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Volumn 5, Issue 11, 2004, Pages 1053-1057

On the mechanism of protein palmitoylation

Author keywords

Autoacylation; DHHC proteins; Palmitoylation; S acylation; Ykt6

Indexed keywords

ACYLTRANSFERASE; ANKYRIN REPEAT CONTAINING PROTEIN 1; ASPARTIC ACID; COENZYME A; CYSTEINE; EFFECTOR OF RAS FUNCTION PROTEIN; HISTIDINE; HYBRID PROTEIN; MEMBRANE PROTEIN; OLEIC ACID; PALMITIC ACID; PALMITOLEIC ACID; PALMITOYLTRANSFERASE; PROTEIN N MYRISTOYLTRANSFERASE; RAS PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SNARE PROTEIN; SONIC HEDGEHOG PROTEIN; STEARIC ACID; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; TRANSFERASE; UNCLASSIFIED DRUG; VAC8 PROTEIN; WNT PROTEIN; YKT6 PROTEIN; ZINC FINGER PROTEIN;

EID: 10044268365     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.7400277     Document Type: Review
Times cited : (115)

References (57)
  • 1
    • 3042542949 scopus 로고    scopus 로고
    • Akr1p-dependent palmitoylation of Yck2p yeast casein kinase 1 is necessary and sufficient for plasma membrane targeting
    • Babu P, Deschenes RJ, Robinson LC (2004) Akr1p-dependent palmitoylation of Yck2p yeast casein kinase 1 is necessary and sufficient for plasma membrane targeting. J Biol Chem 279: 27138-27147
    • (2004) J. Biol. Chem. , vol.279 , pp. 27138-27147
    • Babu, P.1    Deschenes, R.J.2    Robinson, L.C.3
  • 2
    • 0032031584 scopus 로고    scopus 로고
    • Pseudo-enzymatic S-acylation of myristoylated Yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic 5-acylation in vivo
    • Bano MC, Jackson CS, Magee AI (1998) Pseudo-enzymatic S-acylation of myristoylated Yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic 5-acylation in vivo. Biochem J 330: 723-731
    • (1998) Biochem. J. , vol.330 , pp. 723-731
    • Bano, M.C.1    Jackson, C.S.2    Magee, A.I.3
  • 3
    • 0032883098 scopus 로고    scopus 로고
    • Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
    • Bartels DJ, Mitchell DA, Dong X, Deschenes RJ (1999) Erf2 a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Mol Cell Biol 19: 6775-6787
    • (1999) Mol. Cell Biol. , vol.19 , pp. 6775-6787
    • Bartels, D.J.1    Mitchell, D.A.2    Dong, X.3    Deschenes, R.J.4
  • 4
    • 17144467725 scopus 로고    scopus 로고
    • Insider information: How palmitoylation of Ras makes it a signaling double agent
    • Berthiaume LG (2002) Insider information: how palmitoylation of Ras makes it a signaling double agent. Sci STKE 2002: PE41
    • (2002) Sci. STKE , vol.2002
    • Berthiaume, L.G.1
  • 5
    • 0029145798 scopus 로고
    • Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristoylated proteins
    • Berthiaume L, Resh MD (1995) Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristoylated proteins. J Biol Chem 270: 22399-22405
    • (1995) J. Biol. Chem. , vol.270 , pp. 22399-22405
    • Berthiaume, L.1    Resh, M.D.2
  • 6
    • 0028980377 scopus 로고
    • Myelin P0 glycoprotein and a synthetic peptide containing the palmitoylation site are both autoacylated
    • Bharadwaj M, Bizzozero OA (1995) Myelin P0 glycoprotein and a synthetic peptide containing the palmitoylation site are both autoacylated. J Neurochem 65: 1805-1815
    • (1995) J. Neurochem. , vol.65 , pp. 1805-1815
    • Bharadwaj, M.1    Bizzozero, O.A.2
  • 9
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Bijlmakers MJ, Marsh M (2003) The on-off story of protein palmitoylation. Trends Cell Biol 13: 32-42
    • (2003) Trends Cell Biol. , vol.13 , pp. 32-42
    • Bijlmakers, M.J.1    Marsh, M.2
  • 10
    • 0035830701 scopus 로고    scopus 로고
    • Structural determinants influencing the reaction of cysteine-containing peptides with palmitoyl-coenzyme A and other thioesters
    • Bizzozero OA, Bixler HA, Pastuszyn A (2001) Structural determinants influencing the reaction of cysteine-containing peptides with palmitoyl-coenzyme A and other thioesters. Biochim Biophys Acta 1545: 278-288
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 278-288
    • Bizzozero, O.A.1    Bixler, H.A.2    Pastuszyn, A.3
  • 12
    • 0030890881 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a protein-palmitoyl acyltransferase from human erythrocytes
    • Das AK, Dasgupta B, Bhattacharya R, Basu J (1997) Purification and biochemical characterization of a protein-palmitoyl acyltransferase from human erythrocytes. J Biol Chem 272: 11021-11025
    • (1997) J. Biol. Chem. , vol.272 , pp. 11021-11025
    • Das, A.K.1    Dasgupta, B.2    Bhattacharya, R.3    Basu, J.4
  • 14
    • 0842285407 scopus 로고    scopus 로고
    • The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion
    • Dietrich LE, Gurezka R, Veit M, Ungermann C (2004) The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion. EMBO J 23: 45-53
    • (2004) EMBO J. , vol.23 , pp. 45-53
    • Dietrich, L.E.1    Gurezka, R.2    Veit, M.3    Ungermann, C.4
  • 15
    • 0041689887 scopus 로고    scopus 로고
    • Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae
    • Dong X, Mitchell DA, Lobo S, Zhao L, Bartels DJ, Deschenes RJ (2003) Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae. Mol Cell Biol 23: 6574-6584
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6574-6584
    • Dong, X.1    Mitchell, D.A.2    Lobo, S.3    Zhao, L.4    Bartels, D.J.5    Deschenes, R.J.6
  • 16
    • 0029814190 scopus 로고    scopus 로고
    • Autoacylation of G protein α subunits
    • Duncan JA, Gilman AG (1996) Autoacylation of G protein α subunits. J Biol Chem 271: 23594-23600
    • (1996) J. Biol. Chem. , vol.271 , pp. 23594-23600
    • Duncan, J.A.1    Gilman, A.G.2
  • 18
    • 0030897513 scopus 로고    scopus 로고
    • Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling
    • Faergeman NJ, Knudsen J (1997) Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling. Biochem J 323: 1-12
    • (1997) Biochem. J. , vol.323 , pp. 1-12
    • Faergeman, N.J.1    Knudsen, J.2
  • 19
    • 0033934481 scopus 로고    scopus 로고
    • Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane
    • Feng Y, Davis NG (2000) Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane. Mol Cell Biol 20: 5350-5359
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5350-5359
    • Feng, Y.1    Davis, N.G.2
  • 21
    • 0031739531 scopus 로고    scopus 로고
    • Yel013p (Vac8p), an armadillo repeat protein related to plakoglobin and importin-α is associated with the yeast vacuole membrane
    • Fleckenstein D, Rohde M, Klionsky DJ, Rudiger M (1998) Yel013p (Vac8p), an armadillo repeat protein related to plakoglobin and importin-α is associated with the yeast vacuole membrane. J Cell Sci 111: 3109-3118
    • (1998) J. Cell Sci. , vol.111 , pp. 3109-3118
    • Fleckenstein, D.1    Rohde, M.2    Klionsky, D.J.3    Rudiger, M.4
  • 22
    • 0030015868 scopus 로고    scopus 로고
    • Homotypic vacuole fusion requires Sec17p (yeast α-SNAP) and Sec18p (yeast NSF)
    • Haas A, Wickner W (1996) Homotypic vacuole fusion requires Sec17p (yeast α-SNAP) and Sec18p (yeast NSF). EMBO J 15: 3296-3305
    • (1996) EMBO J. , vol.15 , pp. 3296-3305
    • Haas, A.1    Wickner, W.2
  • 24
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • Hancock JF (2003) Ras proteins: different signals from different locations. Nat Rev Mol Cell Biol 4: 373-384
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 27
    • 0025231709 scopus 로고
    • Purification of protein fatty acyltransferase and determination of its distribution and topology
    • Kasinathan C, Grzelinska E, Okazaki K, Slomiany BL, Slomiany A (1990) Purification of protein fatty acyltransferase and determination of its distribution and topology. J Biol Chem 265: 5139-5144
    • (1990) J. Biol. Chem. , vol.265 , pp. 5139-5144
    • Kasinathan, C.1    Grzelinska, E.2    Okazaki, K.3    Slomiany, B.L.4    Slomiany, A.5
  • 30
    • 0030955679 scopus 로고    scopus 로고
    • Acyl-CoA binding proteins inhibit the nonenzymic S-acylation of cysteinyl-containing peptide sequences by long-chain acyl-CoAs
    • Leventis R, Juel G, Knudsen JK, Silvius JR (1997) Acyl-CoA binding proteins inhibit the nonenzymic S-acylation of cysteinyl-containing peptide sequences by long-chain acyl-CoAs. Biochemistry 36: 5546-5553
    • (1997) Biochemistry , vol.36 , pp. 5546-5553
    • Leventis, R.1    Juel, G.2    Knudsen, J.K.3    Silvius, J.R.4
  • 31
    • 0037031868 scopus 로고    scopus 로고
    • Mass spectrometric analysis of GAP-43/neuromodulin reveals the presence of a variety of fatty acylated species
    • Liang X, Lu Y, Neubert TA, Resh MD (2002) Mass spectrometric analysis of GAP-43/neuromodulin reveals the presence of a variety of fatty acylated species. J Biol Chem 277: 33032-33040
    • (2002) J. Biol. Chem. , vol.277 , pp. 33032-33040
    • Liang, X.1    Lu, Y.2    Neubert, T.A.3    Resh, M.D.4
  • 32
    • 1542349837 scopus 로고    scopus 로고
    • The N-terminal SH4 region of the Src family kinase Fyn is modified by methylation and heterogeneous fatty acylation: Role in membrane targeting, cell adhesion, and spreading
    • Liang X, Lu Y, Wilkes M, Neubert TA, Resh MD (2004) The N-terminal SH4 region of the Src family kinase Fyn is modified by methylation and heterogeneous fatty acylation: role in membrane targeting, cell adhesion, and spreading. J Biol Chem 279: 8133-8139
    • (2004) J. Biol. Chem. , vol.279 , pp. 8133-8139
    • Liang, X.1    Lu, Y.2    Wilkes, M.3    Neubert, T.A.4    Resh, M.D.5
  • 33
    • 0038321812 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein palmitoylation
    • Linder ME, Deschenes RJ (2003) New insights into the mechanisms of protein palmitoylation. Biochemistry 42: 4311-4320
    • (2003) Biochemistry , vol.42 , pp. 4311-4320
    • Linder, M.E.1    Deschenes, R.J.2
  • 34
    • 1242306884 scopus 로고    scopus 로고
    • Model organisms lead the way to protein palmitoylation
    • Linder ME, Deschenes RJ (2004) Model organisms lead the way to protein palmitoylation. J Cell Sci 117: 521-526
    • (2004) J. Cell Sci. , vol.117 , pp. 521-526
    • Linder, M.E.1    Deschenes, R.J.2
  • 35
    • 0029789954 scopus 로고    scopus 로고
    • Purification of a protein palmitoyltransferase that acts on H-Ras protein and on a C-terminal N-Ras peptide
    • erratum in J Biol Chem (1999) 274: 3252
    • Liu L, Dudler T, Gelb MH (1996) Purification of a protein palmitoyltransferase that acts on H-Ras protein and on a C-terminal N-Ras peptide. J Biol Chem 271: 23269-23276; erratum in J Biol Chem (1999) 274: 3252
    • (1996) J. Biol. Chem. , vol.271 , pp. 23269-23276
    • Liu, L.1    Dudler, T.2    Gelb, M.H.3
  • 36
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo S, Greentree WK, Linder ME, Deschenes RJ (2002) Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J Biol Chem 277: 41268-41273
    • (2002) J. Biol. Chem. , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 37
    • 2942742564 scopus 로고    scopus 로고
    • Novel lipid modifications of secreted protein signals
    • Mann RK, Beachy PA (2004) Novel lipid modifications of secreted protein signals. Annu Rev Biochem 73: 891-923
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 891-923
    • Mann, R.K.1    Beachy, P.A.2
  • 38
    • 4243518910 scopus 로고    scopus 로고
    • Influence of the pK(a) value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases
    • Mossner E, Iwai H, Glockshuber R (2000) Influence of the p K(a) value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases. FEBS Lett 477: 21-26
    • (2000) FEBS Lett. , vol.477 , pp. 21-26
    • Mossner, E.1    Iwai, H.2    Glockshuber, R.3
  • 40
    • 0031669618 scopus 로고    scopus 로고
    • YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance
    • Pan X, Goldfarb DS (1998) YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance. J Cell Sci 111: 2137-2147
    • (1998) J. Cell Sci. , vol.111 , pp. 2137-2147
    • Pan, X.1    Goldfarb, D.S.2
  • 41
    • 0028033931 scopus 로고
    • Cysteine-containing pepticle sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface
    • Quesnel S, Silvius JR (1994) Cysteine-containing pepticle sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface. Biochemistry 33: 13340-13348
    • (1994) Biochemistry , vol.33 , pp. 13340-13348
    • Quesnel, S.1    Silvius, J.R.2
  • 42
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta 1451: 1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 43
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1 p is a palmitoyl transferase
    • Roth AF, Feng Y, Chen L, Davis NG (2002) The yeast DHHC cysteine-rich domain protein Akr1 p is a palmitoyl transferase. J Cell Biol 159: 23-28
    • (2002) J. Cell Biol. , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 44
    • 0029767683 scopus 로고    scopus 로고
    • Lipid-modified, cysteinyl-containing peptides of diverse structures are efficiently S-acylated at the plasma membrane of mammalian cells
    • Schroeder H, Leventis R, Shahinian S, Walton PA, Silvius JR (1996) Lipid-modified, cysteinyl-containing peptides of diverse structures are efficiently S-acylated at the plasma membrane of mammalian cells. J Cell Biol 134: 647-660
    • (1996) J. Cell Biol. , vol.134 , pp. 647-660
    • Schroeder, H.1    Leventis, R.2    Shahinian, S.3    Walton, P.A.4    Silvius, J.R.5
  • 45
    • 0030696229 scopus 로고    scopus 로고
    • S-acylation and plasma membrane targeting of the farnesylated carboxyl-terminal peptide of N-RAS in mammalian fibroblasts
    • Schroeder H, Leventis R, Rex S, Schelhaas M, Nagele E, Waldmann H, Silvius JR (1997) S-acylation and plasma membrane targeting of the farnesylated carboxyl-terminal peptide of N-RAS in mammalian fibroblasts. Biochemistry 36: 13102-13109
    • (1997) Biochemistry , vol.36 , pp. 13102-13109
    • Schroeder, H.1    Leventis, R.2    Rex, S.3    Schelhaas, M.4    Nagele, E.5    Waldmann, H.6    Silvius, J.R.7
  • 46
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys JE, Linder ME (2004) Palmitoylation of intracellular signaling proteins: regulation and function. Annu Rev Biochem 73: 559-587
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 47
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC (2001) Nitrosylation: the prototypic redox-based signaling mechanism. Cell 106: 675-683
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 48
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • Sun J, Xin C, Eu JP, Stamler JS, Meissner G (2001) Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc Natl Acad Sci USA 98: 11158-11162
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 49
    • 0035958644 scopus 로고    scopus 로고
    • An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p
    • Tochio H, Tsui MM, Banfield DK, Zhang M (2001) An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p. Science 293: 698-702
    • (2001) Science , vol.293 , pp. 698-702
    • Tochio, H.1    Tsui, M.M.2    Banfield, D.K.3    Zhang, M.4
  • 50
    • 0033957849 scopus 로고    scopus 로고
    • Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin
    • Veit M (2000) Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin. Biochem J 345: 145-151
    • (2000) Biochem. J. , vol.345 , pp. 145-151
    • Veit, M.1
  • 51
    • 0031680028 scopus 로고    scopus 로고
    • Palmitoylation of rhodopsin with S-protein acyltransferase: Enzyme catalyzed reaction versus autocatalytic acylation
    • erratum in (1999) 1436: 630
    • Veit M, Sachs K, Heckelmann M, Maretzki D, Hofmann KP, Schmidt MF (1998) Palmitoylation of rhodopsin with S-protein acyltransferase: enzyme catalyzed reaction versus autocatalytic acylation. Biochim Biophys Acta 1394: 90-98; erratum in (1999) 1436: 630
    • (1998) Biochim. Biophys. Acta , vol.1394 , pp. 90-98
    • Veit, M.1    Sachs, K.2    Heckelmann, M.3    Maretzki, D.4    Hofmann, K.P.5    Schmidt, M.F.6
  • 52
    • 0035876373 scopus 로고    scopus 로고
    • Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion
    • Veit M, Laage R, Dietrich L, Wang L, Ungermann C (2001) Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion. EMBO J 20: 3145-3155
    • (2001) EMBO J. , vol.20 , pp. 3145-3155
    • Veit, M.1    Laage, R.2    Dietrich, L.3    Wang, L.4    Ungermann, C.5
  • 53
    • 0037431058 scopus 로고    scopus 로고
    • Biochemical characterization of the vacuolar palmitoyl acyltransferase
    • Veit M, Dietrich LEP, Ungermann C (2003) Biochemical characterization of the vacuolar palmitoyl acyltransferase. FEBS Lett 540: 101-105
    • (2003) FEBS Lett. , vol.540 , pp. 101-105
    • Veit, M.1    Dietrich, L.E.P.2    Ungermann, C.3
  • 54
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole
    • Wang YX, Catlett NL, Weisman LS (1998) Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J Cell Biol 140: 1063-1074
    • (1998) J. Cell Biol. , vol.140 , pp. 1063-1074
    • Wang, Y.X.1    Catlett, N.L.2    Weisman, L.S.3
  • 55
    • 0035860689 scopus 로고    scopus 로고
    • Fusion of docked membranes requires the armadillo repeat protein Vac8p
    • Wang YX, Kauffman EJ, Duex JE, Weisman LS (2001) Fusion of docked membranes requires the armadillo repeat protein Vac8p. J Biol Chem 276: 35133-35140
    • (2001) J. Biol. Chem. , vol.276 , pp. 35133-35140
    • Wang, Y.X.1    Kauffman, E.J.2    Duex, J.E.3    Weisman, L.S.4
  • 56
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation
    • Xu L, Eu JP, Meissner G, Stamler JS (1998) Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S nitrosylation. Science 279:234-237
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 57
    • 0346668323 scopus 로고    scopus 로고
    • Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins
    • Zhao L, Lobo S, Deng X, Ault AD, Deschenes RJ (2002) Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins. J Biol Chem 277: 49352-49359
    • (2002) J. Biol. Chem. , vol.277 , pp. 49352-49359
    • Zhao, L.1    Lobo, S.2    Deng, X.3    Ault, A.D.4    Deschenes, R.J.5


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