Results 311 to 320 of about 86,589 (350)
Some of the next articles are maybe not open access.
Physarum Tropomyosin-Troponin Complex
The Journal of Biochemistry, 1975The relaxing protein (TM-TN complex) was isolated from plasmodia of Physarum. SDS-gel electrophoresis revealed that the relaxing protein consists of tropomyosin subunits with a molecular weight of 35,000 troponin subunits with molecular weights of 38,000 (T) and 24,000 (I) and several other components. No component corresponding to muscle troponinC (MW-
Yuji Tonomura, Toyoki Kato
openaire +3 more sources
Calcium-induced flexibility changes in the troponin C–troponin I complex
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000The contraction of vertebrate striated muscle is modulated by Ca(2+) binding to the regulatory protein troponin C (TnC). Ca(2+) binding causes conformational changes in TnC which alter its interaction with the inhibitory protein troponin I (TnI), initiating the regulatory process.
John H. Collins +9 more
openaire +3 more sources
Journal of Molecular Biology, 1975
Abstract The structure of the actin-tropomyosin complex, which represents on active form of the thin filaments of skeletal muscle and the actin-tropomyosin-troponin T-troponin I complex, which represents an inhibited form, have been studied by three-dimensional reconstruction from electron micrographs.
Hugh E. Huxley +3 more
openaire +3 more sources
Abstract The structure of the actin-tropomyosin complex, which represents on active form of the thin filaments of skeletal muscle and the actin-tropomyosin-troponin T-troponin I complex, which represents an inhibited form, have been studied by three-dimensional reconstruction from electron micrographs.
Hugh E. Huxley +3 more
openaire +3 more sources
The components of the troponin complex and development in skeletal muscle
Experimental Cell Research, 1980Abstract 1. 1. Using the immunoperoxidase staining technique with monospecific antibodies to the polymorphic forms of the components of the troponin complex, two types of cells could be distinguished in rat leg muscles at 18 days' gestation. 2. 2.
S. Victor Perry, Gurtej K. Dhoot
openaire +3 more sources
Structure of the insect troponin complex 1 1Edited by M. F. Moody
Journal of Molecular Biology, 1999Isolated troponin-tropomyosin complex from Lethocerus indicus asynchronous flight muscle forms paracrystals on a positively charged lipid monolayer. Single particle analysis was carried out on individual complexes selected from electron micrographs of negatively stained paracrystals.
Thomas Wendt, Kevin Leonard
openaire +3 more sources
Proximity relationship in the binary complex formed between troponin I and troponin C
Journal of Molecular Biology, 1986We have determined six molecular distances among four sites in the binary complex formed between troponin C (TnC) and troponin I (TnI) by fluorescence resonance energy transfer between donor and acceptor probes that were either an intrinsic fluorophore (Trp158 of TnI) or extrinsic probes attached to the sites.
Herbert C. Cheung, Chien-Kao Wang
openaire +3 more sources
Human cardiac troponin complex. Structure and functions
Biochemistry (Moscow), 2013Troponin complex is a component of skeletal and cardiac muscle thin filaments. It consists of three subunits - troponin I, T, and C, and it plays a crucial role in muscle activity, connecting changes in intracellular Ca2+ concentration with generation of contraction.
openaire +3 more sources
Biochemistry, 2000
Troponin I (TnI) is the component of the troponin complex, TnI, TnC, TnT, that is responsible for inhibition of actomyosin ATPase activity. Using the fluorescence of pyrene-labeled tropomyosin (Tm), we probed the interaction of TnI and TnIC with Tm on the reconstituted muscle thin filament.
X Zhou, E P Morris, Sherwin S. Lehrer
openaire +3 more sources
Troponin I (TnI) is the component of the troponin complex, TnI, TnC, TnT, that is responsible for inhibition of actomyosin ATPase activity. Using the fluorescence of pyrene-labeled tropomyosin (Tm), we probed the interaction of TnI and TnIC with Tm on the reconstituted muscle thin filament.
X Zhou, E P Morris, Sherwin S. Lehrer
openaire +3 more sources
A Binary Complex of Troponin-I and Troponin-T from Akazara Scallop Striated Adductor Muscle1
The Journal of Biochemistry, 1991A binary complex consisting of Mr 19,000 and Mr 40,000 components was co-purified with troponin from a crude troponin fraction of Akazara scallop (Chlamys nipponensis akazara) striated adductor muscle. This complex is incapable of conferring Ca(2+)-sensitivity to rabbit reconstituted actomyosin Mg-ATPase activity, rather strongly inhibiting it, but ...
Takao Ojima, Kiyoyoshi Nishita
openaire +3 more sources
Extraction and Replacement of the Tropomyosin–Troponin Complex in Isolated Myofibrils
2010Tropomyosin (Tm) is an essential component in the regulation of striated muscle contraction. Questions about Tm functional role have been difficult to study because sarcomere Tm content is not as easily manipulated as Troponin (Tn). Here we describe the method we recently developed to replace Tm-Tn of skeletal and cardiac myofibrils from animals and ...
SCELLINI, BEATRICE +3 more
openaire +4 more sources