Исследование соотношения в мышцах С- и Х-белков в норме и при патологии
p align="left">Bennett P., Starr R., Elliott A., Offer G. (1985) The structure of C-protein and X-protein molecules and a polymer of X-protein // J. Mol. Biol. V. 184. P. 297-309.

Blake C.C.F., Serpel L.C. (1996) Synchrotron X-ray studies suggest that the core of the transtyretin amyloid fibrils is a continuous в-sheet helix // Structure V. 4. P. 989-998.

Blake C.C.F., Serpel L.C. Sunde M., Sangren O., Lundgren E. (1996) A molecular model of the amyloid fibrils. The nature and origin of amyloid fibrils.// Ciba Found. Simp. V. 199. P. 6-21.

Callaway J.E., Bechtel P.J. (1981) C-protein from rabbit soleus (red) muscle // Biochem. J. V. 195. P. 463-469.

Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., Dobson Ch. (1999) Designing conditions for in vitro formation of protofilaments and fibrils // PNAS V. 96. P. 3590-3594.

Dobson C.M. (2001) The structural basis of protein folding and its links with human disease // Phil. Trans. Roy. Soc. Ser. B. V. 356. P. 133-145.

Draper M. H., Hodge A.J. (1949) Electron microscopy of muscle // Austr. J. Exp. Biol. Med. Sci. V. 27. P. 465-483.

Fandrich M., Fletcher M.A., Dobson S.M. (2001) Amyloid fibrils from muscle myoglobin // Nature V. 410. P. 165-166.

Flashman E., Redwood C., Moolman-Smook J., Watkins H. (2004) Cardiac myosin binding protein C: its role in physiology and disease // Circ. Res. V. 94 (10). P. 1279-1289.

Franzini-Armstrong G., Porter K.R. (1964) Sarcolemmal invaginations constituting the T-system in fish muscle tiber // J. Cell Biol. V. 22. P. 675-696.

Freiburg A., Gautel M. (1996) A molecular map of the interactions between titin and myosin binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy // Eur. J. Biochem. V. 235. P. 317-323.

Fritz J.D., Swartz D.R., Greaser M.L. (1989) Factors affecting polyacrilamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins // Analyt. Biochem. V. 180. P. 205-210.

Funatsu T., Kono E., Higuchi H., Kimura S., Ishiwata S., Yoshioka T., Maruyama K., Tsukita S. (1993) Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments // J. Cell Biol. V. 120. P. 711-724.

Fьrst D.O., Osborn M., Nave R., Weber K. (1988) The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line // J. Cell Biol. V. 106. P. 1563-1572.

Fьrst D.O., Vinkemeier U., Weber K. (1992) Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full-length human cDNA // J Cell Sci. V. 102. P. 769-778.

Glenner G., Eanes E., Bladen H., Linke R. (1974) в-plated sheet fibrils. A comparison of native amyloid with synthetic protein fibrils // J. Histochem. Cytochem. V. 22. P. 1141-1158.

Godfrey J.E., Harrington W.F. (1970) Self-association in the myosin system at high ionic strength. II. Evidence for the presence of a monomer-dimmer equilibrium // Biochemistry. V. 9 (4). P. 894-908.

Goedert M. (2001) б-Synuclein and neurodegenerative diseases // Nature Rev. Neurosci. V. 2. P. 492-501.

Goldsbury C.S., Wirtz S., Mьller S.A., Sunderji S., Wicki P., Aebi U., Frey P. (2000) studies on the in vitro assembly of Aв(1-40): implications for the search for Aв fibril formation inhibitors // J. of Struct. Biol. V. 130. P. 217-231.

Gregorio C.C., Granzier H., Sorimachi H., Labeit S. (1999) Muscle assembly: a titanic achievement? // Curr. Opin. Cell Biol. V. 11. P. 18-25.

Guijarro J.I., Sunde M., Jones J.A., Campbell I.D., Dobson C.M. (1998) Amyloid fibril formation by an SH3 domain // Proc. Natl. Acad. Sci. USA V. 95. P.4224-4228.

Hanson J., O'Brien E. J., Bennett P. M. (1971) Structure of the myosin-containing filament assembly (A-segment) separated from frog skeletal muscle // J. Mol. Biol. V. 58. P. 865-871.

Hartzell H.C. (1985) Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase //J. Moll. Biol. V. 186. P. 185-195.

Hartzell H.C., Glass D.B. (1984) Phosphorylation of purified cardiac muscle C-protein by purified cAMF-dependent and endogenous Ca2+-calmodulin-dependent protein kinases // J. Biol. Chem. V. 259. P. 15587-15596.

Hartzell H.C., Titus L. (1982) Effect of cholinergic and adrenergic agonists on phosphorylation of a 165000-dalton myofibrillar protein in intact amphibian cardiac muscle // J. Biol. Chem. V. 257. P. 2111-2120.

Hashimoto M., Rockenstein E., Crews L., Masliah E. (2003) Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases // Neuromolekular Med. V. 4. P. 21-36.

Houmeida A., Holt J., Tskhovrebova L., Trinick J. (1995) Studies of the interaction between titin and myosin // J. Cell Biol. V. 131. P. 1471-1481.

Hwang W., Zhang Sh., Kamm R.D., Karplus M. (2004) Kinetic control of dimmer structure formation in amyloid fibrillogenesis // PNAS V. 101. P. 12916-12921.

Improta S., Politou A.S., Pastore A. (1996) Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity // Structure V. 4. P. 323-337.

Itoh Y., Kimura S., Suzuki T., Ohashi K., Maruyama K. (1986) Native connectin from porcine cardiac muscle // J. Biochem. V. 100. P. 439-447.

Jeacocre S.A., England P.J. (1980) Phosphorylation of a myofibrillar protein of Mr 150000 in perfused rat heart, and the tentative identification of this as C-protein // FEBS Letters. V. 122. P. 129-132.

Juszczyk P., Kolodziejczyk A.S., Grzonka Z. (2005) Circular dichroism and aggregation studies of amyloid в (11-28) fragment and its variants // Acta Biochim. Pol. V. 52. P. 425-431.

Kelly J.W. (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways // Curr. Opin. Struct. Biol. V. 8. P. 101-106.

Kielley W.W., Harrington W.F. (1960) A model for the myosin molecule // Biochim. Biophys. Acta. V. 41 (3). P. 401-421.

Kim Y., Randolph T.W., Stevens F.J., Carpenter J.F. (2002) Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amylodogenic protein // J. Biol. Chem. V. 277. P. 27240-27246.

Klunk W.E., Pettegrew J.W., Abraham D.J. (1989) Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation // J. Histochem. Cytochem. V. 37. P. 1273-1281.

Koretz J.F., Irving T.C., Wang K. (1993) Filamentous aggregates of native titin and binding of C-protein and AMP-desaminase // Arch. Biochem. Biophys. V. 304 (2). 305-309.

Krebs M.R., Bromley E.H., Donald A.M. (2005) The binding of thioflavin-T to amyloid fibrils: localisation and implications. // J. Struct. Biol. V. 149. P. 30-37.

Kulikovskaya I., McClellan G., Flavigny J., Carrier L., Winegrad S. (2003) Effect of MyBP-C binding to actin on contractility in heart muscle // J. Gen. Physiol. V. 122 (6). 761-774.

Kunst G, Kress KR, Gruen M, Uttenweiler D, Gautel M, Fink RH. (2000) Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2 // Circ Res. V. 86 (1). P. 51-58.

Labeit S. & Kolmerer B. (1995) Titins, giant proteins in charge of muscle ultrastructure and elasticity // Science. V. 270. P. 293-296.

Laemmli H. (1970) Clevage of structural proteins during the assembly of the head of bacterophage T4 // Nature. V. 227 (5259). P. 680-685.

Lee E.K., Park Y.W., Dong Y.Sh., Mook-Jung I., Yoo Yu. J. (2006) Cytosolic amyloid-в peptide 42 escaping from degradation induces cell death // Biochem. Biophys. Res. Communs. V. 344. P. 471-477.

LeVine III H. (1993) Thioflavine T interaction with synthetic Alzheimer's disease в-amyloid peptides: detection of amyloid aggregation in solution // Prot. Sci. V. 2. P. 404-410.

LeVine III H. (1995) Thioflavine T interactions with amyloid в-sheet structures // Amyloid. V. 2. P. 1-6.

Lim M.S., Sutherland C., Walsh M.P. (1985) Phosphorylation of bovine cardiac C-protein by protein kinase C // Biochem. Biophys. Res. Communs. V. 132. P. 1187-1195.

Linke W.A., Kulke M., Li H., Fujita-Becker S., Naegoe C., Manstein D.J., Gautel M., Fernandez J.M. (2002) PEVK domain on titin: an entropic spring with actin-binding properties // J. Struct. Biol. V. 137. P. 194-205.

Liversage A.D., Holmes D., Knight P.J., Tskhovrebova L., Trinick J. (2001) Titin and the sarcomere symmetry paradox // J. Mol. Biol. V. 305. P. 401-409.

Maruyama K., Kimura S., Ohashi K., Kuwano Y. (1981) Connectin, an elastic protein of muscle. Identification of “titin” with connectin // J. Biochem. V. 89. P. 701-709.

Maruyama K., Matsubara R., Natori Y., Nonomura S., Kimura S., Ohashi K., Murakami F., Handa S., Eguchi G. (1977) Connectin, an elastic protein of muscle // J. Biochem. V. 82. P. 317-337.

McClellan G., Kulikovskaya I., Winegrad S. (2001) Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C // Biophys. J. V. 81 (2). P. 1083-1092.

McClellan G., Kulikovskaya I., Flavigny J., Carrier L., Winegrad S. (2004) Effect of cardiac myosin-binding protein C on stability of the thick filament // J. Mol. Cell Cardiol. V. 37 (4). P. 823-835.

Mohamed A.S., Dignam J.D., Schlender K.K. (1998) Cardiac myosin-binding protein C (MyBP-C): identification of protein kinase A and protein kinase C phosphorylation sites // Arch. Biochem. Biophys. V. 358 (2). P. 313-319.

Moos C. (1981) Fluorescence microscope study of the binding of added C-protein to skeletal muscle myofibrils // J. Cell Biol. V. 90 P. 25-31.

Moos C., Dubin J., Mason C., Besterman J. (1976) Binding of C-protein to F-actin // Biophys. J. V. 16. P. 47a.

Moos C., Mason C.M., Besterman J. M., Feng I-N. M., Dubin J.H. (1978) The binding of skeletal muscle C-protein to F-actin and its relation to the interaction of actin with myosin subfragment-1 // J. Mol. Biol. V. 124. P. 571-586.

Moos C., Offer G., Starr R., Bennett P. (1975) Interaction of C-protein with myosin, myosin rod and light meromyosin // J. Mol. Biol. V. 97. P. 1-9.

Muhle-Goll C., Pastore A., Nilges M. (1998) The 3D structure of a type I module from titin: a prototype of intracellular fibronectin type III domains // Structure. V. 6. P. 1291-1302.

Nave R., Furst D.O., Weber K. (1989) Visualization of the polarity of isolated titin molecules: a single globular head on a long thin rod as the M band anchoring domain? // J. Cell Biol. V. 109. P. 2177-2187.

Offer G., Moos C., Starr R., (1973) A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization // J. Mol. Biol. V. 74. P. 653-676.

O'Nuallain B., Williams A.D., Westermark P., Wetzel R. (2004) Seeding specificity in amyloid growth induced by heterologous fibrils // J. Biol. Chem. V. 279. P. 17490-17499.

Pepe F. A. (1967) The myosin filament. I. Structural organization from antibody staining observed in electron microscopy // J. Mol. Biol. V. 27. P. 203-225.

Podlubnaya Z.A., Freydina N.A., Lednev V.V. (1990) The axial repeats in paracrystals of light meromyosin and its complex with C-protein // Gen. Physiol. Biophts. V. 9. P. 301-310.

Qahwash I., Weiland K., Lu Yi., Sarver R., Kletzien R., Yan R. (2003) Identification of a mutant amyloid peptide that predominantly forms neurotoxic protofibrillar aggregates // J. Biol. Chem. V. 278. P. 23187-23195.

Rees M.K., Young M. (1967) Studies on the isolation and molecular properties of homogenous globular actin. Evidence for a single polypeptide chain structure // J. Biol. Chem. V. 242 (19). P. 4449-4458.

Safer D., Pepe F.A. (1980) Axial packing in light meromyosin paracrystals // J. Mol. Biol. V. 136. P. 343-358.

Sato N., Kawakami T., Nakayama A., Suzuki H., Kasahara H., Obitana T. (2003) A novel variant of cardiac myosin-bihding protein-C that is unable to assemble into

Shirahama T., Cohen A.S. (1967) High-resolution electron microscopic analysis of the amyloid fibril. // J. Cell. Biol. V. 33. P. 679-708.

Sipe J.D., Cohen A.S. (2000) History of the amyloid fibril. // J. Struct. Biol. V. 130. P. 88-98.

Siragelo I., Malmo C., Iannuzzi C., Mezzogiorno A., Bianco .R., Papa M., Irace G. (2004) Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F // J. Biol. Chem. V. 279. P. 13183-13189.

Soteriou A., Gamage M., Trinick J. (1993) A survey of interactions made by the giant protein titin // J. Cell Sci. V. 14. P. 119-123.

Squire J.M. (1981) The structural basis of muscular contraction // New York. London. P. 349.

Starr R. & Offer G. (1971) Polypeptide chains of intermediate molecular weight in myosin preparations // FEBS Lett. V. 15. P. 40-44.

Starr R. & Offer G. (1983) H-protein and X-protein. Two new components of the thick filaments of vertebrate skeletal muscle // J. Mol. Biol. V. 170. P. 675-698.

Starr R., Offer G. (1978) Interaction of C-protein with heavy meromyosin and subfragment-2 // Biochem. J. V. 171. P. 813-816.

Starr R., Offer G. (1982) Preparation of C-protein, H-protein, X-protein and phosphofructokinase // In: Methods in enzymology. New York. London. V. 85. Part B. P. 130-138.

Stine W.B., Dahlgren K.N., Krafft G.A., LaDu M.J. (2003) In vitro characterization for amyloid-в peptide oligomerization and fibrillogenesis // J. of Biol. Chem. V. 278. P. 11612-11622.

Stelzer J., Patel J., Moss R. (2006) Protein kinase A-medieted acceleration of the stretch activation responce in murine skinned myocardium is eliminated by ablation of cMyBP-C // Circ. Res. V. 13. P. 884-890.

Sunde M., Blake C.C.F. (1997) The structure of amyloid fibrils by electron microscopy and X-ray diffraction. // Adv. Prot. Chem. V. 50. P. 123-159.

Suzuki J., Kimura S., Maruyama K. (1994) Electron microscope filament lengths of connectin and its fragments // J. Biochem. V. 116. P. 406-410.

Suzuki K., Terry R.D. (1967) Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia. // Acta Neuropathol. (Berl.). V. 8. P. 276-284.

Tan S.Y., Perys M.B. (1994) Histopahtology // Amyloidosis. V. 25. P. 403-414.

Trinick J., Knight P., Whiting A. (1984) Purification and properties of native titin // J. Mol. Biol. V. 180. P. 331-356.

Tskhovrebova L., Trinick J. (1997) Direct visualization of extensibility in isolated titin molecules // J. Mol. Biol. V. 265. P. 100-106.

Uversky V.N., Fink A.L. (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded // Biochim. Biophys. Acta. V. 1698. P. 131-153.

Vaughan K.T., Weber F.E., Einheber S., Fichman D.A. (1993) Molecular cloning of chiken myosin-binding protein (MyBP) H (86-kDa protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs. // J. Biol. Chem. V. 268. P. 3670-3676.

Wang K., McClure J., Tu A. (1979) Titin: major myofibrillar components of striated muscle // Proc.Natl Acad. Sci.USA. V. 76 (8). P. 3698-3702.

Wang K & Wright J. (1988) Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z-line // J Cell Biol. V. 107 (6 Pt 1). P. 2199-212.

Weber F.E., Vaughan K.T., Reinach F.C., Fischman D.A. (1993) Complete sequence of human fast-type and slow-type muscle myosin-binding-protein C (MyBP-C). Differential expression, conserved domain structure and chromosome assignment // Eur J Biochem. V. 216 (2). P.661-669.

Weisberg A., Winegrad S. (1996) Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle // Proc. Natl. Acad. Sci. U S A. V. 93 (17). P. 8999-9003.

Weisberg A., Winegrad S. (1998) Relation between crossbridge structure and actomyosin ATPase activity in rat heart // Circ Res. V. 83 (1). P. 60-72

Yamamoto K. & Moos K. (1983) The C-protein of rabbit red, white, and cardiac muscles // J. Biol. Chem. V. 258 (13). P. 8395-8401.

Yamamoto K. (1984) Characterization of H-protein, a component of skeletal muscle myofibrils // J. Biol. Chem. V. 259. P. 7163-7168.

Zerovnik E. (2002) Amyloid fibril formation // Eur. J. Biochem. V. 269. P. 3362-3371.

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