ArticleBiophysical journal2008
Negative charges at protein kinase C sites of troponin I stabilize the inactive state of actin.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.
- Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation.Frontiers in physiology · 2022Pooled it
- Basic residues within the cardiac troponin T C terminus are required for full inhibition of muscle contraction and limit activation by calcium.The Journal of biological chemistry · 2019Article
- Stepwise C-Terminal Truncation of Cardiac Troponin T Alters Function at Low and Saturating CaBiophysical journal · 2018Article
- The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform.Expert review of proteomics · 2017Review
- Functional communication between PKC-targeted cardiac troponin I phosphorylation sites.Archives of biochemistry and biophysics · 2017Article
- Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.Biochemistry · 2017Article
- Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility.Archives of biochemistry and biophysics · 2016Review
- Functionally conservative substitutions at cardiac troponin I S43/45.Archives of biochemistry and biophysics · 2016Article
- Independent modulation of contractile performance by cardiac troponin I Ser43 and Ser45 in the dynamic sarcomere.Journal of molecular and cellular cardiology · 2015Article
- Disease causing mutations of troponin alter regulated actin state distributions.Journal of muscle research and cell motility · 2012Review
- The C-terminus of troponin T is essential for maintaining the inactive state of regulated actin.Biophysical journal · 2012Article
- Thin filament mutations: developing an integrative approach to a complex disorder.Circulation research · 2011Review
- Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin.Biochemical and biophysical research communications · 2011Article
- Low temperature dynamic mapping reveals unexpected order and disorder in troponin.The Journal of biological chemistry · 2010Article
- Molecular dynamics studies on troponin (TnI-TnT-TnC) complexes: insight into the regulation of muscle contraction.Journal of biomolecular structure & dynamics · 2010Article
- Kinetics of regulated actin transitions measured by probes on tropomyosin.Biophysical journal · 2010Article
- Calcium sensitivity, force frequency relationship and cardiac troponin I: critical role of PKA and PKC phosphorylation sites.Journal of molecular and cellular cardiology · 2010Article
- Why does troponin I have so many phosphorylation sites? Fact and fancy.Journal of molecular and cellular cardiology · 2010Article
- Phosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments.The Journal of biological chemistry · 2010Article
- Differential effects of phosphorylation of regions of troponin I in modifying cooperative activation of cardiac thin filaments.Journal of molecular and cellular cardiology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Alterations in the troponin complex can lead to increases or decreases in contractile activity. Most mutations of troponin that cause hypertrophic cardiomyopathy increase the activity of cardiac muscle fibers. In at least some cases these mutants stabilize the active state of regulated actin. In contrast, phosphorylation of troponin I at residues 43, 45, and 144 inhibits muscle contractility. To determine if alterations of troponin I that reduce activity do stabilize the inactive state of actin, we introduced negative charges at residues 43, 45, and 144 of troponin I to mimic a constitutively phosphorylated state. At saturating calcium, all mutants decreased ATPase rates relative to wild-type actin-tropomyosin-troponin. Reduced activation of ATPase activity was seen with a single mutation at S45E and was not further altered by mutating the other two sites. In the presence of low concentrations of NEM-S1, wild-type troponin was more active than the mutants. At high NEM-S1, the rates of wild-type and mutants approached the same limiting value. Changes in Ca(2+) affinity also support the idea that the equilibrium between states of actin-tropomyosin-troponin was shifted to the inactive state by mutations that mimic troponin I phosphorylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.