Interpreting cardiac muscle force-length dynamics using a novel functional model
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Acceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chainFunctional consequence of mutation in rat cardiac troponin T is affected differently by myosin heavy chain isoformsTroponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle.Model representation of the nonlinear step response in cardiac muscle.Effects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments.Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation.Kinetics of cardiac myosin isoforms in mouse myocardium are affected differently by presence of myosin binding protein-CCOOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle.The functional effect of dilated cardiomyopathy mutation (R144W) in mouse cardiac troponin T is differently affected by α- and β-myosin heavy chain isoformsDynamics of cross-bridge cycling, ATP hydrolysis, force generation, and deformation in cardiac muscleAlanine or aspartic acid substitutions at serine23/24 of cardiac troponin I decrease thin filament activation, with no effect on crossbridge detachment kineticsThe N-terminal extension of cardiac troponin T stabilizes the blocked state of cardiac thin filamentEffects of R92 mutations in mouse cardiac troponin T are influenced by changes in myosin heavy chain isoform.Cardiomyopathy-Related Mutations in Cardiac Troponin C, L29Q and G159D, Have Divergent Effects on Rat Cardiac Myofiber Contractile Dynamics.Thick-to-thin filament surface distance modulates cross-bridge kinetics in Drosophila flight muscleActivation dependence of stretch activation in mouse skinned myocardium: implications for ventricular functionRat cardiac troponin T mutation (F72L)-mediated impact on thin filament cooperativity is divergently modulated by α- and β-myosin heavy chain isoforms.A Priori Identifiability Analysis of Cardiovascular Models.Cardiac myosin isoforms exhibit differential rates of MgADP release and MgATP binding detected by myocardial viscoelasticity.Deletion of 1-43 amino acids in cardiac myosin essential light chain blunts length dependency of Ca(2+) sensitivity and cross-bridge detachment kinetics.Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent ActivationThe tropomyosin binding region of cardiac troponin T modulates crossbridge recruitment dynamics in rat cardiac muscle fibers.Interplay Between the Effects of Dilated Cardiomyopathy Mutation (R206L) and the Protein Kinase C Phosphomimic (T204E) of Rat Cardiac Troponin T Are Differently Modulated by α- and β-Myosin Heavy Chain Isoforms.Increased Titin Compliance Reduced Length-Dependent Contraction and Slowed Cross-Bridge Kinetics in Skinned Myocardial Strips from Rbm (20ΔRRM) Mice.Dilated Cardiomyopathy Mutation (R134W) in Mouse Cardiac Troponin T Induces Greater Contractile Deficits against α-Myosin Heavy Chain than against β-Myosin Heavy Chain.L71F mutation in rat cardiac troponin T augments crossbridge recruitment and detachment dynamics against α-myosin heavy chain, but not against β-myosin heavy chain.Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.Cardiomyopathy-related mutation (A30V) in mouse cardiac troponin T divergently alters the magnitude of stretch activation in α- and β-myosin heavy chain fibers.Interplay between the effects of a Protein Kinase C phosphomimic (T204E) and a dilated cardiomyopathy mutation (K211Δ or R206W) in rat cardiac troponin T blunts the magnitude of muscle length-mediated crossbridge recruitment against the β-myosin heaLength-dependent effects on cardiac contractile dynamics are different in cardiac muscle containing α- or β-myosin heavy chain.Elevated rates of force development and MgATP binding in F764L and S532P myosin mutations causing dilated cardiomyopathy.A strain-dependency of Myosin off-rate must be sensitive to frequency to predict the B-process of sinusoidal analysis.Contributions of stretch activation to length-dependent contraction in murine myocardium.The effect of cardiomyopathy mutation (R97L) in mouse cardiac troponin T on the muscle length-mediated recruitment of crossbridges is modified divergently by α- and β-myosin heavy chain.A quantitative analysis of cardiac myocyte relaxation: a simulation study.Omecamtiv Mecarbil Abolishes Length-Mediated Increase in Guinea Pig Cardiac Myofiber Ca2+ Sensitivity.Hypertrophic cardiomyopathy mutation in cardiac troponin T (R95H) attenuates length-dependent activation in guinea pig cardiac muscle fibers.I-Wire Heart-on-a-Chip II: Biomechanical analysis of contractile, three-dimensional cardiomyocyte tissue constructs.Myosin MgADP release rate decreases at longer sarcomere length to prolong myosin attachment time in skinned rat myocardium.Effects of pseudo-phosphorylated rat cardiac troponin T are differently modulated by α- and β-myosin heavy chain isoforms.
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Q28510291-24868DA7-95A2-411D-AC8A-5B4C0097521DQ28580787-94DB0A56-1C44-4769-9079-CE2182849195Q28581503-783411C4-16C8-4AAE-A641-7BF912AC3431Q34028229-46903D52-69A2-4265-AC6F-765F3392ECAAQ34385850-C1CCCF2B-E3C9-42A9-9472-7EE7E884057AQ34608313-28815F57-CCC8-42B5-887F-A02B3BB78269Q34642017-657BC4BF-E456-4799-88A2-98FE8741E015Q35159441-E0385E6E-BBD8-406D-8AA8-F26805CB1F17Q35437348-582DA5B2-083C-43C8-B6B1-99D01191DB4BQ35940982-17861DDA-48C8-4A12-856C-F1D21EF0D698Q36117053-23DC818A-E49C-477A-A036-5158E508F9CBQ36207947-14BB3813-5872-4AD3-8017-65EA398EC69EQ36235612-305C07F5-6ABE-470B-925E-85CDB5038E46Q36248424-E706F42C-D29F-4A18-8852-559EA749B668Q36248954-AB2650CF-E41F-4245-9706-899BE9B17A2CQ36295575-BE5FECCA-DA89-447E-8205-C86195357CCEQ36339391-08035B6D-1C62-451D-99D0-C242DEEA92A4Q36418270-2C787D17-8903-4630-BB4B-715AB1BBE63FQ36504143-CEBBDA3C-05F8-4A83-953D-0A169AE5100BQ36528078-9503FCA1-1A65-4405-AC89-9234DE8B379FQ36579173-19119316-6597-4F7A-91B2-7E4AA9E71207Q36788034-6C022350-64ED-4065-8295-FF2F97F0E489Q37090750-7518A877-EA0A-4C7E-9FD6-F6398AD83292Q37137855-41CE047E-DDC0-4F3D-8925-F206D829D17BQ37306367-3F46F628-BB7B-43B0-BB05-63D0AB17E616Q39099962-542A942F-333C-4765-BD5F-C90152360BD4Q39223604-157BC77B-57E1-4EDC-9618-17CAC0B8E6B0Q39260207-AB55A7C8-F246-49E2-BADE-B008F7201A64Q39605306-E6F88F6F-68B3-48C9-BB8C-6EB4ED5E6ED0Q40265069-885681FB-02D6-4FAC-A9FC-288696459D89Q41287417-A57DBC2B-D4D7-494E-89D6-C8B71804D741Q41458977-FA85B59A-02ED-4D97-9170-FD70E7FE2BCEQ41839713-C923FFE0-6965-40E5-B982-E1911066D02AQ41997993-AFA824F8-4AE5-4899-9CD3-171C2FC2E05AQ43203647-9730F73B-F5F7-40FC-B239-E69B6A7E6888Q46650156-A7BBF6BC-786E-4A94-93E5-B772D0C7B20EQ47904402-B7A2587E-CD44-4500-AA4C-B35389B93CFAQ50552639-636E8F35-43BA-4D30-A15B-D42D53B22475Q53313887-304C83AC-CFAD-4968-AD37-923BB403ABD5Q55070756-9E153AFE-1B90-4C63-B0EE-3E45AF31E3A5
P2860
Interpreting cardiac muscle force-length dynamics using a novel functional model
description
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2004
@ast
im April 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/04/01)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/04/01)
@nl
наукова стаття, опублікована у квітні 2004
@uk
مقالة علمية (نشرت في أبريل 2004)
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name
Interpreting cardiac muscle force-length dynamics using a novel functional model
@ast
Interpreting cardiac muscle force-length dynamics using a novel functional model
@en
Interpreting cardiac muscle force-length dynamics using a novel functional model
@nl
type
label
Interpreting cardiac muscle force-length dynamics using a novel functional model
@ast
Interpreting cardiac muscle force-length dynamics using a novel functional model
@en
Interpreting cardiac muscle force-length dynamics using a novel functional model
@nl
prefLabel
Interpreting cardiac muscle force-length dynamics using a novel functional model
@ast
Interpreting cardiac muscle force-length dynamics using a novel functional model
@en
Interpreting cardiac muscle force-length dynamics using a novel functional model
@nl
P2093
P2860
P3181
P1476
Interpreting cardiac muscle force-length dynamics using a novel functional model
@en
P2093
Bryan K. Slinker
Kenneth B. Campbell
Murali Chandra
Robert D. Kirkpatrick
William C. Hunter
P2860
P304
H1535–1545
P3181
P356
10.1152/AJPHEART.01029.2003
P577
2004-04-01T00:00:00Z