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Volumn 76, Issue 13, 2011, Pages 1507-1527

Tropomyosin: Double helix from the protein world

Author keywords

coiled coil proteins; regulation of muscle contraction; tropomyosin

Indexed keywords


EID: 84856622487     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297911130098     Document Type: Review
Times cited : (61)

References (137)
  • 1
    • 0000547129 scopus 로고
    • 1:CAS:528:DyaH1MXhtlehuw%3D%3D
    • K. Bailey 1948 Biochem. J. 43 271 279 1:CAS:528:DyaH1MXhtlehuw%3D%3D
    • (1948) Biochem. J. , vol.43 , pp. 271-279
    • Bailey, K.1
  • 3
    • 0000920828 scopus 로고
    • 1:CAS:528:DyaG2cXhsVw%3D 10.1107/S0365110X53001964
    • F. H. C. Crick 1953 Acta Cryst. 6 689 697 1:CAS:528:DyaG2cXhsVw%3D 10.1107/S0365110X53001964
    • (1953) Acta Cryst. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 5
    • 0017853508 scopus 로고
    • 624724 1:CAS:528:DyaE1cXhsVOlu7c%3D
    • D. Stone L. B. Smillie 1978 J. Biol. Chem. 253 1137 1148 624724 1:CAS:528:DyaE1cXhsVOlu7c%3D
    • (1978) J. Biol. Chem. , vol.253 , pp. 1137-1148
    • Stone, D.1    Smillie, L.B.2
  • 6
    • 0016774006 scopus 로고
    • 1059125 1:CAS:528:DyaE2MXmtVaqtbw%3D 10.1073/pnas.72.9.3377
    • S. S. Lehrer 1975 Proc. Natl. Acad. Sci. USA 72 3377 3381 1059125 1:CAS:528:DyaE2MXmtVaqtbw%3D 10.1073/pnas.72.9.3377
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3377-3381
    • Lehrer, S.S.1
  • 7
    • 0016777712 scopus 로고
    • 1195399 1:CAS:528:DyaE28XislWlug%3D%3D 10.1016/S0022-2836(75)80084-2
    • D. A. Parry 1975 J. Mol. Biol. 98 519 535 1195399 1:CAS:528: DyaE28XislWlug%3D%3D 10.1016/S0022-2836(75)80084-2
    • (1975) J. Mol. Biol. , vol.98 , pp. 519-535
    • Parry, D.A.1
  • 8
    • 0016747961 scopus 로고
    • 1195388 1:CAS:528:DyaE28XhtlOhug%3D%3D 10.1016/S0022-2836(75)80118-5
    • A. D. McLachlan M. Stewart L. B. Smillie 1975 J. Mol. Biol. 98 281 291 1195388 1:CAS:528:DyaE28XhtlOhug%3D%3D 10.1016/S0022-2836(75)80118-5
    • (1975) J. Mol. Biol. , vol.98 , pp. 281-291
    • McLachlan, A.D.1    Stewart, M.2    Smillie, L.B.3
  • 10
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • DOI 10.1016/S0962-8924(00)01898-5, PII S0962892400018985
    • P. Burkhard J. Stetefeld S. V. Strelkov 2001 Trends Cell Sci. 11 82 88 1:CAS:528:DC%2BD3MXpslyktg%3D%3D 10.1016/S0962-8924(00)01898-5 (Pubitemid 32144755)
    • (2001) Trends in Cell Biology , vol.11 , Issue.2 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 11
    • 0026571898 scopus 로고
    • 1739975 10.1016/0092-8674(92)90145-3
    • E. K. O'shea R. Ruthkowski P. Kim 1992 Cell 68 699 708 1739975 10.1016/0092-8674(92)90145-3
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1    Ruthkowski, R.2    Kim, P.3
  • 12
    • 0036710244 scopus 로고    scopus 로고
    • Comparison of in vivo selection and rational design of heterodimeric coiled coils
    • DOI 10.1016/S0969-2126(02)00838-9, PII S0969212602008389
    • K. M. Arndt J. N. Pelletier K. M. Miller A. Plickthun T. Alber 2002 Structure 10 1235 1248 12220495 1:CAS:528:DC%2BD38XntVais74%3D 10.1016/S0969-2126(02)00838-9 (Pubitemid 35254012)
    • (2002) Structure , vol.10 , Issue.9 , pp. 1235-1248
    • Arndt, K.M.1    Pelletier, J.N.2    Muller, K.M.3    Pluckthun, A.4    Alber, T.5
  • 16
    • 0035823858 scopus 로고    scopus 로고
    • Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host [13]
    • DOI 10.1021/ja016652k
    • Y. Tang D. A. Tirrell 2001 J. Am. Chem. Soc. 123 11089 11090 11686725 1:CAS:528:DC%2BD3MXntl2lsrg%3D 10.1021/ja016652k (Pubitemid 33042035)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.44 , pp. 11089-11090
    • Tang, Y.1    Tirrell, D.A.2
  • 17
    • 0028364239 scopus 로고
    • The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded a-helical coiled-coils
    • DOI 10.1006/jmbi.1994.1250
    • N. E. Zhou C. M. Kay R. S. Hodges 1994 J. Mol. Biol. 237 500 512 8151708 1:CAS:528:DyaK2cXltVahsbY%3D 10.1006/jmbi.1994.1250 (Pubitemid 24156420)
    • (1994) Journal of Molecular Biology , vol.237 , Issue.4 , pp. 500-512
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 18
    • 4344575287 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD2cXhsFKgsLk%3D
    • J. M. Mason K. M. Arndt 2004 Chem. BioChem. 5 170 176 1:CAS:528:DC%2BD2cXhsFKgsLk%3D
    • (2004) Chem. BioChem. , vol.5 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 19
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in α-helical coiled coils: Stutters and stammers
    • DOI 10.1002/(SICI)1097-0134(199610)26:2<134::AID-PROT3>3.0.CO;2-G
    • J. H. Brown C. Cohen D. Parry 1996 Proteins 26 134 145 8916221 1:CAS:528:DyaK28XntVKhu7w%3D 10.1002/(SICI)1097-0134(199610)26:2<134::AID- PROT3>3.0.CO;2-G (Pubitemid 26365307)
    • (1996) Proteins: Structure, Function and Genetics , vol.26 , Issue.2 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.D.3
  • 20
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • DOI 10.1006/jmbi.1999.2528
    • H. Herrmann M. Haner M. Brettel N.-O. Ku U. Aebi 1999 J. Mol. Biol. 286 1403 1420 10064706 1:CAS:528:DyaK1MXhsVCltLc%3D 10.1006/jmbi.1999.2528 (Pubitemid 29121725)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.5 , pp. 1403-1420
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Ku, N.-O.4    Aebi, U.5
  • 21
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • DOI 10.1038/371037a0
    • P. A. Bullough F. M. Hughson J. J. Skehel D. C. Wiley 1994 Nature 371 37 43 8072525 1:CAS:528:DyaK2cXmt1Cmsbw%3D 10.1038/371037a0 (Pubitemid 24277462)
    • (1994) Nature , vol.371 , Issue.6492 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 22
    • 0031808074 scopus 로고    scopus 로고
    • 9649402 1:CAS:528:DyaK1cXktlWmt7c%3D 10.1016/S0006-3495(98)77529-0
    • C. N. Pace J. M. Scholtz 1998 Biophys. J. 75 422 427 9649402 1:CAS:528:DyaK1cXktlWmt7c%3D 10.1016/S0006-3495(98)77529-0
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 23
    • 0041315637 scopus 로고    scopus 로고
    • Clustering of large hydrophobes in the hydrophobic core of two-stranded α-helical coiled-coils controls protein folding and stability
    • DOI 10.1074/jbc.M305306200
    • S. C. Kwok R. S. Hodges 2003 J. Biol. Chem. 278 35248 35254 12842878 1:CAS:528:DC%2BD3sXntVWqtbY%3D 10.1074/jbc.M305306200 (Pubitemid 37102291)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35248-35254
    • Kwok, S.C.1    Hodges, R.S.2
  • 24
    • 2442655493 scopus 로고    scopus 로고
    • Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded α-helical coiled-coils
    • DOI 10.1074/jbc.M401074200
    • S. C. Kwok R. S. Hodges 2004 J. Biol. Chem. 279 21576 21588 15020585 1:CAS:528:DC%2BD2cXjvV2ms74%3D 10.1074/jbc.M401074200 (Pubitemid 38656569)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21576-21588
    • Kwok, S.C.1    Hodges, R.S.2
  • 25
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: Distribution, properties and function
    • DOI 10.1023/A:1010303732441
    • S. V. Perry 2001 J. Muscle Res. Cell Motil. 22 5 49 11563548 1:CAS:528:DC%2BD3MXntFGqsrk%3D 10.1023/A:1010303732441 (Pubitemid 32831636)
    • (2001) Journal of Muscle Research and Cell Motility , vol.22 , Issue.1 , pp. 5-49
    • Perry, S.V.1
  • 26
    • 0024486421 scopus 로고
    • 2643110 1:CAS:528:DyaL1MXhtlSks7s%3D 10.1073/pnas.86.1.90
    • H. P. Liu A. Bretscher 1989 Proc. Natl. Acad. Sci. USA 86 90 93 2643110 1:CAS:528:DyaL1MXhtlSks7s%3D 10.1073/pnas.86.1.90
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 90-93
    • Liu, H.P.1    Bretscher, A.2
  • 28
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: Divining rods for actin cytoskeleton function
    • DOI 10.1016/j.tcb.2005.04.007, PII S0962892405001091
    • P. W. Gunning G. Schevzov A. J. Kee E. C. Hardeman 2005 Trends Cell Biol. 15 333 341 15953552 1:CAS:528:DC%2BD2MXlt1Srt78%3D 10.1016/j.tcb.2005.04.007 (Pubitemid 40805330)
    • (2005) Trends in Cell Biology , vol.15 , Issue.6 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 30
    • 60849113734 scopus 로고    scopus 로고
    • 19209820 1:CAS:528:DC%2BC3cXhsFyjsbzI 10.1007/978-0-387-85766-4-12
    • A. J. Kee E. C. Hardeman 2008 Adv. Exp. Med. Biol. 644 143 157 19209820 1:CAS:528:DC%2BC3cXhsFyjsbzI 10.1007/978-0-387-85766-4-12
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 143-157
    • Kee, A.J.1    Hardeman, E.C.2
  • 31
    • 43549114084 scopus 로고    scopus 로고
    • β-Tropomyosin mutations alter tropomyosin isoform composition
    • DOI 10.1111/j.1468-1331.2008.02131.x
    • J. Nilsson H. Taijsharghi 2008 Eur. J. Neurol. 15 573 578 18422639 1:STN:280:DC%2BD1czgvFyrug%3D%3D 10.1111/j.1468-1331.2008.02131.x (Pubitemid 351677510)
    • (2008) European Journal of Neurology , vol.15 , Issue.6 , pp. 573-578
    • Nilsson, J.1    Tajsharghi, H.2
  • 33
    • 0035860720 scopus 로고    scopus 로고
    • 11457840 1:CAS:528:DC%2BD3MXmvFClur0%3D 10.1074/jbc.M104750200
    • J. Strand M. Nili E. Homsher L. S. Tobacman 2001 J. Biol. Chem. 276 34832 34839 11457840 1:CAS:528:DC%2BD3MXmvFClur0%3D 10.1074/jbc.M104750200
    • (2001) J. Biol. Chem. , vol.276 , pp. 34832-34839
    • Strand, J.1    Nili, M.2    Homsher, E.3    Tobacman, L.S.4
  • 34
    • 77951975707 scopus 로고    scopus 로고
    • 20026408 1:CAS:528:DC%2BC3cXkvFKksr4%3D 10.1016/j.jsb.2009.12.017
    • X. Li W. Lehman S. Fischer K. C. Holmes 2010 J. Struct. Biol. 170 307 312 20026408 1:CAS:528:DC%2BC3cXkvFKksr4%3D 10.1016/j.jsb.2009.12.017
    • (2010) J. Struct. Biol. , vol.170 , pp. 307-312
    • Li, X.1    Lehman, W.2    Fischer, S.3    Holmes, K.C.4
  • 35
    • 0017849306 scopus 로고
    • 628011 1:CAS:528:DyaE1cXhtFKltro%3D 10.1016/0022-2836(78)90413-8
    • S. S. Lehrer 1978 J. Mol. Biol. 118 209 226 628011 1:CAS:528: DyaE1cXhtFKltro%3D 10.1016/0022-2836(78)90413-8
    • (1978) J. Mol. Biol. , vol.118 , pp. 209-226
    • Lehrer, S.S.1
  • 38
    • 0027265825 scopus 로고
    • 8401212 1:CAS:528:DyaK2cXlvFyksLY%3D 10.1002/pro.5560020809
    • N. Greenfield S. Hitchcock-DeGregori 1993 Protein Sci. 2 1263 1273 8401212 1:CAS:528:DyaK2cXlvFyksLY%3D 10.1002/pro.5560020809
    • (1993) Protein Sci. , vol.2 , pp. 1263-1273
    • Greenfield, N.1    Hitchcock-Degregori, S.2
  • 39
  • 40
    • 0019321960 scopus 로고
    • 7440542 1:CAS:528:DyaL3cXmtleit7s%3D
    • P. Graceffa S. S. Lehrer 1980 J. Biol. Chem. 255 11296 11300 7440542 1:CAS:528:DyaL3cXmtleit7s%3D
    • (1980) J. Biol. Chem. , vol.255 , pp. 11296-11300
    • Graceffa, P.1    Lehrer, S.S.2
  • 41
    • 0025895385 scopus 로고
    • 2016303 1:CAS:528:DyaK3MXisVejtbY%3D
    • Y. Ishii S. S. Lehrer 1991 J. Biol. Chem. 266 6894 6903 2016303 1:CAS:528:DyaK3MXisVejtbY%3D
    • (1991) J. Biol. Chem. , vol.266 , pp. 6894-6903
    • Ishii, Y.1    Lehrer, S.S.2
  • 42
    • 0014116140 scopus 로고
    • 6049467 1:CAS:528:DyaF2sXkslSmsrc%3D 10.1021/bi00860a020
    • T. Ooi 1967 Biochemistry 6 2433 2439 6049467 1:CAS:528:DyaF2sXkslSmsrc%3D 10.1021/bi00860a020
    • (1967) Biochemistry , vol.6 , pp. 2433-2439
    • Ooi, T.1
  • 43
    • 0017359421 scopus 로고
    • Digestion of tropomyosin with trypsin
    • DOI 10.1016/0014-5793(77)80072-0
    • A. Gorecka W. Drabikowski 1977 FEBS Lett. 75 145 148 852575 1:CAS:528:DyaE2sXhs1KltLY%3D 10.1016/0014-5793(77)80072-0 (Pubitemid 8080298)
    • (1977) FEBS Letters , vol.75 , Issue.1 , pp. 145-148
    • Gorecka, A.1    Drabikowski, W.2
  • 44
    • 0019424237 scopus 로고
    • 7451462 1:CAS:528:DyaL3MXmtVansA%3D%3D
    • M. D. Pato A. S. Mak L. B. Smillie 1981 J. Biol. Chem. 256 593 601 7451462 1:CAS:528:DyaL3MXmtVansA%3D%3D
    • (1981) J. Biol. Chem. , vol.256 , pp. 593-601
    • Pato, M.D.1    Mak, A.S.2    Smillie, L.B.3
  • 45
    • 0021174871 scopus 로고
    • Local structural changes in tropomyosin detected by a trypsin-probe method
    • DOI 10.1021/bi00315a040
    • H. Ueno 1984 Biochemistry 23 4791 4798 6498161 1:CAS:528: DyaL2cXlt1Ghsr0%3D 10.1021/bi00315a040 (Pubitemid 14012286)
    • (1984) Biochemistry , vol.23 , Issue.20 , pp. 4791-4798
    • Ueno, H.1
  • 46
    • 43749096824 scopus 로고    scopus 로고
    • 18165684 1:CAS:528:DC%2BD1cXivFyjsbo%3D 10.1074/jbc.M707485200
    • J. P. Sumida E. Wu S. S. Lehrer 2008 J. Biol. Chem. 283 6728 6734 18165684 1:CAS:528:DC%2BD1cXivFyjsbo%3D 10.1074/jbc.M707485200
    • (2008) J. Biol. Chem. , vol.283 , pp. 6728-6734
    • Sumida, J.P.1    Wu, E.2    Lehrer, S.S.3
  • 50
    • 0019886918 scopus 로고
    • 7272281 1:CAS:528:DyaL3MXktlOntL8%3D 10.1021/bi00516a029
    • D. L. Williams Jr. C. A. Swenson 1981 Biochemistry 20 3856 3864 7272281 1:CAS:528:DyaL3MXktlOntL8%3D 10.1021/bi00516a029
    • (1981) Biochemistry , vol.20 , pp. 3856-3864
    • Williams, Jr.D.L.1    Swenson, C.A.2
  • 52
    • 0020483742 scopus 로고
    • 7166753 1:CAS:528:DyaL38XlsFygsrY%3D 10.1016/0022-2836(82)90299-6
    • S. A. Potekhin P. L. Privalov 1982 J. Mol. Biol. 159 519 535 7166753 1:CAS:528:DyaL38XlsFygsrY%3D 10.1016/0022-2836(82)90299-6
    • (1982) J. Mol. Biol. , vol.159 , pp. 519-535
    • Potekhin, S.A.1    Privalov, P.L.2
  • 53
    • 0026143165 scopus 로고
    • 1868164 1:CAS:528:DyaK3MXks1OjsLg%3D 10.1002/bip.360310504
    • J. M. Sturtevant M. E. Holtzer A. Holtzer 1991 Biopolymers 31 489 495 1868164 1:CAS:528:DyaK3MXks1OjsLg%3D 10.1002/bip.360310504
    • (1991) Biopolymers , vol.31 , pp. 489-495
    • Sturtevant, J.M.1    Holtzer, M.E.2    Holtzer, A.3
  • 55
    • 10044280728 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy mutations in α-tropomyosin, Asp175Asn and Glut180Gly, on the thermal unfolding of actin-bound tropomyosin
    • DOI 10.1529/biophysj.104.048793
    • E. Kremneva S. Boussouf O. Nikolaeva R. Maytum M. A. Geeves D. I. Levitsky 2004 Biophys. J. 87 3922 3933 15454401 1:CAS:528:DC%2BD2cXhtVOmtbnK 10.1529/biophysj.104.048793 (Pubitemid 39602898)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 3922-3933
    • Kremneva, E.1    Boussouf, S.2    Nikolaeva, O.3    Maytum, R.4    Geeves, M.A.5    Levitsky, D.I.6
  • 64
    • 0033985268 scopus 로고    scopus 로고
    • Crystal structure of tropomyosin at 7 angstroms resolution
    • DOI 10.1002/(SICI)1097-0134(20000101)38:1<49::AID-PROT6>3.0.CO;2-B
    • F. G. Whitby G. N. Phillips Jr. 2000 Proteins 38 49 59 10651038 1:CAS:528:DC%2BD3cXis1OmtQ%3D%3D 10.1002/(SICI)1097-0134(20000101)38:1<49:: AID-PROT6>3.0.CO;2-B (Pubitemid 30020602)
    • (2000) Proteins: Structure, Function and Genetics , vol.38 , Issue.1 , pp. 49-59
    • Whitby, F.G.1    Phillips Jr., G.N.2
  • 68
    • 0036842026 scopus 로고    scopus 로고
    • 12414708 1:CAS:528:DC%2BD38Xos1Crtrc%3D 10.1016/S0006-3495(02)75285-5
    • N. J. Greenfield T. Palm S. E. Hitchcock-DeGregori 2002 Biophys. J. 83 2754 2766 12414708 1:CAS:528:DC%2BD38Xos1Crtrc%3D 10.1016/S0006-3495(02)75285-5
    • (2002) Biophys. J. , vol.83 , pp. 2754-2766
    • Greenfield, N.J.1    Palm, T.2    Hitchcock-Degregori, S.E.3
  • 69
    • 77954003079 scopus 로고    scopus 로고
    • 20506487 1:CAS:528:DC%2BC3cXotVWhsr4%3D 10.1002/pro.415
    • J. H. Brown 2010 Protein Sci. 19 1366 1375 20506487 1:CAS:528: DC%2BC3cXotVWhsr4%3D 10.1002/pro.415
    • (2010) Protein Sci. , vol.19 , pp. 1366-1375
    • Brown, J.H.1
  • 70
    • 0016767561 scopus 로고
    • 125100 1:CAS:528:DyaE2MXksFCkt74%3D 10.1021/bi00683a025
    • B. L. Eaton D. R. Kominz E. Eizenberg 1975 Biochemistry 14 2718 2725 125100 1:CAS:528:DyaE2MXksFCkt74%3D 10.1021/bi00683a025
    • (1975) Biochemistry , vol.14 , pp. 2718-2725
    • Eaton, B.L.1    Kominz, D.R.2    Eizenberg, E.3
  • 73
    • 0019882706 scopus 로고
    • 7284001 1:CAS:528:DyaL3MXltFSnt7k%3D 10.1016/S0006-291X(81)80032-0
    • A. S. Mak L. B. Smillie 1981 Biochem. Biophys. Res. Commun. 101 208 214 7284001 1:CAS:528:DyaL3MXltFSnt7k%3D 10.1016/S0006-291X(81)80032-0
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 208-214
    • Mak, A.S.1    Smillie, L.B.2
  • 81
    • 78650832959 scopus 로고    scopus 로고
    • 21203426 1:CAS:528:DC%2BC3MXjvVSqsw%3D%3D 10.1371/journal.pone.0015801
    • M. Johnson A. T. Coulton M. A. Geeves D. P. Mulvihill 2010 PLoS One 5 e15801 21203426 1:CAS:528:DC%2BC3MXjvVSqsw%3D%3D 10.1371/journal.pone.0015801
    • (2010) PLoS One , vol.5 , pp. 15801
    • Johnson, M.1    Coulton, A.T.2    Geeves, M.A.3    Mulvihill, D.P.4
  • 83
    • 77953261060 scopus 로고    scopus 로고
    • 20465283 1:CAS:528:DC%2BC3cXmtlCrt70%3D 10.1021/bi100349a
    • J. Frye V. A. Klenchin I. Rayment 2010 Biochemistry 49 4908 4920 20465283 1:CAS:528:DC%2BC3cXmtlCrt70%3D 10.1021/bi100349a
    • (2010) Biochemistry , vol.49 , pp. 4908-4920
    • Frye, J.1    Klenchin, V.A.2    Rayment, I.3
  • 84
    • 60849130990 scopus 로고    scopus 로고
    • 19209815 1:CAS:528:DC%2BC3cXhsFyjsb%2FJ 10.1007/978-0-387-85766-4-7
    • L. S. Tobacman 2008 Adv. Exp. Med. Biol. 644 85 94 19209815 1:CAS:528:DC%2BC3cXhsFyjsb%2FJ 10.1007/978-0-387-85766-4-7
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 85-94
    • Tobacman, L.S.1
  • 85
    • 0017072908 scopus 로고
    • 131972 1:CAS:528:DyaE28XksFygt78%3D 10.1126/science.131972
    • B. L. Eaton 1976 Science 192 1337 1339 131972 1:CAS:528: DyaE28XksFygt78%3D 10.1126/science.131972
    • (1976) Science , vol.192 , pp. 1337-1339
    • Eaton, B.L.1
  • 86
    • 17544365077 scopus 로고    scopus 로고
    • Opposite effects of myosin subfragment 1 on binding of cardiac troponin and tropomyosin to the thin filament
    • DOI 10.1074/jbc.271.22.12867
    • M. Cassell L. S. Tobacman 1996 J. Biol. Chem. 271 12867 12872 8662810 1:CAS:528:DyaK28XjtlGjtbk%3D 10.1074/jbc.271.22.12867 (Pubitemid 26175860)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.22 , pp. 12867-12872
    • Cassell, M.1    Tobacman, L.S.2
  • 87
    • 0017136639 scopus 로고
    • 950663 1:CAS:528:DyaE28XktFGkur0%3D 10.1016/0022-2836(76)90313-2
    • A. D. McLachlan M. Stewart 1976 J. Mol. Biol. 103 271 298 950663 1:CAS:528:DyaE28XktFGkur0%3D 10.1016/0022-2836(76)90313-2
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 88
    • 0023042854 scopus 로고
    • 3820300 1:CAS:528:DyaL2sXhsFeqsg%3D%3D 10.1016/0022-2836(86)90469-9
    • G. N. Phillips Jr. 1986 J. Mol. Biol. 192 128 131 3820300 1:CAS:528:DyaL2sXhsFeqsg%3D%3D 10.1016/0022-2836(86)90469-9
    • (1986) J. Mol. Biol. , vol.192 , pp. 128-131
    • Phillips, Jr.G.N.1
  • 89
    • 0030067632 scopus 로고    scopus 로고
    • Mapping the functional domains within the carboxyl terminus of α- tropomyosin encoded by the alternatively spliced ninth exon
    • DOI 10.1074/jbc.271.8.4236
    • S. E. Hitchcock-DeGregori Y. An 1996 J. Biol. Chem. 271 3600 3603 8631967 1:CAS:528:DyaK28XhtFOkt7w%3D 10.1074/jbc.271.8.4236 (Pubitemid 26070527)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.8 , pp. 4236-4242
    • Hammell, R.L.1    Hitchcock-DeGregori, S.E.2
  • 90
    • 0025153066 scopus 로고
    • Tropomyosin has discrete actin-binding sites with sevenfold and fourteenfold periodicities
    • DOI 10.1016/0022-2836(90)90343-K
    • S. E. Hitchcock-DeGregori T. A. Varnell 1990 J. Mol. Biol. 214 885 896 2143787 1:CAS:528:DyaK3cXlvVKrsb4%3D 10.1016/0022-2836(90)90343-K (Pubitemid 20263953)
    • (1990) Journal of Molecular Biology , vol.214 , Issue.4 , pp. 885-896
    • Hitchcock-DeGregori, S.E.1    Varnell, T.A.2
  • 91
    • 0030884448 scopus 로고    scopus 로고
    • The sequence of the alternatively spliced sixth exon of α-tropomyosin is critical for cooperative actin binding but not for interaction with troponin
    • DOI 10.1074/jbc.272.36.22409
    • R. L. Hammel S. E. Hitchcock-DeGregori 1997 J. Biol. Chem. 272 22409 22416 10.1074/jbc.272.36.22409 (Pubitemid 27386048)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.36 , pp. 22409-22416
    • Hammell, R.L.1    Hitchcock-DeGregori, S.E.2
  • 92
    • 2242469352 scopus 로고    scopus 로고
    • Functions of tropomyosin's periodic repeats
    • DOI 10.1021/bi026519k
    • S. E. Hitchcock-DeGregori Y. Song N. J. Greenfield 2002 Biochemistry 41 15036 15044 12475253 1:CAS:528:DC%2BD38Xos1KjsLg%3D 10.1021/bi026519k (Pubitemid 35470683)
    • (2002) Biochemistry , vol.41 , Issue.50 , pp. 15036-15044
    • Hitchcock-DeGregori, S.E.1    Song, Y.2    Greenfield, N.J.3
  • 93
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • DOI 10.1016/j.str.2005.09.016, PII S0969212605003965
    • S. E. Hitchcock-DeGregori A. Singh 2006 Structure 14 43 50 16407064 10.1016/j.str.2005.09.016 1:CAS:528:DC%2BD28XksVWruw%3D%3D (Pubitemid 43350072)
    • (2006) Structure , vol.14 , Issue.1 , pp. 43-50
    • Singh, A.1    Hitchcock-Degregori, S.E.2
  • 94
    • 77951977436 scopus 로고    scopus 로고
    • 20036744 1:CAS:528:DC%2BC3cXkvFKksrw%3D 10.1016/j.jsb.2009.12.013
    • S. E. Hitchcock-DeGregori A. Singh 2010 J. Struct. Biol. 170 319 324 20036744 1:CAS:528:DC%2BC3cXkvFKksrw%3D 10.1016/j.jsb.2009.12.013
    • (2010) J. Struct. Biol. , vol.170 , pp. 319-324
    • Hitchcock-Degregori, S.E.1    Singh, A.2
  • 95
    • 0344198181 scopus 로고    scopus 로고
    • Local Destabilization of the Tropomyosin Coiled Coil Gives the Molecular Flexibility Required for Actin Binding
    • DOI 10.1021/bi0348462
    • A. Singh S. E. Hitchcock-DeGregori 2003 Biochemistry 42 14114 14121 14640678 1:CAS:528:DC%2BD3sXovVCls7w%3D 10.1021/bi0348462 (Pubitemid 37499407)
    • (2003) Biochemistry , vol.42 , Issue.48 , pp. 14114-14121
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 96
    • 62449145371 scopus 로고    scopus 로고
    • 19116763 1:CAS:528:DC%2BD1MXivFymu78%3D 10.1007/s10974-008-9157-6
    • K. C. Holmes W. Lehman 2008 J. Muscle Res. Cell Motil. 29 213 219 19116763 1:CAS:528:DC%2BD1MXivFymu78%3D 10.1007/s10974-008-9157-6
    • (2008) J. Muscle Res. Cell Motil. , vol.29 , pp. 213-219
    • Holmes, K.C.1    Lehman, W.2
  • 97
    • 0019318268 scopus 로고
    • 6893586 1:CAS:528:DyaL3cXmtlehsLw%3D 10.1016/0014-5793(80)80263-8
    • A. Wegner 1980 FEBS Lett. 119 245 248 6893586 1:CAS:528: DyaL3cXmtlehsLw%3D 10.1016/0014-5793(80)80263-8
    • (1980) FEBS Lett. , vol.119 , pp. 245-248
    • Wegner, A.1
  • 100
    • 73149102752 scopus 로고    scopus 로고
    • 19883661 1:CAS:528:DC%2BC3cXjsVamuw%3D%3D 10.1016/j.jmb.2009.10.060
    • X. Li K. Holmes W. Lehman H. Jung S. Fischer 2010 J. Mol. Biol. 395 327 339 19883661 1:CAS:528:DC%2BC3cXjsVamuw%3D%3D 10.1016/j.jmb.2009.10.060
    • (2010) J. Mol. Biol. , vol.395 , pp. 327-339
    • Li, X.1    Holmes, K.2    Lehman, W.3    Jung, H.4    Fischer, S.5
  • 101
    • 77951977112 scopus 로고    scopus 로고
    • 10.1016/j.jsb.2010.01.016 1:CAS:528:DC%2BC3cXkvFKksr8%3D
    • X. Li W. Lehman S. Fischer 2011 J. Struct. Biol. 170 313 318 10.1016/j.jsb.2010.01.016 1:CAS:528:DC%2BC3cXkvFKksr8%3D
    • (2011) J. Struct. Biol. , vol.170 , pp. 313-318
    • Li, X.1    Lehman, W.2    Fischer, S.3
  • 102
    • 79951834827 scopus 로고    scopus 로고
    • 21320445 1:CAS:528:DC%2BC3MXhvFKgtbs%3D 10.1016/j.bpj.2010.12.3697
    • X. Li L. S. Tobacman J. Mun R. Craig S. Fischer W. Lehman 2011 Biophys. J. 100 1005 1013 21320445 1:CAS:528:DC%2BC3MXhvFKgtbs%3D 10.1016/j.bpj.2010.12. 3697
    • (2011) Biophys. J. , vol.100 , pp. 1005-1013
    • Li, X.1    Tobacman, L.S.2    Mun, J.3    Craig, R.4    Fischer, S.5    Lehman, W.6
  • 103
    • 0015243824 scopus 로고
    • 4945533 1:CAS:528:DyaE38Xkt1yltg%3D%3D 10.1016/0022-2836(71)90144-6
    • S. Fujime S. Ishiwata 1971 J. Mol. Biol. 62 251 265 4945533 1:CAS:528:DyaE38Xkt1yltg%3D%3D 10.1016/0022-2836(71)90144-6
    • (1971) J. Mol. Biol. , vol.62 , pp. 251-265
    • Fujime, S.1    Ishiwata, S.2
  • 104
    • 0017124861 scopus 로고
    • 133761 1:CAS:528:DyaE28XktFKisLs%3D 10.1016/0092-8674(76)90203-8
    • S. E. Hitchcock L. Carisson U. Lindberg 1976 Cell 7 531 542 133761 1:CAS:528:DyaE28XktFKisLs%3D 10.1016/0092-8674(76)90203-8
    • (1976) Cell , vol.7 , pp. 531-542
    • Hitchcock, S.E.1    Carisson, L.2    Lindberg, U.3
  • 106
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • DOI 10.1146/annurev.cellbio.15.1.185
    • J. R. Bamburg 1999 Annu. Rev. Cell Dev. Biol. 15 185 230 10611961 1:CAS:528:DC%2BD3cXhtVSnurw%3D 10.1146/annurev.cellbio.15.1.185 (Pubitemid 32250375)
    • (1999) Annual Review of Cell and Developmental Biology , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 107
  • 109
    • 0001353052 scopus 로고
    • 13475381 1:STN:280:DyaG1c%2FhvVSksw%3D%3D 10.1083/jcb.3.5.631
    • H. E. Huxley 1957 J. Biophys. Biochem. Cytol. 3 631 648 13475381 1:STN:280:DyaG1c%2FhvVSksw%3D%3D 10.1083/jcb.3.5.631
    • (1957) J. Biophys. Biochem. Cytol. , vol.3 , pp. 631-648
    • Huxley, H.E.1
  • 110
    • 0015914687 scopus 로고
    • 4266351 1:CAS:528:DyaE3sXktFCqs70%3D 10.1016/0022-2836(73)90376-8
    • S. S. Margossian S. Lowey 1973 J. Mol. Biol. 74 313 330 4266351 1:CAS:528:DyaE3sXktFCqs70%3D 10.1016/0022-2836(73)90376-8
    • (1973) J. Mol. Biol. , vol.74 , pp. 313-330
    • Margossian, S.S.1    Lowey, S.2
  • 112
    • 0015846921 scopus 로고
    • 4269253 1:CAS:528:DyaE3sXkslKgtLs%3D
    • C. R. Bagshaw D. R. Trentham 1973 Biochem. J. 133 323 328 4269253 1:CAS:528:DyaE3sXkslKgtLs%3D
    • (1973) Biochem. J. , vol.133 , pp. 323-328
    • Bagshaw, C.R.1    Trentham, D.R.2
  • 113
    • 0017044811 scopus 로고
    • Energetics and mechanism of actomyosin adenosine triphosphatase
    • DOI 10.1021/bi00671a020
    • H. D. White E. W. Taylor 1976 Biochemistry 15 5818 5826 12793 1:CAS:528:DyaE2sXosFegtg%3D%3D 10.1021/bi00671a020 (Pubitemid 8016839)
    • (1976) Biochemistry , vol.15 , Issue.26 , pp. 5818-5826
    • White, H.D.1    Taylor, E.W.2
  • 114
    • 0015214368 scopus 로고
    • 4258719 1:CAS:528:DyaE38XjtFyisQ%3D%3D 10.1021/bi00801a004
    • R. W. Lymn E. W. Taylor 1971 Biochemistry 10 4617 4624 4258719 1:CAS:528:DyaE38XjtFyisQ%3D%3D 10.1021/bi00801a004
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 117
    • 0026534392 scopus 로고
    • 1579164 1:CAS:528:DyaK38XktVGjsrw%3D 10.1038/357156a0
    • M. Irving V. Lombardi G. Piazzesi M. A. Ferenczi 1992 Nature 357 156 158 1579164 1:CAS:528:DyaK38XktVGjsrw%3D 10.1038/357156a0
    • (1992) Nature , vol.357 , pp. 156-158
    • Irving, M.1    Lombardi, V.2    Piazzesi, G.3    Ferenczi, M.A.4
  • 118
    • 0034728847 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD3cXkt1eqsrw%3D 10.1098/rstb.2000.0583
    • K. C. Holmes M. A. Geeves 2000 Phil. Trans. R. Soc. Lond. B 355 419 431 1:CAS:528:DC%2BD3cXkt1eqsrw%3D 10.1098/rstb.2000.0583
    • (2000) Phil. Trans. R. Soc. Lond. B , vol.355 , pp. 419-431
    • Holmes, K.C.1    Geeves, M.A.2
  • 119
    • 0031777885 scopus 로고    scopus 로고
    • 9657517 1:CAS:528:DyaK1cXktlCku78%3D
    • J. M. Squire E. P. Morris 1998 FASEB J. 12 761 771 9657517 1:CAS:528:DyaK1cXktlCku78%3D
    • (1998) FASEB J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 121
    • 0019013686 scopus 로고
    • 6930656 1:CAS:528:DyaL3cXks1eru7Y%3D 10.1073/pnas.77.5.2616
    • L. E. Greene E. Eisenberg 1980 Proc. Natl. Acad. Sci. USA 77 2616 2620 6930656 1:CAS:528:DyaL3cXks1eru7Y%3D 10.1073/pnas.77.5.2616
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2616-2620
    • Greene, L.E.1    Eisenberg, E.2
  • 122
    • 0020490904 scopus 로고
    • 6123507 1:CAS:528:DyaL38XkvVOksL4%3D
    • S. S. Lehrer E. P. Morris 1982 J. Biol. Chem. 257 8073 8080 6123507 1:CAS:528:DyaL38XkvVOksL4%3D
    • (1982) J. Biol. Chem. , vol.257 , pp. 8073-8080
    • Lehrer, S.S.1    Morris, E.P.2
  • 123
    • 0027234056 scopus 로고
    • 8218897 1:CAS:528:DyaK2cXhsFKqs7k%3D 10.1016/S0006-3495(93)81110-X
    • D. F. A. McKillop M. A. Geeves 1993 Biophys. J. 65 693 701 8218897 1:CAS:528:DyaK2cXhsFKqs7k%3D 10.1016/S0006-3495(93)81110-X
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 124
    • 0033579814 scopus 로고    scopus 로고
    • Cooperativity and switching within the three-state model of muscle regulation
    • DOI 10.1021/bi981603e
    • R. Maytum S. S. Lehrer M. A. Geeves 1999 Biochemistry 38 1102 1110 9894007 1:CAS:528:DyaK1cXotFChsbg%3D 10.1021/bi981603e (Pubitemid 29052726)
    • (1999) Biochemistry , vol.38 , Issue.3 , pp. 1102-1110
    • Maytum, R.1    Lehrer, S.S.2    Geeves, M.A.3
  • 125
    • 0030838333 scopus 로고    scopus 로고
    • Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions
    • DOI 10.1021/bi971568w
    • S. S. Lehrer N. L. Golitsina M. A. Geeves 1997 Biochemistry 36 13449 13455 9354612 1:CAS:528:DyaK2sXms1SqsL4%3D 10.1021/bi971568w (Pubitemid 27481590)
    • (1997) Biochemistry , vol.36 , Issue.44 , pp. 13449-13454
    • Lehrer, S.S.1    Golitsina, N.L.2    Geeves, M.A.3
  • 126
  • 128
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • DOI 10.1038/347044a0
    • K. C. Holmes D. Popp W. Gebhard W. Kabsch 1990 Nature 347 44 49 2395461 1:CAS:528:DyaK3cXmtVKqsbs%3D 10.1038/347044a0 (Pubitemid 20280180)
    • (1990) Nature , vol.347 , Issue.6288 , pp. 44-49
    • Holmes, K.C.1    Popp, D.2    Gebhard, W.3    Kabsch, W.4
  • 129
    • 60849116181 scopus 로고    scopus 로고
    • 19209816 1:CAS:528:DC%2BC3cXhsFyjsb%2FL 10.1007/978-0-387-85766-4-8
    • W. Lehman R. Craig 2008 Adv. Exp. Med. Biol. 644 95 109 19209816 1:CAS:528:DC%2BC3cXhsFyjsb%2FL 10.1007/978-0-387-85766-4-8
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 95-109
    • Lehman, W.1    Craig, R.2
  • 131
    • 33847377664 scopus 로고    scopus 로고
    • Mutations in fast skeletal troponin I, troponin T, and β-tropomyosin that cause distal arthrogryposis all increase contractile function
    • DOI 10.1096/fj.06-6899com
    • P. Robinson S. Lipscomb L. Preston E. Altin H. Watkins C. Ashley C. Redwood 2007 FASEB J. 21 896 905 17194691 1:CAS:528:DC%2BD2sXis1ehtrw%3D 10.1096/fj.06-6899com (Pubitemid 46348262)
    • (2007) FASEB Journal , vol.21 , Issue.3 , pp. 896-905
    • Robinson, P.1    Lipscomb, S.2    Preston, L.C.3    Altin, E.4    Watkins, H.5    Ashley, C.C.6    Redwood, C.S.7
  • 132
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: From mutation identification to mechanistic paradigms
    • DOI 10.1016/S0092-8674(01)00242-2
    • J. G. Seidman C. Seidman 2001 Cell 104 557 567 11239412 1:CAS:528:DC%2BD3MXis1Kks70%3D 10.1016/S0092-8674(01)00242-2 (Pubitemid 32201950)
    • (2001) Cell , vol.104 , Issue.4 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 133
    • 0036787237 scopus 로고    scopus 로고
    • 12270949 1:CAS:528:DC%2BD38Xot1Ggurc%3D
    • D. Fatkin R. M. Graham 2002 Physiol. Rev. 82 945 980 12270949 1:CAS:528:DC%2BD38Xot1Ggurc%3D
    • (2002) Physiol. Rev. , vol.82 , pp. 945-980
    • Fatkin, D.1    Graham, R.M.2
  • 134
    • 60849112865 scopus 로고    scopus 로고
    • 19209819 1:CAS:528:DC%2BC3cXhsFyjsbzO 10.1007/978-0-387-85766-4-11
    • D. F. Wieczorek G. Jagatheesan S. Rajan 2008 Adv. Exp. Med. Biol. 644 132 142 19209819 1:CAS:528:DC%2BC3cXhsFyjsbzO 10.1007/978-0-387-85766-4-11
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 132-142
    • Wieczorek, D.F.1    Jagatheesan, G.2    Rajan, S.3
  • 136
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • DOI 10.1016/j.str.2005.09.016, PII S0969212605003965
    • S. E. Hitchcock-DeGregori A. Singh 2006 Structure 14 43 50 16407064 10.1016/j.str.2005.09.016 1:CAS:528:DC%2BD28XksVWruw%3D%3D (Pubitemid 43350072)
    • (2006) Structure , vol.14 , Issue.1 , pp. 43-50
    • Singh, A.1    Hitchcock-Degregori, S.E.2


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