R
Randall B. Lauffer
Researcher at Harvard University
Publications - 62
Citations - 10246
Randall B. Lauffer is an academic researcher from Harvard University. The author has contributed to research in topics: Human serum albumin & Nuclear magnetic resonance spectroscopy. The author has an hindex of 31, co-authored 62 publications receiving 9939 citations. Previous affiliations of Randall B. Lauffer include Pennsylvania State University & Cornell University.
Papers
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Journal ArticleDOI
Gadolinium(III) Chelates as MRI Contrast Agents: Structure, Dynamics, and Applications
TL;DR: A. Relaxivity 2331 E. Outerand Second-Sphere relaxivity 2334 F. Methods of Improving Relaxivity 2336 V. Macromolecular Conjugates 2336.
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Paramagnetic metal complexes as water proton relaxation agents for NMR imaging: theory and design
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Dynamic imaging with lanthanide chelates in normal brain: contrast due to magnetic susceptibility effects.
Arno Villringer,Bruce R. Rosen,John W. Belliveau,Jerome L. Ackerman,Randall B. Lauffer,Richard B. Buxton,Yong-Sheng Chao,Van J. Wedeen,Thomas J. Brady +8 more
TL;DR: The results show that the cause of this effect is the difference in susceptibility between the capillaries, containing the contrast agent, and the surrounding tissue, and field gradients are produced in the tissue and diffusion of water through these gradients leads to a loss of spin phase coherence and thus a decrease in signal intensity.
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MS-325: albumin-targeted contrast agent for MR angiography.
Randall B. Lauffer,D J Parmelee,S U Dunham,H S Ouellet,R P Dolan,S Witte,T J McMurry,R C Walovitch +7 more
TL;DR: As the first gadolinium-based blood pool agent in human trials, MS-325 has the potential to enhance both dynamic and steady-state MR angiograms and provides vascular signal enhancement superior to that provided with other agents.
Journal ArticleDOI
The interaction of MS-325 with human serum albumin and its effect on proton relaxation rates.
Peter Caravan,Normand J. Cloutier,Matthew T. Greenfield,Sarah A. McDermid,Stephen U. Dunham,Jeff W.M. Bulte,John C. Amedio,Richard J. Looby,Ronald M. Supkowski,William DeW. Horrocks,Thomas J. McMurry,Randall B. Lauffer +11 more
TL;DR: The results suggest that MS-325 binds primarily to site II on HSA, and the relaxivity of MS- 325 when bound to HSA is shown to be site dependent.