Results 21 to 30 of about 6,808 (263)

Cardiac Myosin Binding Protein C [PDF]

open access: yesCirculation Research, 1999
Abstract —Myosin binding protein C (MyBP-C) is one of a group of myosin binding proteins that are present in the myofibrils of all striated muscle. The protein is found at 43-nm repeats along 7 to 9 transverse lines in a portion of the A band where crossbridges are found (C zone).
openaire   +2 more sources

Novel blood coagulation molecules: Skeletal muscle myosin and cardiac myosin

open access: yesJournal of Thrombosis and Haemostasis, 2021
Essentials Striated muscle myosins can promote prothrombin activation by FXa or FVa inactivation by APC. Cardiac myosin and skeletal muscle myosin are pro-hemostatic in murine tail cut bleeding models. Infused cardiac myosin exacerbates myocardial injury caused by myocardial ischemia reperfusion.
Deguchi, Hiroshi   +2 more
openaire   +3 more sources

Ensemble Force Changes that Result from Human Cardiac Myosin Mutations and a Small-Molecule Effector

open access: yesCell Reports, 2015
Cardiomyopathies due to mutations in human β-cardiac myosin are a significant cause of heart failure, sudden death, and arrhythmia. To understand the underlying molecular basis of changes in the contractile system’s force production due to such mutations
Tural Aksel   +4 more
doaj   +1 more source

Molecular Characteristics of Canine Cardiac Myosin [PDF]

open access: yesCirculation Research, 1965
Cardiac myosin was obtained from the hearts of normal dogs by conventional extraction and precipitation techniques, followed by ammonium sulfate fractionation in the presence of 2.0 M lithium chloride. The molecular characteristics of this protein preparation are presented. Cardiac myosin prepared by this technique shows less tendency than
R J, LUCHI, E M, KRITCHER, H L, CONN
openaire   +2 more sources

The emergence of Pax7-expressing muscle stem cells during vertebrate head muscle development [PDF]

open access: yes, 2015
Pax7 expressing muscle stem cells accompany all skeletal muscles in the body and in healthy individuals, efficiently repair muscle after injury. Currently, the in vitro manipulation and culture of these cells is still in its infancy, yet muscle stem ...
Anna eNoble   +9 more
core   +2 more sources

Myosinome: A Database of Myosins from Select Eukaryotic Genomes to Facilitate Analysis of Sequence-Structure-Function Relationships

open access: yesBioinformatics and Biology Insights, 2012
Myosins are one of the largest protein superfamilies with 24 classes. They have conserved structural features and catalytic domains yet show huge variation at different domains resulting in a variety of functions.
Divya P. Syamaladevi   +6 more
doaj   +1 more source

Direct regulation of striated muscle myosins by nitric oxide and endogenous nitrosothiols.

open access: yesPLoS ONE, 2010
BackgroundNitric oxide (NO) has long been recognized to affect muscle contraction, both through activation of guanylyl cyclase and through modification of cysteines in proteins to yield S-nitrosothiols. While NO affects the contractile apparatus directly,
Alicia M Evangelista   +7 more
doaj   +1 more source

Loss of function of myosin chaperones triggers Hsf1-mediated transcriptional response in skeletal muscle cells [PDF]

open access: yes, 2015
Quality of sequences obtained with CASAVA 1.8.1 (Illumina) workflow. PF reads passing Illumina chastity filter.
Christelle Etard   +5 more
core   +3 more sources

Discovery of (S)-3′-hydroxyblebbistatin and (S)-3′-aminoblebbistatin : polar myosin II inhibitors with superior research tool properties [PDF]

open access: yes, 2017
In search of myosin II inhibitors with superior research tool properties, a chemical optimization campaign of the blebbistatin scaffold was conducted in this paper. (S)-Blebbistatin is the best known small-molecule inhibitor of myosin II ATPase activity.
Bracke, Marc   +6 more
core   +1 more source

Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes

open access: yeseLife, 2017
Cardiac β-myosin variants cause hypertrophic (HCM) or dilated (DCM) cardiomyopathy by disrupting sarcomere contraction and relaxation. The locations of variants on isolated myosin head structures predict contractility effects but not the prominent ...
Lorenzo Alamo   +6 more
doaj   +1 more source

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