NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers
about
Structure and dynamics of the C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin ICardiac Troponin and Tropomyosin: Structural and Cellular Perspectives to Unveil the Hypertrophic Cardiomyopathy PhenotypeCa(2+)-regulated structural changes in troponinDefining the binding site of levosimendan and its analogues in a regulatory cardiac troponin C-troponin I complexStructure and function of cardiac troponin C (TNNC1): Implications for heart failure, cardiomyopathies, and troponin modulating drugsToward protein structure in situ: comparison of two bifunctional rhodamine adducts of troponin C.Bifunctional rhodamine probes of Myosin regulatory light chain orientation in relaxed skeletal muscle fibers.Structural changes in troponin in response to Ca2+ and myosin binding to thin filaments during activation of skeletal muscle.Orientation of the N-terminal lobe of the myosin regulatory light chain in skeletal muscle fibers.Interaction of cardiac troponin with cardiotonic drugs: a structural perspective.Orientation of the essential light chain region of myosin in relaxed, active, and rigor muscleOrientation and rotational motions of single molecules by polarized total internal reflection fluorescence microscopy (polTIRFM).Regulating the contraction of insect flight muscle.The structural and functional effects of the familial hypertrophic cardiomyopathy-linked cardiac troponin C mutation, L29QHD exchange and PLIMSTEX determine the affinities and order of binding of Ca2+ with troponin C.Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex.Is there nascent structure in the intrinsically disordered region of troponin I?Mutations of hydrophobic residues in the N-terminal domain of troponin C affect calcium binding and exchange with the troponin C-troponin I96-148 complex and muscle force production.
P2860
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P2860
NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@ast
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@en
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@nl
type
label
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@ast
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@en
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@nl
prefLabel
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@ast
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@en
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@nl
P2093
P3181
P356
P1433
P1476
NMR structure of a bifunctiona ...... cence studies in muscle fibers
@en
P2093
Brian D Sykes
David R Trentham
John E T Corrie
Malcolm Irving
Pascal Mercier
Roisean E Ferguson
P304
P3181
P356
10.1021/BI027041N
P407
P577
2003-04-22T00:00:00Z