Search Results - "Ghashghaee, Nazanin Bohlooli"

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  1. 1

    Role of the C-terminus mobile domain of cardiac troponin I in the regulation of thin filament activation in skinned papillary muscle strips by Bohlooli Ghashghaee, Nazanin, Li, King-Lun, Solaro, R. John, Dong, Wen-Ji

    Published in Archives of biochemistry and biophysics (15-06-2018)
    “…The C-terminus mobile domain of cTnI (cTnI-MD) is a highly conserved region which stabilizes the actin-cTnI interaction during the diastole. Upon Ca2+-binding…”
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    Journal Article
  2. 2

    Functional significance of C-terminal mobile domain of cardiac troponin I by Bohlooli Ghashghaee, Nazanin, Tanner, Bertrand C.W., Dong, Wen-Ji

    Published in Archives of biochemistry and biophysics (15-11-2017)
    “…Ca2+-regulation of cardiac contractility is mediated through the troponin complex, which comprises three subunits: cTnC, cTnI, and cTnT. As intracellular…”
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    Journal Article
  3. 3
  4. 4

    Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips by Li, King-Lun, Ghashghaee, Nazanin Bohlooli, Solaro, R. John, Dong, Wenji

    Published in Archives of biochemistry and biophysics (01-07-2016)
    “…Sarcomere length dependent activation (LDA) of myocardial force development is the cellular basis underlying the Frank-Starling law of the heart, but it is…”
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    Journal Article
  5. 5
  6. 6

    Functional Significance of the Mobile Domain of Cardiac Troponin I by Ghashghaee, Nazanin Bohlooli

    Published 2018
    “…Protein-protein interactions between the thick and thin filaments and among thin filament proteins, particularly the troponin complex, play a vital role in…”
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    Dissertation
  7. 7

    Direct interaction between troponin and myosin enhances the ATPase activity of heavy meromyosin by Ghashghaee, Nazanin Bohlooli, Li, King-Lun, Dong, Wen-Ji

    Published in Biológia (01-06-2017)
    “…Contractility of the heart muscle is a result of sliding movements between thick and thin filaments, produced by interactions between actin and myosin during…”
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    Journal Article