Bepridil opens the regulatory N-terminal lobe of cardiac troponin C (Q27622346)

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M L Love

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J A Putkey

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C Cohen

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

9 May 2000

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published in

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volume

97

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issue

10

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page(s)

5140-5

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cites work

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Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution

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Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution

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Binding of a calcium sensitizer, bepridil, to cardiac troponin C. A fluorescence stopped-flow kinetic, circular dichroism, and proton nuclear magnetic resonance study

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Covalent binding of peptides to the N-terminal hydrophobic region of cardiac troponin C has limited effects on function.

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Consensus recommendations for the management of chronic heart failure

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[33] AMoRe: An automated molecular replacement program package

21 January 2018

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12 December 2020

Stimulation of cardiac myofilament force, ATPase activity and troponin C Ca++ binding by bepridil

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12 December 2020

Inhibition of calmodulin by phenothiazines and related drugs: structure-activity relationships

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12 December 2020

Cardiac Troponin I Induced Conformational Changes in Cardiac Troponin C As Monitored by NMR Using Site-Directed Spin and Isotope Labeling

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12 December 2020

Formation of inter- and intramolecular disulfide bonds can activate cardiac troponin C

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12 December 2020

Identification of binding sites for bepridil and trifluoperazine on cardiac troponin C

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12 December 2020

Dynamics and thermodynamics of the regulatory domain of human cardiac troponin C in the apo- and calcium-saturated states

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12 December 2020

Identifiers

DOI

10.1073/PNAS.090098997

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ADS bibcode

2000PNAS...97.5140L

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1 reference

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PubMed publication ID

10792039

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