메뉴 건너뛰기




Volumn 101, Issue 8, 2011, Pages 1968-1977

Mechanical unfolding of cardiac myosin binding protein-C by atomic force microscopy

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; FIBRONECTIN; IMMUNOGLOBULIN; MYOSIN BINDING PROTEIN C; MYOSIN-BINDING PROTEIN C;

EID: 80054712993     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.08.030     Document Type: Article
Times cited : (38)

References (49)
  • 1
    • 0020522788 scopus 로고
    • The C-proteins of rabbit red, white, and cardiac muscles
    • K. Yamamoto, and C. Moos The C-proteins of rabbit red, white, and cardiac muscles J. Biol. Chem. 258 1983 8395 8401 (Pubitemid 13074118)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.13 , pp. 8395-8401
    • Yamamoto, K.1    Moos, C.2
  • 3
    • 77951582392 scopus 로고    scopus 로고
    • Malignant and benign mutations in familial cardiomyopathies: Insights into mutations linked to complex cardiovascular phenotypes
    • Q. Xu, and S. Dewey A.V. Gomes Malignant and benign mutations in familial cardiomyopathies: insights into mutations linked to complex cardiovascular phenotypes J. Mol. Cell. Cardiol. 48 2010 899 909
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 899-909
    • Xu, Q.1    Dewey, S.2    Gomes, A.V.3
  • 4
    • 79953048882 scopus 로고    scopus 로고
    • In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament
    • S.P. Harris, R.G. Lyons, and K.L. Bezold In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament Circ. Res. 108 2011 751 764
    • (2011) Circ. Res. , vol.108 , pp. 751-764
    • Harris, S.P.1    Lyons, R.G.2    Bezold, K.L.3
  • 5
    • 33749654402 scopus 로고    scopus 로고
    • Protein kinase A-mediated acceleration of the stretch activation response in murine skinned myocardium is eliminated by ablation of cMyBP-C
    • DOI 10.1161/01.RES.0000245191.34690.66, PII 0000301220061013000015
    • J.E. Stelzer, J.R. Patel, and R.L. Moss Protein kinase A-mediated acceleration of the stretch activation response in murine skinned myocardium is eliminated by ablation of cMyBP-C Circ. Res. 99 2006 884 890 (Pubitemid 44556388)
    • (2006) Circulation Research , vol.99 , Issue.8 , pp. 884-890
    • Stelzer, J.E.1    Patel, J.R.2    Moss, R.L.3
  • 6
    • 55449118232 scopus 로고    scopus 로고
    • Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function
    • C.W. Tong, and J.E. Stelzer R.L. Moss Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function Circ. Res. 103 2008 974 982
    • (2008) Circ. Res. , vol.103 , pp. 974-982
    • Tong, C.W.1    Stelzer, J.E.2    Moss, R.L.3
  • 7
    • 0016818769 scopus 로고
    • Interaction of C-protein with myosin, myosin rod and light meromyosin
    • C. Moos, and G. Offer P. Bennett Interaction of C-protein with myosin, myosin rod and light meromyosin J. Mol. Biol. 97 1975 1 9
    • (1975) J. Mol. Biol. , vol.97 , pp. 1-9
    • Moos, C.1    Offer, G.2    Bennett, P.3
  • 8
    • 33846277638 scopus 로고    scopus 로고
    • Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod
    • DOI 10.1042/BJ20060500
    • E. Flashman, H. Watkins, and C. Redwood Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod Biochem. J. 401 2007 97 102 (Pubitemid 46114603)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 97-102
    • Flashman, E.1    Watkins, H.2    Redwood, C.3
  • 9
    • 0030030825 scopus 로고    scopus 로고
    • The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle
    • R. Gilbert, and M.G. Kelly D.A. Fischman The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle J. Cell Sci. 109 1996 101 111 (Pubitemid 26037932)
    • (1996) Journal of Cell Science , vol.109 , Issue.1 , pp. 101-111
    • Gilbert, R.1    Kelly, M.G.2    Mikawa, T.3    Fischman, D.A.4
  • 10
    • 0029029027 scopus 로고
    • Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: A modulator of cardiac contraction?
    • M. Gautel, and O. Zuffardi S. Labeit Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction? EMBO J. 14 1995 1952 1960
    • (1995) EMBO J. , vol.14 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Labeit, S.3
  • 11
    • 0032772719 scopus 로고    scopus 로고
    • cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion
    • DOI 10.1016/S0014-5793(99)00727-9, PII S0014579399007279
    • M. Gruen, H. Prinz, and M. Gautel cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion FEBS Lett. 453 1999 254 259 (Pubitemid 29326658)
    • (1999) FEBS Letters , vol.453 , Issue.3 , pp. 254-259
    • Gruen, M.1    Prinz, H.2    Gautel, M.3
  • 12
    • 66449110385 scopus 로고    scopus 로고
    • The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner
    • J.F. Shaffer, R.W. Kensler, and S.P. Harris The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner J. Biol. Chem. 284 2009 12318 12327
    • (2009) J. Biol. Chem. , vol.284 , pp. 12318-12327
    • Shaffer, J.F.1    Kensler, R.W.2    Harris, S.P.3
  • 14
    • 79958862768 scopus 로고    scopus 로고
    • Cytoskeletal protein kinases: Titin and its relations in mechanosensing
    • M. Gautel Cytoskeletal protein kinases: titin and its relations in mechanosensing Pflugers Arch. 462 2011 119 134
    • (2011) Pflugers Arch. , vol.462 , pp. 119-134
    • Gautel, M.1
  • 16
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • J.L. Hutter, and J. Bechhoefer Calibration of atomic-force microscope tips Rev. Sci. Instrum. 64 1993 1868 1873
    • (1993) Rev. Sci. Instrum. , vol.64 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 17
    • 26444601435 scopus 로고
    • Probing biological surfaces
    • C. Bustamante Probing biological surfaces Science 264 1994 296
    • (1994) Science , vol.264 , pp. 296
    • Bustamante, C.1
  • 18
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • M. Rief, and M. Gautel H.E. Gaub Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276 1997 1109 1112 (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 20
    • 18744374455 scopus 로고    scopus 로고
    • Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments
    • DOI 10.1006/jsbi.2002.4458
    • K. Watanabe, and C. Muhle-Goll H. Granzier Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments J. Struct. Biol. 137 2002 248 258 (Pubitemid 35430438)
    • (2002) Journal of Structural Biology , vol.137 , Issue.1-2 , pp. 248-258
    • Watanabe, K.1    Muhle-Goll, C.2    Kellermayer, M.S.Z.3    Labeit, S.4    Granzier, H.5
  • 23
    • 0037131207 scopus 로고    scopus 로고
    • Identification of novel interactions between domains of myosin binding protein-C that are modulated by hypertrophic cardiomyopathy missense mutations
    • DOI 10.1161/01.RES.0000036750.81083.83
    • J. Moolman-Smook, and E. Flashman H. Watkins Identification of novel interactions between domains of yosin binding protein-C that are modulated by hypertrophic cardiomyopathy missense mutations Circ. Res. 91 2002 704 711 (Pubitemid 35204953)
    • (2002) Circulation Research , vol.91 , Issue.8 , pp. 704-711
    • Moolman-Smook, J.1    Flashman, E.2    De Lange, W.3    Li, Z.4    Corfield, V.5    Redwood, C.6    Watkins, H.7
  • 24
    • 0021911378 scopus 로고
    • Structure of C protein purified from cardiac muscle
    • DOI 10.1083/jcb.100.1.208
    • H.C. Hartzell, and W.S. Sale Structure of C protein purified from cardiac muscle J. Cell Biol. 100 1985 208 215 (Pubitemid 15151895)
    • (1985) Journal of Cell Biology , vol.100 , Issue.1 , pp. 208-215
    • Hartzell, H.C.1    Sale, W.S.2
  • 25
    • 0022702757 scopus 로고
    • Electron microscopy of C-protein molecules from chicken skeletal muscle
    • R.C. Swan, and D.A. Fischman Electron microscopy of C-protein molecules from chicken skeletal muscle J. Muscle Res. Cell Motil. 7 1986 160 166
    • (1986) J. Muscle Res. Cell Motil. , vol.7 , pp. 160-166
    • Swan, R.C.1    Fischman, D.A.2
  • 26
    • 40849123741 scopus 로고    scopus 로고
    • Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C
    • C.M. Jeffries, and A.E. Whitten J. Trewhella Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C J. Mol. Biol. 377 2008 1186 1199
    • (2008) J. Mol. Biol. , vol.377 , pp. 1186-1199
    • Jeffries, C.M.1    Whitten, A.E.2    Trewhella, J.3
  • 27
    • 55149084783 scopus 로고    scopus 로고
    • Myosin binding protein C positioned to play a key role in regulation of muscle contraction: Structure and interactions of domain C1
    • A. Ababou, and E. Rostkova M. Pfuhl Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1 J. Mol. Biol. 384 2008 615 630
    • (2008) J. Mol. Biol. , vol.384 , pp. 615-630
    • Ababou, A.1    Rostkova, E.2    Pfuhl, M.3
  • 28
    • 33846099868 scopus 로고    scopus 로고
    • DisProt: The Database of Disordered Proteins
    • M. Sickmeier, and J.A. Hamilton A.K. Dunker DisProt: the Database of Disordered Proteins Nucleic Acids Res. 35 Database issue 2007 D786 D793
    • (2007) Nucleic Acids Res. , vol.35 , Issue.DATABASE ISSUE
    • Sickmeier, M.1    Hamilton, J.A.2    Dunker, A.K.3
  • 29
    • 76849087968 scopus 로고    scopus 로고
    • PONDR-FIT: A meta-predictor of intrinsically disordered amino acids
    • B. Xue, and R.L. Dunbrack V.N. Uversky PONDR-FIT: a meta-predictor of intrinsically disordered amino acids Biochim. Biophys. Acta 1804 2010 996 1010
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 996-1010
    • Xue, B.1    Dunbrack, R.L.2    Uversky, V.N.3
  • 32
    • 33745289067 scopus 로고    scopus 로고
    • Length-dependent prediction of protein intrinsic disorder
    • K. Peng, and P. Radivojac Z. Obradovic Length-dependent prediction of protein intrinsic disorder BMC Bioinformatics 7 2006 208
    • (2006) BMC Bioinformatics , vol.7 , pp. 208
    • Peng, K.1    Radivojac, P.2    Obradovic, Z.3
  • 34
    • 0034472274 scopus 로고    scopus 로고
    • Mechanical properties of titin isoforms
    • discussion 300-284
    • H. Granzier, and M. Helmes K. Trombitas Mechanical properties of titin isoforms Adv. Exp. Med. Biol. 481 2000 283 300 discussion 300-284
    • (2000) Adv. Exp. Med. Biol. , vol.481 , pp. 283-300
    • Granzier, H.1    Helmes, M.2    Trombitas, K.3
  • 36
    • 0033605334 scopus 로고    scopus 로고
    • Mutations in β-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C
    • DOI 10.1006/jmbi.1998.2522
    • M. Gruen, and M. Gautel Mutations in β-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C J. Mol. Biol. 286 1999 933 949 (Pubitemid 29106227)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.3 , pp. 933-949
    • Gruen, M.1    Gautel, M.2
  • 37
    • 69449083856 scopus 로고    scopus 로고
    • The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk
    • M. Bertz, M. Wilmanns, and M. Rief The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk Proc. Natl. Acad. Sci. USA 106 2009 13307 13310
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13307-13310
    • Bertz, M.1    Wilmanns, M.2    Rief, M.3
  • 44
    • 77955336327 scopus 로고    scopus 로고
    • A MAP for bundling microtubules
    • C.E. Walczak, and S.L. Shaw A MAP for bundling microtubules Cell 142 2010 364 367
    • (2010) Cell , vol.142 , pp. 364-367
    • Walczak, C.E.1    Shaw, S.L.2
  • 45
    • 77951023705 scopus 로고    scopus 로고
    • Species-specific differences in the Pro-Ala rich region of cardiac myosin binding protein-C
    • J.F. Shaffer, and S.P. Harris Species-specific differences in the Pro-Ala rich region of cardiac myosin binding protein-C J. Muscle Res. Cell Motil. 30 2009 303 306
    • (2009) J. Muscle Res. Cell Motil. , vol.30 , pp. 303-306
    • Shaffer, J.F.1    Harris, S.P.2
  • 46
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • T. Hoshi, W.N. Zagotta, and R.W. Aldrich Biophysical and molecular mechanisms of Shaker potassium channel inactivation Science 250 1990 533 538 (Pubitemid 120031778)
    • (1990) Science , vol.250 , Issue.4980 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 47
    • 0030708555 scopus 로고    scopus 로고
    • Entropic exclusion by neurofilament sidearms: A mechanism for maintaining interfilament spacing
    • DOI 10.1021/bi9721748
    • H.G. Brown, and J.H. Hoh Entropic exclusion by neurofilament sidearms: a mechanism for maintaining interfilament spacing Biochemistry 36 1997 15035 15040 (Pubitemid 27527966)
    • (1997) Biochemistry , vol.36 , Issue.49 , pp. 15035-15040
    • Brown, H.G.1    Hoh, J.H.2
  • 48
    • 0035163689 scopus 로고    scopus 로고
    • Predicting properties of intrinsically unstructured proteins
    • DOI 10.1016/S0079-6107(01)00012-8, PII S0079610701000128
    • J.N. Bright, T.B. Woolf, and J.H. Hoh Predicting properties of intrinsically unstructured proteins Prog. Biophys. Mol. Biol. 76 2001 131 173 (Pubitemid 33049925)
    • (2001) Progress in Biophysics and Molecular Biology , vol.76 , Issue.3 , pp. 131-173
    • Bright, J.N.1    Woolf, T.B.2    Hoh, J.H.3
  • 49
    • 77957092799 scopus 로고    scopus 로고
    • From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins
    • S. Müller-Späth, and A. Soranno B. Schuler From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins Proc. Natl. Acad. Sci. USA 107 2010 14609 14614
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 14609-14614
    • Müller-Späth, S.1    Soranno, A.2    Schuler, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.