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Volumn 403, Issue 4, 2010, Pages 516-528

α-Actinin Is Required for the Proper Assembly of Z-Disk/Focal-Adhesion-Like Structures and for Efficient Locomotion in Caenorhabditis elegans

Author keywords

Caenorhabditis elegans; Focal adhesion; Muscle; actinin

Indexed keywords

ALPHA ACTININ; INTEGRIN; TALIN; VINCULIN; ACTININ; CAENORHABDITIS ELEGANS PROTEIN;

EID: 77957893213     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.055     Document Type: Article
Times cited : (25)

References (62)
  • 3
    • 0025291522 scopus 로고
    • An interaction between alpha-actinin and the beta 1 integrin subunit in vitro
    • Otey C.A., Pavalko F.M., Burridge K. An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. J. Cell Biol. 1990, 111:721-729.
    • (1990) J. Cell Biol. , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 5
    • 0020506943 scopus 로고
    • 125I-vinculin gel overlay technique
    • 125I-vinculin gel overlay technique. J. Cell Biol. 1983, 97:1283-1287.
    • (1983) J. Cell Biol. , vol.97 , pp. 1283-1287
    • Otto, J.J.1
  • 6
    • 0021214312 scopus 로고
    • An interaction between vinculin and talin
    • Burridge K., Mangeat P. An interaction between vinculin and talin. Nature 1984, 308:744-746.
    • (1984) Nature , vol.308 , pp. 744-746
    • Burridge, K.1    Mangeat, P.2
  • 7
    • 0023196997 scopus 로고
    • Interaction of iodinated vinculin, metavinculin and alpha-actinin with cytoskeletal proteins
    • Belkin A.M., Koteliansky V.E. Interaction of iodinated vinculin, metavinculin and alpha-actinin with cytoskeletal proteins. FEBS Lett. 1987, 220:291-294.
    • (1987) FEBS Lett. , vol.220 , pp. 291-294
    • Belkin, A.M.1    Koteliansky, V.E.2
  • 9
    • 0026673410 scopus 로고
    • Vinculin binding site mapped on talin with an anti-idiotypic antibody
    • Lee S.W., Wulfkuhle J.D., Otto J.J. Vinculin binding site mapped on talin with an anti-idiotypic antibody. J. Biol. Chem. 1992, 267:16355-16358.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16355-16358
    • Lee, S.W.1    Wulfkuhle, J.D.2    Otto, J.J.3
  • 10
    • 0027056757 scopus 로고
    • Further characterisation of the talin-binding site in the cytoskeletal protein vinculin
    • Gilmore A.P., Jackson P., Waites G.T., Critchley D.R. Further characterisation of the talin-binding site in the cytoskeletal protein vinculin. J. Cell Sci. 1992, 103:719-731.
    • (1992) J. Cell Sci. , vol.103 , pp. 719-731
    • Gilmore, A.P.1    Jackson, P.2    Waites, G.T.3    Critchley, D.R.4
  • 11
    • 0027268195 scopus 로고
    • The cytoskeletal protein talin contains at least two distinct vinculin binding domains
    • Gilmore A.P., Wood C., Ohanian V., Jackson P., Patel B., Rees D.J., et al. The cytoskeletal protein talin contains at least two distinct vinculin binding domains. J. Cell Biol. 1993, 122:337-347.
    • (1993) J. Cell Biol. , vol.122 , pp. 337-347
    • Gilmore, A.P.1    Wood, C.2    Ohanian, V.3    Jackson, P.4    Patel, B.5    Rees, D.J.6
  • 12
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson R.P., Craig S.W. An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 1994, 269:12611-12619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 13
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson R.P., Craig S.W. F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 1995, 373:261-264.
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 14
    • 0029009673 scopus 로고
    • The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids
    • Johnson R.P., Craig S.W. The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids. Biochem. Biophys. Res. Commun. 1995, 210:159-164.
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 159-164
    • Johnson, R.P.1    Craig, S.W.2
  • 15
    • 10544241952 scopus 로고    scopus 로고
    • Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site
    • Hemmings L., Rees D.J., Ohanian V., Bolton S.J., Gilmore A.P., Patel B., et al. Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site. J. Cell Sci. 1996, 109:2715-2726.
    • (1996) J. Cell Sci. , vol.109 , pp. 2715-2726
    • Hemmings, L.1    Rees, D.J.2    Ohanian, V.3    Bolton, S.J.4    Gilmore, A.P.5    Patel, B.6
  • 16
    • 0025997389 scopus 로고
    • Cloning, sequencing, and mapping of an alpha-actinin gene from the nematode Caenorhabditis elegans
    • Barstead R.J., Kleiman L., Waterston R.H. Cloning, sequencing, and mapping of an alpha-actinin gene from the nematode Caenorhabditis elegans. Cell Motil. Cytoskelet. 1991, 20:69-78.
    • (1991) Cell Motil. Cytoskelet. , vol.20 , pp. 69-78
    • Barstead, R.J.1    Kleiman, L.2    Waterston, R.H.3
  • 18
    • 0029093546 scopus 로고
    • Association of structural repeats in the alpha-actinin rod domain. Alignment of inter-subunit interactions
    • Flood G., Kahana E., Gilmore A.P., Rowe A.J., Gratzer W.B., Critchley D.R. Association of structural repeats in the alpha-actinin rod domain. Alignment of inter-subunit interactions. J. Mol. Biol. 1995, 252:227-234.
    • (1995) J. Mol. Biol. , vol.252 , pp. 227-234
    • Flood, G.1    Kahana, E.2    Gilmore, A.P.3    Rowe, A.J.4    Gratzer, W.B.5    Critchley, D.R.6
  • 19
    • 0030750630 scopus 로고    scopus 로고
    • Further analysis of the role of spectrin repeat motifs in alpha-actinin dimer formation
    • Flood G., Rowe A.J., Critchley D.R., Gratzer W.B. Further analysis of the role of spectrin repeat motifs in alpha-actinin dimer formation. Eur. Biophys. J. 1997, 25:431-435.
    • (1997) Eur. Biophys. J. , vol.25 , pp. 431-435
    • Flood, G.1    Rowe, A.J.2    Critchley, D.R.3    Gratzer, W.B.4
  • 21
    • 0028173766 scopus 로고
    • Modulation of alpha-actinin levels affects cell motility and confers tumorigenicity on 3T3 cells
    • Gluck U., Ben-Ze'ev A. Modulation of alpha-actinin levels affects cell motility and confers tumorigenicity on 3T3 cells. J. Cell Sci. 1994, 107:1773-1782.
    • (1994) J. Cell Sci. , vol.107 , pp. 1773-1782
    • Gluck, U.1    Ben-Ze'ev, A.2
  • 22
    • 0025734407 scopus 로고
    • Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin
    • Pavalko F.M., Burridge K. Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin. J. Cell Biol. 1991, 114:481-491.
    • (1991) J. Cell Biol. , vol.114 , pp. 481-491
    • Pavalko, F.M.1    Burridge, K.2
  • 23
    • 0025325694 scopus 로고
    • Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z disc integrity and muscle insertions
    • Fyrberg E., Kelly M., Ball E., Fyrberg C., Reedy M.C. Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z disc integrity and muscle insertions. J. Cell Biol. 1990, 110:1999-2011.
    • (1990) J. Cell Biol. , vol.110 , pp. 1999-2011
    • Fyrberg, E.1    Kelly, M.2    Ball, E.3    Fyrberg, C.4    Reedy, M.C.5
  • 24
    • 0032434538 scopus 로고    scopus 로고
    • Characterization of lethal Drosophila melanogaster alpha-actinin mutants
    • Fyrberg C., Ketchum A., Ball E., Fyrberg E. Characterization of lethal Drosophila melanogaster alpha-actinin mutants. Biochem. Genet. 1998, 36:299-310.
    • (1998) Biochem. Genet. , vol.36 , pp. 299-310
    • Fyrberg, C.1    Ketchum, A.2    Ball, E.3    Fyrberg, E.4
  • 25
    • 0026573230 scopus 로고
    • Perturbations of Drosophila alpha-actinin cause muscle paralysis, weakness, and atrophy but do not confer obvious nonmuscle phenotypes
    • Roulier E.M., Fyrberg C., Fyrberg E. Perturbations of Drosophila alpha-actinin cause muscle paralysis, weakness, and atrophy but do not confer obvious nonmuscle phenotypes. J. Cell Biol. 1992, 116:911-922.
    • (1992) J. Cell Biol. , vol.116 , pp. 911-922
    • Roulier, E.M.1    Fyrberg, C.2    Fyrberg, E.3
  • 26
    • 0030220198 scopus 로고    scopus 로고
    • Deficiency of a skeletal muscle isoform of alpha-actinin (alpha-actinin-3) in merosin-positive congenital muscular dystrophy
    • North K.N., Beggs A.H. Deficiency of a skeletal muscle isoform of alpha-actinin (alpha-actinin-3) in merosin-positive congenital muscular dystrophy. Neuromuscular Disord. 1996, 6:229-235.
    • (1996) Neuromuscular Disord. , vol.6 , pp. 229-235
    • North, K.N.1    Beggs, A.H.2
  • 28
    • 54249099032 scopus 로고    scopus 로고
    • Thin filament proteins mutations associated with skeletal myopathies: defective regulation of muscle contraction
    • Ochala J. Thin filament proteins mutations associated with skeletal myopathies: defective regulation of muscle contraction. J. Mol. Med. 2008, 86:1197-1204.
    • (2008) J. Mol. Med. , vol.86 , pp. 1197-1204
    • Ochala, J.1
  • 29
  • 30
    • 0034051681 scopus 로고    scopus 로고
    • Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis
    • Kaplan J.M., Kim S.H., North K.N., Rennke H., Correia L.A., Tong H.Q., et al. Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis. Nat. Genet. 2000, 24:251-256.
    • (2000) Nat. Genet. , vol.24 , pp. 251-256
    • Kaplan, J.M.1    Kim, S.H.2    North, K.N.3    Rennke, H.4    Correia, L.A.5    Tong, H.Q.6
  • 31
    • 33645946089 scopus 로고    scopus 로고
    • Mutational and biological analysis of alpha-actinin-4 in focal segmental glomerulosclerosis
    • Weins A., Kenlan P., Herbert S., Le T.C., Villegas I., Kaplan B.S., et al. Mutational and biological analysis of alpha-actinin-4 in focal segmental glomerulosclerosis. J. Am. Soc. Nephrol. 2005, 16:3694-3701.
    • (2005) J. Am. Soc. Nephrol. , vol.16 , pp. 3694-3701
    • Weins, A.1    Kenlan, P.2    Herbert, S.3    Le, T.C.4    Villegas, I.5    Kaplan, B.S.6
  • 32
    • 0022345717 scopus 로고
    • Muscle organization in Caenorhabditis elegans: localization of proteins implicated in thin filament attachment and I-band organization
    • Francis G.R., Waterston R.H. Muscle organization in Caenorhabditis elegans: localization of proteins implicated in thin filament attachment and I-band organization. J. Cell Biol. 1985, 101:1532-1549.
    • (1985) J. Cell Biol. , vol.101 , pp. 1532-1549
    • Francis, G.R.1    Waterston, R.H.2
  • 33
    • 0029741101 scopus 로고    scopus 로고
    • Talin requires beta-integrin, but not vinculin, for its assembly into focal adhesion-like structures in the nematode Caenorhabditis elegans
    • Moulder G.L., Huang M.M., Waterston R.H., Barstead R.J. Talin requires beta-integrin, but not vinculin, for its assembly into focal adhesion-like structures in the nematode Caenorhabditis elegans. Mol. Biol. Cell 1996, 7:1181-1193.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1181-1193
    • Moulder, G.L.1    Huang, M.M.2    Waterston, R.H.3    Barstead, R.J.4
  • 34
    • 0024319166 scopus 로고
    • The basal component of the nematode dense-body is vinculin
    • Barstead R.J., Waterston R.H. The basal component of the nematode dense-body is vinculin. J. Biol. Chem. 1989, 264:10177-10185.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10177-10185
    • Barstead, R.J.1    Waterston, R.H.2
  • 35
    • 0028990430 scopus 로고
    • Characterization of beta pat-3 heterodimers, a family of essential integrin receptors in C. elegans
    • Gettner S.N., Kenyon C., Reichardt L.F. Characterization of beta pat-3 heterodimers, a family of essential integrin receptors in C. elegans. J. Cell Biol. 1995, 129:1127-1141.
    • (1995) J. Cell Biol. , vol.129 , pp. 1127-1141
    • Gettner, S.N.1    Kenyon, C.2    Reichardt, L.F.3
  • 36
    • 0032978791 scopus 로고    scopus 로고
    • A new fluorescence-based, hydrophobic photolabeling technique for analyzing membrane-associated proteins
    • Hess D., Isenberg G. A new fluorescence-based, hydrophobic photolabeling technique for analyzing membrane-associated proteins. FEBS Lett. 1999, 445:279-282.
    • (1999) FEBS Lett. , vol.445 , pp. 279-282
    • Hess, D.1    Isenberg, G.2
  • 37
    • 0025824367 scopus 로고
    • Vinculin is essential for muscle function in the nematode
    • Barstead R.J., Waterston R.H. Vinculin is essential for muscle function in the nematode. J. Cell Biol. 1991, 114:715-724.
    • (1991) J. Cell Biol. , vol.114 , pp. 715-724
    • Barstead, R.J.1    Waterston, R.H.2
  • 38
    • 0028089203 scopus 로고
    • Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations
    • Williams B.D., Waterston R.H. Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations. J. Cell Biol. 1994, 124:475-490.
    • (1994) J. Cell Biol. , vol.124 , pp. 475-490
    • Williams, B.D.1    Waterston, R.H.2
  • 40
    • 38449083521 scopus 로고    scopus 로고
    • Sarcomere assembly in C. elegans muscle
    • Moerman D.G., Williams B.D. Sarcomere assembly in C. elegans muscle. WormBook 2006, 1-16.
    • (2006) WormBook , pp. 1-16
    • Moerman, D.G.1    Williams, B.D.2
  • 41
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: a structural platform for cytoskeletal protein assemblies
    • Djinovic-Carugo K., Gautel M., Ylanne J., Young P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett. 2002, 513:119-123.
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 43
    • 35848949782 scopus 로고    scopus 로고
    • Two LIM domain proteins and UNC-96 link UNC-97/pinch to myosin thick filaments in Caenorhabditis elegans muscle
    • Qadota H., Mercer K.B., Miller R.K., Kaibuchi K., Benian G.M. Two LIM domain proteins and UNC-96 link UNC-97/pinch to myosin thick filaments in Caenorhabditis elegans muscle. Mol. Biol. Cell 2007, 18:4317-4326.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4317-4326
    • Qadota, H.1    Mercer, K.B.2    Miller, R.K.3    Kaibuchi, K.4    Benian, G.M.5
  • 44
    • 48749118801 scopus 로고    scopus 로고
    • A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (Obscurin) in Caenorhabditis elegans
    • Qadota H., McGaha L.A., Mercer K.B., Stark T.J., Ferrara T.M., Benian G.M. A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (Obscurin) in Caenorhabditis elegans. Mol. Biol. Cell 2008, 19:2424-2432.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2424-2432
    • Qadota, H.1    McGaha, L.A.2    Mercer, K.B.3    Stark, T.J.4    Ferrara, T.M.5    Benian, G.M.6
  • 45
    • 41649092668 scopus 로고    scopus 로고
    • DYC-1, a protein functionally linked to dystrophin in Caenorhabditis elegans is associated with the dense body, where it interacts with the muscle LIM domain protein ZYX-1
    • Lecroisey C., Martin E., Mariol M.C., Granger L., Schwab Y., Labouesse M., et al. DYC-1, a protein functionally linked to dystrophin in Caenorhabditis elegans is associated with the dense body, where it interacts with the muscle LIM domain protein ZYX-1. Mol. Biol. Cell 2008, 19:785-796.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 785-796
    • Lecroisey, C.1    Martin, E.2    Mariol, M.C.3    Granger, L.4    Schwab, Y.5    Labouesse, M.6
  • 46
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S. The genetics of Caenorhabditis elegans. Genetics 1974, 77:71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 47
    • 0031877935 scopus 로고    scopus 로고
    • A new marker for mosaic analysis in Caenorhabditis elegans indicates a fusion between hyp6 and hyp7, two major components of the hypodermis
    • Yochem J., Gu T., Han M. A new marker for mosaic analysis in Caenorhabditis elegans indicates a fusion between hyp6 and hyp7, two major components of the hypodermis. Genetics 1998, 149:1323-1334.
    • (1998) Genetics , vol.149 , pp. 1323-1334
    • Yochem, J.1    Gu, T.2    Han, M.3
  • 48
    • 0028848587 scopus 로고
    • Genetic regulation of mec-3 gene expression implicated in the specification of the mechanosensory neuron cell types in Caenorhabditis elegans
    • Mitani S. Genetic regulation of mec-3 gene expression implicated in the specification of the mechanosensory neuron cell types in Caenorhabditis elegans. Dev. Growth Differ. 1995, 37:551-557.
    • (1995) Dev. Growth Differ. , vol.37 , pp. 551-557
    • Mitani, S.1
  • 50
    • 0025734406 scopus 로고
    • Muscle cell attachment in Caenorhabditis elegans
    • Francis R., Waterston R.H. Muscle cell attachment in Caenorhabditis elegans. J. Cell Biol. 1991, 114:465-479.
    • (1991) J. Cell Biol. , vol.114 , pp. 465-479
    • Francis, R.1    Waterston, R.H.2
  • 51
    • 0028104856 scopus 로고
    • DPY-27: a chromosome condensation protein homolog that regulates C. elegans dosage compensation through association with the X chromosome
    • Chuang P.T., Albertson D.G., Meyer B.J. DPY-27: a chromosome condensation protein homolog that regulates C. elegans dosage compensation through association with the X chromosome. Cell 1994, 79:459-474.
    • (1994) Cell , vol.79 , pp. 459-474
    • Chuang, P.T.1    Albertson, D.G.2    Meyer, B.J.3
  • 52
    • 0032958758 scopus 로고    scopus 로고
    • The cat-1 gene of Caenorhabditis elegans encodes a vesicular monoamine transporter required for specific monoamine-dependent behaviors
    • Duerr J.S., Frisby D.L., Gaskin J., Duke A., Asermely K., Huddleston D., et al. The cat-1 gene of Caenorhabditis elegans encodes a vesicular monoamine transporter required for specific monoamine-dependent behaviors. J. Neurosci. 1999, 19:72-84.
    • (1999) J. Neurosci. , vol.19 , pp. 72-84
    • Duerr, J.S.1    Frisby, D.L.2    Gaskin, J.3    Duke, A.4    Asermely, K.5    Huddleston, D.6
  • 53
    • 0030730833 scopus 로고    scopus 로고
    • Caenorhabditis elegans rab-3 mutant synapses exhibit impaired function and are partially depleted of vesicles
    • Nonet M.L., Staunton J.E., Kilgard M.P., Fergestad T., Hartwieg E., Horvitz H.R., et al. Caenorhabditis elegans rab-3 mutant synapses exhibit impaired function and are partially depleted of vesicles. J. Neurosci. 1997, 17:8061-8073.
    • (1997) J. Neurosci. , vol.17 , pp. 8061-8073
    • Nonet, M.L.1    Staunton, J.E.2    Kilgard, M.P.3    Fergestad, T.4    Hartwieg, E.5    Horvitz, H.R.6
  • 54
    • 0025606427 scopus 로고
    • The unc-86 gene product couples cell lineage and cell identity in C. elegans
    • Finney M., Ruvkun G. The unc-86 gene product couples cell lineage and cell identity in C. elegans. Cell 1990, 63:895-905.
    • (1990) Cell , vol.63 , pp. 895-905
    • Finney, M.1    Ruvkun, G.2
  • 55
    • 0031848145 scopus 로고    scopus 로고
    • The S. cerevisiae CLU1 and D. discoideum cluA genes are functional homologues that influence mitochondrial morphology and distribution
    • Fields S.D., Conrad M.N., Clarke M. The S. cerevisiae CLU1 and D. discoideum cluA genes are functional homologues that influence mitochondrial morphology and distribution. J. Cell Sci. 1998, 111:1717-1727.
    • (1998) J. Cell Sci. , vol.111 , pp. 1717-1727
    • Fields, S.D.1    Conrad, M.N.2    Clarke, M.3
  • 56
    • 0030742877 scopus 로고    scopus 로고
    • Spray-freezing freeze substitution (SFFS) of cell suspensions for improved preservation of ultrastructure
    • Fields S.D., Strout G.W., Russell S.D. Spray-freezing freeze substitution (SFFS) of cell suspensions for improved preservation of ultrastructure. Microsc. Res. Tech. 1997, 38:315-328.
    • (1997) Microsc. Res. Tech. , vol.38 , pp. 315-328
    • Fields, S.D.1    Strout, G.W.2    Russell, S.D.3
  • 57
    • 0014444144 scopus 로고
    • A low-viscosity epoxy resin embedding medium for electron microscopy
    • Spurr A.R. A low-viscosity epoxy resin embedding medium for electron microscopy. J. Ultrastruct. Res. 1969, 26:31-43.
    • (1969) J. Ultrastruct. Res. , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 58
    • 0022616143 scopus 로고
    • An abbreviated method of the double lead stain technique
    • Daddow L.Y. An abbreviated method of the double lead stain technique. J. Submicrosc. Cytol. 1986, 18:221-224.
    • (1986) J. Submicrosc. Cytol. , vol.18 , pp. 221-224
    • Daddow, L.Y.1
  • 61
    • 0034757770 scopus 로고    scopus 로고
    • Proteomics: the move to mixtures
    • Peng J., Gygi S.P. Proteomics: the move to mixtures. J. Mass Spectrom. 2001, 36:1083-1091.
    • (2001) J. Mass Spectrom. , vol.36 , pp. 1083-1091
    • Peng, J.1    Gygi, S.P.2
  • 62
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome
    • Peng J., Elias J.E., Thoreen C.C., Licklider L.J., Gygi S.P. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2:43-50.
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5


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