메뉴 건너뛰기




Volumn 8, Issue 1, 2017, Pages

The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs

Author keywords

[No Author keywords available]

Indexed keywords

6,7 DIHYDRO 4 HYDROXY 3 (2' HYDROXY 1,1' BIPHENYL 4 YL) 6 OXOTHIENO[2,3 B]PYRIDINE 5 CARBONITRILE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; P21 ACTIVATED KINASE 2; PHENFORMIN; SERINE THREONINE PROTEIN KINASE ULK1; THREONINE; PYRONE DERIVATIVE; SALICYLIC ACID DERIVATIVE; THIOPHENE DERIVATIVE;

EID: 85029584631     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/s41467-017-00628-y     Document Type: Article
Times cited : (65)

References (59)
  • 1
    • 84919621076 scopus 로고    scopus 로고
    • AMPK-sensing energy while talking to other signaling pathways
    • Hardie, D. G. AMPK-sensing energy while talking to other signaling pathways. Cell Metab. 20, 939-952 (2014).
    • (2014) Cell Metab. , vol.20 , pp. 939-952
    • Hardie, D.G.1
  • 2
    • 67650914230 scopus 로고    scopus 로고
    • AMPK in health and disease
    • Steinberg, G. R. & Kemp, B. E. AMPK in health and disease. Physiol. Rev. 89, 1025-1078 (2009).
    • (2009) Physiol. Rev. , vol.89 , pp. 1025-1078
    • Steinberg, G.R.1    Kemp, B.E.2
  • 3
    • 78650606464 scopus 로고    scopus 로고
    • A-subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by amp-activated protein kinase (ampk)
    • Oakhill, J. S. et al. ?-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK). Proc. Natl Acad. Sci. USA 107, 19237-19241 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19237-19241
    • Oakhill, J.S.1
  • 4
    • 84892933078 scopus 로고    scopus 로고
    • Investigation of lkb1 ser431 phosphorylation and cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating ampk activity
    • Houde, V. P. et al. Investigation of LKB1 Ser431 phosphorylation and Cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating AMPK activity. Biochem. J. 15, 41-56 (2014).
    • (2014) Biochem. J. , vol.15 , pp. 41-56
    • Houde, V.P.1
  • 5
    • 79954517977 scopus 로고    scopus 로고
    • Structure of mammalian ampk and its regulation by adp
    • Xiao, B. et al. Structure of mammalian AMPK and its regulation by ADP. Nature 472, 230-233 (2011).
    • (2011) Nature , vol.472 , pp. 230-233
    • Xiao, B.1
  • 6
    • 79959338922 scopus 로고    scopus 로고
    • AMPK is a direct adenylate charge-regulated protein kinase
    • Oakhill, J. S. et al. AMPK is a direct adenylate charge-regulated protein kinase. Science 332, 1433-1435 (2011).
    • (2011) Science , vol.332 , pp. 1433-1435
    • Oakhill, J.S.1
  • 7
    • 84863719838 scopus 로고    scopus 로고
    • AMP-activated protein kinase undergoes nucleotide-dependent conformational changes
    • Chen, L. et al. AMP-activated protein kinase undergoes nucleotide-dependent conformational changes. Nat. Struct. Mol. Biol. 19, 716-718 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 716-718
    • Chen, L.1
  • 8
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the amp-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates amp-activated protein kinase
    • Hawley, S. A. et al. Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J. Biol. Chem. 271, 27879-27887 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 27879-27887
    • Hawley, S.A.1
  • 9
    • 85047691317 scopus 로고    scopus 로고
    • CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations
    • Scott, J. W. et al. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 113, 274-284 (2004).
    • (2004) J. Clin. Invest. , vol.113 , pp. 274-284
    • Scott, J.W.1
  • 10
    • 84960416125 scopus 로고    scopus 로고
    • Structural basis of allosteric and synergistic activation of ampk by furan-2-phosphonic derivative c2 binding
    • Langendorf, C. G. et al. Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding. Nat. Commun. 7, 10912 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 10912
    • Langendorf, C.G.1
  • 11
    • 36348978499 scopus 로고    scopus 로고
    • Defining the mechanism of activation of amp-activated protein kinase by the small molecule a-769662, a member of the thienopyridone family
    • Sanders, M. J. et al. Defining the mechanism of activation of AMP-activated protein kinase by the small molecule A-769662, a member of the thienopyridone family. J. Biol. Chem. 282, 32539-32548 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 32539-32548
    • Sanders, M.J.1
  • 12
    • 84890963021 scopus 로고    scopus 로고
    • Structural basis of AMPK regulation by small molecule activators
    • Xiao, B. et al. Structural basis of AMPK regulation by small molecule activators. Nat. Commun. 4, 3017 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 3017
    • Xiao, B.1
  • 13
    • 84901329684 scopus 로고    scopus 로고
    • Small molecule drug A-769662 and AMP synergistically activate naïve AMPK independent of upstream kinase signaling
    • Scott, J. W. et al. Small molecule drug A-769662 and AMP synergistically activate naïve AMPK independent of upstream kinase signaling. Chem. Biol. 21, 619-627 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 619-627
    • Scott, J.W.1
  • 14
    • 84905719900 scopus 로고    scopus 로고
    • Structural basis for AMPK activation: Natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms
    • Calabrese, M. F. et al. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structure 22, 1161-1172 (2014).
    • (2014) Structure , vol.22 , pp. 1161-1172
    • Calabrese, M.F.1
  • 15
    • 84861222690 scopus 로고    scopus 로고
    • The ancient drug salicylate directly activates AMP-activated protein kinase
    • Hawley, S. A. et al. The ancient drug salicylate directly activates AMP-activated protein kinase. Science 336, 918-922 (2012).
    • (2012) Science , vol.336 , pp. 918-922
    • Hawley, S.A.1
  • 16
    • 84935013342 scopus 로고    scopus 로고
    • Inhibition of AMP-activated protein kinase at the allosteric drug-binding site promotes islet insulin release
    • Scott, J. W. et al. Inhibition of AMP-activated protein kinase at the allosteric drug-binding site promotes islet insulin release. Chem. Biol. 22, 705-711 (2015).
    • (2015) Chem. Biol. , vol.22 , pp. 705-711
    • Scott, J.W.1
  • 17
    • 56049112796 scopus 로고    scopus 로고
    • Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes
    • Scott, J. W. et al. Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes. Chem. Biol. 15, 1220-1230 (2008).
    • (2008) Chem. Biol. , vol.15 , pp. 1220-1230
    • Scott, J.W.1
  • 18
    • 84857687439 scopus 로고    scopus 로고
    • AMPK functions as an adenylate charge-regulated protein kinase
    • Oakhill, J. S., Scott, J. W. & Kemp, B. E. AMPK functions as an adenylate charge-regulated protein kinase. Trends Endocrinol. Metab. 23, 125-132 (2012).
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 125-132
    • Oakhill, J.S.1    Scott, J.W.2    Kemp, B.E.3
  • 19
    • 84887189624 scopus 로고    scopus 로고
    • Inhibition of AMPK catabolic action by GSK3
    • Suzuki, T. et al. Inhibition of AMPK catabolic action by GSK3. Mol. Cell 50, 407-419 (2013).
    • (2013) Mol. Cell , vol.50 , pp. 407-419
    • Suzuki, T.1
  • 20
    • 79959963047 scopus 로고    scopus 로고
    • Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop
    • Löffler, A. S. et al. Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop. Autophagy 7, 696-706 (2011).
    • (2011) Autophagy , vol.7 , pp. 696-706
    • Löffler, A.S.1
  • 21
    • 0030870168 scopus 로고    scopus 로고
    • Posttranslational modifications of the 5'-AMP-activated protein kinase ?1 subunit
    • Mitchelhill, K. I. et al. Posttranslational modifications of the 5'-AMP-activated protein kinase ?1 subunit. J. Biol. Chem. 272, 24475-24479 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 24475-24479
    • Mitchelhill, K.I.1
  • 22
    • 80053163909 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) beta1beta2 muscle null mice reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise
    • O'Neill, H. M. et al. AMP-activated protein kinase (AMPK) beta1beta2 muscle null mice reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise. Proc. Natl Acad. Sci. USA 108, 16092-16097 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 16092-16097
    • O'Neill, H.M.1
  • 23
    • 33745840203 scopus 로고    scopus 로고
    • 5-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solid-tumor microenvironments
    • Laderoute, K. R. et al. 5-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solid-tumor microenvironments. Mol. Cell. Biol. 26, 5336-5347 (2016).
    • (2016) Mol. Cell. Biol. , vol.26 , pp. 5336-5347
    • Laderoute, K.R.1
  • 24
    • 84937523899 scopus 로고    scopus 로고
    • Small molecule inhibition of the autophagy kinase ULK1 and identification of ULK1 substrates
    • Egan, D. F. et al. Small molecule inhibition of the autophagy kinase ULK1 and identification of ULK1 substrates. Mol. Cell 59, 285-297 (2015).
    • (2015) Mol. Cell , vol.59 , pp. 285-297
    • Egan, D.F.1
  • 26
    • 42949085382 scopus 로고    scopus 로고
    • A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
    • Erickson, J. R. et al. A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell 133, 462-474 (2008).
    • (2008) Cell , vol.133 , pp. 462-474
    • Erickson, J.R.1
  • 27
    • 13244283230 scopus 로고    scopus 로고
    • Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification
    • Humphries, K. M., Deal, M. S. & Taylor, S. S. Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification. J. Biol. Chem. 280, 2750-2758 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 2750-2758
    • Humphries, K.M.1    Deal, M.S.2    Taylor, S.S.3
  • 30
    • 84885142437 scopus 로고    scopus 로고
    • AMP as a low-energy charge signal autonomously initiates assembly of AXIN-AMPK-LKB1 complex for AMPK activation
    • Zhang, Y.-L. et al. AMP as a low-energy charge signal autonomously initiates assembly of AXIN-AMPK-LKB1 complex for AMPK activation. Cell Metab. 18, 546-555 (2013).
    • (2013) Cell Metab. , vol.18 , pp. 546-555
    • Zhang, Y.-L.1
  • 31
    • 84939426946 scopus 로고    scopus 로고
    • Myristoylation confers noncanonical AMPK functions in autophagy selectivity and mitochondrial surveillance
    • Liang, J. et al. Myristoylation confers noncanonical AMPK functions in autophagy selectivity and mitochondrial surveillance. Nat. Commun. 6, 7926 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 7926
    • Liang, J.1
  • 32
    • 79251587803 scopus 로고    scopus 로고
    • Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
    • Egan, D. F. et al. 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
  • 33
    • 84930606184 scopus 로고    scopus 로고
    • Metformin and salicylate synergistically activate liver AMPK, inhibit lipogenesis and improve insulin sensitivity
    • Ford, R. J. et al. Metformin and salicylate synergistically activate liver AMPK, inhibit lipogenesis and improve insulin sensitivity. Biochem. J. 468, 125-132 (2015).
    • (2015) Biochem. J. , vol.468 , pp. 125-132
    • Ford, R.J.1
  • 34
    • 84937134138 scopus 로고    scopus 로고
    • Salicylate activates AMPK and synergizes with metformin to reduce the survival of prostate and lung cancer cells ex vivo through inhibition of de novo lipogenesis
    • O'Brien, A. J. et al. Salicylate activates AMPK and synergizes with metformin to reduce the survival of prostate and lung cancer cells ex vivo through inhibition of de novo lipogenesis. Biochem. J. 469, 177-187 (2015).
    • (2015) Biochem. J. , vol.469 , pp. 177-187
    • O'Brien, A.J.1
  • 35
    • 84929469439 scopus 로고    scopus 로고
    • Salicylate improves macrophage cholesterol homeostasis via activation of Ampk
    • Fullerton, M. D. et al. Salicylate improves macrophage cholesterol homeostasis via activation of Ampk. J. Lipid Res. 56, 1025-1033 (2015).
    • (2015) J. Lipid Res. , vol.56 , pp. 1025-1033
    • Fullerton, M.D.1
  • 36
    • 84898601973 scopus 로고    scopus 로고
    • A novel direct activator of AMPK inhibits prostate cancer growth by blocking lipogenesis
    • Zadra, G. et al. A novel direct activator of AMPK inhibits prostate cancer growth by blocking lipogenesis. EMBO Mol. Med. 6, 519-538 (2014).
    • (2014) EMBO Mol. Med. , vol.6 , pp. 519-538
    • Zadra, G.1
  • 37
    • 84986538891 scopus 로고    scopus 로고
    • Discovery and preclinical characterization of 6-chloro-5-[4-(1-hydroxycyclobutyl)phenyl]-1H-indole-3-carboxylic acid (PF-06409577), a direct activator of adenosine monophosphate-activated protein kinase (AMPK), for the potential treatment of diabetic nephropathy
    • Cameron, K. O. et al. Discovery and preclinical characterization of 6-chloro-5-[4-(1-hydroxycyclobutyl)phenyl]-1H-indole-3-carboxylic acid (PF-06409577), a direct activator of adenosine monophosphate-activated protein kinase (AMPK), for the potential treatment of diabetic nephropathy. J. Med. Chem. 59, 8068-8081 (2016).
    • (2016) J. Med. Chem. , vol.59 , pp. 8068-8081
    • Cameron, K.O.1
  • 38
    • 67749111502 scopus 로고    scopus 로고
    • The LKB1-AMPK pathway: Metabolism and growth control in tumour suppression
    • Shackleford, D. B. & Shaw, R. J. The LKB1-AMPK pathway: metabolism and growth control in tumour suppression. Nat. Rev. Cancer 9, 563-575 (2009).
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 563-575
    • Shackleford, D.B.1    Shaw, R.J.2
  • 39
    • 0036430469 scopus 로고    scopus 로고
    • Dissociation of AMPK activity and ACC? Phosphorylation in human muscle during prolonged exercise
    • Wojtaszewski, J. F. et al. Dissociation of AMPK activity and ACC? phosphorylation in human muscle during prolonged exercise. Biochem. Biophys. Res. Commun. 298, 309-316 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 309-316
    • Wojtaszewski, J.F.1
  • 40
    • 0345832116 scopus 로고    scopus 로고
    • Knockout of the alpha2 but not alpha1 5?-AMP-activated protein kinase isoform abolishes 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranoside but not contraction-induced glucose uptake in skeletal muscle
    • Jørgensen, S. B. et al. Knockout of the alpha2 but not alpha1 5?-AMP-activated protein kinase isoform abolishes 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranoside but not contraction-induced glucose uptake in skeletal muscle. J. Biol. Chem. 279, 1070-1079 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 1070-1079
    • Jørgensen, S.B.1
  • 41
    • 57049097476 scopus 로고    scopus 로고
    • AMPK-independent pathways regulate skeletal muscle fatty acid oxidation
    • Dzamko, N. et al. AMPK-independent pathways regulate skeletal muscle fatty acid oxidation. J. Physiol. 586, 5819-5831 (2008).
    • (2008) J. Physiol. , vol.586 , pp. 5819-5831
    • Dzamko, N.1
  • 42
    • 84940417303 scopus 로고    scopus 로고
    • Activation of autophagy in human skeletal muscle is dependent on exercise intensity and AMPK activation
    • Schwalm, C. et al. Activation of autophagy in human skeletal muscle is dependent on exercise intensity and AMPK activation. FASEB J. 29, 3515-3526 (2015).
    • (2015) FASEB J. , vol.29 , pp. 3515-3526
    • Schwalm, C.1
  • 43
    • 77749233738 scopus 로고    scopus 로고
    • ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS
    • Alexander, A. et al. ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS. Proc. Natl Acad. Sci. USA 107, 4153-4158 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4153-4158
    • Alexander, A.1
  • 44
    • 84907519033 scopus 로고    scopus 로고
    • The lysosomal v-ATPase-ragulator complex is a common activator for AMPK and mTORC1, acting as a switch between catabolism and anabolism
    • Zhang, S.-C. et al. The lysosomal v-ATPase-ragulator complex is a common activator for AMPK and mTORC1, acting as a switch between catabolism and anabolism. Cell Metab. 20, 526-540 (2014).
    • (2014) Cell Metab. , vol.20 , pp. 526-540
    • Zhang, S.-C.1
  • 45
    • 28844475401 scopus 로고    scopus 로고
    • Regulation of the interaction of Pak2 with Cdc42 via autophosphorylation of serine 141
    • Jung, J. H. & Traugh, J. A. Regulation of the interaction of Pak2 with Cdc42 via autophosphorylation of serine 141. J. Biol. Chem. 280, 40025-40031 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 40025-40031
    • Jung, J.H.1    Traugh, J.A.2
  • 46
    • 0035907371 scopus 로고    scopus 로고
    • P21-activated protein kinase gamma-PAK suppresses programmed cell death of BALB3T3 fibroblasts
    • Jakobi, R., Moertl, E. & Koeppel, M. A. p21-activated protein kinase gamma-PAK suppresses programmed cell death of BALB3T3 fibroblasts. J. Biol. Chem. 276, 16624-16634 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 16624-16634
    • Jakobi, R.1    Moertl, E.2    Koeppel, M.A.3
  • 47
    • 51649124519 scopus 로고    scopus 로고
    • Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation
    • Kundu, M. et al. Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation. Blood 112, 1493-1502 (2008).
    • (2008) Blood , vol.112 , pp. 1493-1502
    • Kundu, M.1
  • 48
    • 84919740196 scopus 로고    scopus 로고
    • Dysregulated autophagy in the RPE is associated with increased susceptibility to oxidative stress and AMD
    • Mitter, S. K. et al. Dysregulated autophagy in the RPE is associated with increased susceptibility to oxidative stress and AMD. Autophagy 10, 1989-2005 (2014).
    • (2014) Autophagy , vol.10 , pp. 1989-2005
    • Mitter, S.K.1
  • 49
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C., Sowa, M. E., Gygi, S. P. & Harper, J. W. Network organization of the human autophagy system. Nature 466, 68-76 (2010).
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 50
    • 84907545906 scopus 로고    scopus 로고
    • AMPK: Positive and negative regulation, and its role in wholebody energy homeostasis
    • Hardie, D. G. AMPK: positive and negative regulation, and its role in wholebody energy homeostasis. Curr. Opin. Cell Biol. 33, 1-7 (2015).
    • (2015) Curr. Opin. Cell Biol. , vol.33 , pp. 1-7
    • Hardie, D.G.1
  • 51
    • 84891745585 scopus 로고    scopus 로고
    • Autophagy regulation by nutrient signaling
    • Russell, R. C., Yuan, H. X. & Guan, K. L. Autophagy regulation by nutrient signaling. Cell Res. 24, 42-57 (2014).
    • (2014) Cell Res. , vol.24 , pp. 42-57
    • Russell, R.C.1    Yuan, H.X.2    Guan, K.L.3
  • 52
    • 84899789746 scopus 로고    scopus 로고
    • ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy
    • Wu, W. et al. ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy. EMBO Rep. 15, 566-575 (2014).
    • (2014) EMBO Rep. , vol.15 , pp. 566-575
    • Wu, W.1
  • 53
    • 84872586081 scopus 로고    scopus 로고
    • Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy
    • Kim, J. et al. Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy. Cell 152, 290-303 (2013).
    • (2013) Cell , vol.152 , pp. 290-303
    • Kim, J.1
  • 54
    • 84903649086 scopus 로고    scopus 로고
    • Novel mechanisms of Na+ retention in obesity: Phosphorylation of NKCC2 and regulation of SPAK/OSR1 by AMPK
    • Davies, M. et al. Novel mechanisms of Na+ retention in obesity: phosphorylation of NKCC2 and regulation of SPAK/OSR1 by AMPK. Am. J. Physiol. Renal Physiol. 307, F96-F106 (2014).
    • (2014) Am. J. Physiol. Renal Physiol. , vol.307 , pp. F96-F106
    • Davies, M.1
  • 55
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P. J., Raijmakers, R., Lemeer, S., Mohammed, S. & Heck, A. J. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat. Protoc. 4, 484-494 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 56
    • 34248640261 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides using titanium dioxide
    • Thingholm, T. E., Jorgensen, T. J., Jensen, O. N. & Larsen, M. R. Highly selective enrichment of phosphorylated peptides using titanium dioxide. Nat. Protoc. 1, 1929-1935 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 1929-1935
    • Thingholm, T.E.1    Jorgensen, T.J.2    Jensen, O.N.3    Larsen, M.R.4
  • 57
    • 84976274986 scopus 로고    scopus 로고
    • The Perseus computational platform for comprehensive analysis of (prote)omics data
    • Tyanova, S. et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat. Methods 13, 731-740 (2016).
    • (2016) Nat. Methods , vol.13 , pp. 731-740
    • Tyanova, S.1
  • 58
    • 57449099865 scopus 로고    scopus 로고
    • Max Quant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 59
    • 84976871411 scopus 로고    scopus 로고
    • 2016 update of the PRIDE database and related tools
    • Vizcaíno, J. A. et al. 2016 update of the PRIDE database and related tools. Nucleic Acids Res. 44, D447-D456 (2016).
    • (2016) Nucleic Acids Res. , vol.44 , pp. D447-D456
    • Vizcaíno, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.