Search Results - (Author, Cooperation:M. Preuss)
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1Chad J. Donahue, Matthew F. Glasser, Todd M. Preuss, James K. Rilling, David C. Van Essen
National Academy of Sciences
Published 2018Staff ViewPublication Date: 2018-05-30Publisher: National Academy of SciencesPrint ISSN: 0027-8424Electronic ISSN: 1091-6490Topics: BiologyMedicineNatural Sciences in GeneralPublished by: -
2J. Yang ; R. J. Loos ; J. E. Powell ; S. E. Medland ; E. K. Speliotes ; D. I. Chasman ; L. M. Rose ; G. Thorleifsson ; V. Steinthorsdottir ; R. Magi ; L. Waite ; A. V. Smith ; L. M. Yerges-Armstrong ; K. L. Monda ; D. Hadley ; A. Mahajan ; G. Li ; K. Kapur ; V. Vitart ; J. E. Huffman ; S. R. Wang ; C. Palmer ; T. Esko ; K. Fischer ; J. H. Zhao ; A. Demirkan ; A. Isaacs ; M. F. Feitosa ; J. Luan ; N. L. Heard-Costa ; C. White ; A. U. Jackson ; M. Preuss ; A. Ziegler ; J. Eriksson ; Z. Kutalik ; F. Frau ; I. M. Nolte ; J. V. Van Vliet-Ostaptchouk ; J. J. Hottenga ; K. B. Jacobs ; N. Verweij ; A. Goel ; C. Medina-Gomez ; K. Estrada ; J. L. Bragg-Gresham ; S. Sanna ; C. Sidore ; J. Tyrer ; A. Teumer ; I. Prokopenko ; M. Mangino ; C. M. Lindgren ; T. L. Assimes ; A. R. Shuldiner ; J. Hui ; J. P. Beilby ; W. L. McArdle ; P. Hall ; T. Haritunians ; L. Zgaga ; I. Kolcic ; O. Polasek ; T. Zemunik ; B. A. Oostra ; M. J. Junttila ; H. Gronberg ; S. Schreiber ; A. Peters ; A. A. Hicks ; J. Stephens ; N. S. Foad ; J. Laitinen ; A. Pouta ; M. Kaakinen ; G. Willemsen ; J. M. Vink ; S. H. Wild ; G. Navis ; F. W. Asselbergs ; G. Homuth ; U. John ; C. Iribarren ; T. Harris ; L. Launer ; V. Gudnason ; J. R. O'Connell ; E. Boerwinkle ; G. Cadby ; L. J. Palmer ; A. L. James ; A. W. Musk ; E. Ingelsson ; B. M. Psaty ; J. S. Beckmann ; G. Waeber ; P. Vollenweider ; C. Hayward ; A. F. Wright ; I. Rudan ; L. C. Groop ; A. Metspalu ; K. T. Khaw ; C. M. van Duijn ; I. B. Borecki ; M. A. Province ; N. J. Wareham ; J. C. Tardif ; H. V. Huikuri ; L. A. Cupples ; L. D. Atwood ; C. S. Fox ; M. Boehnke ; F. S. Collins ; K. L. Mohlke ; J. Erdmann ; H. Schunkert ; C. Hengstenberg ; K. Stark ; M. Lorentzon ; C. Ohlsson ; D. Cusi ; J. A. Staessen ; M. M. Van der Klauw ; P. P. Pramstaller ; S. Kathiresan ; J. D. Jolley ; S. Ripatti ; M. R. Jarvelin ; E. J. de Geus ; D. I. Boomsma ; B. Penninx ; J. F. Wilson ; H. Campbell ; S. J. Chanock ; P. van der Harst ; A. Hamsten ; H. Watkins ; A. Hofman ; J. C. Witteman ; M. C. Zillikens ; A. G. Uitterlinden ; F. Rivadeneira ; L. A. Kiemeney ; S. H. Vermeulen ; G. R. Abecasis ; D. Schlessinger ; S. Schipf ; M. Stumvoll ; A. Tonjes ; T. D. Spector ; K. E. North ; G. Lettre ; M. I. McCarthy ; S. I. Berndt ; A. C. Heath ; P. A. Madden ; D. R. Nyholt ; G. W. Montgomery ; N. G. Martin ; B. McKnight ; D. P. Strachan ; W. G. Hill ; H. Snieder ; P. M. Ridker ; U. Thorsteinsdottir ; K. Stefansson ; T. M. Frayling ; J. N. Hirschhorn ; M. E. Goddard ; P. M. Visscher
Nature Publishing Group (NPG)
Published 2012Staff ViewPublication Date: 2012-09-18Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Body Height/genetics ; *Body Mass Index ; Co-Repressor Proteins ; Female ; *Genetic Variation ; Genome-Wide Association Study ; Humans ; Male ; Nerve Tissue Proteins/genetics ; *Phenotype ; Polymorphism, Single Nucleotide ; Proteins/*genetics ; Repressor Proteins/geneticsPublished by: -
3Hu, Y., Raffield, L. M., Polfus, L. M., Moscati, A., Nadkarni, G., Preuss, M. H., Zhong, X., Wei, Q., Rich, S. S., Li, Y., Wilson, J. G., Correa, A., Loos, R. J. F., Li, B., Auer, P. L., Reiner, A. P., the NHLBI Trans-Omics for Precision Medicine Consortium
American Society of Hematology (ASH)
Published 2018Staff ViewPublication Date: 2018-06-22Publisher: American Society of Hematology (ASH)Print ISSN: 0006-4971Electronic ISSN: 1528-0020Topics: BiologyMedicineKeywords: Red Cells, Iron, and ErythropoiesisPublished by: -
4Rustemeyer, T. ; Preuss, M. ; Von Blomberg, B. M. E. ; Das, P. K. ; Scheper, R. J.
Oxford, UK : Munksgaard International Publishers
Published 2003Staff ViewISSN: 1600-0625Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Allergen-induced emigration and maturation of dendritic cells (DC) are pivotal steps in sparking off allergic contact dermatitis. In vitro models, reflecting these steps, may provide tools for assessment of sensitizing capacities of putative contact allergens. Here, we evaluated the applicability of such models for a panel of methacrylate congeners, the sensitizing properties of which were established previously in clinical and experimental animal studies. First, using interleukin-4 (IL-4)/granulocyte–macrophage colony-stimulating factor (GM-CSF)-induced, blood monocyte-derived DC, hapten-induced up-regulation of maturation/activation markers, including CD80, CD83, CD86, chemokine receptors CXCR4 and CCR5, as well as the drug resistance related molecules P-glycoprotein (Pgp) and lung resistance protein (LRP), were monitored by flow cytometry. Of note, whereas CD86 and CXCR4 were most sensitive in discriminating between the contact sensitizers and irritants included in the panel, i.e. sodium dodecyl sulphate (SDS) and croton oil (CO), assessment of CD83 and LRP expression reflected the relatively lower sensitizing capacity of methyl methacrylate. Second, using ex vivo skin explant cultures, allergen-induced LC migration from epidermal to basal membranous and dermal skin structures was most reliably monitored by CD1a, as compared with Pgp, LRP, HLA-DR or CD54 staining. The extent of CD1a+ LC migration was found to closely correlate with the sensitizing capacities of the panel of test compounds. These results support the view that both in vitro models can provide valuable data on contact sensitizing properties, and add chemokine receptors and drug resistance related molecules to the list of DC membrane markers revealing allergenic signaling.Type of Medium: Electronic ResourceURL: -
5Staff View
ISSN: 0022-4405Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: PsychologyType of Medium: Electronic ResourceURL: -
6Staff View
ISSN: 1618-2650Source: Springer Online Journal Archives 1860-2000Topics: Chemistry and PharmacologyNotes: Summary During SIMS-analysis the sample is naturally destroyed and the experiment is therefore not reproducible. A new Datasystem (Framestore) stores all the relevant data during a depth profile experiment and enables the retrospective analysis, display and dataprocessing.Type of Medium: Electronic ResourceURL: -
7Hasenfuss, G. ; Meyer, M. ; Schillinger, W. ; Preuss, M. ; Pieske, B. ; Just, H.
Springer
Published 1997Staff ViewISSN: 1435-1803Keywords: Calcium ; heart failure ; sarcoplasmic reticulum ; geneexpression ; human myocardiumSource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract There is accumulating evidence that disturbed calcium homeostasis may play a key role in the pathophysiology of human heart failure. Because disturbed calcium handling could result from altered protein expression, levels of calcium handling proteins were quantitated by Western Blot analysis in failing and nonfailing human myocardium from hearts with endstage failing dilated or ischemic cardiomyopathy. Protein levels of the sarcoplasmic reticulum calcium release channel (ryanodine receptor) and of calcium storage proteins (calsequestrin and calreticulin) were similar in failing and nonfailing human myocardium. However, proteins involved in calcium removal from the cytosol were significantly altered in the failing human heart: 1) SR-Ca2+-ATPase, relevant for removal of calcium from the cytosol into the lumen of the sarcoplasmic reticulum, was decreased; 2) phospholamban, which inhibits the SR-Ca2+-ATPase in the basal unphosphorylated state, was slightly decreased; 3) the ratio of SR-Ca2+-ATPase to phospholamban was decreased; 4) the sarcolemmal Na+−Ca2+-exchanger, relevant for transsarcolemmal calcium extrusion was increased in the failing hearts. In summary, altered levels of proteins involved in calcium removal from the cytosol suggest an increase in transsarcolemmal calcium elimination relative to sarcoplasmic reticulum calcium removal. These findings support the concept that reduced function of the sarcoplasmic reticulum to accumulate calcium may reflect a major defect in excitationcontraction coupling in human heart failure.Type of Medium: Electronic ResourceURL: -
8Schillinger, W. ; Lehnart, S.E. ; Prestle, J. ; Preuss, M. ; Pieske, B. ; Maier, L.S. ; Meyer, M. ; Just, H. ; Hasenfuss, G.
Springer
Published 1998Staff ViewISSN: 1435-1803Keywords: Key words Calcium channel – ryanodine receptor – sarcoplasmic reticulum – calcium pump – Na+-Ca2+ exchangerSource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract The data presented indicate that altered systolic and diastolic function in failing human hearts may result from altered expression of calcium cycling proteins. Decreased systolic force production and inversion of the force-frequency relation seem to be related to reduced protein levels of SR Ca2+ ATPase and/or to increased protein levels of the Na+-Ca2+ exchanger resulting in an increased ratio of Na+-Ca2+ exchanger to SR Ca2+ ATPase. Impaired diastolic function may result from reduced SR Ca2+ ATPase and is most pronounced in failing hearts with lack of upregulation of the Na+-Ca2+ exchanger. Thus, failing hearts with reduced SR Ca2+ ATPase protein levels and unchanged Na+-Ca2+ exchanger protein levels exhibit severe impairment of both systolic and diastolic function.Type of Medium: Electronic ResourceURL: