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  • Protein Structure, Tertiary  (575)
  • 03. Hydrosphere::03.04. Chemical and biological::03.04.06. Hydrothermal systems
  • 04. Solid Earth::04.04. Geology::04.04.08. Sediments: dating, processes, transport
  • 04. Solid Earth::04.04. Geology::04.04.10. Stratigraphy
  • 04. Solid Earth::04.06. Seismology::04.06.08. Volcano seismology
  • Acoustics
  • Applied geophysics
  • Data analysis / ~ processing
  • Fluids
  • Textbook of geophysics
  • American Association for the Advancement of Science (AAAS)  (580)
  • Elsevier  (63)
  • Springer  (25)
  • Cambridge Univ. Press  (11)
  • Cambridge U. Press  (6)
  • Soc. of Exploration Geophys.
  • W.H. Freeman
  • 2010-2014  (243)
  • 2000-2004  (428)
  • 1980-1984  (18)
Collection
Keywords
Publisher
Years
Year
  • 1
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    Cambridge U. Press
    In:  New York, Cambridge U. Press, (ISBN 0-521-81734-X)
    Publication Date: 2003
    Keywords: Textbook of physics ; Textbook of geophysics ; Elasticity ; Dynamic ; Waves ; Wave propagation
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  • 2
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    Cambridge U. Press
    In:  New York, Cambridge U. Press, vol. A 744, pp. 6322, (ISBN 0-521-79203-7)
    Publication Date: 2003
    Keywords: Textbook of geophysics ; Seismics (controlled source seismology) ; Three dimensional
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  • 3
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    Elsevier
    In:  Amsterdam, Elsevier, vol. 14 B, pp. 225, (ISBN 3-7643-7011-4)
    Publication Date: 1984
    Keywords: Applied geophysics ; seismic Migration ; Seismics (controlled source seismology) ; Acoustics
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  • 4
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    Cambridge Univ. Press
    In:  New York (306 pp.), Cambridge Univ. Press, vol. 4, no. 3, pp. 2-203, (ISBN 0-521-80604-6, ISBN 0-521-01472-7 paper)
    Publication Date: 2001
    Keywords: Textbook of geophysics ; hot ; spots ; Plate tectonics ; ConvolutionE ; Geol. aspects
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  • 5
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    Cambridge U. Press
    In:  New York, Cambridge U. Press, vol. 15, no. Subvol. b, pp. 220, (ISBN 0-521-52569-1)
    Publication Date: 2004
    Keywords: Textbook of geophysics ; Time series analysis ; Inversion
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  • 6
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    Elsevier
    In:  Amsterdam, 528 pp., Elsevier, vol. 32, no. XVI:, pp. 227-235, (ISBN 0231-12739-1 hb, 0231127383 pb)
    Publication Date: 2000
    Keywords: Seismics (controlled source seismology) ; Applied geophysics ; Wave propagation ; Waves ; Acoustics ; Fluids ; Textbook of geophysics
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  • 7
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    Elsevier
    In:  Amsterdam, 346 pp., Elsevier, vol. 1, no. 1, pp. 65-66, (ISBN 3-936546-23-1, 2. Auflage 2005. 876 Seiten + CD-ROM)
    Publication Date: 2000
    Keywords: Textbook of engineering ; Textbook of geophysics ; Applied geophysics ; recovery ; hydro-carbons
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  • 8
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    Soc. of Exploration Geophys.
    In:  Tulsa, Okl., Soc. of Exploration Geophys., vol. IUGG Volume 18, no. 85, pp. 175, (3-7723-6434-9)
    Publication Date: 1982
    Keywords: Data analysis / ~ processing ; Handbook of geophysics ; Seismics (controlled source seismology)
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  • 9
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    Springer
    In:  New York. 145 pp., Springer, vol. 4, no. Publ. No. 12, pp. 127, (3-540-43395-3)
    Publication Date: 2002
    Keywords: Rheology ; Textbook of geophysics ; Textbook of physics
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  • 10
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    Elsevier
    In:  Amsterdam, Elsevier, vol. Developments in Petroleum Science vol. 15A, no. Publ. No. 12, pp. 9, (ISBN: 0-12-636380-3)
    Publication Date: 1984
    Keywords: Borehole geophys. ; Textbook of geophysics ; GFZ ; RUB ; GMG ; 3.45.8 ; UniL ; IfGuG ; in ; Französisch
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  • 11
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    Cambridge Univ. Press
    In:  Cambridge, Cambridge Univ. Press, vol. 25, no. Publ. No. 12, pp. 95-104, (ISBN: 0-08-043930-6)
    Publication Date: 2000
    Keywords: Textbook of geophysics ; Textbook of physics ; Textbook of mathematics ; cylindrical ; spherical ; coordinates ; vector ; calculus ; scale ; analysis ; linear ; algebra ; Fourier ; analysis ; Fourier transform ; complex ; integration ; Laplacian ; Green ; NOModelling ; potential ; theory ; Cartesian ; tensors ; perturbation ; Taylor ; Stokes
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  • 12
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    Elsevier
    In:  Amsterdam, 253 pp., Elsevier, vol. 10, no. 1, pp. 1-40, (ISBN: 3-540-23712-7)
    Publication Date: 1983
    Keywords: Textbook of geophysics ; Acoustics ; Seismics (controlled source seismology) ; Waves ; Wave propagation
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  • 13
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    Cambridge Univ. Press
    In:  New York, 475 pp., Cambridge Univ. Press, vol. 17, pp. 225, (ISBN 1-4020-1408-2)
    Publication Date: 2000
    Keywords: Waves ; Textbook of physics ; Textbook of geophysics ; Non-linear effects ; Fluids ; Elasticity ; Electromagnetic methods/phenomena ; hydro-dynamics
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  • 14
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    Springer
    In:  New York, 1108 pp., Springer, vol. 96, pp. 225, (ISBN 0-471-95596-5)
    Publication Date: 1981
    Keywords: FROTH ; RUB ; GMG ; 3.15.80 ; Textbook of geophysics ; Seismology ; Waves ; Wavelet processing ; SModelling ; Dislocation ; Elasticity theory of dislocations ; Source
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  • 15
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    Cambridge Univ. Press
    In:  Cambridge, 287 pp., Cambridge Univ. Press, vol. 2, no. 3, pp. 2-203, (ISBN 3-0521-81830-3)
    Publication Date: 2002
    Keywords: Elasticity ; Textbook of geophysics ; Gravimetry, Gravitation ; Rheology ; Inelastic
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  • 16
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    Cambridge Univ. Press
    In:  Cambridge, XIII+248 pp., Cambridge Univ. Press, vol. 7, no. XVI:, pp. 227-235, (ISBN 0231-12739-1 hb, 0231127383 pb)
    Publication Date: 1981
    Keywords: Seismology ; Earthquake ; Textbook of geophysics
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  • 17
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    Elsevier
    In:  Amsterdam, 530 pp., Elsevier, vol. 37, no. XVI:, pp. 227-235, (ISBN 0231-12739-1 hb, 0231127383 pb)
    Publication Date: 2002
    Keywords: Seismics (controlled source seismology) ; Applied geophysics ; Wave propagation ; Waves ; Textbook of geophysics ; Acoustics ; Fluids ; High frequency ... ; Kirchoff ; seismic Migration ; Layers ; Channel waves
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  • 18
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    Springer
    In:  Berlin, 306 pp., Springer, vol. 2, no. XVI:, pp. 1-14, (ISBN: 0-387-30752-4)
    Publication Date: 2000
    Keywords: Textbook of geophysics ; Textbook of geology ; Textbook of mathematics ; Data analysis / ~ processing ; Modelling ; Inversion
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  • 19
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    Elsevier
    In:  Amsterdam, Elsevier, vol. 81A and 81B, no. 22, pp. 65-70, (1405101733, 336 p.)
    Publication Date: 1984
    Keywords: Textbook of geophysics ; Earth model, also for more shallow analyses !
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  • 20
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    Elsevier
    In:  Amsterdam, Elsevier, vol. 65, no. ALEX(01)-FR-77-01, AFTAC Contract F08606-76-C-0025, pp. 95-104, (ISBN: 0-08-044051-7)
    Publication Date: 2000
    Keywords: Seismology ; Textbook of geophysics
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  • 21
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    Elsevier
    In:  Amsterdam, 628 pp., Elsevier, vol. 31, no. 1, pp. 1-40, (ISBN 0-691-01019-6)
    Publication Date: 2002
    Keywords: Textbook of geophysics ; Inversion ; instability ; well-posed ; ill-posed ; problems ; Least-squares ; Backus ; Gilbert ; Non-linear effects ; regularization ; potential ; Electromagnetic methods/phenomena ; Seismology ; Gram ; Schmidt ; Singular value decomposition ; Lanczos ; Green's function ; Tikhonov ; potential ; methods ; Seismics (controlled source seismology) ; Gravimetry, Gravitation ; Geomagnetics ; Textbook of mathematics ; seismic Migration
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  • 22
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    Elsevier
    In:  304 pp., Elsevier, vol. 6, no. 1, pp. 1-40, (ISBN: 0-444-51340-X)
    Publication Date: 2003
    Keywords: Seismology ; Volcanology ; Seismicity ; Seismic networks ; explosions ; tremor ; Tectonics ; Textbook of geophysics
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  • 23
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    Elsevier
    In:  Bull., Polar Proj. OP-O3A4, Signal Processing II: Theories and Applications, Bath, Elsevier, vol. 186, no. XVI:, pp. 689-692, (ISBN: 3-540-23712-7)
    Publication Date: 1983
    Keywords: Seismology ; Seismic arrays ; Spectrum ; Broad-band ; Data analysis / ~ processing ; f-k-Analysis ; Schuessler ; Schussler
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  • 24
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    Elsevier
    In:  Bull., Polar Proj. OP-O3A4, Signal Processing II: Theories and Applications, Leiden, Elsevier, vol. 11, no. XVI:, pp. 673-680, (ISBN: 3-540-23712-7)
    Publication Date: 1983
    Keywords: Seismology ; Seismics (controlled source seismology) ; Filter- ; Data analysis / ~ processing ; Schuessler ; Schussler
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  • 25
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    Springer
    In:  Bull., Open-File Rept., Zahlenwerte und Funktionen aus Naturwiss. und Technik, L.B. V-1b, Berlin, Springer, vol. 81A, no. 16, pp. 141-238, (ISBN 0080419208)
    Publication Date: 1982
    Keywords: Textbook of geophysics ; Fracture ; Rock mechanics ; Rheology
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  • 26
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    W.H. Freeman
    In:  San Francisco, W.H. Freeman, vol. 1, pp. 559-932, (ISBN 0-521-81734-X)
    Publication Date: 1980
    Keywords: Textbook of geophysics ; Seismology ; Band2 ; Spectrum ; Inversion ; Data analysis / ~ processing ; Inhomogeneity ; Dynamic ; cracks and fractures (.NE. fracturing) ; Fracture
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  • 27
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    Springer
    In:  New York, 348 pp., Springer, vol. 8, no. 3, pp. 2-203, (ISBN: 3-540-41598-X)
    Publication Date: 2002
    Keywords: Textbook of geophysics ; Textbook of physics ; Finite Element Method ; Finite difference method ; perfectly ; matched ; Layers ; PML ; Gauss-Labatto ; element ; shape
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  • 28
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    Cambridge U. Press
    In:  New York (573 pp.), Cambridge U. Press, vol. 10, no. 2, pp. 125-169, (ISBN 0-521-00098-X)
    Publication Date: 2001
    Keywords: Geomagnetics ; Physical properties of rocks ; Textbook of geophysics ; Oezdemir ; Ozdemir
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  • 29
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    Elsevier
    In:  Amsterdam, 304 pp., Elsevier, vol. 49, no. 2, pp. 497-504, (ISBN 0-8137-2359-0)
    Publication Date: 2000
    Keywords: Fluids ; Textbook of geophysics ; Textbook of engineering
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  • 30
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    Springer
    In:  New York, 473 pp., Springer, vol. 10, no. Subvol. b, pp. 220, (ISBN 3-540-43160-8)
    Publication Date: 2003
    Keywords: Geodesy ; Textbook of geodesy ; methods ; Data analysis / ~ processing ; Instruments ; Global Positioning System ; Very Long Baseline Interferometry ; InSAR ; geoid ; Gravimetry, Gravitation ; Earth rotation ; Strain ; visions ; for ; the ; future ; state ; of ; the ; science
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  • 31
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    Elsevier
    In:  New York, Elsevier, vol. 15, no. Subvol. b, pp. 220, (ISBN 0-12-305355-2)
    Publication Date: 2004
    Keywords: Rock mechanics ; Fluids ; Stress ; Strength
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  • 32
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    Springer
    In:  New York, Springer, vol. III/12, Supplement to III/4, no. XVI:, pp. 1-14, (ISBN 0-87590-299-5 (soft cover))
    Publication Date: 2002
    Keywords: SOC ; FractureT ; Textbook of geophysics ; Seismicity ; Gutenberg-Richter magnitude frequency b-value ; forest ; fires ; land ; slides
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  • 33
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    Elsevier
    In:  Amsterdam, 300 pp., Elsevier, vol. 34, no. 22, pp. 65-70, (ISBN 3-7643-0253-4)
    Publication Date: 2001
    Keywords: Fluids ; Textbook of geophysics ; Geochemistry
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  • 34
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    Cambridge Univ. Press
    In:  New York, 398 pp., Cambridge Univ. Press, vol. 34, no. 22, pp. 65-70, (ISBN 3-7643-0253-4)
    Publication Date: 2000
    Keywords: Data analysis / ~ processing ; Modelling ; Statistical investigations ; Textbook of physics
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  • 35
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    Soc. of Exploration Geophys.
    In:  Tulsa, Okl., Soc. of Exploration Geophys., vol. 50, no. 22, pp. 65-83, (ISBN 0-87590-422-X)
    Publication Date: 1982
    Keywords: Seismics (controlled source seismology) ; Data analysis / ~ processing
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  • 36
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    Elsevier
    In:  Amsterdam, 360 pp., Elsevier, vol. 26, no. 22, pp. 662-664, (ISBN 0-470-87000-1 (HB), ISBN 0-470-87001-X (PB))
    Publication Date: 2002
    Description: The vertical seismic profile, acquired with an array of 3C receivers and either a single source or several arranged in a multi-component configuration, provides an ideal high fidelity calibration tool for seismic projects involved in the application of seismic anisotropy. This book catalogues the majority of specialized tools necessary to work with P-P, P-S and S-S data from such Vertical seismic profiling surveys at the acquisition design, processing and interpretation stages. In particular, it discusses 3C, 4C, 6C and 9C Vertical seismic profiling, marine and land surveys with near and multiple offsets (walkways), azimuths (walkarounds) or a combination of both. These are considered for TIH or TIV flavours of seismic anisotropy arising from cracks, fractures, sedimentary layering, and shales. The anisotropic adaptation of familiar seismic methods for velocity analysis and inversion, reflected amplitude interpretation, are given together with more multi-component specific algorithms based upon the principles dictated by the vector convolutional model. Thus, multi-component methods are described that provide tests and compensation for source or receiver vector fidelity, tool rotation correction, layer stripping, near-surface correction, wavefield separation, and the Alford rotation with its variants. The work will be of interest to geophysicists involved in research or the application of seismic anisotropy using multi-component seismic. CONTENTS 1. Introduction. 2. Anisotropic replacement media. 3. Fundamentals of seismic anisotropy analysis. 4. Pre-requisites for near-offset Vertical seismic profiling analysis. 5. Anisotropy analysis from near-offset Vertical seismic profiling I - symmetry and uniformity. 6. Anisotropy analysis from far-offset Vertical seismic profiling II - asymmetry and non-uniformity. 7. Multiple-offset Vertical seismic profiling - kinematics. 8. Multiple-offset Vertical seismic profiling - dynamics. 9. The road ahead. Appendix - shear-wave birefringence analysis.
    Keywords: Applied geophysics ; Seismics (controlled source seismology) ; Vertical seismic profiling ; Anisotropy ; Textbook of geophysics
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  • 37
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    Cambridge Univ. Press
    In:  New York (343 pp.), Cambridge Univ. Press, vol. 1, no. Publ. No. 12, pp. 127, (ISBN 0-521-66034-3, ISBN 0-521-66948-0 paper)
    Publication Date: 2001
    Keywords: Textbook of geophysics ; Textbook of geology ; optics ; LASER ; RADAR
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  • 38
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    Elsevier
    In:  Amsterdam, 298 pp., Elsevier, vol. 70, no. Publ. No. 12, pp. 1039-1054, (ISBN 0-444-50971-2)
    Publication Date: 2001
    Keywords: Subduction zone ; Review article ; Hypocentral depth ; Fault plane solution, focal mechanism ; Seismicity ; Mineralogy ; Hilst ; triggering ; Stress ; Rheology ; Geochemistry ; Strength ; Fluids ; ConvolutionE
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  • 39
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    Springer
    In:  Berlin Heidelberg, Springer, vol. 98, no. ALEX(01)-FR-77-01, AFTAC Contract F08606-76-C-0025, pp. 95-104, (ISBN: 1-4020-1592-5)
    Publication Date: 2003
    Keywords: digital signal analysis (also DSP) ; DSP ; Seismology ; Early warning systems (earthquakes, volcanic eruptions, tsunamis etc.) ; earthquake ; warning ; Seismic networks ; Data analysis / ~ processing ; Location ; Detectors ; Time series analysis ; Seismology
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  • 40
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    Elsevier
    In:  Amsterdam, Elsevier, vol. 10, no. ALEX(01)-FR-77-01, AFTAC Contract F08606-76-C-0025, pp. 329, (ISBN: 0-08-043649-8)
    Publication Date: 2001
    Description: Following the breakthrough in the last decade in identifying the key parameters for time and depth imaging in anisotropic media and developing practical methodologies for estimating them from seismic data, this title primarily focuses on the far reaching exploration benefits of anisotropic processing. This volume provides the first comprehensive description of reflection seismic signatures and processing methods in anisotropic media. It identifies the key parameters for time and depth imaging in transversely isotropic media and describes practical methodologies for estimating them from seismic data. Also, it contains a thorough discussion of the important issues of uniqueness and stability of seismic velocity analysis in the presence of anisotropy. The book contains a complete description of anisotropic imaging methods, from the theoretical background to algorithms to implementation issues. Numerous applications to synthetic and field data illustrate the improvements achieved by the anisotropic processing and the possibility of using the estimated anisotropic parameters in lithology discrimination.
    Keywords: Textbook of geophysics ; Seismics (controlled source seismology) ; Reflection seismics ; Anisotropy
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  • 41
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    Cambridge Univ. Press
    In:  New York, Cambridge Univ. Press, vol. 10, no. 1, pp. 1-40, (ISBN 0-521-62272-7, ISBN 0-521-00600-7 paper)
    Publication Date: 2001
    Keywords: Textbook of geophysics ; Gravimetry, Gravitation ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Tectonics ; density
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  • 42
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    Elsevier
    In:  Amsterdam, 300 pp., Elsevier, vol. 4, no. 1, pp. 1-40, (ISBN 0-691-01019-6)
    Publication Date: 2002
    Keywords: Stress ; Tectonics ; Modelling ; Fluids ; Two-dimensional ; percolation ; cracks and fractures (.NE. fracturing) ; Fracture ; Three ; Gorges ; China ; Discrete / Distinct Element Method ; permeability ; Rock mechanics
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  • 43
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    Springer
    In:  Professional Paper, Methods and Applications of Signal Processing in Seismic Network Operations, Berlin Heidelberg, Springer, vol. 98, no. 16, pp. 131-148, (ISBN 0080419208)
    Publication Date: 2003
    Keywords: digital signal analysis (also DSP) ; DSP ; Seismology ; Early warning systems (earthquakes, volcanic eruptions, tsunamis etc.) ; earthquake ; warning ; Seismic networks ; Data analysis / ~ processing ; Location ; Detectors ; Time series analysis ; Seismology ; Boedvarsson ; Bodvarsson
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  • 44
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    W.H. Freeman
    In:  San Francisco, W.H. Freeman, vol. 1, pp. 1-558, (ISBN 0-521-81734-X)
    Publication Date: 1980
    Keywords: Textbook of geophysics ; Seismology ; Band1 ; Elasticity ; Source ; Fault plane solution, focal mechanism ; Waves ; Instruments ; Surface waves ; (The Earth's free) oscillations ; Reflection seismics ; Inhomogeneity ; Detectors
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  • 45
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    Elsevier
    In:  Amsterdam, Elsevier
    Publication Date: 1980
    Keywords: Seismology ; Seismics (controlled source seismology) ; Wave propagation ; Waves ; Textbook of geophysics
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  • 46
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    Springer
    In:  Berlin, Springer, vol. 45, pp. 3. erweiterte u. aktualisierte Auflage, x+419 pp., (ISBN 0-471-95596-5)
    Publication Date: 2000
    Keywords: GIS ; Textbook of geophysics ; geography ; data ; base ; fuzzy ; Data analysis / ~ processing ; interpolation ; SQL
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  • 47
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    Springer
    In:  New York, Springer, vol. 31, no. 3, pp. 2-203, (ISBN 0-87590-533-1)
    Publication Date: 2000
    Keywords: Data analysis / ~ processing ; Error analysis ; Handbook of geophysics ; Handbook of geodesy ; toolbox ; Statistical investigations ; Inversion ; Non-linear effects ; aerial ; images ; Diffraction ; Tomography ; 1214 ; Geodesy ; and ; gravity ; Geopotential ; theory ; and ; determination ; 1224 ; Photogrammetry ; remote ; sensing ; 0902 ; Exploration ; geophysics ; Computational ; methods, ; seismic ; Gruen ; Grun
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  • 48
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    Elsevier
    In:  Amsterdam, 680 pp., Elsevier, vol. 33, no. 2, pp. 125-169, (ISBN: 3-540-42642-6, Approx. 620 p. 30 illus., Hardcover)
    Publication Date: 2001
    Keywords: Borehole geophys. ; Textbook of geophysics ; Electromagnetic methods/phenomena
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  • 49
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    Cambridge Univ. Press
    In:  Cambridge, Cambridge Univ. Press, vol. 2, no. XVI:, pp. 1-14, (ISBN: 0-691-05010-4)
    Publication Date: 1980
    Keywords: Waves ; Elasticity ; Source ; Wave propagation ; Seismology ; Textbook of geophysics
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  • 50
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    Cambridge U. Press
    In:  New York (370 pp.), Cambridge U. Press, vol. 13, no. XVI:, pp. 227-235, (ISBN 0-521-80945-2, ISBN 0-521-00663-5 paper)
    Publication Date: 2001
    Keywords: Waves ; Wave propagation ; Textbook of geophysics ; observations ; (part ; 1), ; theory ; (part ; 2) ; Ray seismics ; Anisotropy ; Attenuation ; Elasticity
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  • 51
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    Elsevier
    In:  Amsterdam, 356 pp., Elsevier, vol. 2, no. XVI:, pp. 1-14, (ISBN: 0-387-30752-4)
    Publication Date: 2001
    Keywords: Textbook of engineering ; Textbook of geophysics ; Statistical investigations
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  • 52
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    Cambridge U. Press
    In:  New York (xii + 534 pp.), Cambridge U. Press, vol. 13, no. XVI:, pp. 227-235, (ISBN 0-521-00665-1)
    Publication Date: 2002
    Keywords: WAVE ; Wave propagation ; Textbook of geophysics ; observations ; (part ; 1), ; theory ; (part ; 2) ; Ray seismics ; Anisotropy ; AnisotropyS ; Earthquake ; Chi-Chi ; Kobe ; Loma ; Prieta ; North ; Ridge ; Tennant ; Creek ; Aftershocks ; Inhomogeneity ; basins ; Data analysis / ~ processing ; Modelling ; wavefiled ; decomposition ; Dispersion ; Three dimensional ; Earth model, also for more shallow analyses ! ; CRUST ; earth mantle ; earth Core ; D-double-prime ; ultra ; Low velocity layer ; NOModelling ; Surface waves ; Tomography ; Receiver functions ; Source ; Moment tensor ; Inversion ; perturbation ; methods ; Handbook of geophysics
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  • 53
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    Elsevier
    In:  Amsterdam, 656 pp., Elsevier, vol. 38, no. XVI:, pp. 227-235, (ISBN: 0-444-50983-6)
    Publication Date: 2003
    Description: The monograph introduces the reader to the world of inductive well logging - an established method for surveying the electrical conductivity of rocks surrounding a borehole. The emphasis is on developing a theory of inductive logging and on understanding logging tools basic physics, since this theory and understanding furnish valuable insights for inventing practical induction logging techniques. The first chapter of the book presents the basic laws of electromagnetism from a point of view that will facilitate the application of the theory to problems in electromagnetic logging. Many topics that play an important role in the design and interpretation of tools readings are covered. The vertical resolution and radial depth of investigation of different induction tools is systematically considered. Special attention is paid to principles of induction logging with transversal induction coils, to transient method of induction logging in media with cylindrical and horizontal interfaces and to the influence of anisotropy on the electromagnetic field measured in a conducting medium. Multi-coil differential induction probes and induction logging based on measuring the inphase component of the secondary field or the quadrature component difference are also described in detail. The last chapter is devoted to mathematical modeling of the response of induction logging tools in 3D geometries. The theory of inductive logging presented in this volume can be applied to logging after drilling as well as logging while drilling. Introduction. 1. Basic electromagnetic laws and Maxwell's equations. 2. Electromagnetic field of the magnetic dipole in a uniform conducting medium. 3. Methods for the solution of direct problems of induction logging. 4. Electromagnetic field of a vertical magnetic dipole on the axis of a borehole 5. Quasistationary magnetic field of a vertical magnetic dipole in a formation with a finite thickness. 6. The two-coil induction probe on the borehole axis, when the bed has a finite thickness. 7. Multi-coil dioeerential induction probes. 8. Induction logging based on measuring the inphase component of the secondary field or the quadrature component difference of type Q Hz(omega1) - omega1/omega2 Q Hz(omega2). 9. Transient induction logging. 10. Principles of induction logging with transversal induction coils. 11. The influence of anisotropy on the field of the magnetic dipole in a conducting medium. 12. Mathematical modeling of the response of induction logging tools in 3D geometries.
    Keywords: Borehole geophys. ; Textbook of geophysics ; Dual Induction Latero log
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  • 54
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    Cambridge Univ. Press
    In:  New York, Cambridge Univ. Press, vol. 22, no. 1, pp. 799-804, (ISBN 1-4020-1777-4 (hb) and ISBN 1-4020-1778-2 (pb))
    Publication Date: 2000
    Keywords: Textbook of geology ; Textbook of geophysics ; Applied geophysics ; Tectonics ; Plate tectonics ; textbook ; for ; future ; non-geophysicists
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  • 55
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    Cambridge Univ. Press
    In:  Cambridge, 2nd. ed. 496 pp., Cambridge Univ. Press, vol. 18, no. Publ. No. 12, pp. 267, (ISBN: 0521652235)
    Publication Date: 2002
    Keywords: Textbook of geophysics ; Seismology ; Tectonics ; Fault zone ; cracks and fractures (.NE. fracturing) ; Rock mechanics ; Laboratory measurements ; Fracture ; rate ; and ; state ; dependent ; Friction ; Stress ; scaling ; GFZ ; M ; 03.0198, ; RUB ; GMG ; 3.15.164
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  • 56
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    Springer
    In:  Berlin, Springer, vol. 4, no. 1, pp. 1-40, (ISBN 0-06-057199-3)
    Publication Date: 2003
    Keywords: Geodesy ; Textbook of geodesy ; Handbook of geodesy ; Data analysis / ~ processing ; KSGSoft ; program ; software ; Filter- ; Error analysis
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  • 57
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    Springer
    In:  Bull., Open-File Rept., Methods and Applications of Signal Processing in Seismic Network Operations, Berlin Heidelberg, Springer, vol. 98, no. 16, pp. 149-172, (ISBN 1-86239-165-3, vi + 330 pp.)
    Publication Date: 2003
    Keywords: digital signal analysis (also DSP) ; DSP ; Seismology ; Early warning systems (earthquakes, volcanic eruptions, tsunamis etc.) ; Seismic networks ; Data analysis / ~ processing ; Location ; Detectors ; Time series analysis ; Seismology
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-23
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907122/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907122/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falke, Joseph J -- R01 GM040731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1480-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biophysics Program and the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA. falke@colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859184" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry ; Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Nitrogen/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermodynamics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, John H -- Elledge, Stephen J -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1822-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228708" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BRCA1 Protein/metabolism ; BRCA2 Protein/*chemistry/*metabolism ; Binding Sites ; Breast Neoplasms/genetics ; Crystallography, X-Ray ; DNA/*metabolism ; DNA Damage ; *DNA Repair ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/metabolism ; Female ; Genes, BRCA1 ; Genes, BRCA2 ; Genetic Predisposition to Disease ; Humans ; Mice ; Ovarian Neoplasms/genetics ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rad51 Recombinase ; Rats ; Recombination, Genetic ; Replication Protein A
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 60
    Publication Date: 2002-06-22
    Description: Positive-strand RNA viruses such as poliovirus replicate their genomes on intracellular membranes of their eukaryotic hosts. Electron microscopy has revealed that purified poliovirus RNA-dependent RNA polymerase forms planar and tubular oligomeric arrays. The structural integrity of these arrays correlates with cooperative RNA binding and RNA elongation and is sensitive to mutations that disrupt intermolecular contacts predicted by the polymerase structure. Membranous vesicles isolated from poliovirus-infected cells contain structures consistent with the presence of two-dimensional polymerase arrays on their surfaces during infection. Therefore, host cytoplasmic membranes may function as physical foundations for two-dimensional polymerase arrays, conferring the advantages of surface catalysis to viral RNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyle, John M -- Bullitt, Esther -- Bienz, Kurt -- Kirkegaard, Karla -- AI-42119/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2218-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077417" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Inclusion Bodies, Viral/metabolism/ultrastructure ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Poliovirus/*enzymology/physiology ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; RNA Replicase/*chemistry/isolation & purification/*metabolism/ultrastructure ; RNA, Viral/biosynthesis/*metabolism ; Viral Core Proteins/metabolism ; Virus Replication
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 61
    Publication Date: 2002-02-09
    Description: Double-stranded RNA-mediated gene interference (RNAi) in Caenorhabditis elegans systemically inhibits gene expression throughout the organism. To investigate how gene-specific silencing information is transmitted between cells, we constructed a strain that permits visualization of systemic RNAi. We used this strain to identify systemic RNA interference-deficient (sid) loci required to spread gene-silencing information between tissues but not to initiate or maintain an RNAi response. One of these loci, sid-1, encodes a conserved protein with predicted transmembrane domains. SID-1 is expressed in cells sensitive to RNAi, is localized to the cell periphery, and is required cell-autonomously for systemic RNAi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winston, William M -- Molodowitch, Christina -- Hunter, Craig P -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2456-9. Epub 2002 Feb 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834782" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/embryology/*genetics/metabolism ; Caenorhabditis elegans Proteins/chemistry/*genetics/*physiology ; Calmodulin-Binding Proteins/genetics ; Cytoplasm/metabolism ; Embryo, Nonmammalian/physiology ; *Gene Silencing ; Genes, Helminth ; Germ Cells/metabolism ; Green Fluorescent Proteins ; Intestines/metabolism ; Luminescent Proteins/genetics ; Membrane Proteins/chemistry/*genetics/*physiology ; Molecular Sequence Data ; Mosaicism ; Muscle Proteins/genetics ; Muscles/metabolism ; Mutation ; Protein Structure, Tertiary ; RNA, Double-Stranded/*genetics/metabolism ; RNA, Helminth/*genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Transgenes
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 62
    Publication Date: 2003-07-12
    Description: Direct interaction between platelet receptor glycoprotein Ibalpha (GpIbalpha) and thrombin is required for platelet aggregation and activation at sites of vascular injury. Abnormal GpIbalpha-thrombin binding is associated with many pathological conditions,including occlusive arterial thrombosis and bleeding disorders. The crystal structure of the GpIbalpha-thrombin complex at 2.6 angstrom resolution reveals simultaneous interactions of GpIbalpha with exosite I of one thrombin molecule,and with exosite II of a second thrombin molecule. In the crystal lattice,the periodic arrangement of GpIbalpha-thrombin complexes mirrors a scaffold that could serve as a driving force for tight platelet adhesion. The details of these interactions reconcile GpIbalpha-thrombin binding modes that are presently controversial,highlighting two distinct interfaces that are potential targets for development of novel antithrombotic drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dumas, John J -- Kumar, Ravindra -- Seehra, Jasbir -- Somers, William S -- Mosyak, Lidia -- New York, N.Y. -- Science. 2003 Jul 11;301(5630):222-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical and Screening Sciences, Wyeth, 200 Cambridge Park Drive, Cambridge, MA 02140, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12855811" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Blood Platelets/chemistry/physiology ; Crystallization ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Platelet Adhesiveness ; *Platelet Aggregation ; Platelet Glycoprotein GPIb-IX Complex/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thrombin/*chemistry/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2003-02-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hederstedt, Lars -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):671-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Organism Biology, Lund University, SE-22362 Lund, Sweden. lars.hederstedt@cob.lu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560540" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Anaerobiosis ; Binding Sites ; Crystallography, X-Ray ; Electron Transport ; Electron Transport Complex II ; Escherichia coli/*enzymology ; Flavin-Adenine Dinucleotide/metabolism ; Heme/chemistry/metabolism ; Models, Molecular ; Multienzyme Complexes/antagonists & inhibitors/*chemistry/*metabolism ; Oxidation-Reduction ; Oxidoreductases/antagonists & inhibitors/*chemistry/*metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Reactive Oxygen Species/metabolism ; Succinate Dehydrogenase/antagonists & inhibitors/*chemistry/*metabolism ; Succinic Acid/metabolism ; Ubiquinone/chemistry/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2003-06-07
    Description: Rice is the world's most important food crop and a model for cereal research. At 430 megabases in size, its genome is the most compact of the cereals. We report the sequence of chromosome 10, the smallest of the 12 rice chromosomes (22.4 megabases), which contains 3471 genes. Chromosome 10 contains considerable heterochromatin with an enrichment of repetitive elements on 10S and an enrichment of expressed genes on 10L. Multiple insertions from organellar genomes were detected. Collinearity was apparent between rice chromosome 10 and sorghum and maize. Comparison between the draft and finished sequence demonstrates the importance of finished sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice Chromosome 10 Sequencing Consortium -- R01-LM06845/LM/NLM NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 6;300(5625):1566-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791992" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosomes, Plant/*genetics ; Computational Biology ; DNA Transposable Elements ; DNA, Chloroplast/genetics ; DNA, Mitochondrial/genetics ; DNA, Plant/genetics ; Edible Grain/genetics ; *Evolution, Molecular ; Expressed Sequence Tags ; Genes, Plant ; *Genome, Plant ; Heterochromatin ; Oryza/*genetics/physiology ; Plant Diseases/genetics ; Plant Proteins/chemistry/*genetics/physiology ; Protein Structure, Tertiary ; Proteome ; Repetitive Sequences, Nucleic Acid ; Retroelements ; *Sequence Analysis, DNA ; Zea mays/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 65
    Publication Date: 2003-06-14
    Description: In eukaryotes, the combinatorial association of sequence-specific DNA binding proteins is essential for transcription. We have used protein arrays to test 492 pairings of a nearly complete set of coiled-coil strands from human basic-region leucine zipper (bZIP) transcription factors. We find considerable partnering selectivity despite the bZIPs' homologous sequences. The interaction data are of high quality, as assessed by their reproducibility, reciprocity, and agreement with previous observations. Biophysical studies in solution support the relative binding strengths observed with the arrays. New associations provide insights into the circadian clock and the unfolded protein response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, John R S -- Keating, Amy E -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2097-101. Epub 2003 Jun 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Basic-Leucine Zipper Transcription Factors ; Chromatography, High Pressure Liquid ; Circadian Rhythm ; Circular Dichroism ; Cyclic AMP Response Element-Binding Protein/chemistry/metabolism ; DNA-Binding Proteins/chemistry/isolation & purification/*metabolism ; Dimerization ; G-Box Binding Factors ; Humans ; *Leucine Zippers ; Peptides/chemistry/isolation & purification/metabolism ; *Protein Array Analysis ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Signal Transduction ; Temperature ; Thermodynamics ; Transcription Factors/*chemistry/isolation & purification/*metabolism
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  • 66
    Publication Date: 2003-05-10
    Description: Multidrug efflux pumps cause serious problems in cancer chemotherapy and treatment of bacterial infections. Yet high-resolution structures of ligand transporter complexes have previously been unavailable. We obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands. The structures show that three molecules of ligands bind simultaneously to the extremely large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions. Each ligand uses a slightly different subset of AcrB residues for binding. The bound ligand molecules often interact with each other, stabilizing the binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Edward W -- McDermott, Gerry -- Zgurskaya, Helen I -- Nikaido, Hiroshi -- Koshland, Daniel E Jr -- AI 09644/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2003 May 9;300(5621):976-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738864" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Infective Agents/chemistry/metabolism ; Anti-Infective Agents, Local/chemistry/metabolism ; Binding Sites ; Carrier Proteins/*chemistry/isolation & purification/*metabolism ; Cell Membrane/chemistry ; Chemistry, Physical ; Ciprofloxacin/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Dequalinium/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/isolation & purification/*metabolism ; Ethidium/chemistry/metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Membrane Proteins/*chemistry/isolation & purification/*metabolism ; Models, Molecular ; Multidrug Resistance-Associated Proteins ; Physicochemical Phenomena ; Protein Binding ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rhodamines/chemistry/metabolism ; Static Electricity
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  • 67
    Publication Date: 2003-07-19
    Description: We collected and completely sequenced 28,469 full-length complementary DNA clones from Oryza sativa L. ssp. japonica cv. Nipponbare. Through homology searches of publicly available sequence data, we assigned tentative protein functions to 21,596 clones (75.86%). Mapping of the cDNA clones to genomic DNA revealed that there are 19,000 to 20,500 transcription units in the rice genome. Protein informatics analysis against the InterPro database revealed the existence of proteins presented in rice but not in Arabidopsis. Sixty-four percent of our cDNAs are homologous to Arabidopsis proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice Full-Length cDNA Consortium -- National Institute of Agrobiological Sciences Rice Full-Length cDNA Project Team -- Kikuchi, Shoshi -- Satoh, Kouji -- Nagata, Toshifumi -- Kawagashira, Nobuyuki -- Doi, Koji -- Kishimoto, Naoki -- Yazaki, Junshi -- Ishikawa, Masahiro -- Yamada, Hitomi -- Ooka, Hisako -- Hotta, Isamu -- Kojima, Keiichi -- Namiki, Takahiro -- Ohneda, Eisuke -- Yahagi, Wataru -- Suzuki, Kohji -- Li, Chao Jie -- Ohtsuki, Kenji -- Shishiki, Toru -- Foundation of Advancement of International Science Genome Sequencing & Analysis Group -- Otomo, Yasuhiro -- Murakami, Kazuo -- Iida, Yoshiharu -- Sugano, Sumio -- Fujimura, Tatsuto -- Suzuki, Yutaka -- Tsunoda, Yuki -- Kurosaki, Takashi -- Kodama, Takeko -- Masuda, Hiromi -- Kobayashi, Michie -- Xie, Quihong -- Lu, Min -- Narikawa, Ryuya -- Sugiyama, Akio -- Mizuno, Kouichi -- Yokomizo, Satoko -- Niikura, Junko -- Ikeda, Rieko -- Ishibiki, Junya -- Kawamata, Midori -- Yoshimura, Akemi -- Miura, Junichirou -- Kusumegi, Takahiro -- Oka, Mitsuru -- Ryu, Risa -- Ueda, Mariko -- Matsubara, Kenichi -- RIKEN -- Kawai, Jun -- Carninci, Piero -- Adachi, Jun -- Aizawa, Katsunori -- Arakawa, Takahiro -- Fukuda, Shiro -- Hara, Ayako -- Hashizume, Wataru -- Hayatsu, Norihito -- Imotani, Koichi -- Ishii, Yoshiyuki -- Itoh, Masayoshi -- Kagawa, Ikuko -- Kondo, Shinji -- Konno, Hideaki -- Miyazaki, Ai -- Osato, Naoki -- Ota, Yoshimi -- Saito, Rintaro -- Sasaki, Daisuke -- Sato, Kenjiro -- Shibata, Kazuhiro -- Shinagawa, Akira -- Shiraki, Toshiyuki -- Yoshino, Masayasu -- Hayashizaki, Yoshihide -- Yasunishi, Ayako -- New York, N.Y. -- Science. 2003 Jul 18;301(5631):376-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, National Institute of Agrobiological Sciences, 2-1-2 Kannon-dai, Tsukuba, Ibaraki 305-8602, Japan. skikuchi@nias.affrc.go.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12869764" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Cloning, Molecular ; Computational Biology ; DNA, Complementary ; Databases, Nucleic Acid ; Databases, Protein ; Genes, Plant ; *Genome, Plant ; Molecular Sequence Data ; Open Reading Frames ; Oryza/*genetics ; Plant Proteins/chemistry/genetics/physiology ; Protein Structure, Tertiary ; RNA, Antisense/genetics ; *Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid ; Transcription Factors/chemistry/genetics ; Transcription, Genetic
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  • 68
    Publication Date: 2003-09-23
    Description: Although critical for development, immunity, wound healing, and metastasis, integrins represent one of the few classes of plasma membrane receptors for which the basic signaling mechanism remains a mystery. We investigated cytoplasmic conformational changes in the integrin LFA-1 (alphaLbeta2) in living cells by measuring fluorescence resonance energy transfer between cyan fluorescent protein-fused and yellow fluorescent protein-fused alphaL and beta2 cytoplasmic domains. In the resting state these domains were close to each other, but underwent significant spatial separation upon either intracellular activation of integrin adhesiveness (inside-out signaling) or ligand binding (outside-in signaling). Thus, bidirectional integrin signaling is accomplished by coupling extracellular conformational changes to an unclasping and separation of the alpha and beta cytoplasmic domains, a distinctive mechanism for transmitting information across the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Minsoo -- Carman, Christopher V -- Springer, Timothy A -- CA31798/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 19;301(5640):1720-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CBR Institute for Biomedical Research, Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14500982" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Antigens, CD11a/*chemistry ; Antigens, CD18/*chemistry ; Bacterial Proteins ; Cell Adhesion ; Cell Membrane/*metabolism ; Chemokine CXCL12 ; Chemokines, CXC/metabolism ; Cytoplasm/*chemistry ; Dimerization ; Fluorescence Resonance Energy Transfer ; Green Fluorescent Proteins ; Humans ; Intercellular Adhesion Molecule-1/metabolism ; Ligands ; Luminescent Proteins ; Lymphocyte Function-Associated Antigen-1/chemistry/*metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, CXCR4/metabolism ; Recombinant Fusion Proteins/chemistry ; *Signal Transduction ; Talin/chemistry/metabolism ; Transfection ; Tumor Cells, Cultured
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  • 69
    Publication Date: 2000-08-01
    Description: The path of the nucleic acids through a transcription elongation complex was tracked by mapping cross-links between bacterial RNA polymerase (RNAP) and transcript RNA or template DNA onto the x-ray crystal structure. In the resulting model, the downstream duplex DNA is nestled in a trough formed by the beta' subunit and enclosed on top by the beta subunit. In the RNAP channel, the RNA/DNA hybrid extends from the enzyme active site, along a region of the beta subunit harboring rifampicin resistance mutations, to the beta' subunit "rudder." The single-stranded RNA is then extruded through another channel formed by the beta-subunit flap domain. The model provides insight into the functional properties of the transcription complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korzheva, N -- Mustaev, A -- Kozlov, M -- Malhotra, A -- Nikiforov, V -- Goldfarb, A -- Darst, S A -- GM30717/GM/NIGMS NIH HHS/ -- GM49242/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):619-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Public Health Research Institute, 455 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10915625" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cross-Linking Reagents ; Crystallography, X-Ray ; DNA/chemistry/genetics/*metabolism ; DNA Primers ; DNA-Directed RNA Polymerases/*chemistry/genetics/metabolism ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligoribonucleotides/chemistry/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Messenger/chemistry/genetics/*metabolism ; Templates, Genetic ; Thermus/enzymology ; *Transcription, Genetic
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  • 70
    Publication Date: 2000-09-01
    Description: Activation of the transcription factor nuclear factor (NF)-kappaB by proinflammatory stimuli leads to increased expression of genes involved in inflammation. Activation of NF-kappaB requires the activity of an inhibitor of kappaB (IkappaB)-kinase (IKK) complex containing two kinases (IKKalpha and IKKbeta) and the regulatory protein NEMO (NF-kappaB essential modifier). An amino-terminal alpha-helical region of NEMO associated with a carboxyl-terminal segment of IKKalpha and IKKbeta that we term the NEMO-binding domain (NBD). A cell-permeable NBD peptide blocked association of NEMO with the IKK complex and inhibited cytokine-induced NF-kappaB activation and NF-kappaB-dependent gene expression. The peptide also ameliorated inflammatory responses in two experimental mouse models of acute inflammation. The NBD provides a target for the development of drugs that would block proinflammatory activation of the IKK complex without inhibiting basal NF-kappaB activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉May, M J -- D'Acquisto, F -- Madge, L A -- Glockner, J -- Pober, J S -- Ghosh, S -- AI 33443/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1550-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10968790" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/chemistry/pharmacology ; COS Cells ; Cells, Cultured ; E-Selectin/biosynthesis/genetics ; Endothelium, Vascular/metabolism ; Gene Expression Regulation ; HeLa Cells ; Humans ; I-kappa B Kinase ; Inflammation/drug therapy ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; NF-kappa B/*metabolism ; Peptides/chemistry/*pharmacology ; Point Mutation ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism
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  • 71
    Publication Date: 2000-01-15
    Description: Murine T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain gammadelta T cell receptors (TCRs) in the absence of other components. The crystal structure of T22b at 3.1 angstroms reveals similarities to MHC class I molecules, but one side of the normal peptide-binding groove is severely truncated, which allows direct access to the beta-sheet floor. Potential gammadelta TCR-binding sites can be inferred from functional mapping of T10 and T22 point mutants and allelic variants. Thus, T22 represents an unusual variant of the MHC-like fold and indicates that gammadelta and alphabeta TCRs interact differently with their respective MHC ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wingren, C -- Crowley, M P -- Degano, M -- Chien, Y -- Wilson, I A -- AI33431/AI/NIAID NIH HHS/ -- CA58896/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):310-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10634787" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Substitution ; Animals ; Binding Sites ; Crystallography, X-Ray ; Glycosylation ; Histocompatibility Antigens Class I/*chemistry ; Hydrogen Bonding ; Ligands ; Mice ; Models, Molecular ; Point Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry/immunology/metabolism ; Receptors, Antigen, T-Cell, gamma-delta/immunology/*metabolism ; Surface Properties ; beta 2-Microglobulin/chemistry
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  • 72
    Publication Date: 2000-12-16
    Description: The completion of the Arabidopsis thaliana genome sequence allows a comparative analysis of transcriptional regulators across the three eukaryotic kingdoms. Arabidopsis dedicates over 5% of its genome to code for more than 1500 transcription factors, about 45% of which are from families specific to plants. Arabidopsis transcription factors that belong to families common to all eukaryotes do not share significant similarity with those of the other kingdoms beyond the conserved DNA binding domains, many of which have been arranged in combinations specific to each lineage. The genome-wide comparison reveals the evolutionary generation of diversity in the regulation of transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riechmann, J L -- Heard, J -- Martin, G -- Reuber, L -- Jiang, C -- Keddie, J -- Adam, L -- Pineda, O -- Ratcliffe, O J -- Samaha, R R -- Creelman, R -- Pilgrim, M -- Broun, P -- Zhang, J Z -- Ghandehari, D -- Sherman, B K -- Yu, G -- New York, N.Y. -- Science. 2000 Dec 15;290(5499):2105-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mendel Biotechnology, 21375 Cabot Boulevard, Hayward, CA 94545, USA. jriechmann@mendelbio.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11118137" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Arabidopsis/chemistry/*genetics ; Caenorhabditis elegans/chemistry/*genetics ; DNA/metabolism ; Drosophila melanogaster/chemistry/*genetics ; Eukaryotic Cells ; Evolution, Molecular ; Gene Duplication ; *Genome ; Genome, Plant ; Protein Binding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/chemistry/*genetics ; Transcription Factors/chemistry/*genetics/metabolism
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  • 73
    Publication Date: 2000-07-06
    Description: A conserved domain in the extracellular region of the 60- and 80-kilodalton tumor necrosis factor receptors (TNFRs) was identified that mediates specific ligand-independent assembly of receptor trimers. This pre-ligand-binding assembly domain (PLAD) is physically distinct from the domain that forms the major contacts with ligand, but is necessary and sufficient for the assembly of TNFR complexes that bind TNF-alpha and mediate signaling. Other members of the TNFR superfamily, including TRAIL receptor 1 and CD40, show similar homotypic association. Thus, TNFRs and related receptors appear to function as preformed complexes rather than as individual receptor subunits that oligomerize after ligand binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, F K -- Chun, H J -- Zheng, L -- Siegel, R M -- Bui, K L -- Lenardo, M J -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2351-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Antigens, CD/chemistry/metabolism ; Apoptosis ; Binding Sites ; Cross-Linking Reagents ; Dimerization ; Energy Transfer ; Fluorescence ; Humans ; Ligands ; Macromolecular Substances ; Mutation ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Tumor Necrosis Factor/*chemistry/*metabolism ; Receptors, Tumor Necrosis Factor, Type I ; Receptors, Tumor Necrosis Factor, Type II ; Recombinant Fusion Proteins/chemistry/metabolism ; *Signal Transduction ; Succinimides ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/*metabolism
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  • 74
    Publication Date: 2000-08-19
    Description: In thioredoxin reductase (TrxR) from Escherichia coli, cycles of reduction and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend on rate-limiting rearrangements of the FAD and NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) domains. We describe the structure of the flavin-reducing conformation of E. coli TrxR at a resolution of 3.0 angstroms. The orientation of the two domains permits reduction of FAD by NADPH and oxidation of the enzyme dithiol by the protein substrate, thioredoxin. The alternate conformation, described by Kuriyan and co-workers, permits internal transfer of reducing equivalents from reduced FAD to the active-site disulfide. Comparison of these structures demonstrates that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lennon, B W -- Williams, C H Jr -- Ludwig, M L -- GM16429/GM/NIGMS NIH HHS/ -- GM18723/GM/NIGMS NIH HHS/ -- GM21444/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1190-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947986" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Crystallography, X-Ray ; Escherichia coli/*enzymology ; Flavin-Adenine Dinucleotide/metabolism ; Hydrogen Bonding ; Models, Molecular ; NADP/metabolism ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Tertiary ; Thioredoxin-Disulfide Reductase/*chemistry/*metabolism ; Thioredoxins/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-05-08
    Description: Human herpesviruses are large and structurally complex viruses that cause a variety of diseases. The three-dimensional structure of the herpesvirus capsid has been determined at 8.5 angstrom resolution by electron cryomicroscopy. More than 30 putative alpha helices were identified in the four proteins that make up the 0.2 billion-dalton shell. Some of these helices are located at domains that undergo conformational changes during capsid assembly and DNA packaging. The unique spatial arrangement of the heterotrimer at the local threefold positions accounts for the asymmetric interactions with adjacent capsid components and the unusual co-dependent folding of its subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Z H -- Dougherty, M -- Jakana, J -- He, J -- Rixon, F J -- Chiu, W -- New York, N.Y. -- Science. 2000 May 5;288(5467):877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10797014" target="_blank"〉PubMed〈/a〉
    Keywords: Capsid/*chemistry/*ultrastructure ; Capsid Proteins ; Cryoelectron Microscopy ; Herpesvirus 1, Human/chemistry/*ultrastructure ; Image Processing, Computer-Assisted ; Models, Molecular ; Molecular Weight ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-02-24
    Description: RNA editing is a fascinating phenomenon that is found in both animal and plant cells. By converting an adenosine base to an inosine (which behaves like guanosine) in RNA that has already been transcribed, certain RNA sequences (and hence the amino acids they encode) are altered. In a Perspective, Keegan, Gallo and O'Connell explore new results showing that activity of the editing enzyme ADAR1 is crucial for normal development of red blood cells in mouse embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keegan, L P -- Gallo, A -- O'Connell, M A -- New York, N.Y. -- Science. 2000 Dec 1;290(5497):1707-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, UK. liam.keegan@hgu.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11186391" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/metabolism ; Adenosine Deaminase/chemistry/*genetics/*metabolism ; Animals ; Base Pairing ; Central Nervous System/metabolism ; Chimera ; Drosophila/genetics/metabolism ; Embryo, Mammalian/cytology ; Embryo, Nonmammalian ; *Erythropoiesis ; Gene Dosage ; Hematopoietic Stem Cells/cytology/enzymology ; Inosine/metabolism ; Liver/metabolism ; Mice ; Mutation ; Phenotype ; Protein Structure, Tertiary ; *RNA Editing ; RNA Precursors/metabolism ; RNA, Double-Stranded/metabolism ; RNA-Binding Proteins ; Receptors, AMPA/genetics ; Stem Cells/cytology/enzymology ; Teratoma/genetics/pathology
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  • 77
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-03-31
    Description: All cellular organisms use specialized RNA polymerases called "primases" to synthesize RNA primers for the initiation of DNA replication. The high-resolution crystal structure of a primase, comprising the catalytic core of the Escherichia coli DnaG protein, was determined. The core structure contains an active-site architecture that is unrelated to other DNA or RNA polymerase palm folds, but is instead related to the "toprim" fold. On the basis of the structure, it is likely that DnaG binds nucleic acid in a groove clustered with invariant residues and that DnaG is positioned within the replisome to accept single-stranded DNA directly from the replicative helicase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keck, J L -- Roche, D D -- Lynch, A S -- Berger, J M -- New York, N.Y. -- Science. 2000 Mar 31;287(5462):2482-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, 229 Stanley Hall, no. 3206, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10741967" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; DNA Helicases/chemistry/metabolism ; DNA Primase/*chemistry/*metabolism ; DNA Replication ; DNA, Bacterial/metabolism ; DNA, Single-Stranded/*metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Escherichia coli/*enzymology/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/biosynthesis ; Recombinant Proteins/chemistry/metabolism ; Templates, Genetic
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  • 78
    Publication Date: 2000-08-26
    Description: Polyadenylate [poly(A)] polymerase (PAP) catalyzes the addition of a polyadenosine tail to almost all eukaryotic messenger RNAs (mRNAs). The crystal structure of the PAP from Saccharomyces cerevisiae (Pap1) has been solved to 2.6 angstroms, both alone and in complex with 3'-deoxyadenosine triphosphate (3'-dATP). Like other nucleic acid polymerases, Pap1 is composed of three domains that encircle the active site. The arrangement of these domains, however, is quite different from that seen in polymerases that use a template to select and position their incoming nucleotides. The first two domains are functionally analogous to polymerase palm and fingers domains. The third domain is attached to the fingers domain and is known to interact with the single-stranded RNA primer. In the nucleotide complex, two molecules of 3'-dATP are bound to Pap1. One occupies the position of the incoming base, prior to its addition to the mRNA chain. The other is believed to occupy the position of the 3' end of the mRNA primer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bard, J -- Zhelkovsky, A M -- Helmling, S -- Earnest, T N -- Moore, C L -- Bohm, A -- R01 GM57218-01A2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1346-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958780" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Deoxyadenine Nucleotides/*chemistry/*metabolism ; Hydrogen Bonding ; Manganese/metabolism ; Models, Molecular ; Mutation ; Polynucleotide Adenylyltransferase/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/metabolism ; RNA, Messenger/metabolism ; Ribosomal Protein S6 ; Ribosomal Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*enzymology
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-23
    Description: Nascent polypeptides emerging from the ribosome and not yet folded may at least transiently present degradation signals similar to those recognized by the ubiquitin system in misfolded proteins. The ubiquitin sandwich technique was used to detect and measure cotranslational protein degradation in living cells. More than 50 percent of nascent protein molecules bearing an amino-terminal degradation signal can be degraded cotranslationally, never reaching their mature size before their destruction by processive proteolysis. Thus, the folding of nascent proteins, including abnormal ones, may be in kinetic competition with pathways that target these proteins for degradation cotranslationally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turner, G C -- Varshavsky, A -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2117-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11000112" target="_blank"〉PubMed〈/a〉
    Keywords: Cysteine Endopeptidases/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Endopeptidases/metabolism ; Fungal Proteins/metabolism ; *Ligases ; Multienzyme Complexes/metabolism ; Peptides/*metabolism ; Proteasome Endopeptidase Complex ; *Protein Biosynthesis ; Protein Folding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; *Saccharomyces cerevisiae Proteins ; Tetrahydrofolate Dehydrogenase/metabolism ; *Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; beta-Galactosidase/metabolism
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  • 80
    Publication Date: 2000-11-10
    Description: Reciprocal gene activation and restriction during cell type differentiation from a common lineage is a hallmark of mammalian organogenesis. A key question, then, is whether a critical transcriptional activator of cell type-specific gene targets can also restrict expression of the same genes in other cell types. Here, we show that whereas the pituitary-specific POU domain factor Pit-1 activates growth hormone gene expression in one cell type, the somatotrope, it restricts its expression from a second cell type, the lactotrope. This distinction depends on a two-base pair spacing in accommodation of the bipartite POU domains on a conserved growth hormone promoter site. The allosteric effect on Pit-1, in combination with other DNA binding factors, results in the recruitment of a corepressor complex, including nuclear receptor corepressor N-CoR, which, unexpectedly, is required for active long-term repression of the growth hormone gene in lactotropes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scully, K M -- Jacobson, E M -- Jepsen, K -- Lunyak, V -- Viadiu, H -- Carriere, C -- Rose, D W -- Hooshmand, F -- Aggarwal, A K -- Rosenfeld, M G -- R01 DK18477/DK/NIDDK NIH HHS/ -- R01 DK54802/DK/NIDDK NIH HHS/ -- R01 GM49327/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 10;290(5494):1127-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Endocrinology and Metabolism, School of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11073444" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Base Sequence ; Binding Sites ; Cell Line ; Conserved Sequence ; Crystallization ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Female ; *Gene Expression Regulation ; Genes, Reporter ; Growth Hormone/*genetics ; Male ; Mice ; Mice, Transgenic ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/genetics/metabolism ; Nuclear Receptor Co-Repressor 1 ; Pituitary Gland/cytology/*metabolism ; Prolactin/*genetics ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Tertiary ; Rats ; Repressor Proteins/chemistry/genetics/*metabolism ; Transcription Factor Pit-1 ; Transcription Factors/chemistry/genetics/*metabolism ; Transcriptional Activation
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  • 81
    Publication Date: 2000-02-26
    Description: The signal recognition particle (SRP), a protein-RNA complex conserved in all three kingdoms of life, recognizes and transports specific proteins to cellular membranes for insertion or secretion. We describe here the 1.8 angstrom crystal structure of the universal core of the SRP, revealing protein recognition of a distorted RNA minor groove. Nucleotide analog interference mapping demonstrates the biological importance of observed interactions, and genetic results show that this core is functional in vivo. The structure explains why the conserved residues in the protein and RNA are required for SRP assembly and defines a signal sequence recognition surface composed of both protein and RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Batey, R T -- Rambo, R P -- Lucast, L -- Rha, B -- Doudna, J A -- New York, N.Y. -- Science. 2000 Feb 18;287(5456):1232-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10678824" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Base Pairing ; Binding Sites ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli/chemistry/genetics/metabolism ; *Escherichia coli Proteins ; Guanosine Triphosphate/metabolism ; Hydrogen Bonding ; Magnesium/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Potassium/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Bacterial/*chemistry/genetics/metabolism ; Signal Recognition Particle/*chemistry/metabolism ; Transformation, Bacterial ; Water/metabolism
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-03-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gillooly, D J -- Stenmark, H -- New York, N.Y. -- Science. 2001 Feb 9;291(5506):993-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Norwegian Radium Hospital, Montebello, N-0310 Oslo, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11232585" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Vesicular Transport ; Binding Sites ; Carrier Proteins/chemistry/*metabolism ; Cell Membrane/metabolism ; Clathrin/metabolism ; Coated Pits, Cell-Membrane/metabolism ; *Endocytosis ; Models, Biological ; Nerve Tissue Proteins/chemistry/*metabolism ; Neuropeptides/chemistry/*metabolism ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphoproteins/chemistry/*metabolism ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Vesicular Transport Proteins
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  • 83
    Publication Date: 2001-04-21
    Description: Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cramer, P -- Bushnell, D A -- Kornberg, R D -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 8;292(5523):1863-76. Epub 2001 Apr 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11313498" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; DNA, Fungal/chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Magnesium/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; RNA Polymerase II/*chemistry/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Fungal/biosynthesis/chemistry/metabolism ; RNA, Messenger/biosynthesis/chemistry/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; Transcription Factors/metabolism ; *Transcription, Genetic
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-08-11
    Description: Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or antagonistic interaction affinities for chromatin-associated proteins, which in turn dictate dynamic transitions between transcriptionally active or transcriptionally silent chromatin states. The combinatorial nature of histone amino-terminal modifications thus reveals a "histone code" that considerably extends the information potential of the genetic code. We propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenuwein, T -- Allis, C D -- GM53512/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1074-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology (IMP) at the Vienna Biocenter, Dr. Bohrgasse 7, A-1030 Vienna, Austria. jenuwein@nt.imp.univie.ac.at〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11498575" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Animals ; Chromatin/chemistry/metabolism/ultrastructure ; *Gene Expression Regulation ; *Gene Silencing ; Genomic Imprinting ; Histones/chemistry/genetics/*metabolism ; Methylation ; Molecular Sequence Data ; Phosphorylation ; Protein Structure, Tertiary ; Transcription, Genetic ; Transcriptional Activation
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  • 85
    Publication Date: 2001-11-10
    Description: We describe a molecular switch based on the controlled methylation of nucleosome and the transcriptional cofactors, the CREB-binding proteins (CBP)/p300. The CBP/p300 methylation site is localized to an arginine residue that is essential for stabilizing the structure of the KIX domain, which mediates CREB recruitment. Methylation of KIX by coactivator-associated arginine methyltransferase 1 (CARM1) blocks CREB activation by disabling the interaction between KIX and the kinase inducible domain (KID) of CREB. Thus, CARM1 functions as a corepressor in cyclic adenosine monophosphate signaling pathway via its methyltransferase activity while acting as a coactivator for nuclear hormones. These results provide strong in vivo and in vitro evidence that histone methylation plays a key role in hormone-induced gene activation and define cofactor methylation as a new regulatory mechanism in hormone signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, W -- Chen, H -- Du, K -- Asahara, H -- Tini, M -- Emerson, B M -- Montminy, M -- Evans, R M -- 9R01DK57978/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, Department of Biological Chemistry, University of California Davis Cancer Center/Basic Science, Sacramento, CA 95817, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701890" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Apoptosis ; Cell Line ; Cyclic AMP Response Element-Binding Protein/metabolism ; Dimerization ; E1A-Associated p300 Protein ; *Gene Expression Regulation ; Genes, Reporter ; Histone Acetyltransferases ; Histones/metabolism ; Methylation ; Molecular Sequence Data ; Nerve Growth Factor/pharmacology ; Nuclear Proteins/chemistry/*metabolism ; PC12 Cells ; Protein Structure, Tertiary ; Protein-Arginine N-Methyltransferases/*metabolism ; Rats ; Receptors, Retinoic Acid/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Somatostatin/genetics ; Trans-Activators/chemistry/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Transfection ; Tretinoin/metabolism/pharmacology
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  • 86
    Publication Date: 2001-03-17
    Description: Chloroplasts relocate their positions in a cell in response to the intensity of incident light, moving to the side wall of the cell to avoid strong light, but gathering at the front face under weak light to maximize light interception. Here, Arabidopsis thaliana mutants defective in the avoidance response were isolated, and the mutated gene was identified as NPL1 (NPH-like 1), a homolog of NPH1 (nonphototropic hypocotyl 1), a blue light receptor used in phototropism. Hence, NPL1 is likely a blue light receptor regulating the avoidance response under strong light.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kagawa, T -- Sakai, T -- Suetsugu, N -- Oikawa, K -- Ishiguro, S -- Kato, T -- Tabata, S -- Okada, K -- Wada, M -- New York, N.Y. -- Science. 2001 Mar 16;291(5511):2138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉"Unit Process and Combined Circuit," PRESTO, Japan Science and Technology Corporation, 1-8, Honcho 4-chome, Kawaguchi-city, Saitama 332-0012, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11251116" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Arabidopsis/genetics/*physiology/ultrastructure ; *Arabidopsis Proteins ; Cell Membrane/metabolism ; Chloroplasts/*physiology ; Genes, Plant ; *Light ; Movement ; Mutation ; Phosphoproteins/chemistry/physiology ; Phototropism ; Plant Leaves/metabolism ; Plant Proteins/chemistry/*genetics/*physiology ; Plant Structures/metabolism ; Protein Structure, Tertiary ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism
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  • 87
    Publication Date: 2001-06-26
    Description: Clinical studies with the Abl tyrosine kinase inhibitor STI-571 in chronic myeloid leukemia demonstrate that many patients with advanced stage disease respond initially but then relapse. Through biochemical and molecular analysis of clinical material, we find that drug resistance is associated with the reactivation of BCR-ABL signal transduction in all cases examined. In six of nine patients, resistance was associated with a single amino acid substitution in a threonine residue of the Abl kinase domain known to form a critical hydrogen bond with the drug. This substitution of threonine with isoleucine was sufficient to confer STI-571 resistance in a reconstitution experiment. In three patients, resistance was associated with progressive BCR-ABL gene amplification. These studies provide evidence that genetically complex cancers retain dependence on an initial oncogenic event and suggest a strategy for identifying inhibitors of STI-571 resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorre, M E -- Mohammed, M -- Ellwood, K -- Hsu, N -- Paquette, R -- Rao, P N -- Sawyers, C L -- GM07185/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 3;293(5531):876-80. Epub 2001 Jun 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Antineoplastic Agents/metabolism/pharmacology/therapeutic use ; Base Sequence ; Benzamides ; Blast Crisis/genetics ; Cell Line ; Drug Resistance, Neoplasm/genetics ; Fusion Proteins, bcr-abl/*metabolism ; Gene Amplification ; *Genes, abl ; Humans ; Hydrogen Bonding ; Imatinib Mesylate ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/*drug therapy/*genetics ; Molecular Sequence Data ; Philadelphia Chromosome ; Phosphorylation ; Piperazines/metabolism/*pharmacology/therapeutic use ; Point Mutation ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-abl/antagonists & ; inhibitors/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins c-crk ; Pyrimidines/metabolism/*pharmacology/therapeutic use ; Recurrence ; Signal Transduction
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bell, A C -- West, A G -- Felsenfeld, G -- New York, N.Y. -- Science. 2001 Jan 19;291(5503):447-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892-0540, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11228144" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/chemistry/*genetics ; Drosophila/genetics ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Gene Silencing ; *Genome ; Genomic Imprinting ; Humans ; Models, Genetic ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; *Regulatory Sequences, Nucleic Acid ; Saccharomyces cerevisiae/genetics ; Vertebrates/genetics
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  • 89
    Publication Date: 2001-06-09
    Description: The p53 protein is present in low amounts in normally growing cells and is activated in response to physiological insults. MDM2 regulates p53 either through inhibiting p53's transactivating function in the nucleus or by targeting p53 degradation in the cytoplasm. We identified a previously unknown nuclear export signal (NES) in the amino terminus of p53, spanning residues 11 to 27 and containing two serine residues phosphorylated after DNA damage, which was required for p53 nuclear export in colloboration with the carboxyl-terminal NES. Serine-15-phosphorylated p53 induced by ultraviolet irradiation was not exported. Thus, DNA damage-induced phosphorylation may achieve optimal p53 activation by inhibiting both MDM2 binding to, and the nuclear export of, p53.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Y -- Xiong, Y -- CA65572/CA/NCI NIH HHS/ -- K01 CA087580/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 8;292(5523):1910-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, and Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, NC 27599-7295, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11397945" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Sequence ; Animals ; Cell Fusion ; Cell Line ; Cell Nucleus/*metabolism ; Cells, Cultured ; Cytoplasm/metabolism ; *DNA Damage ; Mice ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Phosphorylation ; Phosphoserine/metabolism ; *Protein Sorting Signals ; Protein Structure, Tertiary ; Proteins/genetics/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Recombinant Fusion Proteins/metabolism ; Transfection ; Tumor Suppressor Protein p14ARF ; Tumor Suppressor Protein p53/*chemistry/genetics/*metabolism ; Ubiquitins/metabolism ; Ultraviolet Rays
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  • 90
    Publication Date: 2001-12-01
    Description: Heterotrimeric GTP-binding proteins (G proteins) control cellular functions by transducing signals from the outside to the inside of cells. Regulator of G protein signaling (RGS) proteins are key modulators of the amplitude and duration of G protein-mediated signaling through their ability to serve as guanosine triphosphatase-activating proteins (GAPs). We have identified RGS-PX1, a Galpha(s)-specific GAP. The RGS domain of RGS-PX1 specifically interacted with Galpha(s), accelerated its GTP hydrolysis, and attenuated Galpha(s)-mediated signaling. RGS-PX1 also contains a Phox (PX) domain that resembles those in sorting nexin (SNX) proteins. Expression of RGS-PX1 delayed lysosomal degradation of the EGF receptor. Because of its bifunctional role as both a GAP and a SNX, RGS-PX1 may link heterotrimeric G protein signaling and vesicular trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, B -- Ma, Y C -- Ostrom, R S -- Lavoie, C -- Gill, G N -- Insel, P A -- Huang, X Y -- Farquhar, M G -- AG14563/AG/NIA NIH HHS/ -- CA58689/CA/NCI NIH HHS/ -- DK17780/DK/NIDDK NIH HHS/ -- GM56904/GM/NIGMS NIH HHS/ -- HL53773/HL/NHLBI NIH HHS/ -- HL63885/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1939-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0651, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729322" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-2 Receptor Agonists ; Amino Acid Sequence ; Animals ; COS Cells ; Carrier Proteins/chemistry/*metabolism ; Cattle ; Cell Line ; Cyclic AMP/metabolism ; Endosomes/chemistry/metabolism ; GTP-Binding Protein alpha Subunits, Gs/antagonists & inhibitors/*metabolism ; GTPase-Activating Proteins/chemistry/*metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; Protein Binding ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Protein Transport ; RGS Proteins/chemistry/*metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Receptors, Adrenergic, beta-2/genetics/metabolism ; Sequence Alignment ; Signal Transduction ; Sorting Nexins ; Substrate Specificity ; *Vesicular Transport Proteins
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmer, C -- New York, N.Y. -- Science. 2001 Jul 6;293(5527):29-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11441158" target="_blank"〉PubMed〈/a〉
    Keywords: Acoustics ; Animals ; Cues ; Fishes/physiology ; Seals, Earless/*physiology ; Swimming ; Vibrissae/*physiology ; *Water Movements
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  • 92
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De La Cruz, E M -- Pollard, T D -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):616-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474090" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Depolymerizing Factors ; Actins/*chemistry/*metabolism ; Adenosine Diphosphate/chemistry/*metabolism ; Adenosine Triphosphate/chemistry/metabolism ; Biopolymers/chemistry/metabolism ; *Contractile Proteins ; Crystallography, X-Ray ; Hydrolysis ; Microfilament Proteins/metabolism ; Phosphates/metabolism ; Profilins ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Rhodamines/metabolism ; Thymosin/metabolism
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  • 93
    Publication Date: 2001-06-02
    Description: The GGAs are a multidomain protein family implicated in protein trafficking between the Golgi and endosomes. Here, the VHS domain of GGA2 was shown to bind to the acidic cluster-dileucine motif in the cytoplasmic tail of the cation-independent mannose 6-phosphate receptor (CI-MPR). Receptors with mutations in this motif were defective in lysosomal enzyme sorting. The hinge domain of GGA2 bound clathrin, suggesting that GGA2 could be a link between cargo molecules and clathrin-coated vesicle assembly. Thus, GGA2 binding to the CI-MPR is important for lysosomal enzyme targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, Y -- Doray, B -- Poussu, A -- Lehto, V P -- Kornfeld, S -- R01 CA-08759/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 1;292(5522):1716-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11387476" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Vesicular Transport ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; *Carrier Proteins ; Cations ; Clathrin/metabolism ; Dipeptides/chemistry/metabolism ; L Cells (Cell Line) ; Lysosomes/*enzymology ; Mice ; Molecular Sequence Data ; Mutation ; Protein Sorting Signals ; Protein Structure, Tertiary ; *Protein Transport ; Proteins/chemistry/genetics/*metabolism ; Rats ; Receptor, IGF Type 2/*chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Solubility ; Transcription Factor AP-1/metabolism ; Transport Vesicles/metabolism ; Two-Hybrid System Techniques ; trans-Golgi Network/metabolism
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  • 94
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-06-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thornton, J M -- New York, N.Y. -- Science. 2001 Jun 15;292(5524):2095-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University College Department of Biochemistry and Molecular Biology, London WC1E 6BT, UK. thornton@biochem.ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11408660" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Computational Biology ; Computer Simulation ; Databases, Factual ; Evolution, Molecular ; Genome ; *Models, Molecular ; Peptide Library ; *Protein Conformation ; Protein Structure, Tertiary ; Proteins/*chemistry/*physiology ; Proteome ; Sequence Homology, Amino Acid
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  • 95
    Publication Date: 2001-06-30
    Description: The pollen extracellular matrix contains proteins mediating species specificity and components needed for efficient pollination. We identified all proteins 〉10 kilodaltons in the Arabidopsis pollen coating and showed that most of the corresponding genes reside in two genomic clusters. One cluster encodes six lipases, whereas the other contains six lipid-binding oleosin genes, including GRP17, a gene that promotes efficient pollination. Individual oleosins exhibit extensive divergence between ecotypes, but the entire cluster remains intact. Analysis of the syntenic region in Brassica oleracea revealed even greater divergence, but a similar clustering of the genes. Such allelic flexibility may promote speciation in plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayfield, J A -- Fiebig, A -- Johnstone, S E -- Preuss, D -- New York, N.Y. -- Science. 2001 Jun 29;292(5526):2482-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, The University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11431566" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/chemistry/*genetics ; *Arabidopsis Proteins ; Brassica/chemistry/genetics ; Expressed Sequence Tags ; Genes, Plant ; Genetic Variation ; Genome, Plant ; Lipase/*chemistry/genetics ; Molecular Sequence Data ; *Multigene Family ; Phosphotransferases/chemistry/genetics ; Plant Proteins/*chemistry/genetics ; Pollen/*chemistry ; Protein Structure, Tertiary ; *Proteome ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Alignment
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  • 96
    Publication Date: 2001-09-08
    Description: Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is required both for binding to prosurvival Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors by association with dynein light chain 2. Certain damage signals, such as loss of cell attachment (anoikis), unleash Bmf, allowing it to translocate and bind prosurvival Bcl-2 proteins. Thus, at least two mammalian BH3-only proteins, Bmf and Bim, function to sense intracellular damage by their localization to distinct cytoskeletal structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puthalakath, H -- Villunger, A -- O'Reilly, L A -- Beaumont, J G -- Coultas, L -- Cheney, R E -- Huang, D C -- Strasser, A -- CA 80188/CA/NCI NIH HHS/ -- R29 DC003299/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1829-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Walter and Eliza Hall Institute of Medical Research, Melbourne, P.O. Royal Melbourne Hospital, 3050 VIC, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546872" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; *Anoikis ; Apoptosis Regulatory Proteins ; Calmodulin-Binding Proteins/*metabolism ; Carrier Proteins/*chemistry/genetics/*metabolism ; Cell Line ; Cytoskeleton/metabolism ; *Drosophila Proteins ; Dyneins ; Gene Expression Profiling ; Humans ; *Membrane Proteins ; Mice ; Molecular Motor Proteins/*metabolism ; Molecular Sequence Data ; Mutation ; Myeloid Cell Leukemia Sequence 1 Protein ; *Myosin Type V ; Neoplasm Proteins/genetics/metabolism ; Nerve Tissue Proteins/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; Protein Transport ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-bcl-2/chemistry/genetics/metabolism ; RNA, Messenger/analysis/genetics ; Transfection ; Two-Hybrid System Techniques
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
    Publication Date: 2001-05-12
    Description: Epigenetic silenced alleles of the Arabidopsis SUPERMAN locus (the clark kent alleles) are associated with dense hypermethylation at noncanonical cytosines (CpXpG and asymmetric sites, where X = A, T, C, or G). A genetic screen for suppressors of a hypermethylated clark kent mutant identified nine loss-of-function alleles of CHROMOMETHYLASE3 (CMT3), a novel cytosine methyltransferase homolog. These cmt3 mutants display a wild-type morphology but exhibit decreased CpXpG methylation of the SUP gene and of other sequences throughout the genome. They also show reactivated expression of endogenous retrotransposon sequences. These results show that a non-CpG DNA methyltransferase is responsible for maintaining epigenetic gene silencing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lindroth, A M -- Cao, X -- Jackson, J P -- Zilberman, D -- McCallum, C M -- Henikoff, S -- Jacobsen, S E -- GM07104/GM/NIGMS NIH HHS/ -- GM07185/GM/NIGMS NIH HHS/ -- GM29009/GM/NIGMS NIH HHS/ -- GM60398/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 15;292(5524):2077-80. Epub 2001 May 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cell and Developmental Biology, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11349138" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/*genetics/metabolism ; *Arabidopsis Proteins ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; CpG Islands ; Crosses, Genetic ; Cytosine/metabolism ; *DNA Methylation ; DNA-Cytosine Methylases/chemistry/*genetics/*metabolism ; Dinucleoside Phosphates/metabolism ; Gene Expression Regulation, Plant ; *Gene Silencing ; Genes, Plant ; Molecular Sequence Data ; Mutagenesis ; Oligonucleotides/*metabolism ; Phenotype ; Protein Structure, Tertiary ; Retroelements ; Transcription Factors/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-12-01
    Description: There seem to be numerous pathways for exporting mRNAs from the nucleus to the cytoplasm. But working out which set of export adaptors and receptors transport individual mRNAs has been very difficult. In a Perspective, Moore and Rosbash discuss a new strategy using cell-penetrating peptide inhibitors for unraveling the routes of mRNA export in living cells (Gallouzi and Steitz).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, M J -- Rosbash, M -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1841-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, MA 02454, USA. mmoore@brandeis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729289" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antennapedia Homeodomain Protein ; *Antigens, Surface ; Biological Transport/drug effects ; Cell Membrane Permeability ; Cell Nucleus/drug effects/*metabolism ; Cytoplasm/drug effects/*metabolism ; ELAV Proteins ; ELAV-Like Protein 1 ; Fatty Acids, Unsaturated/metabolism/pharmacology ; Gene Products, rev/chemistry/metabolism ; HIV/genetics ; Homeodomain Proteins/chemistry/metabolism ; Humans ; Karyopherins/*metabolism ; Neuropeptides/metabolism ; Nuclear Proteins/metabolism ; *Nucleocytoplasmic Transport Proteins ; Peptide Fragments/chemistry/metabolism/pharmacology ; Protein Binding/drug effects ; Protein Structure, Tertiary ; RNA, Messenger/genetics/*metabolism ; RNA-Binding Proteins/antagonists & inhibitors/chemistry/*metabolism ; *Receptors, Cytoplasmic and Nuclear ; Saccharomyces cerevisiae Proteins/metabolism ; *Transcription Factors ; rev Gene Products, Human Immunodeficiency Virus
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Higgins, C F -- Linton, K J -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1782-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Clinical Sciences Centre, Imperial College School of Medicine, Hammersmith Hospital Campus, DuCane Road, London W12 0NN, UK. christopher.higgins@csc.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546861" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Bacterial Proteins/*chemistry/metabolism ; Cell Membrane/metabolism ; Crystallization ; Crystallography, X-Ray/methods ; Dimerization ; Escherichia coli/*chemistry ; Membrane Proteins/*chemistry/metabolism ; Models, Biological ; P-Glycoprotein/chemistry/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 2001-03-27
    Description: Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a partially active mutant. These dynamics are indicative of exchange between inactive and active conformations. Both states are populated in unphosphorylated NtrC, and phosphorylation shifts the equilibrium toward the active species. These results support a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkman, B F -- Lipson, D -- Wemmer, D E -- Kern, D -- GM62117/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2429-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Magnetic Resonance Facility at Madison (NMRFAM), Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11264542" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; *Bacterial Proteins ; Binding Sites ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Models, Molecular ; Motion ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Signal Transduction ; Time ; *Trans-Activators ; *Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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