메뉴 건너뛰기




Volumn 6, Issue , 2017, Pages

Identification and dynamics of the human ZDHHC16-ZDHHC6 palmitoylation cascade

Author keywords

[No Author keywords available]

Indexed keywords

CYS 328 PROTEIN; PALMITOYL PROTEIN THIOESTERASE; PEPTIDES AND PROTEINS; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; ZDHHC16 PROTEIN; ZDHHC6 PROTEIN; ACYLTRANSFERASE; CYSTEINE; LYPLA2 PROTEIN, HUMAN; THIOL ESTER HYDROLASE; ZDHHC16 PROTEIN, HUMAN; ZDHHC6 PROTEIN, HUMAN;

EID: 85029228870     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.27826     Document Type: Article
Times cited : (90)

References (55)
  • 1
    • 30944443590 scopus 로고    scopus 로고
    • Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis
    • PMID: 16401723
    • Abrami L, Leppla SH, van der Goot FG. 2006. Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis. The Journal of Cell Biology 172:309-320. DOI: https://doi.org/10.1083/jcb.200507067, PMID: 16401723
    • (2006) The Journal of Cell Biology , vol.172 , pp. 309-320
    • Abrami, L.1    Leppla, S.H.2    Van Der Goot, F.G.3
  • 2
    • 55749113392 scopus 로고    scopus 로고
    • Functional interactions between anthrax toxin receptors and the WNT signalling protein LRP6
    • PMID: 18717822
    • Abrami L, Kunz B, Deuquet J, Bafico A, Davidson G, van der Goot FG. 2008. Functional interactions between anthrax toxin receptors and the WNT signalling protein LRP6. Cellular Microbiology 10:2509-2519. DOI: https://doi.org/10.1111/j.1462-5822.2008.01226.x, PMID: 18717822
    • (2008) Cellular Microbiology , vol.10 , pp. 2509-2519
    • Abrami, L.1    Kunz, B.2    Deuquet, J.3    Bafico, A.4    Davidson, G.5    Van Der Goot, F.G.6
  • 6
    • 84897987131 scopus 로고    scopus 로고
    • Mechanistic effects of protein palmitoylation and the cellular consequences thereof
    • PMID: 24534427
    • Blaskovic S, Adibekian A, Blanc M, van der Goot GF. 2014. Mechanistic effects of protein palmitoylation and the cellular consequences thereof. Chemistry and Physics of Lipids 180:44-52. DOI: https://doi.org/10.1016/j. chemphyslip.2014.02.001, PMID: 24534427
    • (2014) Chemistry and Physics of Lipids , vol.180 , pp. 44-52
    • Blaskovic, S.1    Adibekian, A.2    Blanc, M.3    Van Der Goot, G.F.4
  • 7
    • 0029681614 scopus 로고    scopus 로고
    • Extending the quasi-steady state approximation by changing variables
    • PMID: 881 9753
    • Borghans JA, de Boer RJ, Segel LA. 1996. Extending the quasi-steady state approximation by changing variables. Bulletin of Mathematical Biology 58:43-63. DOI: https://doi.org/10.1007/BF02458281, PMID: 881 9753
    • (1996) Bulletin of Mathematical Biology , vol.58 , pp. 43-63
    • Borghans, J.A.1    De Boer, R.J.2    Segel, L.A.3
  • 8
    • 84968919580 scopus 로고    scopus 로고
    • A potential role for protein palmitoylation and zDHHC16 in DNA damage response
    • PMID: 27159997
    • Cao N, Li JK, Rao YQ, Liu H, Wu J, Li B, Zhao P, Zeng L, Li J. 2016. A potential role for protein palmitoylation and zDHHC16 in DNA damage response. BMC Molecular Biology 17:12. DOI: https://doi.org/10.1186/s12867-016-0065-9, PMID: 27159997
    • (2016) BMC Molecular Biology , vol.17 , pp. 12
    • Cao, N.1    Li, J.K.2    Rao, Y.Q.3    Liu, H.4    Wu, J.5    Li, B.6    Zhao, P.7    Zeng, L.8    Li, J.9
  • 10
    • 84926624340 scopus 로고    scopus 로고
    • The physiology of protein S-acylation
    • PMID: 25834228
    • Chamberlain LH, Shipston MJ. 2015. The physiology of protein S-acylation. Physiological Reviews 95:341-376. DOI: https://doi.org/10.1152/physrev.00032.2014, PMID: 25834228
    • (2015) Physiological Reviews , vol.95 , pp. 341-376
    • Chamberlain, L.H.1    Shipston, M.J.2
  • 11
    • 84976907223 scopus 로고    scopus 로고
    • ZDHHC7-mediated S-palmitoylation of scribble regulates cell polarity
    • PMID: 27380321
    • Chen B, Zheng B, DeRan M, Jarugumilli GK, Fu J, Brooks YS, Wu X. 2016. ZDHHC7-mediated S-palmitoylation of scribble regulates cell polarity. Nature Chemical Biology 12:686-693. DOI: https://doi.org/10.1038/nchembio. 2119, PMID: 27380321
    • (2016) Nature Chemical Biology , vol.12 , pp. 686-693
    • Chen, B.1    Zheng, B.2    Deran, M.3    Jarugumilli, G.K.4    Fu, J.5    Brooks, Y.S.6    Wu, X.7
  • 12
    • 84973522267 scopus 로고    scopus 로고
    • Palmitoylation regulates the intracellular trafficking and stability of c-Met
    • PMID: 270816 99
    • Coleman DT, Gray AL, Kridel SJ, Cardelli JA. 2016. Palmitoylation regulates the intracellular trafficking and stability of c-Met. Oncotarget 7:32664-32677. DOI: https://doi.org/10.18632/oncotarget.8706, PMID: 270816 99
    • (2016) Oncotarget , vol.7 , pp. 32664-32677
    • Coleman, D.T.1    Gray, A.L.2    Kridel, S.J.3    Cardelli, J.A.4
  • 13
    • 85022016434 scopus 로고    scopus 로고
    • Global, site-specific analysis of neuronal protein S-acylation
    • PMID: 28680068
    • Collins MO, Woodley KT, Choudhary JS. 2017. Global, site-specific analysis of neuronal protein S-acylation. Scientific Reports 7:4683. DOI: https://doi.org/10.1038/s41598-017-04580-1, PMID: 28680068
    • (2017) Scientific Reports , vol.7 , pp. 4683
    • Collins, M.O.1    Woodley, K.T.2    Choudhary, J.S.3
  • 14
    • 78649734941 scopus 로고    scopus 로고
    • Palmitoylation and depalmitoylation dynamics at a glance
    • PMID: 21084560
    • Conibear E, Davis NG. 2010. Palmitoylation and depalmitoylation dynamics at a glance. Journal of Cell Science 123:4007-4010. DOI: https://doi.org/10.1242/jcs.059287, PMID: 21084560
    • (2010) Journal of Cell Science , vol.123 , pp. 4007-4010
    • Conibear, E.1    Davis, N.G.2
  • 15
    • 84959576199 scopus 로고    scopus 로고
    • Model-driven understanding of palmitoylation dynamics: Regulated acylation of the endoplasmic reticulum chaperone calnexin
    • PMID: 26900856
    • Dallavilla T, Abrami L, Sandoz PA, Savoglidis G, Hatzimanikatis V, van der Goot FG. 2016. Model-driven understanding of palmitoylation dynamics: regulated acylation of the endoplasmic reticulum chaperone calnexin. PLOS Computational Biology 12:e1004774. DOI: https://doi.org/10.1371/journal.pcbi.1004774, PMID: 26900856
    • (2016) PLOS Computational Biology , vol.12
    • Dallavilla, T.1    Abrami, L.2    Sandoz, P.A.3    Savoglidis, G.4    Hatzimanikatis, V.5    Van Der Goot, F.G.6
  • 16
    • 84864283092 scopus 로고    scopus 로고
    • RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase
    • PMID: 22728137
    • Fairbank M, Huang K, El-Husseini A, Nabi IR. 2012. RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase. FEBS Letters 586:2488-2493. DOI: https://doi.org/10.1016/j.febslet.2012.06.011, PMID: 22728137
    • (2012) FEBS Letters , vol.586 , pp. 2488-2493
    • Fairbank, M.1    Huang, K.2    El-Husseini, A.3    Nabi, I.R.4
  • 17
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • PMID: 12724530
    • Foster LJ, De Hoog CL, Mann M. 2003. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. PNAS 100:5813-5818. DOI: https://doi.org/10.1073/pnas.0631608100, PMID: 12724530
    • (2003) PNAS , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 18
    • 84919487651 scopus 로고    scopus 로고
    • Stable expression and function of the inositol 1,4,5-triphosphate receptor requires palmitoylation by a DHHC6/selenoprotein K complex
    • PMID: 25368151
    • Fredericks GJ, Hoffmann FW, Rose AH, Osterheld HJ, Hess FM, Mercier F, Hoffmann PR. 2014. Stable expression and function of the inositol 1,4,5-triphosphate receptor requires palmitoylation by a DHHC6/selenoprotein K complex. PNAS 111:16478-16483. DOI: https://doi.org/10.1073/pnas.1417176111, PMID: 25368151
    • (2014) PNAS , vol.111 , pp. 16478-16483
    • Fredericks, G.J.1    Hoffmann, F.W.2    Rose, A.H.3    Osterheld, H.J.4    Hess, F.M.5    Mercier, F.6    Hoffmann, P.R.7
  • 19
    • 84942746886 scopus 로고    scopus 로고
    • Selenoprotein K and protein palmitoylation
    • PMID: 26058750
    • Fredericks GJ, Hoffmann PR. 2015. Selenoprotein K and protein palmitoylation. Antioxidants & Redox Signaling 23:854-862. DOI: https://doi.org/10.1089/ars.2015.6375, PMID: 26058750
    • (2015) Antioxidants & Redox Signaling , vol.23 , pp. 854-862
    • Fredericks, G.J.1    Hoffmann, P.R.2
  • 20
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • PMID: 20168314
    • Fukata Y, Fukata M. 2010. Protein palmitoylation in neuronal development and synaptic plasticity. Nature Reviews Neuroscience 11:161-175. DOI: https://doi.org/10.1038/nrn2788, PMID: 20168314
    • (2010) Nature Reviews Neuroscience , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 21
    • 84961789517 scopus 로고    scopus 로고
    • Local palmitoylation cycles and specialized membrane domain organization
    • PMID: 26781831
    • Fukata Y, Murakami T, Yokoi N, Fukata M. 2016. Local palmitoylation cycles and specialized membrane domain organization. Current topics in membranes 77:97-141. DOI: https://doi.org/10.1016/bs.ctm.2015.10.003, PMID: 26781831
    • (2016) Current Topics in Membranes , vol.77 , pp. 97-141
    • Fukata, Y.1    Murakami, T.2    Yokoi, N.3    Fukata, M.4
  • 22
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • PMID: 6947258
    • Goldbeter A, Koshland DE. 1981. An amplified sensitivity arising from covalent modification in biological systems. PNAS 78:6840-6844. DOI: https://doi.org/10.1073/pnas.78.11.6840, PMID: 6947258
    • (1981) PNAS , vol.78 , pp. 6840-6844
    • Goldbeter, A.1    Koshland, D.E.2
  • 23
    • 80655128141 scopus 로고    scopus 로고
    • Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signals
    • PMID: 21926431
    • Gorleku OA, Barns AM, Prescott GR, Greaves J, Chamberlain LH. 2011. Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signals. Journal of Biological Chemistry 286: 39573-39584. DOI: https://doi.org/10.1074/jbc.M111.272369, PMID: 21926431
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 39573-39584
    • Gorleku, O.A.1    Barns, A.M.2    Prescott, G.R.3    Greaves, J.4    Chamberlain, L.H.5
  • 26
    • 84875972777 scopus 로고    scopus 로고
    • Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with that of proto-oncogene H-ras product and growth-associated protein-43
    • PMID: 23396970
    • Kong E, Peng S, Chandra G, Sarkar C, Zhang Z, Bagh MB, Mukherjee AB. 2013. Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with that of proto-oncogene H-ras product and growth-associated protein-43. Journal of Biological Chemistry 288:9112-9125. DOI: https://doi.org/10.1074/jbc.M112.421073, PMID: 23396970
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 9112-9125
    • Kong, E.1    Peng, S.2    Chandra, G.3    Sarkar, C.4    Zhang, Z.5    Bagh, M.B.6    Mukherjee, A.B.7
  • 27
    • 84881230382 scopus 로고    scopus 로고
    • Oligomerization of DHHC protein S-acyltransferases
    • PMID: 23793055
    • Lai J, Linder ME. 2013. Oligomerization of DHHC protein S-acyltransferases. Journal of Biological Chemistry 288: 22862-22870. DOI: https://doi.org/10.1074/jbc.M113.458794, PMID: 23793055
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 22862-22870
    • Lai, J.1    Linder, M.E.2
  • 29
    • 0037047404 scopus 로고    scopus 로고
    • Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity
    • PMID: 12021275
    • Li B, Cong F, Tan CP, Wang SX, Goff SP. 2002. Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity. Journal of Biological Chemistry 277:28870-28876. DOI: https://doi.org/10.1074/jbc. M202388200, PMID: 12021275
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 28870-28876
    • Li, B.1    Cong, F.2    Tan, C.P.3    Wang, S.X.4    Goff, S.P.5
  • 30
    • 84855253929 scopus 로고    scopus 로고
    • DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells
    • PMID: 22081607
    • Li Y, Martin BR, Cravatt BF, Hofmann SL. 2012. DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells. Journal of Biological Chemistry 287:523-530. DOI: https://doi.org/10.1074/jbc.M111.306183, PMID: 22081607
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 523-530
    • Li, Y.1    Martin, B.R.2    Cravatt, B.F.3    Hofmann, S.L.4
  • 31
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • PMID: 12193598
    • Lobo S, Greentree WK, Linder ME, Deschenes RJ. 2002. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. Journal of Biological Chemistry 277:41268-41273. DOI: https://doi.org/10.1074/jbc. M206573200, PMID: 12193598
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 32
    • 80054036585 scopus 로고    scopus 로고
    • Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3
    • PMID: 21785166
    • Merrick BA, Dhungana S, Williams JG, Aloor JJ, Peddada S, Tomer KB, Fessler MB. 2011. Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3. Molecular & Cellular Proteomics 10:M110.006007. DOI: https://doi.org/10.1074/mcp.M110. 006007, PMID: 21785166
    • (2011) Molecular & Cellular Proteomics , vol.10
    • Merrick, B.A.1    Dhungana, S.2    Williams, J.G.3    Aloor, J.J.4    Peddada, S.5    Tomer, K.B.6    Fessler, M.B.7
  • 36
    • 85016830065 scopus 로고    scopus 로고
    • Individual S-acylated cysteines differentially contribute to H-Ras endomembrane trafficking and acylation/deacylation cycles
    • PMID: 28179458
    • Pedro MP, Vilcaes AA, Gomez GA, Daniotti JL. 2017. Individual S-acylated cysteines differentially contribute to H-Ras endomembrane trafficking and acylation/deacylation cycles. Molecular Biology of the Cell 28:962-974. DOI: https://doi.org/10.1091/mbc.E16-08-0603, PMID: 28179458
    • (2017) Molecular Biology of the Cell , vol.28 , pp. 962-974
    • Pedro, M.P.1    Vilcaes, A.A.2    Gomez, G.A.3    Daniotti, J.L.4
  • 37
    • 84975782043 scopus 로고    scopus 로고
    • Cardiac sodium channel palmitoylation regulates channel availability and myocyte excitability with implications for arrhythmia generation
    • PMID: 27337590
    • Pei Z, Xiao Y, Meng J, Hudmon A, Cummins TR. 2016. Cardiac sodium channel palmitoylation regulates channel availability and myocyte excitability with implications for arrhythmia generation. Nature Communications 7: 12035. DOI: https://doi.org/10.1038/ncomms12035, PMID: 27337590
    • (2016) Nature Communications , vol.7 , pp. 12035
    • Pei, Z.1    Xiao, Y.2    Meng, J.3    Hudmon, A.4    Cummins, T.R.5
  • 38
    • 84964324810 scopus 로고    scopus 로고
    • Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation
    • PMID: 27044110
    • Percher A, Ramakrishnan S, Thinon E, Yuan X, Yount JS, Hang HC. 2016. Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation. PNAS 113:4302-4307. DOI: https://doi.org/10.1073/pnas. 1602244113, PMID: 27044110
    • (2016) PNAS , vol.113 , pp. 4302-4307
    • Percher, A.1    Ramakrishnan, S.2    Thinon, E.3    Yuan, X.4    Yount, J.S.5    Hang, H.C.6
  • 40
    • 84966668561 scopus 로고    scopus 로고
    • Inhibition of DHHC20-Mediated EGFR palmitoylation creates a dependence on EGFR signaling
    • PMID: 27153536
    • Runkle KB, Kharbanda A, Stypulkowski E, Cao XJ, Wang W, Garcia BA, Witze ES. 2016. Inhibition of DHHC20-Mediated EGFR palmitoylation creates a dependence on EGFR signaling. Molecular Cell 62:385-396. DOI: https://doi.org/10.1016/j.molcel.2016.04.003, PMID: 27153536
    • (2016) Molecular Cell , vol.62 , pp. 385-396
    • Runkle, K.B.1    Kharbanda, A.2    Stypulkowski, E.3    Cao, X.J.4    Wang, W.5    Garcia, B.A.6    Witze, E.S.7
  • 41
    • 0027238044 scopus 로고
    • A reversibly palmitoylated resident protein (P63) of an ER-Golgi intermediate compartment is related to a circulatory shock resuscitation protein
    • Schweizer A, Rohrer J, Jenö P, DeMaio A, Buchman TG, Hauri HP. 1993. A reversibly palmitoylated resident protein (p63) of an ER-Golgi intermediate compartment is related to a circulatory shock resuscitation protein. Journal of Cell Science 104:685-694.
    • (1993) Journal of Cell Science , vol.104 , pp. 685-694
    • Schweizer, A.1    Rohrer, J.2    Jenö, P.3    Demaio, A.4    Buchman, T.G.5    Hauri, H.P.6
  • 42
    • 85029211549 scopus 로고    scopus 로고
    • PMID: 8314870
    • PMID: 8314870
  • 43
    • 84940446233 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology and function by stearoylation of TFR1
    • PMID: 26214738
    • Senyilmaz D, Virtue S, Xu X, Tan CY, Griffin JL, Miller AK, Vidal-Puig A, Teleman AA. 2015. Regulation of mitochondrial morphology and function by stearoylation of TFR1. Nature 525:124-128. DOI: https://doi.org/10.1038/nature14601, PMID: 26214738
    • (2015) Nature , vol.525 , pp. 124-128
    • Senyilmaz, D.1    Virtue, S.2    Xu, X.3    Tan, C.Y.4    Griffin, J.L.5    Miller, A.K.6    Vidal-Puig, A.7    Teleman, A.A.8
  • 44
    • 84987847736 scopus 로고    scopus 로고
    • ZDHHC16 modulates FGF/ERK dependent proliferation of neural stem/progenitor cells in the zebrafish telencephalon
    • PMID: 26663717
    • Shi W, Chen X, Wang F, Gao M, Yang Y, Du Z, Wang C, Yao Y, He K, Hao A. 2016. ZDHHC16 modulates FGF/ERK dependent proliferation of neural stem/progenitor cells in the zebrafish telencephalon. Developmental neurobiology 76. DOI: https://doi.org/10.1002/dneu.22372, PMID: 26663717
    • (2016) Developmental Neurobiology , pp. 76
    • Shi, W.1    Chen, X.2    Wang, F.3    Gao, M.4    Yang, Y.5    Du, Z.6    Wang, C.7    Yao, Y.8    He, K.9    Hao, A.10
  • 46
    • 24744466287 scopus 로고    scopus 로고
    • DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H-and N-Ras
    • PMID: 16000296
    • Swarthout JT, Lobo S, Farh L, Croke MR, Greentree WK, Deschenes RJ, Linder ME. 2005. DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H-and N-Ras. Journal of Biological Chemistry 280:31141-31148. DOI: https://doi.org/10.1074/jbc.M504113200, PMID: 16000296
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 31141-31148
    • Swarthout, J.T.1    Lobo, S.2    Farh, L.3    Croke, M.R.4    Greentree, W.K.5    Deschenes, R.J.6    Linder, M.E.7
  • 47
    • 84971578053 scopus 로고    scopus 로고
    • Palmitoylated claudin7 captured in glycolipid-enriched membrane microdomains promotes metastasis via associated transmembrane and cytosolic molecules
    • PMID: 27120791
    • Thuma F, Heiler S, Schnölzer M, Zöller M. 2016. Palmitoylated claudin7 captured in glycolipid-enriched membrane microdomains promotes metastasis via associated transmembrane and cytosolic molecules. Oncotarget 7:30659-30677. DOI: https://doi.org/10.18632/oncotarget.8928, PMID: 27120791
    • (2016) Oncotarget , vol.7 , pp. 30659-30677
    • Thuma, F.1    Heiler, S.2    Schnölzer, M.3    Zöller, M.4
  • 48
    • 84891880503 scopus 로고    scopus 로고
    • The autodepalmitoylating activity of APT maintains the spatial organization of palmitoylated membrane proteins
    • PMID: 24411241
    • Vartak N, Papke B, Grecco HE, Rossmannek L, Waldmann H, Hedberg C, Bastiaens PI. 2014. The autodepalmitoylating activity of APT maintains the spatial organization of palmitoylated membrane proteins. Biophysical Journal 106:93-105. DOI: https://doi.org/10.1016/j.bpj.2013.11.024, PMID: 24411241
    • (2014) Biophysical Journal , vol.106 , pp. 93-105
    • Vartak, N.1    Papke, B.2    Grecco, H.E.3    Rossmannek, L.4    Waldmann, H.5    Hedberg, C.6    Bastiaens, P.I.7
  • 49
    • 84981294741 scopus 로고    scopus 로고
    • Acyl protein thioesterase 1 and 2 (APT-1, APT-2) inhibitors palmostatin B, ML348 and ML349 have different effects on NRAS mutant melanoma cells
    • PMID: 26771141
    • Vujic I, Sanlorenzo M, Esteve-Puig R, Vujic M, Kwong A, Tsumura A, Murphy R, Moy A, Posch C, Monshi B, Rappersberger K, Ortiz-Urda S. 2016. Acyl protein thioesterase 1 and 2 (APT-1, APT-2) inhibitors palmostatin B, ML348 and ML349 have different effects on NRAS mutant melanoma cells. Oncotarget 7:7297-7306. DOI: https://doi.org/10.18632/oncotarget.6907, PMID: 26771141
    • (2016) Oncotarget , vol.7 , pp. 7297-7306
    • Vujic, I.1    Sanlorenzo, M.2    Esteve-Puig, R.3    Vujic, M.4    Kwong, A.5    Tsumura, A.6    Murphy, R.7    Moy, A.8    Posch, C.9    Monshi, B.10    Rappersberger, K.11    Ortiz-Urda, S.12
  • 50
    • 84937926691 scopus 로고    scopus 로고
    • S-acylation of the insulin-responsive aminopeptidase (IRAP): Quantitative analysis and identification of modified cysteines
    • PMID: 26198666
    • Werno MW, Chamberlain LH. 2015. S-acylation of the insulin-responsive aminopeptidase (IRAP): quantitative analysis and identification of modified cysteines. Scientific Reports 5:12413. DOI: https://doi.org/10.1038/srep12413, PMID: 26198666
    • (2015) Scientific Reports , vol.5 , pp. 12413
    • Werno, M.W.1    Chamberlain, L.H.2
  • 51
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes
    • PMID: 19801377
    • Yang W, Di Vizio D, Kirchner M, Steen H, Freeman MR. 2010. Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes. Molecular & Cellular Proteomics 9:54-70. DOI: https://doi.org/10.1074/mcp.M800448-MCP200, PMID: 19801377
    • (2010) Molecular & Cellular Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5
  • 53
    • 77955892540 scopus 로고    scopus 로고
    • Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3
    • PMID: 20601941
    • Yount JS, Moltedo B, Yang YY, Charron G, Moran TM, Ló pez CB, Hang HC. 2010. Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3. Nature Chemical Biology 6:610-614. DOI: https://doi. org/10.1038/nchembio.405, PMID: 20601941
    • (2010) Nature Chemical Biology , vol.6 , pp. 610-614
    • Yount, J.S.1    Moltedo, B.2    Yang, Y.Y.3    Charron, G.4    Moran, T.M.5    Ló Pez, C.B.6    Hang, H.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.