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PubMed:24344137 JSONTXT 32 Projects

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Id Subject Object Predicate Lexical cue
T1 0-114 Sentence denotes The hypertrophic cardiomyopathy myosin mutation R453C alters ATP binding and hydrolysis of human cardiac β-myosin.
T2 115-224 Sentence denotes The human hypertrophic cardiomyopathy mutation R453C results in one of the more severe forms of the myopathy.
T3 225-398 Sentence denotes Arg-453 is found in a conserved surface loop of the upper 50-kDa domain of the myosin motor domain and lies between the nucleotide binding pocket and the actin binding site.
T4 399-527 Sentence denotes It connects to the cardiomyopathy loop via a long α-helix, helix O, and to Switch-2 via the fifth strand of the central β-sheet.
T5 528-625 Sentence denotes The mutation is, therefore, in a position to perturb a wide range of myosin molecular activities.
T6 626-767 Sentence denotes We report here the first detailed biochemical kinetic analysis of the motor domain of the human β-cardiac myosin carrying the R453C mutation.
T7 768-817 Sentence denotes A recent report of the same mutation (Sommese, R.
T8 818-863 Sentence denotes F., Sung, J., Nag, S., Sutton, S., Deacon, J.
T9 864-890 Sentence denotes C., Choe, E., Leinwand, L.
T10 891-922 Sentence denotes A., Ruppel, K., and Spudich, J.
T11 923-938 Sentence denotes A. (2013) Proc.
T12 939-944 Sentence denotes Natl.
T13 945-950 Sentence denotes Acad.
T14 951-955 Sentence denotes Sci.
T15 956-962 Sentence denotes U.S.A.
T16 963-1077 Sentence denotes 110, 12607-12612) found reduced ATPase and in vitro motility but increased force production using an optical trap.
T17 1078-1183 Sentence denotes Surprisingly, our results show that the mutation alters few biochemical kinetic parameters significantly.
T18 1184-1395 Sentence denotes The exceptions are the rate constants for ATP binding to the motor domain (reduced by 35%) and the ATP hydrolysis step/recovery stroke (slowed 3-fold), which could be the rate-limiting step for the ATPase cycle.
T19 1396-1575 Sentence denotes Effects of the mutation on the recovery stroke are consistent with a perturbation of Switch-2 closure, which is required for the recovery stroke and the subsequent ATP hydrolysis.