메뉴 건너뛰기




Volumn 43, Issue , 2015, Pages 240-245

Palmitoylation and palmitoyl-transferases in Plasmodium parasites

Author keywords

Palmitoylation; Palmitoyltransferase; Plasmodium falciparum

Indexed keywords

ACYLTRANSFERASE; PALMITOYL TRANSFERASE; TRANSFERASE; UNCLASSIFIED DRUG; PALMITIC ACID; SERINE PALMITOYLTRANSFERASE;

EID: 84934941230     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140289     Document Type: Article
Times cited : (18)

References (35)
  • 2
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Bozdech, Z., Llinas, M., Pulliam, B. L., Wong, E. D., Zhu, J. and DeRisi, J. L. (2003) The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum. PLoS Biol. 1, E5
    • (2003) PLoS Biol. , vol.1 , pp. E5
    • Bozdech, Z.1    Llinas, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    DeRisi, J.L.6
  • 3
    • 84869114925 scopus 로고    scopus 로고
    • The cellular and molecular basis for malaria parasite invasion of the human red blood cell
    • Cowman, A. F., Berry, D. and Baum, J. (2012) The cellular and molecular basis for malaria parasite invasion of the human red blood cell. J. Cell Biol. 198, 961-971
    • (2012) J. Cell Biol. , vol.198 , pp. 961-971
    • Cowman, A.F.1    Berry, D.2    Baum, J.3
  • 4
    • 80054901700 scopus 로고    scopus 로고
    • The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries
    • Treeck, M., Sanders, J. L., Elias, J. E. and Boothroyd, J. C. (2011) The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries. Cell Host Microbe 10, 410-419
    • (2011) Cell Host Microbe , vol.10 , pp. 410-419
    • Treeck, M.1    Sanders, J.L.2    Elias, J.E.3    Boothroyd, J.C.4
  • 6
    • 84899004901 scopus 로고    scopus 로고
    • Phosphoinositide metabolism links cGMP-dependent protein kinase G to essential Ca (2) (+) signals at key decision points in the life cycle of malaria parasites
    • Brochet, M., Collins, M. O., Smith, T. K., Thompson, E., Sebastian, S., Volkmann, K., Schwach, F., Chappell, L., Gomes, A. R., Berriman, M. et al. (2014) Phosphoinositide metabolism links cGMP-dependent protein kinase G to essential Ca (2) (+) signals at key decision points in the life cycle of malaria parasites. PLoS Biol. 12, e1001806
    • (2014) PLoS Biol. , vol.12 , pp. e1001806
    • Brochet, M.1    Collins, M.O.2    Smith, T.K.3    Thompson, E.4    Sebastian, S.5    Volkmann, K.6    Schwach, F.7    Chappell, L.8    Gomes, A.R.9    Berriman, M.10
  • 7
    • 84890644637 scopus 로고    scopus 로고
    • Status of large-scale analysis of posttranslational modifications by mass spectrometryMol
    • Olsen, J. V. and Mann, M. (2013) Status of large-scale analysis of posttranslational modifications by mass spectrometryMol. Cell. Proteomics 12, 3444-3452
    • (2013) Cell. Proteomics , vol.12 , pp. 3444-3452
    • Olsen, J.V.1    Mann, M.2
  • 8
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel, R. C. and Green, W. N. (2004) Labeling and quantifying sites of protein palmitoylation. Biotechniques 36, 276-285 PubMed
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 9
    • 55249119967 scopus 로고    scopus 로고
    • Chemical probes for profiling fatty acid-associated proteins in living cells
    • Raghavan, A., Charron, G., Flexner, J. and Hang, H. C. (2008) Chemical probes for profiling fatty acid-associated proteins in living cells. Bioorg. Med. Chem. Lett. 18, 5982-5986
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5982-5986
    • Raghavan, A.1    Charron, G.2    Flexner, J.3    Hang, H.C.4
  • 12
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • Martin, B. R. and Cravatt, B. F. (2009) Large-scale profiling of protein palmitoylation in mammalian cells. Nat. Methods 6, 135-138
    • (2009) Nat. Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 13
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S. E., Foster, L. J. and Mann, M. (2003) Mass spectrometric-based approaches in quantitative proteomics. Methods 29, 124-130
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 14
    • 84865125774 scopus 로고    scopus 로고
    • Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis
    • Jones, M. L., Collins, M. O., Goulding, D., Choudhary, J. S. and Rayner, J. C. (2012) Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis. Cell Host Microbe 12, 246-258
    • (2012) Cell Host Microbe , vol.12 , pp. 246-258
    • Jones, M.L.1    Collins, M.O.2    Goulding, D.3    Choudhary, J.S.4    Rayner, J.C.5
  • 15
    • 0032883098 scopus 로고    scopus 로고
    • Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
    • Bartels, D. J., Mitchell, D. A., Dong, X. and Deschenes, R. J. (1999) Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Mol. Cell Biol. 19, 6775-6787 PubMed
    • (1999) Mol. Cell Biol. , vol.19 , pp. 6775-6787
    • Bartels, D.J.1    Mitchell, D.A.2    Dong, X.3    Deschenes, R.J.4
  • 16
    • 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., Dong, X., Ault, A. D. and Deschenes, R. J. (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    Dong, X.3    Ault, A.D.4    Deschenes, R.J.5
  • 17
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase
    • Roth, A. F., Feng, Y., Chen, L. and Davis, N. G. (2002) The yeast DHHC cysteine-rich domain protein Akr1p 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
  • 19
    • 79955649200 scopus 로고    scopus 로고
    • DHHC palmitoyl transferases: Substrate interactions and (patho) physiology
    • Greaves, J. and Chamberlain, L. H. (2011) DHHC palmitoyl transferases: substrate interactions and (patho) physiology. Trends Biochem. Sci. 36, 245-253
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 245-253
    • Greaves, J.1    Chamberlain, L.H.2
  • 20
    • 2342611064 scopus 로고    scopus 로고
    • Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite
    • Billker, O., Dechamps, S., Tewari, R., Wenig, G., Franke-Fayard, B. and Brinkmann, V. (2004) Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite. Cell 117, 503-514
    • (2004) Cell , vol.117 , pp. 503-514
    • Billker, O.1    Dechamps, S.2    Tewari, R.3    Wenig, G.4    Franke-Fayard, B.5    Brinkmann, V.6
  • 21
    • 0035853753 scopus 로고    scopus 로고
    • Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase
    • Kieschnick, H., Wakefield, T., Narducci, C. A. and Beckers, C. (2001) Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase. J. Biol. Chem. 276, 12369-12377
    • (2001) J. Biol. Chem. , vol.276 , pp. 12369-12377
    • Kieschnick, H.1    Wakefield, T.2    Narducci, C.A.3    Beckers, C.4
  • 23
    • 79956295210 scopus 로고    scopus 로고
    • Differential regulation of two palmitoylation sites in the cytoplasmic tail of the beta1-adrenergic receptor
    • Zuckerman, D. M., Hicks, S. W., Charron, G., Hang, H. C. and Machamer, C. E. (2011) Differential regulation of two palmitoylation sites in the cytoplasmic tail of the beta1-adrenergic receptor. J. Biol. Chem. 286, 19014-19023
    • (2011) J. Biol. Chem. , vol.286 , pp. 19014-19023
    • Zuckerman, D.M.1    Hicks, S.W.2    Charron, G.3    Hang, H.C.4    Machamer, C.E.5
  • 24
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes
    • Yang, W., Di Vizio, D., Kirchner, M., Steen, H. and Freeman, M. R. (2010) Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes. Mol. Cell. Proteomics 9, 54-70
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5
  • 26
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R., Zougman, A., Nagaraj, N. and Mann, M. (2009) Universal sample preparation method for proteome analysis. Nat. Methods 6, 359-362
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 28
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann, K. and Stoffel, W. (1993) TMbase - A database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 374, 166
    • (1993) Biol. Chem. Hoppe-seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 29
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • Letunic, I., Doerks, T. and Bork, P. (2011) SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40, D302-305
    • (2011) Nucleic Acids Res. , vol.40 , pp. D302-D305
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 30
    • 80053345905 scopus 로고    scopus 로고
    • SignalP4.0: Discriminating signal peptides from transmembrane regions
    • Petersen, T. N., Brunak, S., von Heijne, G. and Nielsen, H. (2011) SignalP4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 8, 785-786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 31
    • 84868332245 scopus 로고    scopus 로고
    • The Plasmodium falciparum schizont phosphoproteome reveals extensive phosphatidylinositol and cAMP-protein kinase A signaling
    • Lasonder, E., Green, J. L., Camarda, G., Talabani, H., Holder, A. A., Langsley, G. and Alano, P. (2012) The Plasmodium falciparum schizont phosphoproteome reveals extensive phosphatidylinositol and cAMP-protein kinase A signaling. J. Proteome Res. 11, 5323-5337
    • (2012) J. Proteome Res. , vol.11 , pp. 5323-5337
    • Lasonder, E.1    Green, J.L.2    Camarda, G.3    Talabani, H.4    Holder, A.A.5    Langsley, G.6    Alano, P.7
  • 33
    • 84898860672 scopus 로고    scopus 로고
    • Confident and sensitive phosphoproteomics using combinations of collision induced dissociation and electron transfer dissociation
    • Collins, M. O., Wright, J. C., Jones, M., Rayner, J. C. and Choudhary, J. S. (2014) Confident and sensitive phosphoproteomics using combinations of collision induced dissociation and electron transfer dissociation. J. Proteomics 103, 1-14
    • (2014) J. Proteomics , vol.103 , pp. 1-14
    • Collins, M.O.1    Wright, J.C.2    Jones, M.3    Rayner, J.C.4    Choudhary, J.S.5
  • 34
    • 84873406471 scopus 로고    scopus 로고
    • Conditional genome engineering in Toxoplasma gondii uncovers alternative invasion mechanisms
    • Andenmatten, N., Egarter, S., Jackson, A. J., Jullien, N., Herman, J. P. and Meissner, M. (2013) Conditional genome engineering in Toxoplasma gondii uncovers alternative invasion mechanisms. Nat. Methods 10, 125-127
    • (2013) Nat. Methods , vol.10 , pp. 125-127
    • Andenmatten, N.1    Egarter, S.2    Jackson, A.J.3    Jullien, N.4    Herman, J.P.5    Meissner, M.6
  • 35
    • 84877817952 scopus 로고    scopus 로고
    • Robust inducible Cre recombinase activity in the human malaria parasite Plasmodium falciparum enables efficient gene deletion within a single asexual erythrocytic growth cycle
    • Collins, C. R., Das, S., Wong, E. H., Andenmatten, N., Stallmach, R., Hackett, F., Herman, J. P., Muller, S., Meissner, M. and Blackman, M. J. (2013) Robust inducible Cre recombinase activity in the human malaria parasite Plasmodium falciparum enables efficient gene deletion within a single asexual erythrocytic growth cycle. Mol. Microbiol. 88, 687-701
    • (2013) Mol. Microbiol. , vol.88 , pp. 687-701
    • Collins, C.R.1    Das, S.2    Wong, E.H.3    Andenmatten, N.4    Stallmach, R.5    Hackett, F.6    Herman, J.P.7    Muller, S.8    Meissner, M.9    Blackman, M.J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.