Search Results - (Author, Cooperation:W. J. Nelson)
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1Latest Papers from Table of Contents or Articles in PressD. J. Dickinson ; W. J. Nelson ; W. I. Weis
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-03-12Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Actin Cytoskeleton/metabolism ; Cadherins/metabolism ; *Cell Polarity ; Cellulose/metabolism ; Dictyostelium/cytology/growth & development/*physiology/ultrastructure ; Epithelial Cells/*physiology/ultrastructure ; Epithelium/*physiology ; Intercellular Junctions/metabolism ; Morphogenesis ; Protozoan Proteins/chemistry/genetics/*metabolism ; RNA Interference ; alpha Catenin/chemistry/genetics/*metabolism ; beta Catenin/*metabolismPublished by: -
2Latest Papers from Table of Contents or Articles in PressB. W. Benham-Pyle ; B. L. Pruitt ; W. J. Nelson
American Association for the Advancement of Science (AAAS)
Published 2015Staff ViewPublication Date: 2015-05-30Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Adaptor Proteins, Signal Transducing/*biosynthesis/metabolism ; Animals ; Cadherins/*metabolism ; Cell Adhesion/genetics ; Cell Cycle/*genetics ; Cell Nucleus/metabolism ; Cell Proliferation ; Dogs ; Epithelial Cells/cytology/metabolism/physiology ; Madin Darby Canine Kidney Cells ; Phosphoproteins/*biosynthesis/metabolism ; *Stress, Mechanical ; *Transcription, Genetic ; beta Catenin/*biosynthesis/metabolismPublished by: -
3Latest Papers from Table of Contents or Articles in PressC. D. Buckley ; J. Tan ; K. L. Anderson ; D. Hanein ; N. Volkmann ; W. I. Weis ; W. J. Nelson ; A. R. Dunn
American Association for the Advancement of Science (AAAS)
Published 2014Staff ViewPublication Date: 2014-11-02Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Actin Cytoskeleton/*metabolism ; Actins/*metabolism ; Adherens Junctions/*metabolism ; Caco-2 Cells ; Cadherins/*metabolism ; Catenins/*metabolism ; Cell Adhesion ; Humans ; *Mechanotransduction, Cellular ; Protein BindingPublished by: -
4Latest Papers from Table of Contents or Articles in PressStaff View
Publication Date: 2018-05-11Publisher: American Heart Association (AHA)Print ISSN: 1942-325XElectronic ISSN: 1942-3268Topics: MedicineKeywords: Electrophysiology, Epidemiology, Genetic, Association StudiesPublished by: -
5Latest Papers from Table of Contents or Articles in PressC. E. Tinberg ; S. D. Khare ; J. Dou ; L. Doyle ; J. W. Nelson ; A. Schena ; W. Jankowski ; C. G. Kalodimos ; K. Johnsson ; B. L. Stoddard ; D. Baker
Nature Publishing Group (NPG)
Published 2013Staff ViewPublication Date: 2013-09-06Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Binding Sites ; Biotechnology ; *Computer Simulation ; Crystallography, X-Ray ; Digoxigenin/chemistry/*metabolism ; *Drug Design ; Estradiol/chemistry/metabolism ; Ligands ; Models, Molecular ; Progesterone/chemistry/metabolism ; Protein Binding ; Proteins/*chemistry/*metabolism ; Reproducibility of Results ; Substrate SpecificityPublished by: -
6Articles: DFG German National LicensesJohnson, D. C. ; Benfield, R. E. ; Edwards, P. P. ; Nelson, W. J. H. ; Vargas, M. D.
[s.l.] : Nature Publishing Group
Published 1985Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The magnetic susceptibilities of a series of cluster carbonyl compounds of osmium have been measured by a high-sensitivity Faraday method and the evolution of certain aspects of ‘metallic’ behaviour in the high-nuclearity clusters is revealed by a steady increase in the excess molecular ...Type of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesStaff View
ISSN: 1573-4978Source: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Abstract Neurofilaments were isolated from porcine spinal cord and separated into their subunit proteins (68 Kd NFP, 145 Kd NFP, 200 Kd NFP) by ion exchange chromatography on DEAE-cellulose in 6 M urea. The individual proteins were reacted with total rRNA from Ehrlich ascites tumor cells and the reaction products analysed by sucrose gradient centrifugation at low ionic strength and in the presence of EDTA. All three proteins interacted with rRNA with a preference for 18S rRNA. Competition experiments with native and heat-denatured calf thymus DNA showed that the affinities of the 68 Kd and 145 Kd NFPs were considerably higher for denatured DNA than for rRNA and that native DNA was only a weak competitor. The binding of the 200 Kd NFP to rRNA was unaffected by native and by denatured DNA. When denatured DNA was reacted with a mixture of the 68 Kd and 145 Kd NFPs, the two proteins interacted independently with the nucleic acid, giving rise to two different populations of deoxyribonucleoprotein particles. This segregation is the result of the cooperative interaction of the neurofilament proteins with single-stranded DNA. It could not be observed with rRNA or bacteriophage MS2 RNA. The results clearly show that the 68 Kd and 145 Kd NFPs are single-stranded RNA- and DNA-binding proteins, whereas the 200 Kd NFP seems to be only a single-stranded RNA-binding protein.Type of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesStaff View
ISSN: 1573-4978Source: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Abstract If in a low ionic strength extract of Triton X-100-resistant residual cell structures derived from Ehrlich ascites tumour (EAT) cells Mg2+ was chelated by EDTA, vimentin became associated with unfolded ribosomal subunits. The first molecular characterization of this association has shown that (1) vimentin binds to the RNA moiety of the ribosomes, (2) vimentin has a higher affinity for unfolded small ribosomal subunits or 18S rRNA than for unfolded large ribosomal subunits or 28S rRNA, (3) the limited degradation of vimentin by the vimentin-specific, Ca2+-activated proteinase, with the formation of a 48 Kd breakdown product, abolishes its affinity for rRNA, (4) the association products are rather sensitive to moderate concentrations of KCl and Mg2+, and (5) reductive alkylation of vimentin with pyridoxal-5′-phosphate and NaBH4 has no effect on the affinity of vimentin for rRNA. Actin and tubulin do not interact with EAT cell rRNA under the above ionic conditions.Type of Medium: Electronic ResourceURL: -
9Articles: DFG German National LicensesBrown, N. M. D. ; Nelson, W. J. ; Cook, B. ; Louden, J. D.
Chichester [u.a.] : Wiley-Blackwell
Published 1979Staff ViewISSN: 0377-0486Keywords: Chemistry ; Analytical Chemistry and SpectroscopySource: Wiley InterScience Backfile Collection 1832-2000Topics: Chemistry and PharmacologyPhysicsNotes: Here is reported for the first time using surface laser Raman spectroscopy the presence of graphitic carbon in thin films (50-100 Å thick) of inagnesium oxide grown directly on magnesium metal by both thermal and d.c. plasma oxidation. The two characteristic and identifying bands are located at 1330 and 1615 cm-1.Additional Material: 1 Ill.Type of Medium: Electronic ResourceURL: