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898 citation(s) found for "Cook, D A".

A cost analysis of a tele-oncology practice in the United States
Doolittle, Gary C. , Williams, Arthur R., Spaulding, Ashley, Spaulding, Ryan , Cook, David J.

Mayo Clinic

Journal of Telemedicine and Telecare | December 4, 2004 | Volume: 10 | Issue: 1_suppl | Pages: 27-29

10.1258/1357633042614429 | PMID 15603601 Get It

Oncology services have been provided by telemedicine from the University of Kansas Medical Center (KUMC) for almost 10 years. We have analysed the costs associated with providing tele-oncology clinics to a rural Kansas town for two fiscal years, 1995 and 2000. The aim was to compare recent tele-oncology costs with those of the first year of tele-oncology practice. A study conducted in 1995 showed that the average cost was $812 per telemedicine consultation. Data from fiscal year 2000 showed that the average cost was $410 per telemedicine consultation, a decrease of almost 50%. As the tele-oncology practice in Kansas continues to grow, it can be expected that the costs associated with providing tele-oncology services will continue to decline.
Management of Insulin Therapy in Urban Diabetes Patients Is Facilitated by Use of an Intelligent Dosing System
Mann, Linda J., King, Esther C., New, Katina M., Vaughn, Pamela S., Dames, Faye, Dunbar, Virginia G., Caudle, J., Tsui, Circe, McMichael, John , Cook, Curtiss B. , George, Christopher D.

Mayo Clinic

Diabetes Technology & Therapeutics | June 4, 2004 | Volume: 6 | Issue: 3 | Pages: 326-335

10.1089/152091504774198016 | PMID 15198835 Get It

Differential Trafficking of Transforming Growth Factor-β Receptors and Ligand in Polarized Epithelial Cells
Doré, Jules J.E., Edens, Maryanne, Barnard, J. A., Mitchell, Hugh , Wilkes, Mark C. , Leof, Edward B. , Murphy, Stephen J. , Coffey, Robert J.

Mayo Clinic

Molecular Biology of the Cell | April 12, 2004 | Volume: 15 | Issue: 6 | Pages: 2853-2862

10.1091/mbc.e04-02-0097 | PMID 15075369 Get It

Epithelial cells in vivo form tight cell-cell associations that spatially separate distinct apical and basolateral domains. These domains provide discrete cellular processes essential for proper tissue and organ development. Using confocal imaging and selective plasma membrane domain activation, the type I and type II transforming growth factor-β (TGFβ) receptors were found to be localized specifically at the basolateral surfaces of polarized Madin-Darby canine kidney (MDCK) cells. Receptors concentrated predominantly at the lateral sites of cell-cell contact, adjacent to the gap junctional complex. Cytoplasmic domain truncations for each receptor resulted in the loss of specific lateral domain targeting and dispersion to both the apical and basal domains. Whereas receptors concentrate basolaterally in regions of direct cell-cell contact in nonpolarized MDCK cell monolayers, receptor staining was absent from areas of noncell contact. In contrast to the defined basolateral polarity observed for the TGFβ receptor complex, TGFβ ligand secretion was found to be from the apical surfaces. Confocal imaging of MDCK cells with an antibody to TGFβ1 confirmed a predominant apical localization, with a stark absence at the basal membrane. These findings indicate that cell adhesion regulates the localization of TGFβ receptors in polarized epithelial cultures and that the response to TGFβ is dependent upon the spatial distribution and secretion of TGFβ receptors and ligand, respectively.
Improved Specificity of Newborn Screening for Congenital Adrenal Hyperplasia by Second-Tier Steroid Profiling Using Tandem Mass Spectrometry
Lacey, Jean M., Minutti, Carla , Magera, Mark J , Tauscher, Angela L., Casetta, Bruno , McCann, Mark, Lymp, James, Hahn, Si Houn , Rinaldo, Piero, Matern, Dietrich

Mayo Clinic

Clinical Chemistry | February 23, 2004 | Volume: 50 | Issue: 3 | Pages: 621-625

10.1373/clinchem.2003.027193 | PMID 14656905 Get It

Abstract Background: Newborn screening for congenital adrenal hyperplasia (CAH) involves measurement of 17α-hydroxyprogesterone (17-OHP), usually by immunoassay. Because this testing has been characterized by high false-positive rates, we developed a steroid profiling method that uses liquid chromatography–tandem mass spectrometry (LC-MS/MS) to measure 17-OHP, androstenedione, and cortisol simultaneously in blood spots. Methods: Whole blood was eluted from a 4.8-mm (3/16-inch) dried-blood spot by an aqueous solution containing the deuterium-labeled internal standard d8-17-OHP. 17-OHP, androstenedione, and cortisol were extracted into diethyl ether, which was subsequently evaporated and the residue dissolved in LC mobile phase. This extract was injected into a LC-MS/MS equipped with pneumatically assisted electrospray. The steroids were quantified in the selected-reaction monitoring mode by use of peak areas in reference to the stable-isotope-labeled internal standard. We analyzed 857 newborn blood spots, including 14 blood spots of confirmed CAH cases and 101 of false-positive cases by conventional screening. Results: Intra- and interassay CVs for 17-OHP were 7.2–20% and 3.9–18%, respectively, at concentrations of 2, 30, and 50 μg/L. At a cutoff for 17-OHP of 12.5 μg/L and a cutoff of 3.75 for the sum of peak areas for 17-OHP and androstenedione divided by the peak area for cortisol, 86 of the 101 false-positive samples were within reference values by LC-MS/MS, whereas the 742 normal and 14 true-positive results obtained by conventional screening were correctly classified. Conclusion: Steroid profiling in blood spots can identify false-positive results obtained by conventional newborn screening for CAH.
Cell-Type-Specific Activation of PAK2 by Transforming Growth Factor β Independent of Smad2 and Smad3
Wilkes, Mark C. , Garamszegi, Nandor, Leof, Edward B. , Murphy, Stephen J.

Mayo Clinic

Molecular and Cellular Biology | November 11, 2003 | Volume: 23 | Issue: 23 | Pages: 8878-8889

10.1128/mcb.23.23.8878-8889.2003 | PMID 14612425 Get It

Recurrent Familial Hypocalcemia Due to Germline Mosaicism for an Activating Mutation of the Calcium-Sensing Receptor Gene
Hendy, Geoffrey N. , Minutti, Carla , Canaff, Lucie , Pidasheva, Svetlana, Yang, Bing , Nouhi, Zaynab, Zimmerman, Donald, Wei, Cuihong, Cole, David E.C.

Mayo Clinic

The Journal of Clinical Endocrinology & Metabolism | August 14, 2003 | Volume: 88 | Issue: 8 | Pages: 3674-3681

10.1210/jc.2003-030409 | PMID 12915654 Get It

Ring chromosome 8 syndrome: Further characterization
Tonk, Vijay S. , Kukolich, Mary K. , Khan, Ashraf A. , Jalal, Syed M., Morgan, David L.

Mayo Clinic

American Journal of Medical Genetics | August 25, 2002 | Volume: 90 | Issue: 2 | Pages: 162-164

10.1002/(sici)1096-8628(20000117)90:2<162::aid-ajmg14>3.0.co;2-# | PMID 10607957 Get It

The dynamins: Redundant or distinct functions for an expanding family of related GTPases?
Henley, John R. , Cook, Tiffany , McNiven, Mark A. , Urrutia, Raúl

Mayo Clinic

Proceedings of the National Academy of Sciences | July 26, 2002 | Volume: 94 | Issue: 2 | Pages: 377-384

10.1073/pnas.94.2.377 | PMID 9012790 Get It

In the 7 years since dynamin was first isolated from bovine brain in search of novel microtubule-based motors, our understanding of this enzyme has expanded significantly. We now know that brain dynamin belongs to a family of large GTPases, which mediate vesicle trafficking. Furthermore, this enzymatic activity is markedly increased through association with microtubules, acidic phospholipids, and certain regulatory proteins that contain Src homology 3 (SH3) domains. From functional, genetic, and cellular manipulations, it is now generally accepted that dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event. These observations have confirmed at least one function of dynamin that was predicted from seminal studies on a pleiotropic mutant, shibire ts ( shi ts ) in Drosophila melanogaster. Of equal interest is the finding that there are multiple dynamin gene products, including two that are expressed in a tissue-specific manner, and they share marked homology with a larger family of distinct but related proteins. Therefore, it is attractive to speculate that the different dynamins may participate in related cellular functions, such as distinct endocytic processes and even secretion. In turn, dynamin could play an important role in cell growth, cell spreading, and neurite outgrowth. The purpose of this review is to enumerate on the expansive dynamin literature and to discuss the nomenclature, expression, and putative functions of this growing and interesting family of proteins.