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D Sodickson

Publications and source records attributed to D Sodickson.

2 recordsLinked to original sources

[Acceleration of cardiovascular MRI using parallel imaging: basic principles, practical considerations, clinical applications and future directions].

Cardiovascular Magnetic Resonance (CVMR) imaging has proven to be of clinical value for non-invasive diagnostic imaging of cardiovascular diseases. CVMR requires rapid imaging; however, the speed of conventional MRI is fundamentally limited due to its sequential approach to image acquisition, in which data points are collected one after the other in the presence of sequentially-applied magnetic field gradients and radiofrequency pulses. Parallel MRI uses arrays of radiofrequency coils to acquire multiple data points simultaneously, and thereby to increase imaging speed and efficiency beyond the limits of purely gradient-based approaches. The resulting improvements in imaging speed can be used in various ways, including shortening long examinations, improving spatial resolution and anatomic coverage, improving temporal resolution, enhancing image quality, overcoming physiological constraints, detecting and correcting for physiologic motion, and streamlining work flow. Examples of these strategies will be provided in this review, after some of the fundamentals of parallel imaging methods now in use for cardiovascular MRI are outlined. The emphasis will rest upon basic principles and clinical state-of-the art cardiovascular MRI applications. In addition, practical aspects such as signal-to-noise ratio considerations, tailored parallel imaging protocols and potential artifacts will be discussed, and current trends and future directions will be explored.

Calibration↗

An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding.

Substitution of a cysteine in the extracellular mouth of the pore of the Shaker-delta K+ channel permits allosteric inhibition of the channel by Zn2+ or Cd2+ ions at micromolar concentrations. Cd2+ binds weakly to the open state but drives the channel into the slow (C-type) inactivated state, which has a Kd for Cd2+ of approximately 0.2 microM. There is a 45,000-fold increase in affinity when the channel changes from open to inactivated. These results indicate that C-type inactivation involves a structural change in the external mouth of the pore. This structural change is reflected in the T449C mutant as state-dependent metal affinity, which may result either from a change in proximity of the introduced cysteine residues of the four subunits or from a change of the exposure of this residue on the surface of the protein.

Allosteric Regulation↗