N, Mandelkow EM, Manon S, Manov I, Mao K, Mao X, Mao Z, Marambaud P, Marazziti D, Marcel YL, Marchbank K, Marchetti P, Marciniak SJ, Marcondes M, Mardi M, Marfe G, Marino G, Markaki M, Marten MR, Martin SJ, Martinand- Mari C, Martinet W, Martinez-Vicente M, Masini M, Matarrese P, Matsuo S, Matteoni R, Mayer A, Mazure NM, McConkey DJ, Mc- Connell MJ, McDermott C, McDonald C, McInerney GM, McKenna SL, McLaughlin B, McLean PJ, McMaster CR, McQuibban GA, Meijer AJ, Meisler MH, Melendez A, Melia TJ, Melino G, Mena MA, Menendez JA, Menna-Barreto RF, Menon MB, Menzies FM, Mercer CA, Merighi A, Merry DE, Meschini S, Meyer CG, Meyer TF, Miao CY, Miao JY, Michels PA, Michiels C, Mijaljica D, Milojkovic A, Minucci S, Miracco C, Miranti CK, Mitroulis I, Miyazawa K, Mizushima N, Mograbi B, Mohseni S, Molero X, Mollereau B, Mollinedo F, Momoi T, Monastyrska I, Monick MM, Monteiro MJ, Moore MN, Mora R, Moreau K, Moreira PI, Moriyasu Y, Moscat J, Mostowy S, Mottram JC, Motyl T, Moussa CE, Muller S, Munger K, Munz C, Murphy LO, Murphy ME, Musaro A, Mysorekar I, Nagata E, Nagata K, Nahimana A, Nair U, Nakagawa T, Nakahira K, Nakano H, Nakatogawa H, Nanjundan M, Naqvi NI, Narendra DP, Narita M, Navarro M, Nawrocki ST, Nazarko TY, Nemchenko A, Netea MG, Neufeld TP, Ney PA, Nezis IP, Nguyen HP, Nie D, Nishino I, Nislow C, Nixon RA, Noda T, Noegel AA, Nogalska A, Noguchi S, Notterpek L, Novak I, Nozaki T, Nukina N, Nurnberger T, Nyfeler B, Obara K, Oberley TD, Oddo S, Ogawa M, Ohashi T, Okamoto K, Oleinick NL, Oliver FJ, Olsen LJ, Olsson S, Opota O, Osborne TF, Ostrander GK, Otsu K, Ou JH, Ouimet M, Overholtzer M, Ozpolat B, Paganetti P, Pagnini U, Pallet N, Palmer GE, Palumbo C, Pan T, Panaretakis T, Pandey UB, Papackova Z, Papassideri I, Paris I, Park J, Park OK, Parys JB, Parzych KR, Patschan S, Patterson C, Pattingre S, Pawelek JM, Peng J, Perlmutter DH, Perrotta I, Perry G, Pervaiz S, Peter M, Peters GJ, Petersen M, Petrovski G, Phang JM, Piacentini M, Pierre P, Pierrefite-Carle V, Pierron G, Pinkas-Kramarski R, Piras A, Piri N, Platanias LC, Poggeler S, Poirot M, Poletti A, Pous C, Pozuelo-Rubio M, Praetorius-Ibba M, Prasad A, Prescott M, Priault M, Produit- Zengaffinen N, Progulske-Fox A, Proikas-Cezanne T, Przedborski S, Przyklenk K, Puertollano R, Puyal J, Qian SB, Qin L, Qin ZH, Quaggin SE, Raben N, Rabinowich H, Rabkin SW, Rahman I, Rami A, Ramm G, Randall G, Randow F, Rao VA, Rathmell JC, Ravikumar B, Ray SK, Reed BH, Reed JC, Reggiori F, Regnier-Vigouroux A, Reichert AS, Reiners JJ, Jr, Reiter RJ, Ren J, Revuelta JL, Rhodes CJ, Ritis K, Rizzo E, Robbins J, Roberge M, Roca H, Roccheri MC, Rocchi S, Rodemann HP, Rodriguez de Cordoba S, Rohrer B, Roninson IB, Rosen K, Rost-Roszkowska MM, Rouis M, Rouschop KM, Rovetta F, Rubin BP, Rubinsztein DC, Ruckdeschel K, Rucker EB, 3rd, Rudich A, Rudolf E, Ruiz-Opazo N, Russo R, Rusten TE, Ryan KM, Ryter SW, Sabatini DM, Sadoshima J, Saha T, Saitoh T, Sakagami H, Sakai Y, Salekdeh GH, Salomoni P, Salvaterra PM, Salvesen G, Salvioli R, Sanchez AM, Sanchez-Alcazar JA, Sanchez- Prieto R, Sandri M, Sankar U, Sansanwal P, Santambrogio L, Saran S, Sarkar S, Sarwal M, Sasakawa C, Sasnauskiene A, Sass M, Sato K, Sato M, Schapira AH, Scharl M, Schatzl HM, Scheper W, Schiaffino S, Schneider C, Schneider ME, Schneider-Stock R, Schoenlein PV, Schorderet DF, Schuller C, Schwartz GK, Scorrano L, Sealy L, Seglen PO, Segura-Aguilar J, Seiliez I, Seleverstov O, Sell C, Seo JB, Separovic D, Setaluri V, Setoguchi T, Settembre C, Shacka JJ, Shanmugam M, Shapiro IM, Shaulian E, Shaw RJ, Shelhamer JH, Shen HM, Shen WC, Sheng ZH, Shi Y, Shibuya K, Shidoji Y, Shieh JJ, Shih CM, Shimada Y, Shimizu S, Shintani T, Shirihai OS, Shore GC, Sibirny AA, Sidhu SB, Sikorska B, Silva-Zacarin EC, Simmons A, Simon AK, Simon HU, Simone C, Simonsen A, Sinclair DA, Singh R, Sinha D, Sinicrope FA, Sirko A, Siu PM, Sivridis E, Skop V, Skulachev VP, Slack RS, Smaili SS, Smith DR, Soengas MS, Soldati T, Song X, Sood AK, Soong TW, Sotgia F, Spector SA, Spies CD, Springer W, Srinivasula SM, Stefanis L, Steffan JS, Stendel R, Stenmark H, Stephanou A, Stern ST, Sternberg C, Stork B, Stralfors P, Subauste CS, Sui X, Sulzer D, Sun J, Sun SY, Sun ZJ, Sung JJ, Suzuki K, Suzuki T, Swanson MS, Swanton C, Sweeney ST, Sy LK, Szabadkai G, Tabas I, Taegtmeyer H, Tafani M, Takacs-Vellai K, Takano Y, Takegawa K, Takemura G, Takeshita F, Talbot NJ, Tan KS, Tanaka K, Tang D, Tanida I, Tannous BA, Tavernarakis N, Taylor GS, Taylor GA, Taylor JP, Terada LS, Terman A, Tettamanti G, Thevissen K, Thompson CB, Thorburn A, Thumm M, Tian F, Tian Y, Tocchini-Valentini G, Tolkovsky AM, Tomino Y, Tonges L, Tooze SA, Tournier C, Tower J, Towns R, Trajkovic V, Travassos LH, Tsai TF, Tschan MP, Tsubata T, Tsung A, Turk B, Turner LS, Tyagi SC, Uchiyama Y, Ueno T, Umekawa M, Umemiya-Shirafuji R, Unni VK, Vaccaro MI, Valente EM, Van den Berghe G, van der Klei IJ, van Doorn W, van Dyk LF, van Egmond M, van Grunsven LA, Vandenabeele P, Vandenberghe WP, Vanhorebeek I, Vaquero EC, Velasco G, Vellai T, Vicencio JM, Vierstra RD, Vila M, Vindis C, Viola G, Viscomi MT, Voitsekhovskaja OV, von Haefen C, Votruba M, Wada K, Wade-Martins R, Walker CL, Walsh CM, Walter J, Wan XB, Wang A, Wang C, Wang D, Wang F, Wang G, Wang H, Wang HG, Wang HD, Wang J, Wang K, Wang M, Wang RC, Wang X, Wang YJ, Wang Y, Wang Z, Wang ZC, Wansink DG, Ward DM, Watada H, Waters SL, Webster P, Wei L, Weihl CC, Weiss WA, Welford SM, Wen LP, Whitehouse CA, Whitton JL, Whitworth AJ, Wileman T, Wiley JW, Wilkinson S, Willbold D, Williams RL, Williamson PR, Wouters BG, Wu C, Wu DC, Wu WK, Wyttenbach A, Xavier RJ, Xi Z, Xia P, Xiao G, Xie Z, Xu DZ, Xu J, Xu L, Xu X, Yamamoto A, Yamashina S, Yamashita M, Yan X, Yanagida M, Yang DS, Yang E, Yang JM, Yang SY, Yang W, Yang WY, Yang Z, Yao MC, Yao TP, Yeganeh B, Yen WL, Yin JJ, Yin XM, Yoo OJ, Yoon G, Yoon SY, Yorimitsu T, Yoshikawa Y, Yoshimori T, Yoshimoto K, You HJ, Youle RJ, Younes A, Yu L, Yu SW, Yu WH, Yuan ZM, Yue Z, Yun CH, Yuzaki M, Zabirnyk O, Silva-Zacarin E, Zacks D, Zacksenhaus E, Zaffaroni N, Zakeri Z, Zeh HJ, 3rd, Zeitlin SO, Zhang H, Zhang HL, Zhang J, Zhang JP, Zhang L, Zhang MY, Zhang XD, Zhao M, Zhao YF, Zhao Y, Zhao ZJ, Zheng X, Zhivotovsky B, Zhong Q, Zhou CZ, Zhu C, Zhu WG, Zhu XF, Zhu X, Zhu Y, Zoladek T, Zong WX, Zorzano A, Zschocke J, and Zuckerbraun B. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy 8: 445-544, 2012.
-
(2012)
Autophagy
, vol.8
, pp. 445-544
-
-
Klionsky, D.J.1
Abdalla, F.C.2
Abeliovich, H.3
Abraham, R.T.4
Acevedo- Arozena, A.5
Adeli, K.6
Agholme, L.7
Agnello, M.8
Agostinis, P.9
Aguirre- Ghiso, J.A.10
Ahn, H.J.11
Ait-Mohamed, O.12
Ait-Si-Ali, S.13
Akematsu, T.14
Akira, S.15
Al-Younes, H.M.16
Al-Zeer, M.A.17
Albert, M.L.18
Albin, R.L.19
Alegre-Abarrategui, J.20
Aleo, M.F.21
Alirezaei, M.22
Almasan, A.23
Almonte-Becerril, M.24
Amano, A.25
Amaravadi, R.26
Amarnath, S.27
Amer, A.O.28
Rieu-Abadie, N.29
Anantharam, V.30
Ann, D.K.31
Anoopkumar-Dukie, S.32
Aoki, H.33
Apostolova, N.34
Arancia, G.35
Aris, J.P.36
Asanuma, K.37
Asare, N.Y.38
Ashida, H.39
Askanas, V.40
Askew, D.S.41
Auberger, P.42
Baba, M.43
Backues, S.K.44
Baehrecke, E.H.45
Bahr, B.A.46
Bai, X.Y.47
Bailly, Y.48
Baiocchi, R.49
Baldini, G.50
Balduini, W.51
Ballabio, A.52
Bamber, B.A.53
Bampton, E.T.54
Banhegyi, G.55
Bartholomew, C.R.56
Bassham, D.C.57
Bast, R.C.58
Batoko, H.59
Bay, B.H.60
Beau, I.61
Bechet, D.M.62
Begley, T.J.63
Behl, C.64
Behrends, C.65
Bekri, S.66
Bellaire, B.67
Bendall, L.J.68
Benetti, L.69
Berliocchi, L.70
Bernardi, H.71
Bernassola, F.72
Besteiro, S.73
Bhatia-Kissova, I.74
Bi, X.75
Biard-Piechaczyk, M.76
Blum, J.S.77
Boise, L.H.78
Bonaldo, P.79
Boone, D.L.80
Bornhauser, B.C.81
Bortoluci, K.R.82
Bossis, I.83
Bost, F.84
Bourquin, J.P.85
Boya, P.86
Boyer-Guittaut, M.87
Bozhkov, P.V.88
Brady, N.R.89
Brancolini, C.90
Brech, A.91
Brenman, J.E.92
Brennand, A.93
Bresnick, E.H.94
Brest, P.95
Bridges, D.96
Bristol, M.L.97
Brookes, P.S.98
Brown, E.J.99
Brumell, J.H.100
Brunetti-Pierri, N.101
Brunk, U.T.102
Bulman, D.E.103
Bultman, S.J.104
Bultynck, G.105
Burbulla, L.F.106
Bursch, W.107
Butchar, J.P.108
Buzgariu, W.109
Bydlowski, S.P.110
Cadwell, K.111
Cahova, M.112
Cai, D.113
Cai, J.114
Cai, Q.115
Calabretta, B.116
Calvo-Garrido, J.117
Camougrand, N.118
Campanella, M.119
Campos-Salinas, J.120
Candi, E.121
Cao, L.122
Caplan, A.B.123
Carding, S.R.124
Cardoso, S.M.125
Carew, J.S.126
Carlin, C.R.127
Carmignac, V.128
Carneiro, L.A.129
Carra, S.130
Caruso, R.A.131
Casari, G.132
Casas, C.133
Castino, R.134
Cebollero, E.135
Cecconi, F.136
Celli, J.137
Chaachouay, H.138
Chae, H.J.139
Chai, C.Y.140
Chan, D.C.141
Chan, E.Y.142
Chang, R.C.143
Che, C.M.144
Chen, C.C.145
Chen, G.C.146
Chen, G.Q.147
Chen, M.148
Chen, Q.149
Chen, S.S.150
Chen, W.151
Chen, X.152
Chen, Y.G.153
Chen, Y.154
Chen, Y.J.155
Chen, Z.156
Cheng, A.157
Cheng, C.H.158
Cheng, Y.159
Cheong, H.160
Cheong, J.H.161
Cherry, S.162
Chess-Williams, R.163
Cheung, Z.H.164
Chevet, E.165
Chiang, H.L.166
Chiarelli, R.167
Chiba, T.168
Chin, L.S.169
Chiou, S.H.170
Chisari, F.V.171
Cho, C.H.172
Cho, D.H.173
Choi, A.M.174
Choi, D.175
Choi, K.S.176
Choi, M.E.177
Chouaib, S.178
Choubey, D.179
Choubey, V.180
Chu, C.T.181
Chuang, T.H.182
Chueh, S.H.183
Chun, T.184
Chwae, Y.J.185
Chye, M.L.186
Ciarcia, R.187
Ciriolo, M.R.188
Clague, M.J.189
Clark, R.S.190
Clarke, P.G.191
Clarke, R.192
Codogno, P.193
Coller, H.A.194
Colombo, M.I.195
Comincini, S.196
Condello, M.197
Condorelli, F.198
Cookson, M.R.199
Coombs, G.H.200
Coppens, I.201
Corbalan, R.202
Cossart, P.203
Costelli, P.204
Costes, S.205
Coto-Montes, A.206
Couve, E.207
Coxon, F.P.208
Cregg, J.M.209
Crespo, J.L.210
Cronje, M.J.211
Cuervo, A.M.212
Cullen, J.J.213
Czaja, M.J.214
D’amelio, M.215
Darfeuille-Michaud, A.216
Davids, L.M.217
Davies, F.E.218
De Felici, M.219
De Groot, J.F.220
De Haan, C.A.221
De Martino, L.222
De Milito, A.223
De Tata, V.224
Debnath, J.225
Degterev, A.226
Dehay, B.227
Delbridge, L.M.228
Demarchi, F.229
Deng, Y.Z.230
Dengjel, J.231
Dent, P.232
Denton, D.233
Deretic, V.234
Desai, S.D.235
Devenish, R.J.236
Di Gioacchino, M.237
Di Paolo, G.238
Di Pietro, C.239
Diaz- Araya, G.240
Diaz-Laviada, I.241
Diaz-Meco, M.T.242
Diaz-Nido, J.243
Dikic, I.244
Dinesh-Kumar, S.P.245
Ding, W.X.246
Distelhorst, C.W.247
Diwan, A.248
Djavaheri- Mergny, M.249
Dokudovskaya, S.250
Dong, Z.251
Dorsey, F.C.252
Dosenko, V.253
Dowling, J.J.254
Doxsey, S.255
Dreux, M.256
Drew, M.E.257
Duan, Q.258
Duchosal, M.A.259
Duff, K.260
Dugail, I.261
Durbeej, M.262
Duszenko, M.263
Edelstein, C.L.264
Edinger, A.L.265
Egea, G.266
Eichinger, L.267
Eissa, N.T.268
Ekmekcioglu, S.269
El-Deiry, W.S.270
Elazar, Z.271
Elgendy, M.272
Ellerby, L.M.273
Eng, K.E.274
Engelbrecht, A.M.275
Engelender, S.276
Erenpreisa, J.277
Escalante, R.278
Esclatine, A.279
Eskelinen, E.L.280
Espert, L.281
Espina, V.282
Fan, H.283
Fan, J.284
Fan, Q.W.285
Fan, Z.286
Fang, S.287
Fang, Y.288
Fanto, M.289
Fanzani, A.290
Farkas, T.291
Farre, J.C.292
Faure, M.293
Fechheimer, M.294
Feng, C.G.295
Feng, J.296
Feng, Q.297
Feng, Y.298
Fesus, L.299
Feuer, R.300
Figueiredo-Pereira, M.E.301
Fimia, G.M.302
Fingar, D.C.303
Finkbeiner, S.304
Finkel, T.305
Finley, K.D.306
Fiorito, F.307
Fisher, E.A.308
Fisher, P.B.309
Flajolet, M.310
Florez-McClure, M.L.311
Florio, S.312
Fon, E.A.313
Fornai, F.314
Fortunato, F.315
Fotedar, R.316
Fowler, D.H.317
Fox, H.S.318
Franco, R.319
Frankel, L.B.320
Fransen, M.321
Fuentes, J.M.322
Fueyo, J.323
Fujii, J.324
Fujisaki, K.325
Fujita, E.326
Fukuda, M.327
Furukawa, R.H.328
Gaestel, M.329
Gailly, P.330
Gajewska, M.331
Galliot, B.332
Galy, V.333
Ganesh, S.334
Ganetzky, B.335
Ganley, I.G.336
Gao, F.B.337
Gao, G.F.338
Gao, J.339
Garcia, L.340
Garcia-Manero, G.341
Garcia-Marcos, M.342
Garmyn, M.343
Gartel, A.L.344
Gatti, E.345
Gautel, M.346
Gawriluk, T.R.347
Gegg, M.E.348
Geng, J.349
Germain, M.350
Gestwicki, J.E.351
Gewirtz, D.A.352
Ghavami, S.353
Ghosh, P.354
Giammarioli, A.M.355
Giatromanolaki, A.N.356
Gibson, S.B.357
Gilkerson, R.W.358
Ginger, M.L.359
Ginsberg, H.N.360
Golab, J.361
Goligorsky, M.S.362
Golstein, P.363
Gomez- Manzano, C.364
Goncu, E.365
Gongora, C.366
Gonzalez, C.D.367
Gonzalez, R.368
Gonzalez- Estevez, C.369
Gonzalez-Polo, R.A.370
Gonzalez-Rey, E.371
Gorbunov, N.V.372
Gorski, S.373
Goruppi, S.374
Gottlieb, R.A.375
Gozuacik, D.376
Granato, G.E.377
Grant, G.D.378
Green, K.N.379
Gregorc, A.380
Gros, F.381
Grose, C.382
Grunt, T.W.383
Gual, P.384
Guan, J.L.385
Guan, K.L.386
Guichard, S.M.387
Gukovskaya, A.S.388
Gukovsky, I.389
Gunst, J.390
Gustafsson, A.B.391
Halayko, A.J.392
Hale, A.N.393
Halonen, S.K.394
Hamasaki, M.395
Han, F.396
Han, T.397
Hancock, M.K.398
Hansen, M.399
Harada, H.400
Harada, M.401
Hardt, S.E.402
Harper, J.W.403
Harris, A.L.404
Harris, J.405
Harris, S.D.406
Hashimoto, M.407
Haspel, J.A.408
Hayashi, S.409
Hazelhurst, L.A.410
He, C.411
He, Y.W.412
Hebert, M.J.413
Heidenreich, K.A.414
Helfrich, M.H.415
Helgason, G.V.416
Henske, E.P.417
Herman, B.418
Herman, P.K.419
Hetz, C.420
Hilfiker, S.421
Hill, J.A.422
Hocking, L.J.423
Hofman, P.424
Hofmann, T.G.425
Hohfeld, J.426
Holyoake, T.L.427
Hong, M.H.428
Hood, D.A.429
Hotamisligil, G.S.430
Houwerzijl, E.J.431
Hoyer-Hansen, M.432
Hu, B.433
Hu, C.A.434
Hu, H.M.435
Hua, Y.436
Huang, C.437
Huang, J.438
Huang, S.439
Huang, W.P.440
Huber, T.B.441
Huh, W.K.442
Hung, T.H.443
Hupp, T.R.444
Hur, G.M.445
Hurley, J.B.446
Hussain, S.N.447
Hussey, P.J.448
Hwang, J.J.449
Hwang, S.450
Ichihara, A.451
Ilkhanizadeh, S.452
Inoki, K.453
Into, T.454
Iovane, V.455
Iovanna, J.L.456
Ip, N.Y.457
Isaka, Y.458
Ishida, H.459
Isidoro, C.460
Isobe, K.461
Iwasaki, A.462
Izquierdo, M.463
Izumi, Y.464
Jaakkola, P.M.465
Jaattela, M.466
Jackson, G.R.467
Jackson, W.T.468
Janji, B.469
Jendrach, M.470
Jeon, J.H.471
Jeung, E.B.472
Jiang, H.473
Jiang, J.X.474
Jiang, M.475
Jiang, Q.476
Jiang, X.477
Jimenez, A.478
Jin, M.479
Jin, S.480
Joe, C.O.481
Johansen, T.482
Johnson, D.E.483
Johnson, G.V.484
Jones, N.L.485
Joseph, B.486
Joseph, S.K.487
Joubert, A.M.488
Juhasz, G.489
Juillerat-Jeanneret, L.490
Jung, C.H.491
Jung, Y.K.492
Kaarniranta, K.493
Kaasik, A.494
Kabuta, T.495
Kadowaki, M.496
Kagedal, K.497
Kamada, Y.498
Kaminskyy, V.O.499
Kampinga, H.H.500
Kanamori, H.501
Kang, C.502
Kang, K.B.503
Kang, K.I.504
Kang, R.505
Kang, Y.A.506
Kanki, T.507
Kanneganti, T.D.508
Kanno, H.509
Kanthasamy, A.G.510
Kanthasamy, A.511
Karantza, V.512
Kaushal, G.P.513
Kaushik, S.514
Kawazoe, Y.515
Ke, P.Y.516
Kehrl, J.H.517
Kelekar, A.518
Kerkhoff, C.519
Kessel, D.H.520
Khalil, H.521
Kiel, J.A.522
Kiger, A.A.523
Kihara, A.524
Kim, D.R.525
Kim, D.H.526
Kim, E.K.527
Kim, H.R.528
Kim, J.S.529
Kim, J.H.530
Kim, J.C.531
Kim, J.K.532
Kim, P.K.533
Kim, S.W.534
Kim, Y.S.535
Kim, Y.536
Kimchi, A.537
Kimmelman, A.C.538
King, J.S.539
Kinsella, T.J.540
Kirkin, V.541
Kirshenbaum, L.A.542
Kitamoto, K.543
Kitazato, K.544
Klein, L.545
Klimecki, W.T.546
Klucken, J.547
Knecht, E.548
Ko, B.C.549
Koch, J.C.550
Koga, H.551
Koh, J.Y.552
Koh, Y.H.553
Koike, M.554
Komatsu, M.555
Kominami, E.556
Kong, H.J.557
Kong, W.J.558
Korolchuk, V.I.559
Kotake, Y.560
Koukourakis, M.I.561
Kouri Flores, J.B.562
Kovacs, A.L.563
Kraft, C.564
Krainc, D.565
Kramer, H.566
Kretz-Remy, C.567
Krichevsky, A.M.568
Kroemer, G.569
Kruger, R.570
Krut, O.571
Ktistakis, N.T.572
Kuan, C.Y.573
Kucharczyk, R.574
Kumar, A.575
Kumar, R.576
Kumar, S.577
Kundu, M.578
Kung, H.J.579
Kurz, T.580
Kwon, H.J.581
La Spada, A.R.582
Lafont, F.583
Lamark, T.584
Landry, J.585
Lane, J.D.586
Lapaquette, P.587
Laporte, J.F.588
Laszlo, L.589
Lavandero, S.590
Lavoie, J.N.591
Layfield, R.592
Lazo, P.A.593
Le, W.594
Le Cam, L.595
Ledbetter, D.J.596
Lee, A.J.597
Lee, B.W.598
Lee, G.M.599
Lee, J.600
Lee, J.H.601
Lee, M.602
Lee, M.S.603
Lee, S.H.604
Leeuwenburgh, C.605
Legembre, P.606
Legouis, R.607
Lehmann, M.608
Lei, H.Y.609
Lei, Q.Y.610
Leib, D.A.611
Leiro, J.612
Lemasters, J.J.613
Lemoine, A.614
Lesniak, M.S.615
Lev, D.616
Levenson, V.V.617
Levine, B.618
Levy, E.619
Li, F.620
Li, J.L.621
Li, L.622
Li, S.623
Li, W.624
Li, X.J.625
Li, Y.B.626
Li, Y.P.627
Liang, C.628
Liang, Q.629
Liao, Y.F.630
Liberski, P.P.631
Lieberman, A.632
Lim, H.J.633
Lim, K.L.634
Lim, K.635
Lin, C.F.636
Lin, F.C.637
Lin, J.638
Lin, J.D.639
Lin, K.640
Lin, W.W.641
Lin, W.C.642
Lin, Y.L.643
Linden, R.644
Lingor, P.645
Lippincott-Schwartz, J.646
Lisanti, M.P.647
Liton, P.B.648
Liu, B.649
Liu, C.F.650
Liu, K.651
Liu, L.652
Liu, Q.A.653
Liu, W.654
Liu, Y.C.655
Liu, Y.656
Lockshin, R.A.657
Lok, C.N.658
Lonial, S.659
Loos, B.660
Lopez-Berestein, G.661
Lopez-Otin, C.662
Lossi, L.663
Lotze, M.T.664
Low, P.665
Lu, B.666
Lu, Z.667
Luciano, F.668
Lukacs, N.W.669
Lund, A.H.670
Lynch-Day, M.A.671
Ma, Y.672
Macian, F.673
Mackeigan, J.P.674
Macleod, K.F.675
Madeo, F.676
Maiuri, L.677
Maiuri, M.C.678
Malagoli, D.679
Malicdan, M.C.680
Malorni, W.681
Man, N.682
Mandelkow, E.M.683
Manon, S.684
Manov, I.685
Mao, K.686
Mao, X.687
Mao, Z.688
Marambaud, P.689
Marazziti, D.690
Marcel, Y.L.691
Marchbank, K.692
Marchetti, P.693
Marciniak, S.J.694
Marcondes, M.695
Mardi, M.696
Marfe, G.697
Marino, G.698
Markaki, M.699
Marten, M.R.700
Martin, S.J.701
Martinand- Mari, C.702
Martinet, W.703
Martinez-Vicente, M.704
Masini, M.705
Matarrese, P.706
Matsuo, S.707
Matteoni, R.708
Mayer, A.709
Mazure, N.M.710
McConkey, D.J.711
McConnell, M.J.712
McDermott, C.713
McDonald, C.714
McInerney, G.M.715
McKenna, S.L.716
McLaughlin, B.717
McLean, P.J.718
McMaster, C.R.719
McQuibban, G.A.720
Meijer, A.J.721
Meisler, M.H.722
Melendez, A.723
Melia, T.J.724
Melino, G.725
Mena, M.A.726
Menendez, J.A.727
Menna-Barreto, R.F.728
Menon, M.B.729
Menzies, F.M.730
Mercer, C.A.731
Merighi, A.732
Merry, D.E.733
Meschini, S.734
Meyer, C.G.735
Meyer, T.F.736
Miao, C.Y.737
Miao, J.Y.738
Michels, P.A.739
Michiels, C.740
Mijaljica, D.741
Milojkovic, A.742
Minucci, S.743
Miracco, C.744
Miranti, C.K.745
Mitroulis, I.746
Miyazawa, K.747
Mizushima, N.748
Mograbi, B.749
Mohseni, S.750
Molero, X.751
Mollereau, B.752
Mollinedo, F.753
Momoi, T.754
Monastyrska, I.755
Monick, M.M.756
Monteiro, M.J.757
Moore, M.N.758
Mora, R.759
Moreau, K.760
Moreira, P.I.761
Moriyasu, Y.762
Moscat, J.763
Mostowy, S.764
Mottram, J.C.765
Motyl, T.766
Moussa, C.E.767
Muller, S.768
Munger, K.769
Munz, C.770
Murphy, L.O.771
Murphy, M.E.772
Musaro, A.773
Mysorekar, I.774
Nagata, E.775
Nagata, K.776
Nahimana, A.777
Nair, U.778
Nakagawa, T.779
Nakahira, K.780
Nakano, H.781
Nakatogawa, H.782
Nanjundan, M.783
Naqvi, N.I.784
Narendra, D.P.785
Narita, M.786
Navarro, M.787
Nawrocki, S.T.788
Nazarko, T.Y.789
Nemchenko, A.790
Netea, M.G.791
Neufeld, T.P.792
Ney, P.A.793
Nezis, I.P.794
Nguyen, H.P.795
Nie, D.796
Nishino, I.797
Nislow, C.798
Nixon, R.A.799
Noda, T.800
Noegel, A.A.801
Nogalska, A.802
Noguchi, S.803
Notterpek, L.804
Novak, I.805
Nozaki, T.806
Nukina, N.807
Nurnberger, T.808
Nyfeler, B.809
Obara, K.810
Oberley, T.D.811
Oddo, S.812
Ogawa, M.813
Ohashi, T.814
Okamoto, K.815
Oleinick, N.L.816
Oliver, F.J.817
Olsen, L.J.818
Olsson, S.819
Opota, O.820
Osborne, T.F.821
Ostrander, G.K.822
Otsu, K.823
Ou, J.H.824
Ouimet, M.825
Overholtzer, M.826
Ozpolat, B.827
Paganetti, P.828
Pagnini, U.829
Pallet, N.830
Palmer, G.E.831
Palumbo, C.832
Pan, T.833
Panaretakis, T.834
Pandey, U.B.835
Papackova, Z.836
Papassideri, I.837
Paris, I.838
Park, J.839
Park, O.K.840
Parys, J.B.841
Parzych, K.R.842
Patschan, S.843
Patterson, C.844
Pattingre, S.845
Pawelek, J.M.846
Peng, J.847
Perlmutter, D.H.848
Perrotta, I.849
Perry, G.850
Pervaiz, S.851
Peter, M.852
Peters, G.J.853
Petersen, M.854
Petrovski, G.855
Phang, J.M.856
Piacentini, M.857
Pierre, P.858
Pierrefite-Carle, V.859
Pierron, G.860
Pinkas-Kramarski, R.861
Piras, A.862
Piri, N.863
Platanias, L.C.864
Poggeler, S.865
Poirot, M.866
Poletti, A.867
Pous, C.868
Pozuelo-Rubio, M.869
Praetorius-Ibba, M.870
Prasad, A.871
Prescott, M.872
Priault, M.873
Produit- Zengaffinen, N.874
Progulske-Fox, A.875
Proikas-Cezanne, T.876
Przedborski, S.877
Przyklenk, K.878
Puertollano, R.879
Puyal, J.880
Qian, S.B.881
Qin, L.882
Qin, Z.H.883
Quaggin, S.E.884
Raben, N.885
Rabinowich, H.886
Rabkin, S.W.887
Rahman, I.888
Rami, A.889
Ramm, G.890
Randall, G.891
Randow, F.892
Rao, V.A.893
Rathmell, J.C.894
Ravikumar, B.895
Ray, S.K.896
Reed, B.H.897
Reed, J.C.898
Reggiori, F.899
Regnier-Vigouroux, A.900
Reichert, A.S.901
Reiners, J.J.902
Reiter, R.J.903
Ren, J.904
Revuelta, J.L.905
Rhodes, C.J.906
Ritis, K.907
Rizzo, E.908
Robbins, J.909
Roberge, M.910
Roca, H.911
Roccheri, M.C.912
Rocchi, S.913
Rodemann, H.P.914
Rodriguez De Cordoba, S.915
Rohrer, B.916
Roninson, I.B.917
Rosen, K.918
Rost-Roszkowska, M.M.919
Rouis, M.920
Rouschop, K.M.921
Rovetta, F.922
Rubin, B.P.923
Rubinsztein, D.C.924
Ruckdeschel, K.925
Rucker, E.B.926
Rudich, A.927
Rudolf, E.928
Ruiz-Opazo, N.929
Russo, R.930
Rusten, T.E.931
Ryan, K.M.932
Ryter, S.W.933
Sabatini, D.M.934
Sadoshima, J.935
Saha, T.936
Saitoh, T.937
Sakagami, H.938
Sakai, Y.939
Salekdeh, G.H.940
Salomoni, P.941
Salvaterra, P.M.942
Salvesen, G.943
Salvioli, R.944
Sanchez, A.M.945
Sanchez-Alcazar, J.A.946
Sanchez- Prieto, R.947
Sandri, M.948
Sankar, U.949
Sansanwal, P.950
Santambrogio, L.951
Saran, S.952
Sarkar, S.953
Sarwal, M.954
Sasakawa, C.955
Sasnauskiene, A.956
Sass, M.957
Sato, K.958
Sato, M.959
Schapira, A.H.960
Scharl, M.961
Schatzl, H.M.962
Scheper, W.963
Schiaffino, S.964
Schneider, C.965
Schneider, M.E.966
Schneider-Stock, R.967
Schoenlein, P.V.968
Schorderet, D.F.969
Schuller, C.970
Schwartz, G.K.971
Scorrano, L.972
Sealy, L.973
Seglen, P.O.974
Segura-Aguilar, J.975
Seiliez, I.976
Seleverstov, O.977
Sell, C.978
Seo, J.B.979
Separovic, D.980
Setaluri, V.981
Setoguchi, T.982
Settembre, C.983
Shacka, J.J.984
Shanmugam, M.985
Shapiro, I.M.986
Shaulian, E.987
Shaw, R.J.988
Shelhamer, J.H.989
Shen, H.M.990
Shen, W.C.991
Sheng, Z.H.992
Shi, Y.993
Shibuya, K.994
Shidoji, Y.995
Shieh, J.J.996
Shih, C.M.997
Shimada, Y.998
Shimizu, S.999
Shintani, T.1000
Shirihai, O.S.1001
Shore, G.C.1002
Sibirny, A.A.1003
Sidhu, S.B.1004
Sikorska, B.1005
Silva-Zacarin, E.C.1006
Simmons, A.1007
Simon, A.K.1008
Simon, H.U.1009
Simone, C.1010
Simonsen, A.1011
Sinclair, D.A.1012
Singh, R.1013
Sinha, D.1014
Sinicrope, F.A.1015
Sirko, A.1016
Siu, P.M.1017
Sivridis, E.1018
Skop, V.1019
Skulachev, V.P.1020
Slack, R.S.1021
Smaili, S.S.1022
Smith, D.R.1023
Soengas, M.S.1024
Soldati, T.1025
Song, X.1026
Sood, A.K.1027
Soong, T.W.1028
Sotgia, F.1029
Spector, S.A.1030
Spies, C.D.1031
Springer, W.1032
Srinivasula, S.M.1033
Stefanis, L.1034
Steffan, J.S.1035
Stendel, R.1036
Stenmark, H.1037
Stephanou, A.1038
Stern, S.T.1039
Sternberg, C.1040
Stork, B.1041
Stralfors, P.1042
Subauste, C.S.1043
Sui, X.1044
Sulzer, D.1045
Sun, J.1046
Sun, S.Y.1047
Sun, Z.J.1048
Sung, J.J.1049
Suzuki, K.1050
Suzuki, T.1051
Swanson, M.S.1052
Swanton, C.1053
Sweeney, S.T.1054
Sy, L.K.1055
Szabadkai, G.1056
Tabas, I.1057
Taegtmeyer, H.1058
Tafani, M.1059
Takacs-Vellai, K.1060
Takano, Y.1061
Takegawa, K.1062
Takemura, G.1063
Takeshita, F.1064
Talbot, N.J.1065
Tan, K.S.1066
Tanaka, K.1067
Tang, D.1068
Tanida, I.1069
Tannous, B.A.1070
Tavernarakis, N.1071
Taylor, G.S.1072
Taylor, G.A.1073
Taylor, J.P.1074
Terada, L.S.1075
Terman, A.1076
Tettamanti, G.1077
Thevissen, K.1078
Thompson, C.B.1079
Thorburn, A.1080
Thumm, M.1081
Tian, F.1082
Tian, Y.1083
Tocchini-Valentini, G.1084
Tolkovsky, A.M.1085
Tomino, Y.1086
Tonges, L.1087
Tooze, S.A.1088
Tournier, C.1089
Tower, J.1090
Towns, R.1091
Trajkovic, V.1092
Travassos, L.H.1093
Tsai, T.F.1094
Tschan, M.P.1095
Tsubata, T.1096
Tsung, A.1097
Turk, B.1098
Turner, L.S.1099
Tyagi, S.C.1100
Uchiyama, Y.1101
Ueno, T.1102
Umekawa, M.1103
Umemiya-Shirafuji, R.1104
Unni, V.K.1105
Vaccaro, M.I.1106
Valente, E.M.1107
Van Den Berghe, G.1108
Van Der Klei, I.J.1109
Van Doorn, W.1110
Van Dyk, L.F.1111
Van Egmond, M.1112
Van Grunsven, L.A.1113
Vandenabeele, P.1114
Vandenberghe, W.P.1115
Vanhorebeek, I.1116
Vaquero, E.C.1117
Velasco, G.1118
Vellai, T.1119
Vicencio, J.M.1120
Vierstra, R.D.1121
Vila, M.1122
Vindis, C.1123
Viola, G.1124
Viscomi, M.T.1125
Voitsekhovskaja, O.V.1126
Von Haefen, C.1127
Votruba, M.1128
Wada, K.1129
Wade-Martins, R.1130
Walker, C.L.1131
Walsh, C.M.1132
Walter, J.1133
Wan, X.B.1134
Wang, A.1135
Wang, C.1136
Wang, D.1137
Wang, F.1138
Wang, G.1139
Wang, H.1140
Wang, H.G.1141
Wang, H.D.1142
Wang, J.1143
Wang, K.1144
Wang, M.1145
Wang, R.C.1146
Wang, X.1147
Wang, Y.J.1148
Wang, Y.1149
Wang, Z.1150
Wang, Z.C.1151
Wansink, D.G.1152
Ward, D.M.1153
Watada, H.1154
Waters, S.L.1155
Webster, P.1156
Wei, L.1157
Weihl, C.C.1158
Weiss, W.A.1159
Welford, S.M.1160
Wen, L.P.1161
Whitehouse, C.A.1162
Whitton, J.L.1163
Whitworth, A.J.1164
Wileman, T.1165
Wiley, J.W.1166
Wilkinson, S.1167
Willbold, D.1168
Williams, R.L.1169
Williamson, P.R.1170
Wouters, B.G.1171
Wu, C.1172
Wu, D.C.1173
Wu, W.K.1174
Wyttenbach, A.1175
Xavier, R.J.1176
Xi, Z.1177
Xia, P.1178
Xiao, G.1179
Xie, Z.1180
Xu, D.Z.1181
Xu, J.1182
Xu, L.1183
Xu, X.1184
Yamamoto, A.1185
Yamashina, S.1186
Yamashita, M.1187
Yan, X.1188
Yanagida, M.1189
Yang, D.S.1190
Yang, E.1191
Yang, J.M.1192
Yang, S.Y.1193
Yang, W.1194
Yang, W.Y.1195
Yang, Z.1196
Yao, M.C.1197
Yao, T.P.1198
Yeganeh, B.1199
Yen, W.L.1200
Yin, J.J.1201
Yin, X.M.1202
Yoo, O.J.1203
Yoon, G.1204
Yoon, S.Y.1205
Yorimitsu, T.1206
Yoshikawa, Y.1207
Yoshimori, T.1208
Yoshimoto, K.1209
You, H.J.1210
Youle, R.J.1211
Younes, A.1212
Yu, L.1213
Yu, S.W.1214
Yu, W.H.1215
Yuan, Z.M.1216
Yue, Z.1217
Yun, C.H.1218
Yuzaki, M.1219
Zabirnyk, O.1220
Silva-Zacarin, E.1221
Zacks, D.1222
Zacksenhaus, E.1223
Zaffaroni, N.1224
Zakeri, Z.1225
Zeh, H.J.1226
Zeitlin, S.O.1227
Zhang, H.1228
Zhang, H.L.1229
Zhang, J.1230
Zhang, J.P.1231
Zhang, L.1232
Zhang, M.Y.1233
Zhang, X.D.1234
Zhao, M.1235
Zhao, Y.F.1236
Zhao, Y.1237
Zhao, Z.J.1238
Zheng, X.1239
Zhivotovsky, B.1240
Zhong, Q.1241
Zhou, C.Z.1242
Zhu, C.1243
Zhu, W.G.1244
Zhu, X.F.1245
Zhu, X.1246
Zhu, Y.1247
Zoladek, T.1248
Zong, W.X.1249
Zorzano, A.1250
Zschocke, J.1251
Zuckerbraun, B.1252
more..
-
52
-
-
58149084405
-
Ordered organelle degradation during starvation-induced autophagy
-
Kristensen AR, Schandorff S, Hoyer-Hansen M, Nielsen MO, Jaattela M, Dengjel J, Andersen JS. Ordered organelle degradation during starvation-induced autophagy. Mol Cell Proteomics 7: 2419-2428, 2008.
-
(2008)
Mol Cell Proteomics
, vol.7
, pp. 2419-2428
-
-
Kristensen, A.R.1
Schandorff, S.2
Hoyer-Hansen, M.3
Nielsen, M.O.4
Jaattela, M.5
Dengjel, J.6
Ersen, J.S.7
-
53
-
-
34250900953
-
LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: Caution in the interpretation of LC3 localization
-
Kuma A, Matsui M, Mizushima N. LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: caution in the interpretation of LC3 localization. Autophagy 3: 323-328, 2007.
-
(2007)
Autophagy
, vol.3
, pp. 323-328
-
-
Kuma, A.1
Matsui, M.2
Mizushima, N.3
-
54
-
-
77951157657
-
Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney
-
Kume S, Uzu T, Horiike K, Chin-Kanasaki M, Isshiki K, Araki S, Sugimoto T, Haneda M, Kashiwagi A, Koya D. Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney. J Clin Invest 120: 1043-1055, 2010.
-
(2010)
J Clin Invest
, vol.120
, pp. 1043-1055
-
-
Kume, S.1
Uzu, T.2
Horiike, K.3
Chin-Kanasaki, M.4
Isshiki, K.5
Araki, S.6
Sugimoto, T.7
Haneda, M.8
Kashiwagi, A.9
Koya, D.10
-
55
-
-
0037021505
-
The metabolic syndrome and total and cardiovascular disease mortality in middle-aged men
-
Lakka HM, Laaksonen DE, Lakka TA, Niskanen LK, Kumpusalo E, Tuomilehto J, Salonen JT. The metabolic syndrome and total and cardiovascular disease mortality in middle-aged men. JAMA 288: 2709-2716, 2002.
-
(2002)
JAMA
, vol.288
, pp. 2709-2716
-
-
Lakka, H.M.1
Laaksonen, D.E.2
Lakka, T.A.3
Niskanen, L.K.4
Kumpusalo, E.5
Tuomilehto, J.6
Salonen, J.T.7
-
56
-
-
55549096745
-
SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation
-
Lan F, Cacicedo JM, Ruderman N, Ido Y. SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation. J Biol Chem 283: 27628-27635, 2008.
-
(2008)
J Biol Chem
, vol.283
, pp. 27628-27635
-
-
Lan, F.1
Cacicedo, J.M.2
Ruderman, N.3
Ido, Y.4
-
57
-
-
84864120303
-
Translational evidence that impaired autophagy contributes to arterial ageing
-
LaRocca TJ, Henson GD, Thorburn A, Sindler AL, Pierce GL, Seals DR. Translational evidence that impaired autophagy contributes to arterial ageing. J Physiol 590: 3305-3316, 2012.
-
(2012)
J Physiol
, vol.590
, pp. 3305-3316
-
-
Larocca, T.J.1
Henson, G.D.2
Thorburn, A.3
Sindler, A.L.4
Pierce, G.L.5
Seals, D.R.6
-
58
-
-
84897115531
-
On ceramides, other sphingolipids and impaired glucose homeostasis
-
Larsen PJ, Tennagels N. On ceramides, other sphingolipids and impaired glucose homeostasis. Mol Metab 3: 252-260, 2014.
-
(2014)
Mol Metab
, vol.3
, pp. 252-260
-
-
Larsen, P.J.1
Tennagels, N.2
-
59
-
-
82755195229
-
Fatty acids suppress autophagic turnover in beta-cells
-
Las G, Serada SB, Wikstrom JD, Twig G, Shirihai OS. Fatty acids suppress autophagic turnover in beta-cells. J Biol Chem 286: 42534-42544, 2011.
-
(2011)
J Biol Chem
, vol.286
, pp. 42534-42544
-
-
Las, G.1
Serada, S.B.2
Wikstrom, J.D.3
Twig, G.4
Shirihai, O.S.5
-
60
-
-
41549138483
-
A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
-
Lee IH, Cao L, Mostoslavsky R, Lombard DB, Liu J, Bruns NE, Tsokos M, Alt FW, Finkel T. A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proc Natl Acad Sci USA 105: 3374-3379, 2008.
-
(2008)
Proc Natl Acad Sci USA
, vol.105
, pp. 3374-3379
-
-
Lee, I.H.1
Cao, L.2
Mostoslavsky, R.3
Lombard, D.B.4
Liu, J.5
Bruns, N.E.6
Tsokos, M.7
Alt, F.W.8
Finkel, T.9
-
62
-
-
84904514591
-
AMPK activation prevents excess nutrient-induced hepatic lipid accumulation by inhibiting mTORC1 signaling and endoplasmic reticulum stress response
-
Li H, Min Q, Ouyang C, Lee J, He C, Zou MH, Xie Z. AMPK activation prevents excess nutrient-induced hepatic lipid accumulation by inhibiting mTORC1 signaling and endoplasmic reticulum stress response. Biochim Biophys Acta 1842: 1844-1854, 2014.
-
(2014)
Biochim Biophys Acta
, vol.1842
, pp. 1844-1854
-
-
Li, H.1
Min, Q.2
Ouyang, C.3
Lee, J.4
He, C.5
Zou, M.H.6
Xie, Z.7
-
63
-
-
84902536913
-
Prevalence and clinical characteristics of lower limb atherosclerotic lesions in newly diagnosed patients with ketosis-onset diabetes: A cross-sectional study
-
Li MF, Ren Y, Zhao CC, Zhang R, Li LX, Liu F, Lu JX, Tu YF, Zhao WJ, Bao YQ, Jia WP. Prevalence and clinical characteristics of lower limb atherosclerotic lesions in newly diagnosed patients with ketosis-onset diabetes: a cross-sectional study. Diabetol Metab Syndr 6: 71, 2014.
-
(2014)
Diabetol Metab Syndr
, vol.6
-
-
Li, M.F.1
Ren, Y.2
Zhao, C.C.3
Zhang, R.4
Li, L.X.5
Liu, F.6
Lu, J.X.7
Tu, Y.F.8
Zhao, W.J.9
Bao, Y.Q.10
Jia, W.P.11
-
64
-
-
79959963047
-
Ulk1- mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop
-
Loffler AS, Alers S, Dieterle AM, Keppeler H, Franz-Wachtel M, Kundu M, Campbell DG, Wesselborg S, Alessi DR, Stork B. Ulk1- mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop. Autophagy 7: 696-706, 2011.
-
(2011)
Autophagy
, vol.7
, pp. 696-706
-
-
Loffler, A.S.1
Alers, S.2
Dieterle, A.M.3
Keppeler, H.4
Franz-Wachtel, M.5
Kundu, M.6
Campbell, D.G.7
Wesselborg, S.8
Alessi, D.R.9
Stork, B.10
-
65
-
-
84879411171
-
Palmitate induces apoptosis in mouse aortic endothelial cells and endothelial dysfunction in mice fed high-calorie and high-cholesterol diets
-
Lu Y, Qian L, Zhang Q, Chen B, Gui L, Huang D, Chen G, Chen L. Palmitate induces apoptosis in mouse aortic endothelial cells and endothelial dysfunction in mice fed high-calorie and high-cholesterol diets. Life Sci 92: 1165-1173, 2013.
-
(2013)
Life Sci
, vol.92
, pp. 1165-1173
-
-
Lu, Y.1
Qian, L.2
Zhang, Q.3
Chen, B.4
Gui, L.5
Huang, D.6
Chen, G.7
Chen, L.8
-
66
-
-
79952797615
-
Identification of PTPsigma as an autophagic phosphatase
-
Martin KR, Xu Y, Looyenga BD, Davis RJ, Wu CL, Tremblay ML, Xu HE, MacKeigan JP. Identification of PTPsigma as an autophagic phosphatase. J Cell Sci 124: 812-819, 2011.
-
(2011)
J Cell Sci
, vol.124
, pp. 812-819
-
-
Martin, K.R.1
Xu, Y.2
Looyenga, B.D.3
Davis, R.J.4
Wu, C.L.5
Tremblay, M.L.6
Xu, H.E.7
Mackeigan, J.P.8
-
67
-
-
0031425839
-
AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle
-
Merrill GF, Kurth EJ, Hardie DG, Winder WW. AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle. Am J Physiol Endocrinol Metab 273: E1107-E1112, 1997.
-
(1997)
Am J Physiol Endocrinol Metab
, vol.273
, pp. E1107-E1112
-
-
Merrill, G.F.1
Kurth, E.J.2
Hardie, D.G.3
Winder, W.W.4
-
68
-
-
34250303104
-
Genomewide analysis of histone lysine methylation variations caused by diabetic conditions in human monocytes
-
Miao F, Wu X, Zhang L, Yuan YC, Riggs AD, Natarajan R. Genomewide analysis of histone lysine methylation variations caused by diabetic conditions in human monocytes. J Biol Chem 282: 13854-13863, 2007.
-
(2007)
J Biol Chem
, vol.282
, pp. 13854-13863
-
-
Miao, F.1
Wu, X.2
Zhang, L.3
Yuan, Y.C.4
Riggs, A.D.5
Natarajan, R.6
-
69
-
-
0037339730
-
Nocturnal and postprandial free fatty acid kinetics in normal and type 2 diabetic subjects: Effects of insulin sensitization therapy
-
Miles JM, Wooldridge D, Grellner WJ, Windsor S, Isley WL, Klein S, Harris WS. Nocturnal and postprandial free fatty acid kinetics in normal and type 2 diabetic subjects: effects of insulin sensitization therapy. Diabetes 52: 675-681, 2003.
-
(2003)
Diabetes
, vol.52
, pp. 675-681
-
-
Miles, J.M.1
Wooldridge, D.2
Grellner, W.J.3
Windsor, S.4
Isley, W.L.5
Klein, S.6
Harris, W.S.7
-
70
-
-
0035911162
-
Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
-
Mizushima N, Yamamoto A, Hatano M, Kobayashi Y, Kabeya Y, Suzuki K, Tokuhisa T, Ohsumi Y, Yoshimori T. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol 152: 657-668, 2001.
-
(2001)
J Cell Biol
, vol.152
, pp. 657-668
-
-
Mizushima, N.1
Yamamoto, A.2
Hatano, M.3
Kobayashi, Y.4
Kabeya, Y.5
Suzuki, K.6
Tokuhisa, T.7
Ohsumi, Y.8
Yoshimori, T.9
-
71
-
-
84880478801
-
Functional loss of two ceramide synthases elicits autophagy-dependent lifespan extension in C
-
Mosbech MB, Kruse R, Harvald EB, Olsen AS, Gallego SF, Hannibal- Bach HK, Ejsing CS, Faergeman NJ. Functional loss of two ceramide synthases elicits autophagy-dependent lifespan extension in C. elegans. PLos One 8: e70087, 2013.
-
(2013)
Elegans. Plos One
, vol.8
-
-
Mosbech, M.B.1
Kruse, R.2
Harvald, E.B.3
Olsen, A.S.4
Gallego, S.F.5
Hannibal- Bach, H.K.6
Ejsing, C.S.7
Faergeman, N.J.8
-
72
-
-
84863513522
-
A novel inverse relationship between metformin-triggered AMPK-SIRT1 signaling and p53 protein abundance in high glucoseexposed HepG2 cells
-
Nelson LE, Valentine RJ, Cacicedo JM, Gauthier MS, Ido Y, Ruderman NB. A novel inverse relationship between metformin-triggered AMPK-SIRT1 signaling and p53 protein abundance in high glucoseexposed HepG2 cells. Am J Physiol Cell Physiol 303: C4-C13, 2012.
-
(2012)
Am J Physiol Cell Physiol
, vol.303
, pp. C4-C13
-
-
Nelson, L.E.1
Valentine, R.J.2
Cacicedo, J.M.3
Gauthier, M.S.4
Ido, Y.5
Ruderman, N.B.6
-
73
-
-
84867278754
-
Oxidative stress impairs autophagic flux in prion protein-deficient hippocampal cells
-
Oh JM, Choi EK, Carp RI, Kim YS. Oxidative stress impairs autophagic flux in prion protein-deficient hippocampal cells. Autophagy 8: 1448-1461, 2012.
-
(2012)
Autophagy
, vol.8
, pp. 1448-1461
-
-
Oh, J.M.1
Choi, E.K.2
Carp, R.I.3
Kim, Y.S.4
-
74
-
-
0020146576
-
Endogenous triacylglycerol metabolism in diabetic heart
-
Paulson DJ, Crass MF 3rd. Endogenous triacylglycerol metabolism in diabetic heart. Am J Physiol Heart Circ Physiol 242: H1084-H1094, 1982.
-
(1982)
Am J Physiol Heart Circ Physiol
, vol.242
, pp. H1084-H1094
-
-
Paulson, D.J.1
Crass, M.F.2
-
75
-
-
84859448447
-
Autophagy links inflammasomes to atherosclerotic progression
-
Razani B, Feng C, Coleman T, Emanuel R, Wen H, Hwang S, Ting JP, Virgin HW, Kastan MB, Semenkovich CF. Autophagy links inflammasomes to atherosclerotic progression. Cell Metab 15: 534-544, 2012.
-
(2012)
Cell Metab
, vol.15
, pp. 534-544
-
-
Razani, B.1
Feng, C.2
Coleman, T.3
Emanuel, R.4
Wen, H.5
Hwang, S.6
Ting, J.P.7
Virgin, H.W.8
Kastan, M.B.9
Semenkovich, C.F.10
-
76
-
-
0024244339
-
Measurement of plasma glucose, free fatty acid, lactate, and insulin for 24 h in patients with NIDDM
-
Reaven GM, Hollenbeck C, Jeng CY, Wu MS, Chen YD. Measurement of plasma glucose, free fatty acid, lactate, and insulin for 24 h in patients with NIDDM. Diabetes 37: 1020-1024, 1988.
-
(1988)
Diabetes
, vol.37
, pp. 1020-1024
-
-
Reaven, G.M.1
Hollenbeck, C.2
Jeng, C.Y.3
Wu, M.S.4
Chen, Y.D.5
-
78
-
-
77953821528
-
Diabetes mellitus, fasting blood glucose concentration, and risk of vascular disease: A collaborative meta-analysis of 102 prospective studies
-
Sarwar N, Gao P, Seshasai SR, Gobin R, Kaptoge S, Di Angelantonio E, Ingelsson E, Lawlor DA, Selvin E, Stampfer M, Stehouwer CD, Lewington S, Pennells L, Thompson A, Sattar N, White IR, Ray KK, Danesh J. Diabetes mellitus, fasting blood glucose concentration, and risk of vascular disease: a collaborative meta-analysis of 102 prospective studies. Lancet 375: 2215-2222, 2010.
-
(2010)
Lancet
, vol.375
, pp. 2215-2222
-
-
Sarwar, N.1
Gao, P.2
Seshasai, S.R.3
Gobin, R.4
Kaptoge, S.5
Di Angelantonio, E.6
Ingelsson, E.7
Lawlor, D.A.8
Selvin, E.9
Stampfer, M.10
Stehouwer, C.D.11
Lewington, S.12
Pennells, L.13
Thompson, A.14
Sattar, N.15
White, I.R.16
Ray, K.K.17
Danesh, J.18
-
79
-
-
34247186472
-
Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
-
Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26: 1749-1760, 2007.
-
(2007)
EMBO J
, vol.26
, pp. 1749-1760
-
-
Scherz-Shouval, R.1
Shvets, E.2
Fass, E.3
Shorer, H.4
Gil, L.5
Elazar, Z.6
-
80
-
-
33748934390
-
Improving macrovascular outcomes in type 2 diabetes: Outcome studies in cardiovascular risk and metabolic control
-
Schneider CA. Improving macrovascular outcomes in type 2 diabetes: Outcome studies in cardiovascular risk and metabolic control. Curr Med Res Opin 22, Suppl 2: S15-S26, 2006.
-
(2006)
Curr Med Res Opin
, vol.22
, pp. S15-S26
-
-
Schneider, C.A.1
-
81
-
-
57849131142
-
Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells
-
Suchankova G, Nelson LE, Gerhart-Hines Z, Kelly M, Gauthier MS, Saha AK, Ido Y, Puigserver P, Ruderman NB. Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells. Biochem Biophys Res Commun 378: 836-841, 2009.
-
(2009)
Biochem Biophys Res Commun
, vol.378
, pp. 836-841
-
-
Suchankova, G.1
Nelson, L.E.2
Gerhart-Hines, Z.3
Kelly, M.4
Gauthier, M.S.5
Saha, A.K.6
Ido, Y.7
Puigserver, P.8
Ruderman, N.B.9
-
82
-
-
0028073143
-
Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase
-
Sullivan JE, Brocklehurst KJ, Marley AE, Carey F, Carling D, Beri RK. Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase. FEBS Lett 353: 33-36, 1994.
-
(1994)
FEBS Lett
, vol.353
, pp. 33-36
-
-
Sullivan, J.E.1
Brocklehurst, K.J.2
Marley, A.E.3
Carey, F.4
Carling, D.5
Beri, R.K.6
-
83
-
-
33845707278
-
Statins activate AMP-activated protein kinase in vitro and in vivo
-
Sun W, Lee TS, Zhu M, Gu C, Wang Y, Zhu Y, Shyy JY. Statins activate AMP-activated protein kinase in vitro and in vivo. Circulation 114: 2655-2662, 2006.
-
(2006)
Circulation
, vol.114
, pp. 2655-2662
-
-
Sun, W.1
Lee, T.S.2
Zhu, M.3
Gu, C.4
Wang, Y.5
Zhu, Y.6
Shyy, J.Y.7
-
84
-
-
84867627541
-
SIRT1 inactivation induces inflammation through the dysregulation of autophagy in human THP-1 cells
-
Takeda-Watanabe A, Kitada M, Kanasaki K, Koya D. SIRT1 inactivation induces inflammation through the dysregulation of autophagy in human THP-1 cells. Biochem Biophys Res Commun 427: 191-196, 2012.
-
(2012)
Biochem Biophys Res Commun
, vol.427
, pp. 191-196
-
-
Takeda-Watanabe, A.1
Kitada, M.2
Kanasaki, K.3
Koya, D.4
-
85
-
-
84869208878
-
Regulation of autophagy and its associated cell death by “sphingolipid rheostat”: Reciprocal role of ceramide and sphingosine 1-phosphate in the mammalian target of rapamycin pathway
-
Taniguchi M, Kitatani K, Kondo T, Hashimoto-Nishimura M, Asano S, Hayashi A, Mitsutake S, Igarashi Y, Umehara H, Takeya H, Kigawa J, Okazaki T. Regulation of autophagy and its associated cell death by “sphingolipid rheostat”: reciprocal role of ceramide and sphingosine 1-phosphate in the mammalian target of rapamycin pathway. J Biol Chem 287: 39898-39910, 2012.
-
(2012)
J Biol Chem
, vol.287
, pp. 39898-39910
-
-
Taniguchi, M.1
Kitatani, K.2
Kondo, T.3
Hashimoto-Nishimura, M.4
Asano, S.5
Hayashi, A.6
Mitsutake, S.7
Igarashi, Y.8
Umehara, H.9
Takeya, H.10
Kigawa, J.11
Okazaki, T.12
-
86
-
-
68249153748
-
Control of autophagy initiation by phosphoinositide 3-phosphatase Jumpy
-
Vergne I, Roberts E, Elmaoued RA, Tosch V, Delgado MA, Proikas- Cezanne T, Laporte J, Deretic V. Control of autophagy initiation by phosphoinositide 3-phosphatase Jumpy. EMBO J 28: 2244-2258, 2009.
-
(2009)
EMBO J
, vol.28
, pp. 2244-2258
-
-
Vergne, I.1
Roberts, E.2
Elmaoued, R.A.3
Tosch, V.4
Delgado, M.A.5
Proikas- Cezanne, T.6
Laporte, J.7
Deretic, V.8
-
87
-
-
80053196866
-
Activation of AMP-activated protein kinase is required for berberine-induced reduction of atherosclerosis in mice: The role of uncoupling protein 2
-
Wang Q, Zhang M, Liang B, Shirwany N, Zhu Y, Zou MH. Activation of AMP-activated protein kinase is required for berberine-induced reduction of atherosclerosis in mice: the role of uncoupling protein 2. PLos One 6: e25436, 2011.
-
(2011)
Plos One
, vol.6
-
-
Wang, Q.1
Zhang, M.2
Liang, B.3
Shirwany, N.4
Zhu, Y.5
Zou, M.H.6
-
88
-
-
84860296724
-
AMP-activated protein kinase, stress responses and cardiovascular diseases
-
Wang S, Song P, Zou MH. AMP-activated protein kinase, stress responses and cardiovascular diseases. Clin Sci (Lond) 122: 555-573, 2012.
-
(2012)
Clin Sci (Lond)
, vol.122
, pp. 555-573
-
-
Wang, S.1
Song, P.2
Zou, M.H.3
-
89
-
-
79955038882
-
Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling
-
Wen H, Gris D, Lei Y, Jha S, Zhang L, Huang MT, Brickey WJ, Ting JP. Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling. Nat Immunol 12: 408-415, 2011.
-
(2011)
Nat Immunol
, vol.12
, pp. 408-415
-
-
Wen, H.1
Gris, D.2
Lei, Y.3
Jha, S.4
Zhang, L.5
Huang, M.T.6
Brickey, W.J.7
Ting, J.P.8
-
90
-
-
84884819157
-
Autophagosome formation-The role of ULK1 and Beclin1-PI3KC3 complexes in setting the stage
-
Wirth M, Joachim J, Tooze SA. Autophagosome formation-The role of ULK1 and Beclin1-PI3KC3 complexes in setting the stage. Semin Cancer Biol 23: 301-309, 2013.
-
(2013)
Semin Cancer Biol
, vol.23
, pp. 301-309
-
-
Wirth, M.1
Joachim, J.2
Tooze, S.A.3
-
91
-
-
0033815967
-
Characterization of the role of AMPactivated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase
-
Woods A, Azzout-Marniche D, Foretz M, Stein SC, Lemarchand P, Ferre P, Foufelle F, Carling D. Characterization of the role of AMPactivated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase. Mol Cell Biol 20: 6704-6711, 2000.
-
(2000)
Mol Cell Biol
, vol.20
, pp. 6704-6711
-
-
Woods, A.1
Azzout-Marniche, D.2
Foretz, M.3
Stein, S.C.4
Lemarchand, P.5
Ferre, P.6
Foufelle, F.7
Carling, D.8
-
92
-
-
34248199965
-
Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase
-
Wu Y, Song P, Xu J, Zhang M, Zou MH. Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase. J Biol Chem 282: 9777-9788, 2007.
-
(2007)
J Biol Chem
, vol.282
, pp. 9777-9788
-
-
Wu, Y.1
Song, P.2
Xu, J.3
Zhang, M.4
Zou, M.H.5
-
93
-
-
47549092694
-
Atg8 controls phagophore expansion during autophagosome formation
-
Xie Z, Nair U, Klionsky DJ. Atg8 controls phagophore expansion during autophagosome formation. Mol Biol Cell 19: 3290-3298, 2008.
-
(2008)
Mol Biol Cell
, vol.19
, pp. 3290-3298
-
-
Xie, Z.1
Nair, U.2
Klionsky, D.J.3
-
94
-
-
83655172387
-
The link between metabolic abnormalities and endothelial dysfunction in type 2 diabetes: An update
-
Zhang H, Dellsperger KC, Zhang C. The link between metabolic abnormalities and endothelial dysfunction in type 2 diabetes: an update. Basic Res Cardiol 107: 237, 2012.
-
(2012)
Basic Res Cardiol
, vol.107
-
-
Zhang, H.1
Dellsperger, K.C.2
Zhang, C.3
-
95
-
-
84863205222
-
Ceramide mediates vascular dysfunction in diet-induced obesity by PP2Amediated dephosphorylation of the eNOS-Akt complex
-
Zhang QJ, Holland WL, Wilson L, Tanner JM, Kearns D, Cahoon JM, Pettey D, Losee J, Duncan B, Gale D, Kowalski CA, Deeter N, Nichols A, Deesing M, Arrant C, Ruan T, Boehme C, McCamey DR, Rou J, Ambal K, Narra KK, Summers SA, Abel ED, Symons JD. Ceramide mediates vascular dysfunction in diet-induced obesity by PP2Amediated dephosphorylation of the eNOS-Akt complex. Diabetes 61: 1848-1859, 2013.
-
(2013)
Diabetes
, vol.61
, pp. 1848-1859
-
-
Zhang, Q.J.1
Holland, W.L.2
Wilson, L.3
Tanner, J.M.4
Kearns, D.5
Cahoon, J.M.6
Pettey, D.7
Losee, J.8
Duncan, B.9
Gale, D.10
Kowalski, C.A.11
Deeter, N.12
Nichols, A.13
Deesing, M.14
Arrant, C.15
Ruan, T.16
Boehme, C.17
McCamey, D.R.18
Rou, J.19
Ambal, K.20
Narra, K.K.21
Summers, S.A.22
Abel, E.D.23
Symons, J.D.24
more..
-
96
-
-
0034773404
-
Role of AMP-activated protein kinase in mechanism of metformin action
-
Zhou G, Myers R, Li Y, Chen Y, Shen X, Fenyk-Melody J, Wu M, Ventre J, Doebber T, Fujii N, Musi N, Hirshman MF, Goodyear LJ, Moller DE. Role of AMP-activated protein kinase in mechanism of metformin action. J Clin Invest 108: 1167-1174, 2001.
-
(2001)
J Clin Invest
, vol.108
, pp. 1167-1174
-
-
Zhou, G.1
Myers, R.2
Li, Y.3
Chen, Y.4
Shen, X.5
Fenyk-Melody, J.6
Wu, M.7
Ventre, J.8
Doebber, T.9
Fujii, N.10
Musi, N.11
Hirshman, M.F.12
Goodyear, L.J.13
Moller, D.E.14
|