메뉴 건너뛰기




Volumn 291, Issue 13, 2016, Pages 6664-6678

Erratum: Conserved amphipathic helices mediate lipid droplet targeting of perilipins 1–3 (Additions and Corrections (2016) 291 (6664–6678) DOI:10.1074/jbc.M115.691048);Conserved amphipathic helices mediate lipid droplet targeting of perilipins 1-3

Author keywords

[No Author keywords available]

Indexed keywords

MICELLES; PHOSPHOLIPIDS; YEAST;

EID: 84964873073     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1016/j.jbc.2021.101490     Document Type: Erratum
Times cited : (99)

References (81)
  • 1
    • 0037113954 scopus 로고    scopus 로고
    • The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition
    • Tauchi-Sato, K., Ozeki, S., Houjou, T., Taguchi, R., and Fujimoto, T. (2002) The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition. J. Biol. Chem. 277, 44507-44512.
    • (2002) J. Biol. Chem , vol.277 , pp. 44507-44512
    • Tauchi-Sato, K.1    Ozeki, S.2    Houjou, T.3    Taguchi, R.4    Fujimoto, T.5
  • 4
    • 84874900503 scopus 로고    scopus 로고
    • Biochemistry and pathophysiology of intravascular and intracellular lipolysis
    • Young, S. G., and Zechner, R. (2013) Biochemistry and pathophysiology of intravascular and intracellular lipolysis. Genes Dev. 27, 459-484.
    • (2013) Genes Dev , vol.27 , pp. 459-484
    • Young, S.G.1    Zechner, R.2
  • 5
    • 84933676570 scopus 로고    scopus 로고
    • The genetics of lipid storage and human lipodystrophies
    • Robbins, A. L., and Savage, D. B. (2015) The genetics of lipid storage and human lipodystrophies. Trends Mol. Med. 21, 433-438.
    • (2015) Trends Mol. Med , vol.21 , pp. 433-438
    • Robbins, A.L.1    Savage, D.B.2
  • 6
    • 36649015243 scopus 로고    scopus 로고
    • Thematic review series: Adipocyte biology. The perilipin family of structural lipid droplet proteins: Stabilization of lipid droplets and control of lipolysis
    • Brasaemle, D. L. (2007) Thematic review series: Adipocyte biology. The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis. J. Lipid Res. 48, 2547-2559.
    • (2007) J. Lipid Res , vol.48 , pp. 2547-2559
    • Brasaemle, D.L.1
  • 7
    • 71749098785 scopus 로고    scopus 로고
    • Perilipin controls lipolysis by regulating the interactions of ABhydrolase containing 5 (Abhd5) and adipose triglyceride lipase (Atgl)
    • Granneman, J. G., Moore, H.-P., Krishnamoorthy, R., and Rathod, M. (2009) Perilipin controls lipolysis by regulating the interactions of ABhydrolase containing 5 (Abhd5) and adipose triglyceride lipase (Atgl). J. Biol. Chem. 284, 34538-34544.
    • (2009) J. Biol. Chem , vol.284 , pp. 34538-34544
    • Granneman, J.G.1    Moore, H.-P.2    Krishnamoorthy, R.3    Rathod, M.4
  • 9
    • 30044438117 scopus 로고    scopus 로고
    • Perilipin targets a novel pool of lipid droplets for lipolytic attack by hormone-sensitive lipase
    • Moore, H.-P., Silver, R. B., Mottillo, E. P., Bernlohr, D. A., and Granneman, J. G. (2005) Perilipin targets a novel pool of lipid droplets for lipolytic attack by hormone-sensitive lipase. J. Biol. Chem. 280, 43109-43120.
    • (2005) J. Biol. Chem , vol.280 , pp. 43109-43120
    • Moore, H.-P.1    Silver, R.B.2    Mottillo, E.P.3    Bernlohr, D.A.4    Granneman, J.G.5
  • 10
    • 40749148508 scopus 로고    scopus 로고
    • Location, location: Protein trafficking and lipolysis in adipocytes
    • Granneman, J. G., and Moore, H.-P. (2008) Location, location: protein trafficking and lipolysis in adipocytes. Trends Endocrinol. Metab. 19, 3-9.
    • (2008) Trends Endocrinol. Metab , vol.19 , pp. 3-9
    • Granneman, J.G.1    Moore, H.-P.2
  • 13
    • 80053406177 scopus 로고    scopus 로고
    • Human frame shift mutations affecting the carboxyl terminus of perilipin increase lipolysis by failing to sequester the adipose triglyceride lipase (ATGL) coactivator AB-hydrolase-containing 5 (ABHD5)
    • Gandotra, S., Lim, K., Girousse, A., Saudek, V., O'Rahilly, S., and Savage, D. B. (2011) Human frame shift mutations affecting the carboxyl terminus of perilipin increase lipolysis by failing to sequester the adipose triglyceride lipase (ATGL) coactivator AB-hydrolase-containing 5 (ABHD5). J. Biol. Chem. 286, 34998-35006.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34998-35006
    • Gandotra, S.1    Lim, K.2    Girousse, A.3    Saudek, V.4    O'Rahilly, S.5    Savage, D.B.6
  • 14
    • 84903467171 scopus 로고    scopus 로고
    • Perilipins 2 and 3 lack a carboxy-terminal domain present in perilipin 1 involved in sequestering ABHD5 and suppressing basal lipolysis
    • Patel, S., Yang, W., Kozusko, K., Saudek, V., and Savage, D. B. (2014) Perilipins 2 and 3 lack a carboxy-terminal domain present in perilipin 1 involved in sequestering ABHD5 and suppressing basal lipolysis. Proc. Natl. Acad. Sci. U.S.A. 111, 9163-9168.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 9163-9168
    • Patel, S.1    Yang, W.2    Kozusko, K.3    Saudek, V.4    Savage, D.B.5
  • 16
    • 78650107057 scopus 로고    scopus 로고
    • Lipolysis- A highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores
    • Lass, A., Zimmermann, R., Oberer, M., and Zechner, R. (2011) Lipolysis-a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores. Prog. Lipid Res. 50, 14-27.
    • (2011) Prog. Lipid Res , vol.50 , pp. 14-27
    • Lass, A.1    Zimmermann, R.2    Oberer, M.3    Zechner, R.4
  • 18
    • 79953160438 scopus 로고    scopus 로고
    • Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase
    • Granneman, J. G., Moore, H.-P., Mottillo, E. P., Zhu, Z., and Zhou, L. (2011) Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase. J. Biol. Chem. 286, 5126-5135.
    • (2011) J. Biol. Chem , vol.286 , pp. 5126-5135
    • Granneman, J.G.1    Moore, H.-P.2    Mottillo, E.P.3    Zhu, Z.4    Zhou, L.5
  • 19
    • 33745907543 scopus 로고    scopus 로고
    • Analysis ofinteraction partners for perilipin and ADRP on lipid droplets
    • Yamaguchi, T., Omatsu, N., Omukae, A., and Osumi, T. (2006) Analysis ofinteraction partners for perilipin and ADRP on lipid droplets. Mol. Cell. Biochem. 284, 167-173.
    • (2006) Mol. Cell. Biochem , vol.284 , pp. 167-173
    • Yamaguchi, T.1    Omatsu, N.2    Omukae, A.3    Osumi, T.4
  • 20
    • 59149104232 scopus 로고    scopus 로고
    • Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation
    • Granneman, J. G., Moore, H.-P., Mottillo, E. P., and Zhu, Z. (2009) Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation. J. Biol. Chem. 284, 3049-3057.
    • (2009) J. Biol. Chem , vol.284 , pp. 3049-3057
    • Granneman, J.G.1    Moore, H.-P.2    Mottillo, E.P.3    Zhu, Z.4
  • 21
    • 0030903768 scopus 로고    scopus 로고
    • Posttranslational regulation of perilipin expression
    • Brasaemle, D. L., Barber, T., Kimmel, A. R., and Londos, C. (1997) Posttranslational regulation of perilipin expression. J. Biol. Chem. 272, 9378-9387.
    • (1997) J. Biol. Chem , vol.272 , pp. 9378-9387
    • Brasaemle, D.L.1    Barber, T.2    Kimmel, A.R.3    Londos, C.4
  • 22
    • 33646017106 scopus 로고    scopus 로고
    • Degradation of perilipin is mediated through ubiquitination-proteasome pathway
    • Xu, G., Sztalryd, C., and Londos, C. (2006) Degradation of perilipin is mediated through ubiquitination-proteasome pathway. Biochim. Biophys. Acta 1761, 83-90.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 83-90
    • Xu, G.1    Sztalryd, C.2    Londos, C.3
  • 24
    • 30044445455 scopus 로고    scopus 로고
    • Post-translational regulation of adipose differentiation- related protein by the ubiquitin/proteasome pathway
    • Xu, G., Sztalryd, C., Lu, X., Tansey, J. T., Gan, J., Dorward, H., Kimmel, A. R., and Londos, C. (2005) Post-translational regulation of adipose differentiation- related protein by the ubiquitin/proteasome pathway. J. Biol. Chem. 280, 42841-42847.
    • (2005) J. Biol. Chem , vol.280 , pp. 42841-42847
    • Xu, G.1    Sztalryd, C.2    Lu, X.3    Tansey, J.T.4    Gan, J.5    Dorward, H.6    Kimmel, A.R.7    Londos, C.8
  • 25
    • 30844437022 scopus 로고    scopus 로고
    • ADRP/adipophilin is degraded through the proteasome-dependent pathway during regression of lipidstoring cells
    • Masuda, Y., Itabe, H., Odaki, M., Hama, K., Fujimoto, Y., Mori, M., Sasabe, N., Aoki, J., Arai, H., and Takano, T. (2006) ADRP/adipophilin is degraded through the proteasome-dependent pathway during regression of lipidstoring cells. J. Lipid Res. 47, 87-98.
    • (2006) J. Lipid Res , vol.47 , pp. 87-98
    • Masuda, Y.1    Itabe, H.2    Odaki, M.3    Hama, K.4    Fujimoto, Y.5    Mori, M.6    Sasabe, N.7    Aoki, J.8    Arai, H.9    Takano, T.10
  • 26
    • 0035895982 scopus 로고    scopus 로고
    • TIP47 associates with lipid droplets
    • Wolins, N. E., Rubin, B., and Brasaemle, D. L. (2001) TIP47 associates with lipid droplets. J. Biol. Chem. 276, 5101-5108.
    • (2001) J. Biol. Chem , vol.276 , pp. 5101-5108
    • Wolins, N.E.1    Rubin, B.2    Brasaemle, D.L.3
  • 28
    • 0037200026 scopus 로고    scopus 로고
    • Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)- related proteins in mammals, Drosophila, and Dictyostelium
    • Miura, S., Gan, J.-W., Brzostowski, J., Parisi, M. J., Schultz, C. J., Londos, C., Oliver, B., and Kimmel, A. R. (2002) Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)- related proteins in mammals, Drosophila, and Dictyostelium. J. Biol. Chem. 277, 32253-32257.
    • (2002) J. Biol. Chem , vol.277 , pp. 32253-32257
    • Miura, S.1    Gan, J.-W.2    Brzostowski, J.3    Parisi, M.J.4    Schultz, C.J.5    Londos, C.6    Oliver, B.7    Kimmel, A.R.8
  • 29
    • 0032076636 scopus 로고    scopus 로고
    • TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • Díaz, E., and Pfeffer, S. R. (1998) TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking. Cell 93, 433-443.
    • (1998) Cell , vol.93 , pp. 433-443
    • Díaz, E.1    Pfeffer, S.R.2
  • 30
    • 79960398841 scopus 로고    scopus 로고
    • Lipid droplets are functionally connected to the endoplasmic reticulum in saccharomyces cerevisiae
    • Jacquier, N., Choudhary, V., Mari, M., Toulmay, A., Reggiori, F., and Schneiter, R. (2011) Lipid droplets are functionally connected to the endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Sci. 124, 2424-2437.
    • (2011) J. Cell Sci , vol.124 , pp. 2424-2437
    • Jacquier, N.1    Choudhary, V.2    Mari, M.3    Toulmay, A.4    Reggiori, F.5    Schneiter, R.6
  • 32
    • 84872472046 scopus 로고    scopus 로고
    • Monotopic topology is required for lipid droplet targeting of ancient ubiquitous protein 1
    • Stevanovic, A., and Thiele, C. (2013) Monotopic topology is required for lipid droplet targeting of ancient ubiquitous protein 1. J. Lipid Res. 54, 503-513.
    • (2013) J. Lipid Res , vol.54 , pp. 503-513
    • Stevanovic, A.1    Thiele, C.2
  • 33
    • 0033071156 scopus 로고    scopus 로고
    • Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells
    • Londos, C., Brasaemle, D. L., Schultz, C. J., Segrest, J. P., and Kimmel, A. R. (1999) Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells. Semin. Cell Dev. Biol. 10, 51-58.
    • (1999) Semin. Cell Dev. Biol , vol.10 , pp. 51-58
    • Londos, C.1    Brasaemle, D.L.2    Schultz, C.J.3    Segrest, J.P.4    Kimmel, A.R.5
  • 34
    • 0037414820 scopus 로고    scopus 로고
    • The central domain is required to target and anchor perilipin A to lipid droplets
    • Garcia, A., Sekowski, A., Subramanian, V., and Brasaemle, D. L. (2003) The central domain is required to target and anchor perilipin A to lipid droplets. J. Biol. Chem. 278, 625-635.
    • (2003) J. Biol. Chem , vol.278 , pp. 625-635
    • Garcia, A.1    Sekowski, A.2    Subramanian, V.3    Brasaemle, D.L.4
  • 35
    • 20544457076 scopus 로고    scopus 로고
    • Hydrophobic sequences target and anchor perilipin A to lipid droplets
    • Subramanian, V., Garcia, A., Sekowski, A., and Brasaemle, D. L. (2004) Hydrophobic sequences target and anchor perilipin A to lipid droplets. J. Lipid Res. 45, 1983-1991.
    • (2004) J. Lipid Res , vol.45 , pp. 1983-1991
    • Subramanian, V.1    Garcia, A.2    Sekowski, A.3    Brasaemle, D.L.4
  • 36
    • 0347065339 scopus 로고    scopus 로고
    • Lipase-selective functional domains of perilipin A differentially regulate constitutive and protein kinase A-stimulated lipolysis
    • Zhang, H. H., Souza, S. C., Muliro, K. V., Kraemer, F. B., Obin, M. S., and Greenberg, A. S. (2003) Lipase-selective functional domains of perilipin A differentially regulate constitutive and protein kinase A-stimulated lipolysis. J. Biol. Chem. 278, 51535-51542.
    • (2003) J. Biol. Chem , vol.278 , pp. 51535-51542
    • Zhang, H.H.1    Souza, S.C.2    Muliro, K.V.3    Kraemer, F.B.4    Obin, M.S.5    Greenberg, A.S.6
  • 37
    • 70350379586 scopus 로고    scopus 로고
    • Functional interaction of hormone-sensitive lipase and perilipin in lipolysis
    • Shen, W.-J., Patel, S., Miyoshi, H., Greenberg, A. S., and Kraemer, F. B. (2009) Functional interaction of hormone-sensitive lipase and perilipin in lipolysis. J. Lipid Res. 50, 2306-2313.
    • (2009) J. Lipid Res , vol.50 , pp. 2306-2313
    • Shen, W.-J.1    Patel, S.2    Miyoshi, H.3    Greenberg, A.S.4    Kraemer, F.B.5
  • 39
    • 0037903214 scopus 로고    scopus 로고
    • Live cell analysis and targeting of the lipid droplet-binding adipocyte differentiation-related protein
    • Targett-Adams, P., Chambers, D., Gledhill, S., Hope, R. G., Coy, J. F., Girod, A., and McLauchlan, J. (2003) Live cell analysis and targeting of the lipid droplet-binding adipocyte differentiation-related protein. J. Biol. Chem. 278, 15998-16007.
    • (2003) J. Biol. Chem , vol.278 , pp. 15998-16007
    • Targett-Adams, P.1    Chambers, D.2    Gledhill, S.3    Hope, R.G.4    Coy, J.F.5    Girod, A.6    McLauchlan, J.7
  • 40
    • 0038546739 scopus 로고    scopus 로고
    • Adipose differentiation-related protein has two independent domains for targeting to lipid droplets
    • Nakamura, N., and Fujimoto, T. (2003) Adipose differentiation-related protein has two independent domains for targeting to lipid droplets. Biochem. Biophys. Res. Commun. 306, 333-338.
    • (2003) Biochem. Biophys. Res. Commun , vol.306 , pp. 333-338
    • Nakamura, N.1    Fujimoto, T.2
  • 42
    • 79958827096 scopus 로고    scopus 로고
    • The adipophilin C terminus is a selffolding membrane-binding domain that is important for milk lipid secretion
    • Chong, B. M., Russell, T. D., Schaack, J., Orlicky, D. J., Reigan, P., Ladinsky, M., and McManaman, J. L. (2011) The adipophilin C terminus is a selffolding membrane-binding domain that is important for milk lipid secretion. J. Biol. Chem. 286, 23254-23265.
    • (2011) J. Biol. Chem , vol.286 , pp. 23254-23265
    • Chong, B.M.1    Russell, T.D.2    Schaack, J.3    Orlicky, D.J.4    Reigan, P.5    Ladinsky, M.6    McManaman, J.L.7
  • 43
    • 33745751795 scopus 로고    scopus 로고
    • Recruitment of TIP47 to lipid droplets is controlled by the putative hydrophobic cleft
    • Ohsaki, Y., Maeda, T., Maeda, M., Tauchi-Sato, K., and Fujimoto, T. (2006) Recruitment of TIP47 to lipid droplets is controlled by the putative hydrophobic cleft. Biochem. Biophys. Res. Commun. 347, 279-287.
    • (2006) Biochem. Biophys. Res. Commun , vol.347 , pp. 279-287
    • Ohsaki, Y.1    Maeda, T.2    Maeda, M.3    Tauchi-Sato, K.4    Fujimoto, T.5
  • 46
    • 84863783823 scopus 로고    scopus 로고
    • Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation
    • Hynson, R. M., Jeffries, C. M., Trewhella, J., and Cocklin, S. (2012) Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation. Proteins 80, 2046-2055.
    • (2012) Proteins , vol.80 , pp. 2046-2055
    • Hynson, R.M.1    Jeffries, C.M.2    Trewhella, J.3    Cocklin, S.4
  • 47
    • 3142640798 scopus 로고    scopus 로고
    • Structure of a lipid droplet protein; the PAT family member TIP47
    • Hickenbottom, S. J., Kimmel, A. R., Londos, C., and Hurley, J. H. (2004) Structure of a lipid droplet protein; the PAT family member TIP47. Structure 12, 1199-1207.
    • (2004) Structure , vol.12 , pp. 1199-1207
    • Hickenbottom, S.J.1    Kimmel, A.R.2    Londos, C.3    Hurley, J.H.4
  • 48
    • 66349128492 scopus 로고    scopus 로고
    • PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores
    • Bickel, P. E., Tansey, J. T., and Welte, M. A. (2009) PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores. Biochim. Biophys. Acta 1791, 419-440.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 419-440
    • Bickel, P.E.1    Tansey, J.T.2    Welte, M.A.3
  • 49
    • 0038054286 scopus 로고    scopus 로고
    • A structural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins
    • Bussell, R. Jr., and Eliezer, D. (2003) A structural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol. 329, 763-778.
    • (2003) J. Mol. Biol , vol.329 , pp. 763-778
    • Bussell, R.1    Eliezer, D.2
  • 51
    • 84861913952 scopus 로고    scopus 로고
    • Lipid droplets and cellular lipid metabolism
    • Walther, T. C., and Farese, R. V (2012) Lipid droplets and cellular lipid metabolism. Annu. Rev. Biochem. 81, 687-714.
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 687-714
    • Walther, T.C.1    Farese, R.V.2
  • 52
    • 79960279832 scopus 로고    scopus 로고
    • Α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding
    • Pranke, I. M., Morello, V., Bigay, J., Gibson, K., Verbavatz, J.-M., Antonny, B., and Jackson, C. L. (2011) α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding. J. Cell Biol. 194, 89-103.
    • (2011) J. Cell Biol , vol.194 , pp. 89-103
    • Pranke, I.M.1    Morello, V.2    Bigay, J.3    Gibson, K.4    Verbavatz, J.-M.5    Antonny, B.6    Jackson, C.L.7
  • 53
    • 51749085388 scopus 로고    scopus 로고
    • HELIQUEST: A web server to screen sequences with specific α-helical properties
    • Gautier, R., Douguet, D., Antonny, B., and Drin, G. (2008) HELIQUEST: A web server to screen sequences with specific α-helical properties. Bioinformatics 24, 2101-2102.
    • (2008) Bioinformatics , vol.24 , pp. 2101-2102
    • Gautier, R.1    Douguet, D.2    Antonny, B.3    Drin, G.4
  • 55
    • 0010581394 scopus 로고
    • Automatic recording apparatus for use in chromatography of amino acids
    • Spackman, D. H., Stein, W. H., and Moore, S. (1958) Automatic recording apparatus for use in chromatography of amino acids. Anal. Chem. 30, 1190-1206.
    • (1958) Anal. Chem , vol.30 , pp. 1190-1206
    • Spackman, D.H.1    Stein, W.H.2    Moore, S.3
  • 56
  • 57
    • 84885459411 scopus 로고    scopus 로고
    • Targeting of the arf-gef gbf1 to lipid droplets and golgi membranes
    • Bouvet, S., Golinelli-Cohen, M.-P., Contremoulins, V., and Jackson, C. L. (2013) Targeting of the Arf-GEF GBF1 to lipid droplets and Golgi membranes. J. Cell Sci. 126, 4794-4805.
    • (2013) J. Cell Sci , vol.126 , pp. 4794-4805
    • Bouvet, S.1    Golinelli-Cohen, M.-P.2    Contremoulins, V.3    Jackson, C.L.4
  • 58
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-W673.
    • (2004) Nucleic Acids Res , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 59
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L., and Wallace, B. A. (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers. 89, 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 60
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260.
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 62
    • 84888101258 scopus 로고    scopus 로고
    • Expression of oleosin and perilipins in yeast promotes formation of lipid droplets from the endoplasmic reticulum
    • Jacquier, N., Mishra, S., Choudhary, V., and Schneiter, R. (2013) Expression of oleosin and perilipins in yeast promotes formation of lipid droplets from the endoplasmic reticulum. J. Cell Sci. 126, 5198-5209.
    • (2013) J. Cell Sci , vol.126 , pp. 5198-5209
    • Jacquier, N.1    Mishra, S.2    Choudhary, V.3    Schneiter, R.4
  • 63
    • 84913553694 scopus 로고    scopus 로고
    • Interaction of the spo20 membrane-sensor motif with phosphatidic acid and other anionic lipids, and influence of the membrane environment
    • Horchani, H., de Saint-Jean, M., Barelli, H., and Antonny, B. (2014) Interaction of the spo20 membrane-sensor motif with phosphatidic acid and other anionic lipids, and influence of the membrane environment. PLoS ONE. 9, e113484.
    • (2014) PLoS ONE , vol.9 , pp. e113484
    • Horchani, H.1    De Saint-Jean, M.2    Barelli, H.3    Antonny, B.4
  • 64
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix
    • Dyson, H. J., Rance, M., Houghten, R. A., Wright, P. E., and Lerner, R. A. (1988) Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J. Mol. Biol. 201, 201-217.
    • (1988) J. Mol. Biol , vol.201 , pp. 201-217
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Wright, P.E.4    Lerner, R.A.5
  • 65
    • 84873375687 scopus 로고    scopus 로고
    • Amphipathic lipid packing sensor motifs: Probing bilayer defects with hydrophobic residues
    • Vanni, S., Vamparys, L., Gautier, R., Drin, G., Etchebest, C., Fuchs, P. F., and Antonny, B. (2013) Amphipathic lipid packing sensor motifs: probing bilayer defects with hydrophobic residues. Biophys. J. 104, 575-584.
    • (2013) Biophys. J , vol.104 , pp. 575-584
    • Vanni, S.1    Vamparys, L.2    Gautier, R.3    Drin, G.4    Etchebest, C.5    Fuchs, P.F.6    Antonny, B.7
  • 66
    • 3242656580 scopus 로고    scopus 로고
    • Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins
    • Saito, H., Lund-Katz, S., and Phillips, M. C. (2004) Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog. Lipid Res. 43, 350-380.
    • (2004) Prog. Lipid Res , vol.43 , pp. 350-380
    • Saito, H.1    Lund-Katz, S.2    Phillips, M.C.3
  • 68
    • 0037424252 scopus 로고    scopus 로고
    • Functional studies on native and mutated forms of perilipins. A role in protein kinase A-mediated lipolysis of triacylglycerols
    • Tansey, J. T., Huml, A. M., Vogt, R., Davis, K. E., Jones, J. M., Fraser, K. A., Brasaemle, D. L., Kimmel, A. R., and Londos, C. (2003) Functional studies on native and mutated forms of perilipins. A role in protein kinase A-mediated lipolysis of triacylglycerols. J. Biol. Chem. 278, 8401-8406.
    • (2003) J. Biol. Chem , vol.278 , pp. 8401-8406
    • Tansey, J.T.1    Huml, A.M.2    Vogt, R.3    Davis, K.E.4    Jones, J.M.5    Fraser, K.A.6    Brasaemle, D.L.7    Kimmel, A.R.8    Londos, C.9
  • 69
    • 33744913055 scopus 로고    scopus 로고
    • MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor
    • Yamaguchi, T., Matsushita, S., Motojima, K., Hirose, F., and Osumi, T. (2006) MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor α. J. Biol. Chem. 281, 14232-14240.
    • (2006) J. Biol. Chem , vol.281 , pp. 14232-14240
    • Yamaguchi, T.1    Matsushita, S.2    Motojima, K.3    Hirose, F.4    Osumi, T.5
  • 71
    • 0030724392 scopus 로고    scopus 로고
    • Adipose differentiation-related protein is an ubiquitously expressed lipid storage droplet-associated protein
    • Brasaemle, D. L., Barber, T., Wolins, N. E., Serrero, G., Blanchette-Mackie, E. J., and Londos, C. (1997) Adipose differentiation-related protein is an ubiquitously expressed lipid storage droplet-associated protein. J. Lipid Res. 38, 2249-2263.
    • (1997) J. Lipid Res , vol.38 , pp. 2249-2263
    • Brasaemle, D.L.1    Barber, T.2    Wolins, N.E.3    Serrero, G.4    Blanchette-Mackie, E.J.5    Londos, C.6
  • 72
    • 33749058310 scopus 로고    scopus 로고
    • A proposed model of fat packaging by exchangeable lipid droplet proteins
    • Wolins, N. E., Brasaemle, D. L., and Bickel, P. E. (2006) A proposed model of fat packaging by exchangeable lipid droplet proteins. FEBS Lett. 580, 5484-5491.
    • (2006) FEBS Lett , vol.580 , pp. 5484-5491
    • Wolins, N.E.1    Brasaemle, D.L.2    Bickel, P.E.3
  • 73
    • 84939469873 scopus 로고    scopus 로고
    • Protein crowding is a determinant of lipid droplet protein composition
    • Kory, N., Thiam, A.-R., Farese, R. V. Jr., and Walther, T. C. (2015) Protein crowding is a determinant of lipid droplet protein composition. Dev. Cell. 34, 351-363.
    • (2015) Dev. Cell , vol.34 , pp. 351-363
    • Kory, N.1    Thiam, A.-R.2    Farese, R.V.3    Walther, T.C.4
  • 74
    • 36649009407 scopus 로고    scopus 로고
    • Adipocyte differentiation-related protein reduces the lipid droplet association of adipose triglyceride lipase and slows triacylglycerol turnover
    • Listenberger, L. L., Ostermeyer-Fay, A. G., Goldberg, E. B., Brown, W. J., and Brown, D. A. (2007) Adipocyte differentiation-related protein reduces the lipid droplet association of adipose triglyceride lipase and slows triacylglycerol turnover. J. Lipid Res. 48, 2751-2761.
    • (2007) J. Lipid Res , vol.48 , pp. 2751-2761
    • Listenberger, L.L.1    Ostermeyer-Fay, A.G.2    Goldberg, E.B.3    Brown, W.J.4    Brown, D.A.5
  • 75
    • 84869040414 scopus 로고    scopus 로고
    • Curvature, lipid packing, and electrostatics of membrane organelles: Defining cellular territories in determining specificity
    • Bigay, J., and Antonny, B. (2012) Curvature, lipid packing, and electrostatics of membrane organelles: defining cellular territories in determining specificity. Dev. Cell 23, 886-895.
    • (2012) Dev. Cell , vol.23 , pp. 886-895
    • Bigay, J.1    Antonny, B.2
  • 76
    • 34248532415 scopus 로고    scopus 로고
    • PROMALS: Toward accurate multiple sequence alignments of distantly related proteins
    • Pei, J., and Grishin, N. V. (2007) PROMALS: Toward accurate multiple sequence alignments of distantly related proteins. Bioinformatics 23, 802-808.
    • (2007) Bioinformatics , vol.23 , pp. 802-808
    • Pei, J.1    Grishin, N.V.2
  • 77
    • 40749144066 scopus 로고    scopus 로고
    • De novo identification of highly diverged protein repeats by probabilistic consistency
    • Biegert, A., and Söding, J. (2008) De novo identification of highly diverged protein repeats by probabilistic consistency. Bioinformatics 24, 807-814.
    • (2008) Bioinformatics , vol.24 , pp. 807-814
    • Biegert, A.1    Söding, J.2
  • 79
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Söding, J. (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics 21, 951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 80
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 81
    • 0027049622 scopus 로고
    • A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1
    • Wimmer, C., Doye, V., Grandi, P., Nehrbass, U., and Hurt, E. C. (1992) A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. EMBO J. 11, 5051-5061.
    • (1992) EMBO J , vol.11 , pp. 5051-5061
    • Wimmer, C.1    Doye, V.2    Grandi, P.3    Nehrbass, U.4    Hurt, E.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.