메뉴 건너뛰기




Volumn 14, Issue 7, 2003, Pages 2617-2629

The Saccharomyces cerevisiae calponin/transgelin homolog Scp1 functions with fimbrin to regulate stability and organization of the actin cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALPONIN; FIMBRIN; FUNGAL PROTEIN; TRANSGELIN; UNCLASSIFIED DRUG;

EID: 0038107547     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-01-0028     Document Type: Article
Times cited : (79)

References (54)
  • 1
    • 0025983823 scopus 로고
    • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo
    • Adams, A.E., Botstein, D., and Drubin, D.G. (1991). Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature 354, 404-408.
    • (1991) Nature , vol.354 , pp. 404-408
    • Adams, A.E.1    Botstein, D.2    Drubin, D.G.3
  • 2
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough, K.R., Stryker, J., Pokala, N., Sanders, M., Crews, P., and Drubin, D.G. (1997). High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137, 399-416.
    • (1997) J. Cell Biol. , vol.137 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 4
    • 0343980401 scopus 로고
    • Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro
    • Bretscher, A. (1981). Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro. Proc. Natl. Acad. Sci. USA 78, 6849-6853.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6849-6853
    • Bretscher, A.1
  • 6
    • 0033598182 scopus 로고    scopus 로고
    • Integrating the actin and vimentin cytoskeletons. Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages
    • Correia, I., Chu, D., Chou, Y.H., Goldman, R.D., and Matsudaira, P. (1999). Integrating the actin and vimentin cytoskeletons. Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages. J. Cell Biol. 146, 831-842.
    • (1999) J. Cell Biol. , vol.146 , pp. 831-842
    • Correia, I.1    Chu, D.2    Chou, Y.H.3    Goldman, R.D.4    Matsudaira, P.5
  • 7
    • 0029966290 scopus 로고    scopus 로고
    • Movement of yeast cortical actin cytoskeleton visualized in vivo
    • Doyle, T., and Botstein, D. (1996). Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc. Natl. Acad. Sci. USA 93, 3886-3891.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3886-3891
    • Doyle, T.1    Botstein, D.2
  • 8
    • 0024192883 scopus 로고
    • Yeast actin-binding proteins: Evidence for a role in morphogenesis
    • Drubin, D.G., Miller, K.G., and Botstein, D. (1988). Yeast actin-binding proteins: evidence for a role in morphogenesis. J. Cell Biol. 107, 2551-2561.
    • (1988) J. Cell Biol. , vol.107 , pp. 2551-2561
    • Drubin, D.G.1    Miller, K.G.2    Botstein, D.3
  • 9
    • 0031444358 scopus 로고    scopus 로고
    • An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast
    • Epp, J.A., and Chant, J. (1997). An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast. Curr. Biol. 7, 921-929.
    • (1997) Curr. Biol. , vol.7 , pp. 921-929
    • Epp, J.A.1    Chant, J.2
  • 12
    • 0031822886 scopus 로고    scopus 로고
    • The single CH domain of calponin is neither sufficient nor necessary for F-actin binding
    • Gimona, M., and Mital, R. (1998). The single CH domain of calponin is neither sufficient nor necessary for F-actin binding. J. Cell Sci. 111, 1813-1821.
    • (1998) J. Cell Sci. , vol.111 , pp. 1813-1821
    • Gimona, M.1    Mital, R.2
  • 13
    • 0032563965 scopus 로고    scopus 로고
    • Single calponin homology domains are not actin-binding domains
    • Gimona, M., and Winder, S. (1998). Single calponin homology domains are not actin-binding domains. Curr. Biol. 8, R674-R675.
    • (1998) Curr. Biol. , vol.8
    • Gimona, M.1    Winder, S.2
  • 14
    • 0027382212 scopus 로고
    • Characterization of wild type and mutant chicken gizzard alpha calponin expressed in E. coli
    • Gong, B.J., Mabuchi, K., Takahashi, K., Nadal-Ginard, B., and Tao, T. (1993). Characterization of wild type and mutant chicken gizzard alpha calponin expressed in E. coli. J. Biochem. 114, 453-456.
    • (1993) J. Biochem. , vol.114 , pp. 453-456
    • Gong, B.J.1    Mabuchi, K.2    Takahashi, K.3    Nadal-Ginard, B.4    Tao, T.5
  • 15
    • 0033545203 scopus 로고    scopus 로고
    • Coronin promotes the rapid assembly and cross-linking of actin filaments and may link the actin and microtubule cytoskeletons in yeast
    • Goode, B.L., Wong, J.J., Butty, A.C., Peter, M., McCormack, A.L., Yates, J.R., Drubin, D.G., and Barnes, G. (1999). Coronin promotes the rapid assembly and cross-linking of actin filaments and may link the actin and microtubule cytoskeletons in yeast. J. Cell Biol. 144, 83-98.
    • (1999) J. Cell Biol. , vol.144 , pp. 83-98
    • Goode, B.L.1    Wong, J.J.2    Butty, A.C.3    Peter, M.4    McCormack, A.L.5    Yates, J.R.6    Drubin, D.G.7    Barnes, G.8
  • 16
    • 0035199446 scopus 로고    scopus 로고
    • Modular complexes that regulate actin assembly in budding yeast
    • Goode, B.L., and Rodal, A.A. (2001). Modular complexes that regulate actin assembly in budding yeast. Curr. Opin. Microbiol. 4, 703-712.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 703-712
    • Goode, B.L.1    Rodal, A.A.2
  • 17
    • 0029921313 scopus 로고    scopus 로고
    • Expression of senescence-induced protein WS3-10 in vivo and in vitro
    • Grigoriev, V.G., Thweatt, R., Moerman, E.J., and Goldstein, S. (1996). Expression of senescence-induced protein WS3-10 in vivo and in vitro. Exp. Gerontol. 31, 145-157.
    • (1996) Exp. Gerontol. , vol.31 , pp. 145-157
    • Grigoriev, V.G.1    Thweatt, R.2    Moerman, E.J.3    Goldstein, S.4
  • 18
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Guthrie, C., and Fink, R. (1991). Guide to yeast genetics and molecular biology. Methods Enzymol. 194, 1-933.
    • (1991) Methods Enzymol. , vol.194 , pp. 1-933
    • Guthrie, C.1    Fink, R.2
  • 19
    • 0030880857 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of the smooth muscle cell calponin gene inhibits proliferation of smooth muscle cells and fibroblasts
    • Jiang, Z., Grange, R.W., Walsh, M.P., and Kamm, K.E. (1997). Adenovirus-mediated transfer of the smooth muscle cell calponin gene inhibits proliferation of smooth muscle cells and fibroblasts. FEBS Lett. 413, 441-445.
    • (1997) FEBS Lett. , vol.413 , pp. 441-445
    • Jiang, Z.1    Grange, R.W.2    Walsh, M.P.3    Kamm, K.E.4
  • 20
    • 0036270964 scopus 로고    scopus 로고
    • Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae
    • Jones, E. (2002). Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae. Methods Enzymol. 351, 127-150.
    • (2002) Methods Enzymol. , vol.351 , pp. 127-150
    • Jones, E.1
  • 21
    • 0028287673 scopus 로고
    • Purification, characterization, and partial sequence analysis of a new 25-kDa actin-binding protein from bovine aorta: A SM22 homolog
    • Kobayashi, R., Kubota, T., and Hidaka, H. (1994). Purification, characterization, and partial sequence analysis of a new 25-kDa actin-binding protein from bovine aorta: a SM22 homolog. Biochem. Biophys. Res. Commun. 198, 1275-1280.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 1275-1280
    • Kobayashi, R.1    Kubota, T.2    Hidaka, H.3
  • 22
    • 0028799614 scopus 로고
    • Interaction of calponin with actin and its functional implications
    • Kolakowski, J., Makuch, R., Stepkowski, D., and Dabrowska, R. (1995). Interaction of calponin with actin and its functional implications. Biochem. J. 306, 199-204.
    • (1995) Biochem. J. , vol.306 , pp. 199-204
    • Kolakowski, J.1    Makuch, R.2    Stepkowski, D.3    Dabrowska, R.4
  • 23
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler, E., and Riezman, H. (1993). Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12, 2855-2862.
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 24
    • 0030781498 scopus 로고    scopus 로고
    • Fibroblast transgelin and smooth muscle SM22alpha are the same protein, the expression of which is down-regulated in many cell lines
    • Lawson, D., Harrison, M., and Shapland, C. (1997). Fibroblast transgelin and smooth muscle SM22alpha are the same protein, the expression of which is down-regulated in many cell lines. Cell Motil. Cytoskeleton 38, 250-257.
    • (1997) Cell Motil. Cytoskeleton , vol.38 , pp. 250-257
    • Lawson, D.1    Harrison, M.2    Shapland, C.3
  • 25
    • 0023655235 scopus 로고
    • An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscles. Purification from bovine aorta
    • Lees-Miller, J.P., Heeley, D.H., and Smillie, L.B. (1987a). An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscles. Purification from bovine aorta. Biochem. J. 244, 705-709.
    • (1987) Biochem. J. , vol.244 , pp. 705-709
    • Lees-Miller, J.P.1    Heeley, D.H.2    Smillie, L.B.3
  • 26
    • 0023644595 scopus 로고
    • Isolation and characterization of an abundant and novel 22-kDa protein (SM22) from chicken gizzard smooth muscle
    • Lees-Miller, J.P., Heeley, D.H., Smillie, L.B., and Kay, C.M. (1987b). Isolation and characterization of an abundant and novel 22-kDa protein (SM22) from chicken gizzard smooth muscle. J. Biol. Chem. 262, 2988-2993.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2988-2993
    • Lees-Miller, J.P.1    Heeley, D.H.2    Smillie, L.B.3    Kay, C.M.4
  • 27
    • 0032567760 scopus 로고    scopus 로고
    • Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis
    • Lippincott, J., and Li, R. (1998). Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J. Cell Biol. 140, 355-366.
    • (1998) J. Cell Biol. , vol.140 , pp. 355-366
    • Lippincott, J.1    Li, R.2
  • 28
    • 0024486421 scopus 로고
    • Purification of tropomyosin from Saccaromyces cerevisiae and identification of related proteins in Schizosaccharomyces and physarum
    • Liu, H., and Bretscher, A. (1989). Purification of tropomyosin from Saccaromyces cerevisiae and identification of related proteins in Schizosaccharomyces and physarum. Proc. Natl. Acad. Sci. USA 86, 90-93.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 90-93
    • Liu, H.1    Bretscher, A.2
  • 29
    • 0028214727 scopus 로고
    • Suppression of calcium-dependent membrane currents in human fibroblasts by replicative senescence and forced expression of a gene sequence encoding a putative calcium-binding protein
    • Liu, S., Thweatt, R., Lumpkin, Jr., C.K., and Goldstein, S. (1994). Suppression of calcium-dependent membrane currents in human fibroblasts by replicative senescence and forced expression of a gene sequence encoding a putative calcium-binding protein. Proc. Natl. Acad. Sci. USA 91, 2186-2190.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2186-2190
    • Liu, S.1    Thweatt, R.2    Lumpkin C.K., Jr.3    Goldstein, S.4
  • 30
    • 0029162355 scopus 로고
    • Characterization of calponin binding to actin
    • Lu, F.W., Freedman, M.V., and Chalovich, J.M. (1995). Characterization of calponin binding to actin. Biochemistry 34, 11864-11871.
    • (1995) Biochemistry , vol.34 , pp. 11864-11871
    • Lu, F.W.1    Freedman, M.V.2    Chalovich, J.M.3
  • 31
    • 0029982386 scopus 로고    scopus 로고
    • Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle
    • Mabuchi, K., Li, Y., Tao, T., and Wang, C.L. (1996). Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle. J. Muscle Res. Cell Motil. 17, 243-260.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 243-260
    • Mabuchi, K.1    Li, Y.2    Tao, T.3    Wang, C.L.4
  • 32
    • 0026034515 scopus 로고
    • Modular organization of actin cross-linking proteins
    • Matsudaira, P. (1991). Modular organization of actin cross-linking proteins. Trends Biochem. Sci. 16, 87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 33
    • 0027324435 scopus 로고
    • Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages
    • Messier, J.M., Shaw, L.M., Chafel, M., Matsudaira, P., and Mercurio, A.M. (1993). Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages. Cell Motil. Cytoskeleton 25, 223-233.
    • (1993) Cell Motil. Cytoskeleton , vol.25 , pp. 223-233
    • Messier, J.M.1    Shaw, L.M.2    Chafel, M.3    Matsudaira, P.4    Mercurio, A.M.5
  • 34
    • 0028933882 scopus 로고
    • Characterization of the regulatory domain of gizzard calponin. Interactions of the 145-163 region with F-actin, calcium-binding proteins, and tropomyosin
    • Mezgueldi, M., Mendre, C., Calas, B., Kassab, R., and Fattoum, A. (1995). Characterization of the regulatory domain of gizzard calponin. Interactions of the 145-163 region with F-actin, calcium-binding proteins, and tropomyosin. J. Biol. Chem. 270, 8867-8876.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8867-8876
    • Mezgueldi, M.1    Mendre, C.2    Calas, B.3    Kassab, R.4    Fattoum, A.5
  • 35
    • 0032518319 scopus 로고    scopus 로고
    • Two distinct actin-binding sites of smooth muscle calponin
    • Mino, T., Yuasa, U., Nakamura, F., Naka, M., and Tanaka, T. (1998). Two distinct actin-binding sites of smooth muscle calponin. Eur. J. Biochem. 251, 262-268.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 262-268
    • Mino, T.1    Yuasa, U.2    Nakamura, F.3    Naka, M.4    Tanaka, T.5
  • 36
    • 0034921574 scopus 로고    scopus 로고
    • Invited review: Crossbridge regulation by thin filament-associated proteins
    • Morgan, K., and Gangopadhyay, S. (2001). Invited review: crossbridge regulation by thin filament-associated proteins. J. Appl. Physiol. 91, 953-962.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 953-962
    • Morgan, K.1    Gangopadhyay, S.2
  • 37
    • 0028265170 scopus 로고
    • Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells
    • North, A.J., Gimona, M., Cross, R.A., and Small, J.V. (1994). Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells. J. Cell Sci. 107, 437-444.
    • (1994) J. Cell Sci. , vol.107 , pp. 437-444
    • North, A.J.1    Gimona, M.2    Cross, R.A.3    Small, J.V.4
  • 38
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli
    • Peranen, J., Rikkonen, M., Hyvonen, M., and Kaariainen, L. (1996). T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236, 371-373.
    • (1996) Anal. Biochem. , vol.236 , pp. 371-373
    • Peranen, J.1    Rikkonen, M.2    Hyvonen, M.3    Kaariainen, L.4
  • 39
    • 0020012723 scopus 로고
    • Methods to characterize actin filament networks
    • Pollard, T.D., and Cooper, J.A. (1982). Methods to characterize actin filament networks. Methods Enzymol. 85, 211-233.
    • (1982) Methods Enzymol. , vol.85 , pp. 211-233
    • Pollard, T.D.1    Cooper, J.A.2
  • 40
    • 0028306815 scopus 로고
    • Cloning and sequencing of cDNAs encoding the actin cross-linking protein transgelin defines a new family of actin-associated proteins
    • published erratum in Cell Motil. Cytoskeleton 1994;29(4):383
    • Prinjha, R.K., Shapland, C.E., Hsuan, J.J., Totty, N.F., Mason, I.J., and Lawson, D. (1994). Cloning and sequencing of cDNAs encoding the actin cross-linking protein transgelin defines a new family of actin-associated proteins [published erratum in Cell Motil. Cytoskeleton 1994;29(4):383]. Cell Motil. Cytoskeleton 28, 243-255.
    • (1994) Cytoskeleton , vol.28 , pp. 243-255
    • Prinjha, R.K.1    Shapland, C.E.2    Hsuan, J.J.3    Totty, N.F.4    Mason, I.J.5    Lawson, D.6
  • 41
    • 0034056057 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast
    • Pruyne, D., and Bretscher, A. (2000). Polarization of cell growth in yeast. J. Cell Sci. 113, 571-585.
    • (2000) J. Cell Sci. , vol.113 , pp. 571-585
    • Pruyne, D.1    Bretscher, A.2
  • 42
    • 0030734377 scopus 로고    scopus 로고
    • Allele-specific suppression by formation of new protein-protein interactions in yeast
    • Sandrock, T.M., O'Dell, J.L., and Adams, A.E. (1997). Allele-specific suppression by formation of new protein-protein interactions in yeast. Genetics 147, 1635-1642.
    • (1997) Genetics , vol.147 , pp. 1635-1642
    • Sandrock, T.M.1    O'Dell, J.L.2    Adams, A.E.3
  • 43
    • 0027252650 scopus 로고
    • Purification and properties of transgelin: A transformation and shape change sensitive actin-gelling protein
    • Shapland, C., Hsuan, J.J., Totty, N.F., and Lawson, D. (1993). Purification and properties of transgelin: a transformation and shape change sensitive actin-gelling protein. J. Cell Biol. 121, 1065-1073.
    • (1993) J. Cell Biol. , vol.121 , pp. 1065-1073
    • Shapland, C.1    Hsuan, J.J.2    Totty, N.F.3    Lawson, D.4
  • 44
    • 0023676769 scopus 로고
    • Identification of new actin-associated polypeptides that are modified by viral transformation and changes in cell shape
    • Shapland, C., Lowings, P., and Lawson, D. (1988). Identification of new actin-associated polypeptides that are modified by viral transformation and changes in cell shape. J. Cell Biol. 107, 153-161.
    • (1988) J. Cell Biol. , vol.107 , pp. 153-161
    • Shapland, C.1    Lowings, P.2    Lawson, D.3
  • 45
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 46
    • 0032446186 scopus 로고    scopus 로고
    • The cytoskeleton of the vertebrate smooth muscle cell
    • Small, J.V., and Gimona, M. (1998). The cytoskeleton of the vertebrate smooth muscle cell. Acta Physiol. Scand. 164, 341-348.
    • (1998) Acta Physiol. Scand. , vol.164 , pp. 341-348
    • Small, J.V.1    Gimona, M.2
  • 47
    • 0028924541 scopus 로고
    • Physical characterization of calponin. A circular dichroism, analytical ultracentrifuge, and electron microscopy study
    • Stafford, W.F., 3rd, Mabuchi, K., Takahashi, K., and Tao, T. (1995). Physical characterization of calponin. A circular dichroism, analytical ultracentrifuge, and electron microscopy study. J. Biol. Chem. 270, 10576-10579.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10576-10579
    • Stafford W.F. III1    Mabuchi, K.2    Takahashi, K.3    Tao, T.4
  • 48
    • 0029931015 scopus 로고    scopus 로고
    • Structure-function relations of smooth muscle calponin. The critical role of serine 175
    • Tang, D.C., Kang, H.M., Jin, J.P., Fraser, E.D., and Walsh, M.P. (1996). Structure-function relations of smooth muscle calponin. The critical role of serine 175. J. Biol. Chem. 271, 8605-8611.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8605-8611
    • Tang, D.C.1    Kang, H.M.2    Jin, J.P.3    Fraser, E.D.4    Walsh, M.P.5
  • 49
    • 0030758697 scopus 로고    scopus 로고
    • Electrostatic effects of smooth muscle calponin on actin assembly
    • Tang, J.X., Szymanski, P.T., Janmey, P.A., and Tao, T. (1997). Electrostatic effects of smooth muscle calponin on actin assembly. Eur. J. Biochem. 247, 432-440.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 432-440
    • Tang, J.X.1    Szymanski, P.T.2    Janmey, P.A.3    Tao, T.4
  • 50
    • 0026779315 scopus 로고
    • A novel gene encoding a smooth muscle protein is overexpressed in senescent human fibroblasts
    • Thweatt, R., Lumpkin, Jr., C.K., and Goldstein, S. (1992). A novel gene encoding a smooth muscle protein is overexpressed in senescent human fibroblasts. Biochem. Biophys. Res. Commun. 187, 1-7.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1-7
    • Thweatt, R.1    Lumpkin C.K., Jr.2    Goldstein, S.3
  • 51
    • 0030565430 scopus 로고    scopus 로고
    • Interaction of smooth muscle calponin and desmin
    • Wang, P., and Gusev, N.B. (1996). Interaction of smooth muscle calponin and desmin. FEBS Lett. 392, 255-258.
    • (1996) FEBS Lett. , vol.392 , pp. 255-258
    • Wang, P.1    Gusev, N.B.2
  • 52
    • 0037089086 scopus 로고    scopus 로고
    • Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics
    • Warren, D.T., Andrews, P.D., Gourlay, C.W., and Ayscough, K.R. (2002). Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics. J. Cell Sci. 115, 1703-1715.
    • (2002) J. Cell Sci. , vol.115 , pp. 1703-1715
    • Warren, D.T.1    Andrews, P.D.2    Gourlay, C.W.3    Ayscough, K.R.4
  • 53
    • 0037222432 scopus 로고    scopus 로고
    • Structural insights into actin binding, branching, and bundling proteins
    • Winder, S.J. (2003). Structural insights into actin binding, branching, and bundling proteins. Curr. Opin. Cell Biol. 15, 14-22.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 14-22
    • Winder, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.