The fate of desmin and titin during the degeneration and regeneration of the soleus muscle of the rat

[1]  Y. Shimada,et al.  Assembly of connectin (titin) in relation to myosin and α-actinin in cultured cardiac myocytes , 1990, Journal of Muscle Research & Cell Motility.

[2]  B. Bullard,et al.  Digestion of proteins associated with the Z-disc by calpain , 1990, Journal of Muscle Research & Cell Motility.

[3]  H. Higuchi,et al.  Behaviour of connectin (titin) and nebulin in skinned muscle fibres released after extreme stretch as revealed by immunoelectron microscopy , 1989, Journal of Muscle Research & Cell Motility.

[4]  C. Maltin,et al.  Regeneration of mammalian skeletal muscle following the injection of the snake-venom toxin, taipoxin , 2004, Cell and Tissue Research.

[5]  R. Vater,et al.  The fate of dystrophin during the degeneration and regeneration of the soleus muscle of the rat , 2004, Acta Neuropathologica.

[6]  M. Cullen,et al.  The distribution of desmin and titin in normal and dystrophic human muscle , 2004, Acta Neuropathologica.

[7]  C. Sewry Histochemical and immunocytochemical studies in neuromuscular diseases , 1994 .

[8]  H. Schmalbruch,et al.  Desmin and vimentin in regenerating muscles , 1992, Muscle & nerve.

[9]  J. Harris,et al.  Neuromuscular transmission at newly formed neuromuscular junctions in the regenerating soleus muscle of the rat. , 1991, The Journal of physiology.

[10]  C. Stoeckert,et al.  Desmin/vimentin intermediate filaments are dispensable for many aspects of myogenesis , 1991, The Journal of cell biology.

[11]  J. Gutiérrez,et al.  Changes in myofibrillar components after skeletal muscle necrosis induced by a myotoxin isolated from the venom of the snake Bothrops asper. , 1990, Experimental and molecular pathology.

[12]  M. Cullen,et al.  Muscle necrosis caused by snake venoms and toxins. , 1990, Electron microscopy reviews.

[13]  C. Harwood,et al.  Dystrophin in skeletal muscle I. Western blot analysis using a monoclonal antibody , 1989, Journal of the Neurological Sciences.

[14]  I. Nonaka,et al.  Immunochemical study of connectin (titin) in neuromuscular diseases using a monoclonal antibody: connectin is degraded extensively in Duchenne muscular dystrophy , 1989, Journal of the Neurological Sciences.

[15]  W. Isaacs,et al.  Biosynthesis of titin in cultured skeletal muscle cells , 1989, The Journal of cell biology.

[16]  K. Weber,et al.  Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly , 1989, The Journal of cell biology.

[17]  J. Trinick,et al.  Does titin regulate the length of muscle thick filaments? , 1989, Journal of molecular biology.

[18]  K. Wang,et al.  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 , 1988, The Journal of cell biology.

[19]  T. Suzuki,et al.  Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. , 1988, Journal of biochemistry.

[20]  K. Weber,et al.  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 , 1988, The Journal of cell biology.

[21]  G. Butler-Browne,et al.  Human desmin gene: utilization as a marker of human muscle differentiation. , 1988, Cellular and molecular biology.

[22]  R. J. Podolsky,et al.  The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments , 1987, The Journal of cell biology.

[23]  B. Geiger Looking for a function , 1987, Nature.

[24]  Simon C Watkins,et al.  Microtubules and desmin filaments during onset of heart hypertrophy in rat: a double immunoelectron microscope study. , 1987, Circulation research.

[25]  B. Geiger Intermediate filaments. Looking for a function. , 1987, Nature.

[26]  E. Kempner,et al.  A physiological role for titin and nebulin in skeletal muscle , 1986, Nature.

[27]  H. Higuchi,et al.  Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy , 1985, The Journal of cell biology.

[28]  P. Traub Intermediate Filaments: A Review , 1985 .

[29]  S. Singer,et al.  Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study , 1985, The Journal of cell biology.

[30]  J. Trinick,et al.  Purification and properties of native titin. , 1984, Journal of molecular biology.

[31]  S. Singer,et al.  Distributions of vimentin and desmin in developing chick myotubes in vivo. I. Immunofluorescence study , 1984, The Journal of cell biology.

[32]  K. Wang,et al.  Titin is an extraordinarily long, flexible, and slender myofibrillar protein. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[33]  J. Harris 2 Polypeptides from Snake Venoms which act on Nerve and Muscle , 1984 .

[34]  J. Harris Polypeptides from snake venoms which act on nerve and muscle. , 1984, Progress in medicinal chemistry.

[35]  S. Singer,et al.  Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken cardiac muscle , 1983, The Journal of cell biology.

[36]  J. Harris,et al.  Phospholipase A2 activity of notexin and its role in muscle damage. , 1981, Toxicon : official journal of the International Society on Toxinology.

[37]  L. Edström,et al.  The distribution of intermediate filament protein (skeletin) in normal and diseased human skeletal muscle An immunohistochemical and electron-microscopic study , 1980, Journal of Neurological Sciences.

[38]  E. Lazarides,et al.  The synthesis and distribution of desmin and vimentin during myogenesis in vitro , 1980, Cell.

[39]  E. Lazarides Intermediate filaments as mechanical integrators of cellular space , 1980, Nature.

[40]  J. Harris,et al.  FURTHER OBSERVATIONS ON THE PATHOLOGICAL RESPONSES OF RAT SKELETAL MUSCLE TO TOXINS ISOLATED FROM THE VENOM OF THE AUSTRALIAN TIGER SNAKE, NOTECHIS SCUTATUS SCUTATUS , 1978, Clinical and experimental pharmacology & physiology.

[41]  Margaret A. Johnson,et al.  Pathological responses of rat skeletal muscle to a single subcutaneous injection of a toxin isolated from the venom of the Australian tiger snake, Notechis scutatus scutatus , 1975 .