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5955 citation(s) found for "Yu, Joseph S".

Is Diabetes Mellitus an Independent Risk Factor for Venous Thromboembolism?
Heit, John A. , Leibson, Cynthia L., Ashrani, Aneel A. , Petterson, Tanya M. , Bailey, Kent R. , Melton, L. Joseph

Arteriosclerosis, Thrombosis, and Vascular Biology | June 19, 2009 | Volume: 29 | Issue: 9 | Pages: 1399-1405

10.1161/atvbaha.109.189290 | PMID 19542020 Get It

Objective— Although diabetes mellitus is reported as a risk factor for venous thromboembolism (VTE), persons with diabetes are frequently hospitalized for medical illness or surgery, or confined to a nursing home, all major VTE risk factors. Consequently, we tested diabetes for an independent association with incident VTE. Methods and Results— Using Rochester Epidemiology Project resources, we identified all Olmsted County, Minn residents who met objective criteria for incident VTE over the 25-year period, 1976 to 2000 (n=1922), and 1 to 2 resident controls per case, matched on age, gender, and length of medical history (n=2115). Complete medical histories in the community were reviewed for previously identified independent VTE risk factors and diabetes-related variables. We tested diabetes and diabetes complications (retinopathy, nephropathy or neuropathy, and ketoacidosis) as potential VTE risk factors, both alone and after adjusting for VTE risk factors. Univariately, diabetes by clinical diagnosis or by stricter criteria (fasting ambulatory blood glucose ≥140 mg/dL or antidiabetic drug therapy), and diabetes complications, were associated with overall incident VTE. However, after controlling for hospitalization for major surgery or medical illness and nursing home confinement, diabetes was no longer associated with VTE. Conclusion— Diabetes mellitus and diabetes complications are not independent risk factors for incident VTE.
Detection and Quantification of Hepatitis C Virus (HCV) by MultiCode-RTx Real-Time PCR Targeting the HCV 3′ Untranslated Region
Mulligan, Elizabeth K., Germer, Jeffery J., Arens, Max Q., D'Amore, Krista L., Bisceglie, Adrian M. Di , Ledeboer, Nathan A., Moser, Michael J., Newman, Andrew, O'Guin, Andy K., Olivo, Paul D. , Podzorski, Diane, Vaughan, Kimberly A., Yao, Joseph D. , Elagin, Slava, Johnson, Scott C.

Journal of Clinical Microbiology | June 18, 2009 | Volume: 47 | Issue: 8 | Pages: 2635-2638

10.1128/jcm.02170-08 | PMID 19535519 Get It

ABSTRACT A prototype, real-time reverse-transcription PCR assay, based on MultiCode-RTx technology, quantifying hepatitis C virus (HCV) RNA by targeting the HCV 3′ untranslated region demonstrated linearity over 7 logs, with a good correlation between the quantitative results of this assay and the results of two commercially available comparator assays for 466 clinical specimens comprising all six HCV genotypes.
The Pyk2 FERM domain as a target to inhibit glioma migration
Loftus, Joseph C. , Tran, Nhan L. , Kloss, Jean , Viso, Carole, Yang, Zhongbo , Berens, Michael E. , Lipinski, Christopher A. , Tran, Nhan L

Molecular Cancer Therapeutics | June 10, 2009 | Volume: 8 | Issue: 6 | Pages: 1505-1514

10.1158/1535-7163.mct-08-1055 | PMID 19509258 Get It

Abstract The invasion of malignant glioma cells into the surrounding normal brain precludes effective clinical treatment. In this report, we investigated the role of the NH2-terminal FERM domain in the regulation of the promigratory function of Pyk2. We report that the substitution of residues that constitute a small cleft on the surface of the F3 module of the FERM domain do not significantly alter Pyk2 expression but result in the loss of Pyk2 phosphorylation. A monoclonal antibody, designated 12A10, specifically targeting the Pyk2 FERM domain was generated and recognizes an epitope located on the β5C-α1C surface of the F3 module of the FERM domain. Amino acid substitutions in the F3 module that resulted in the loss of Pyk2 phosphorylation also inhibited the binding of 12A10, suggesting that the 12A10 epitope overlaps a site that plays a role in Pyk2 activity. Conjugation of 12A10 to a membrane transport peptide led to intracellular accumulation and inhibition of glioma cell migration in a concentration-dependent manner. A single chain Fv fragment of 12A10 was stable when expressed in the intracellular environment, interacted directly with Pyk2, reduced Pyk2 phosphorylation, and inhibited glioma cell migration in vitro. Stable intracellular expression of the 12A10 scFv significantly extended survival in a glioma xenograft model. Together, these data substantiate a central role for the FERM domain in regulation of Pyk2 activity and identify the F3 module as a novel target to inhibit Pyk2 activity and inhibit glioma progression. [Mol Cancer Ther 2009;8(6):1505–14]
Perioperative Myocardial Infarction
Landesberg, Giora, Beattie, W. Scott , Mosseri, Morris , Jaffe, Allan S. , Alpert, Joseph S., Jaffe, Allan S.

Circulation | June 8, 2009 | Volume: 119 | Issue: 22 | Pages: 2936-2944

10.1161/circulationaha.108.828228 | PMID 19506125 Get It

Clinical Reasoning: A 52-year-old man with spells of altered consciousness and severe headaches
Burrus, Tamika M., Burns, Joseph D. , Rabinstein, A.A., Uhm, Joon H. , Huston, John , Lanzino, Giuseppe

Neurology | May 26, 2009 | Volume: 72 | Issue: 21 | Pages: No page available

10.1212/wnl.0b013e3181a711b4 | PMID 19470959 Get It

High-Dose Gadodiamide for Catheter Angiography and CT in Patients With Varying Degrees of Renal Insufficiency: Prevalence of Subsequent Nephrogenic Systemic Fibrosis and Decline in Renal Function
Bridges, Mellena D., Amant, Brandon S. St., McNeil, Rebecca B. , Cernigliaro, Joseph G. , Dwyer, Jamie P. , Fitzpatrick, Peter M., Dwyer, Jamie P

American Journal of Roentgenology | May 19, 2009 | Volume: 192 | Issue: 6 | Pages: 1538-1543

10.2214/ajr.07.3895 | PMID 19457816 Get It

Expression Patterns of Cardiac Myofilament Proteins
Theis, Jeanne L. , Bos, J. Martijn , Theis, Jason D. , Miller, Dylan V. , Schaff, Hartzell V. , Ommen, Steve R. , Moss, Richard L. , Ackerman, Michael J. , Dearani, Joseph A. , Gersh, Bernard J. , Bos, Johan M , Schaff, Hartzell , Theis, Jeanne L

Circulation: Heart Failure | May 14, 2009 | Volume: 2 | Issue: 4 | Pages: 325-333

10.1161/circheartfailure.108.789735 | PMID 19808356 Get It

Background— Mutations in myofilament proteins, most commonly MYBPC3 -encoded myosin-binding protein C and MYH7 -encoded β-myosin heavy chain, can cause hypertrophic cardiomyopathy (HCM). Despite significant advances in structure-function relationships pertaining to the cardiac sarcomere, there is limited knowledge of how a mutation leads to clinical HCM. We, therefore, set out to study expression and localization of myofilament proteins in left ventricular tissue of patients with HCM. Methods and Results— Frozen surgical myectomy specimens from 47 patients with HCM were examined and genotyped for mutations involving 8 myofilament-encoding genes. Myofilament protein levels were quantified by Western blotting with localization graded from immunohistochemical staining of tissue sections. Overall, 25 of 47 (53%) patients had myofilament-HCM, including 12 with MYBPC3-HCM and 9 with MYH7-HCM. As compared with healthy heart tissue, levels of myofilament proteins were increased in patients manifesting a mutation in either gene. Patients with a frameshift mutation predicted to truncate MYBPC3 exhibited marked disturbances in protein localization as compared with missense mutations in either MYBPC3 or MYH7 . Conclusions— In this first expression study in human HCM tissue, increased myofilament protein levels in patients with either MYBPC3 - or MYH7- mediated HCM suggest a poison peptide mechanism. Specifically, the mechanism of dysfunction may vary according to the genetic subgroup suggested by a distinctly abnormal distribution of myofilament proteins in patients manifesting a truncation mutation in MYBPC3 .
Anomalous Quantitation Standard Growth Curves in a Laboratory-Developed Hepatitis C Virus (HCV) RNA Quantification Assay Using the TaqMan HCV Analyte-Specific Reagent
Germer, Jeffrey J., Kathrotiya, Jemee D., Bouse, Carrie F., Mitchell, P. Shawn, Yao, Joseph D.

Journal of Clinical Microbiology | May 7, 2009 | Volume: 47 | Issue: 7 | Pages: 2317-2320

10.1128/jcm.00028-09 | PMID 19420174 Get It

ABSTRACT A retrospective examination of quantitation standard growth curves associated with 1,000 unique clinical serum specimens tested by a laboratory-developed TaqMan hepatitis C virus analyte-specific reagent-based assay revealed anomalous growth curves associated with 0.40% (95% confidence interval, 0.11% to 1.00%) of these specimens.
Utility of Topiramate for the Treatment of Patients with Chronic Migraine in the Presence or Absence of Acute Medication Overuse
Diener, HC, Dodick, DW, Goadsby, Peter J. , Bigal, ME, Bussone, G. , Silberstein, SD, Mathew, N. T., Ascher, Simon B., Morein, Jacqueline, Hulihan, JF, Biondi, DM, Greenberg, SJ, Ascher, Simon B. , Hulihan, Joseph, Goadsby, Peter J

Cephalalgia | April 23, 2009 | Volume: 29 | Issue: 10 | Pages: 1021-1027

10.1111/j.1468-2982.2009.01859.x | PMID 19735529 Get It

Chronic migraine has been linked to the excessive use of acute headache medications. Medication overuse (MO) is commonly considered the most significant risk factor for the progression of migraine from an episodic to a chronic condition. Managing MO is a challenge. Discontinuation of the acute medication can result in withdrawal headache, nausea, vomiting and sleep disturbances. This review summarizes the results from two similarly designed, randomized, placebo- controlled, multicentre studies of chronic migraine conducted in the USA and European Union. Both studies demonstrate the efficacy and safety of the migraine preventive medication, topiramate, for the treatment of chronic migraine in patient populations both with and without MO. These studies may have important implications for the future of chronic migraine management, suggesting that detoxification prior to initiating prophylactic therapy may not be required in all patients if MO is present.