Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Rudolf Hauptmann"'
Autor:
Horst Ahorn, Rudolf Hauptmann, Herbert Nar, Walter Spevak, Alexander Pautsch, Andreas Zoephel
Publikováno v:
Structure. 9:955-965
Background: The insulin-like growth-factor-1 (IGF-1) receptor, which is widely expressed in cells that have undergone oncogenic transformation, is emerging as a novel target in cancer therapy. IGF-1-induced receptor activation results in autophosphor
Autor:
Maria J. Castañón, Susanne Oehler, Günther A. Rezniczek, Rudolf Hauptmann, Gerhard Wiche, Peter Fuchs, Daniel Spazierer, Michael Zörer
Publikováno v:
Human Molecular Genetics. 8:2461-2472
Plectin, the most versatile cytolinker identified to date, has essential functions in maintaining the mechanical integrity of skin, skeletal muscle and heart, as indicated by analyses of plectin-deficient mice and humans. Expression of plectin in a v
Autor:
Peter W. de Leeuw, Cecile Maassen, Chris P. M. Reutelingsperger, Reinoud G.J. van Gool, Waander L. van Heerde, Rudolf Hauptmann, Anton Tiebosch
Publikováno v:
FEBS Letters. 349:120-124
The expression of Annexins V and VIII by human lung, liver, kidney, skin, heart, uterus, spleen and skeletal muscle was investigated by ELISA. All investigated tissues contained Annexin V. Its level varied with the tissue from around 5 microgram (ski
Autor:
Kun-Sang Chang, You-Hong Fan, Peirong Yang, Guenther Adolf, Sanford A. Stass, Rudolf Hauptmann, Asis K. Sarkar, Zhao-Mei Mu
Publikováno v:
Blood. 84:279-286
Annexin VIII is a calcium-dependent phospholipid-binding protein previously identified as a blood anticoagulant based on in vitro studies. However, the physiologic function of annexin VIII remains unknown. In acute promyelocytic leukemia (APL) the an
Autor:
Rudolf Hauptmann, George M. Willems, W. T. Hermens, H.C. Hemker, Chris P. M. Reutelingsperger, Harry A. M. Andree
Publikováno v:
Journal of Biological Chemistry. 265:4923-4928
Vascular anticoagulant alpha (VAC alpha, annexin V) is a member of the family of calcium and phospholipid binding proteins, the annexins. The binding properties of VAC alpha to phospholipid bilayers were studied by ellipsometry. Adsorption was calciu
Publikováno v:
Journal of natural products. 68(3)
Three new secondary metabolites, 2,5-dihydroxy-3-(3,4-dihydroxyphenyl)-6-phenyl-1,4-benzoquinone (3), 2,5-dihydroxy-3-phenyl-6-(3,4,5-trihydroxyphenyl)-1,4-benzoquinone (4), and 2,7,8-trihydroxy-3-phenyl-1,4-dibenzofurandione (5), as well as two know
Autor:
Peter Fuchs, Daniel Spazierer, Irmgard Fischer, Gerhard Wiche, Verena Pröll, Susanne Oehler, Lubomír Janda, Rudolf Hauptmann
Publikováno v:
The Journal of biological chemistry. 278(34)
Based on cDNA cloning and sequencing, human epiplakin has been classified as a member of the plakin protein family of cytolinkers. We report here the characterization of the mouse epiplakin gene locus and the isolation of full-length mouse epiplakin
Autor:
Maria J. Castañón, Candace E. Elliott, Gerhard Wiche, Rudolf Hauptmann, Susanne Oehler, Bruno Becker
Publikováno v:
Genomics. 42(1)
Plectin is a widely expressed protein that is very large in size and that has all the attributes of a multifunctional crosslinking and organizing element of the cytoskeleton. It displays a multidomain structure, versatile binding activities, and subc
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 93(9)
Plectin, a 500-kDa intermediate filament binding protein, has been proposed to provide mechanical strength to cells and tissues by acting as a cross-linking element of the cytoskeleton. To set the basis for future studies on gene regulation, tissue-s
Autor:
Marc C. A. Stuart, Peter M. Frederik, George M. Willems, Chris P. M. Reutelingsperger, Harry A. M. Andree, Rudolf Hauptmann, Ingrid Maurer-Fogy, Wim Th. Hermens
Publikováno v:
Biochemistry. 32(17)
A chimeric protein was produced with the N-terminal domain (amino acids 1-45) of annexin I and the core of annexin V (amino acids 19-320). This protein, annexin IN-VC, has a similar Ca2+ requirement for binding to phospholipid bilayers of 20% phospha