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Understanding cardiac troponin part 1: avoiding troponinitis [PDF]
Emergency Medicine Journal, 2017 Cardiac troponin (cTn) is a highly specific biomarker of myocardial injury and is central to the diagnosis of acute myocardial infarction (AMI). By itself, however, cTn cannot identify the cause of myocardial injury. ‘Troponinitis’ is the condition that leads clinicians to falsely assign a diagnosis of AMI based only on the fact that a patient has an ...
Richard Body, Edward Carlton
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Heart, Lung and Circulation, 2007
Serum Troponin is a sensitive and specific marker of heart muscle damage that is widely used in the assessment of people with chest pain. Its usefulness is, however, sometimes limited by false positive or negative results caused by proteins or fibrin in the patient's blood. More importantly, there is no agreed Troponin I standard at present which means
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Serum Troponin is a sensitive and specific marker of heart muscle damage that is widely used in the assessment of people with chest pain. Its usefulness is, however, sometimes limited by false positive or negative results caused by proteins or fibrin in the patient's blood. More importantly, there is no agreed Troponin I standard at present which means
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Biochemistry, 1984
We have studied the interaction between troponin and tropomyosin by means of a fluorescent probe, N-(1- anilinonaphth -4-yl)maleimide (ANM), attached to the cysteine-190 residues of tropomyosin. The binding of troponin and troponin T to ANM-tropomyosin produces substantial increases in the label fluorescence.
Edward P. Morris, Sherwin S. Lehrer
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We have studied the interaction between troponin and tropomyosin by means of a fluorescent probe, N-(1- anilinonaphth -4-yl)maleimide (ANM), attached to the cysteine-190 residues of tropomyosin. The binding of troponin and troponin T to ANM-tropomyosin produces substantial increases in the label fluorescence.
Edward P. Morris, Sherwin S. Lehrer
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The mobility of troponin C and troponin I in muscle
Journal of Molecular Recognition, 1997In vertebrate skeletal muscle, contraction is initiated by the elevation of the intracellular Ca2+ concentration. The binding of Ca2+ to TnC induces a series of conformational changes which ultimately release the inhibition of the actomyosin ATPase activity by Tnl.
Kálmán Hideg +2 more
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The Journal of Emergency Medicine, 2002
Cardiac troponins I and T are proteins integral to the function of cardiac muscle. They are very sensitive markers for the detection of myocardial damage, and the ability to assay their serum levels accurately and quickly have revolutionized the concepts of minor myocardial injury and infarction.
John, Sarko, Charles V, Pollack
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Cardiac troponins I and T are proteins integral to the function of cardiac muscle. They are very sensitive markers for the detection of myocardial damage, and the ability to assay their serum levels accurately and quickly have revolutionized the concepts of minor myocardial injury and infarction.
John, Sarko, Charles V, Pollack
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The Journal of Biochemistry, 1968
1. A method for isolation of troponin from native tropomyosin was described. 2. Troponin in combination with tropomyosin restored the whole activity of native tropomyosin in sensitizing the interaction of myosin and actin to Ca ion. 3. Troponin was found to bind nearly 4 moles of Ca per 10 5 g, of which most were exchangeable.
Fumiko Ebashi +2 more
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1. A method for isolation of troponin from native tropomyosin was described. 2. Troponin in combination with tropomyosin restored the whole activity of native tropomyosin in sensitizing the interaction of myosin and actin to Ca ion. 3. Troponin was found to bind nearly 4 moles of Ca per 10 5 g, of which most were exchangeable.
Fumiko Ebashi +2 more
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Interactions among Chymotryptic Troponin T Subfragments, Tropomyosin, Troponin I and Troponin C1
The Journal of Biochemistry, 1984The binding of various combinations of chymotryptic troponin T subfragments, troponin I and troponin C to tropomyosin, troponin C and troponin I was examined semiquantitatively by using affinity chromatography. The interaction between troponin T2 and troponin I intensified the interaction between troponin T2 (or troponin T) and tropomyosin.
Iwao Ohtsuki, Masaru Tanokura
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The binding sites of rabbit skeletal troponin-I on troponin-T
Canadian Journal of Biochemistry, 1980Various fragments derived from rabbit skeletal muscle troponin-T (Tn-T) by chemical and (or) proteolytic cleavage were mixed with whole troponin-I (Tn-I) and applied to a Sephadex G-75 gel filtration column in order to determine the binding site of Tn-I on Tn-T. This site of interaction was found to span two distinct regions of Tn-T.
Joyce R. Pearlstone, Lawrence B. Smillie
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Defining the Region of Troponin-I that Binds to Troponin-C
Biochemistry, 1999The kinetics and energetics of the binding of three troponin-I peptides, corresponding to regions 96-131 (TnI96-131), 96-139 (TnI96-139), and 96-148 (TnI96-148), to skeletal chicken troponin-C were investigated using multinuclear, multidimensional NMR spectroscopy.
Ryan T. McKay +4 more
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Recent Development of Cardiac Troponin i Detection
, 2016Cardiovascular disease (CVD) has threatened human lives for decades, and a technique for estimating and healing is still needed. There has been increasing interest in finding CVD diagnostic biomarkers to predict risk. Cardiac troponin I (cTnI) has proven
Xu Han +5 more
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