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  • EARTH RESOURCES AND REMOTE SENSING  (6)
  • Animals  (4)
  • Aeronautics (General)
  • Air Transportation and Safety
  • 2015-2019
  • 1995-1999
  • 1990-1994  (10)
  • 1993  (10)
  • 1
    Publication Date: 1993-05-14
    Description: The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the beta sheets; this results in an expansion of the domain. There is a difference of 30 degrees in the orientation between domains 3 and 4 when compared with domains 1 and 2. The two CD4 fragment structures provide a basis from which models of the overall receptor can be proposed. These models suggest an extended structure comprising two rigid portions joined by a short and possibly flexible linker region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brady, R L -- Dodson, E J -- Dodson, G G -- Lange, G -- Davis, S J -- Williams, A F -- Barclay, A N -- New York, N.Y. -- Science. 1993 May 14;260(5110):979-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of York, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493535" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*chemistry ; Crystallization ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Sequence Alignment ; X-Ray Diffraction
    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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  • 2
    Publication Date: 1993-03-19
    Description: The alpha component of the receptor for ciliary neurotrophic factor (CNTF) differs from other known growth factor receptors in that it is anchored to cell membranes by a glycosylphosphatidylinositol linkage. One possible function of this type of linkage is to allow for the regulated release of this receptor component. Cell lines not normally responsive to CNTF responded to treatment with a combination of CNTF and a soluble form of the CNTF alpha receptor component. These findings not only demonstrate that the CNTF receptor alpha chain is a required component of the functional CNTF receptor complex but also reveal that it can function in soluble form as part of a heterodimeric ligand. Potential physiological roles for the soluble CNTF receptor are suggested by its presence in cerebrospinal fluid and by its release from skeletal muscle in response to peripheral nerve injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Ip, N Y -- Stahl, N -- Scherer, S -- Farruggella, T -- DiStefano, P S -- Curtis, R -- Panayotatos, N -- Gascan, H -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1736-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681218" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/drug effects ; Cell Division/drug effects ; Cell Membrane/metabolism ; Ciliary Neurotrophic Factor ; Cloning, Molecular ; Gene Expression ; Glycosylphosphatidylinositols/metabolism ; Growth Inhibitors/pharmacology ; Hematopoietic Stem Cells/cytology/drug effects ; Humans ; Interleukin-6/pharmacology ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Mice ; Muscle Denervation ; Muscles/innervation/metabolism ; Nerve Tissue Proteins/*pharmacology ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphoric Diester Hydrolases/metabolism ; Phosphotyrosine ; RNA, Messenger/genetics ; Rats ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/chemistry/*physiology ; Signal Transduction/physiology ; Tumor Cells, Cultured ; Tyrosine/analogs & derivatives/metabolism
    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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  • 3
    Publication Date: 1993-06-18
    Description: The ciliary neurotrophic factor (CNTF) receptor complex is shown here to include the CNTF binding protein (CNTFR alpha) as well as the components of the leukemia inhibitory factor (LIF) receptor, LIFR beta (the LIF binding protein) and gp130 [the signal transducer of interleukin-6 (IL-6)]. Thus, the conversion of a bipartite LIF receptor into a tripartite CNTF receptor apparently occurs by the addition of the specificity-conferring element CNTFR alpha. Both CNTF and LIF trigger the association of initially separate receptor components, which in turn results in tyrosine phosphorylation of receptor subunits. Unlike the IL-6 receptor complex in which homodimerization of gp130 appears to be critical for signal initiation, signaling by the CNTF and LIF receptor complexes depends on the heterodimerization of gp130 with LIFR beta. Ligand-induced dimerization of signal-transducing receptor components, also seen with receptor tyrosine kinases, may provide a general mechanism for the transmission of a signal across the cell membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Stahl, N -- Pan, L -- Taga, T -- Kishimoto, T -- Ip, N Y -- Yancopoulos, G D -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8390097" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Cell Line ; Cytokine Receptor gp130 ; Growth Inhibitors/pharmacology ; Interleukin-6/pharmacology ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Macromolecular Substances ; Membrane Glycoproteins/chemistry/*metabolism ; Models, Biological ; Nerve Growth Factors ; Nerve Tissue Proteins/pharmacology ; Phosphorylation ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/chemistry/*metabolism ; *Receptors, Cytokine ; Receptors, Immunologic/chemistry/*metabolism ; Receptors, Interleukin-6 ; Receptors, OSM-LIF ; *Signal Transduction ; Tumor Cells, Cultured ; Tyrosine/metabolism
    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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  • 4
    Publication Date: 1993-03-19
    Description: Tyrosine phosphorylation of proteins is required for signal transduction in cells and for growth regulation. A mitogen-induced gene (PAC-1) has been cloned from human T cells and encodes a 32-kilodalton protein that contains a sequence that defines the enzymatic site of known protein phosphotyrosine phosphatases (PTPases). Other than this sequence, PAC-1 is different from several other known related PTPases exemplified by PTP-1b. PAC-1 is similar to a phosphatase induced by mitogens or heat shock in fibroblasts, a yeast gene, and a vaccinia virus-encoded serine-tyrosine phosphatase (VH1). PAC-1 was predominantly expressed in hematopoietic tissues and localized to the nucleus in transfected COS-7 cells and in mitogen-stimulated T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rohan, P J -- Davis, P -- Moskaluk, C A -- Kearns, M -- Krutzsch, H -- Siebenlist, U -- Kelly, K -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681221" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Cell Line ; Cell Nucleus/enzymology ; Conserved Sequence ; Cytoplasm/enzymology ; Dual Specificity Phosphatase 2 ; Fluorescent Antibody Technique ; Humans ; Immunosorbent Techniques ; Mice ; Mitogens/*pharmacology ; Molecular Sequence Data ; Organ Specificity ; Protein Phosphatase 2 ; Protein Tyrosine Phosphatases/chemistry/*genetics ; RNA/analysis ; Sequence Homology, Amino Acid ; Signal Transduction/physiology ; T-Lymphocytes/enzymology ; Transfection
    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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  • 5
    Publication Date: 2011-08-24
    Description: Data on chlorophyll content and bathymetry of Lake Tahoe obtained on August 9, 1990 by the Airborne Visible/Infrared Imaging Spectrometer (AVIRIS) are compared to concurrent in situ surface and in-water measurements. Measured parameters included profiles of percent transmission of monochromatic light, stimulated chlorophyll fluorescence, photosynthetically available radiation, spectral upwelling and downwelling irradiance, and upwelling radiance. Several analyses were performed illustrating the utility of the AVIRIS over a dark water scene. Image-derived chlorophyll concentration compared extremely well with that measured with bottle samples. A bathymetry map of the shallow parts of the lake was constructed which compares favorably with published lake soundings.
    Keywords: EARTH RESOURCES AND REMOTE SENSING
    Type: Remote Sensing of Environment (ISSN 0034-4257); 44; 2-3; p. 217-230.
    Format: text
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  • 6
    Publication Date: 2011-08-24
    Description: The Visiting Investigator Program (VIP) developed at NASA-Stennis' Science and Technology Laboratory (STL) allows U.S. industry to use the specialized resources of STL in the fields of remote sensing and GIS, with a view to the development of new commercial processes and improved services. Attention is given to the novel agreement mechanisms developed by NASA to implement VIP. These agreements encompass a memorandum of understanding, a technical exchange agreement, a sponsored-transfer agreement, a proprietary work agreement, and a joint endeavor agreement.
    Keywords: EARTH RESOURCES AND REMOTE SENSING
    Type: PE&RS - Photogrammetric Engineering and Remote Sensing (ISSN 0099-1112); 59; 6; p. 935-939.
    Format: text
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  • 7
    Publication Date: 2013-08-31
    Description: As part of research on forest ecosystems, the Jet Propulsion Laboratory (JPL) and collaborating research teams have conducted multi-season airborne synthetic aperture radar (AIRSAR) experiments in three forest ecosystems including temperate pine forest (Duke, Forest, North Carolina), boreal forest (Bonanza Creek Experimental Forest, Alaska), and northern mixed hardwood-conifer forest (Michigan Biological Station, Michigan). The major research goals were to improve understanding of the relationships between radar backscatter and phenological variables (e.g. stand density, tree size, etc.), to improve radar backscatter models of tree canopy properties, and to develop a radar-based scheme for monitoring forest phenological changes. In September 1989, AIRSAR backscatter data were acquired over the Duke Forest. As the aboveground biomass of the loblolly pine forest stands at Duke Forest increased, the SAR backscatter at C-, L-, and P-bands increased and saturated at different biomass levels for the C-band, L-band, and P-band data. We only use the P-band backscatter data and ground measurements here to study the relationships between the backscatter and stand density, the backscatter and mean trunk dbh (diameter at breast height) of trees in the stands, and the backscatter and stand basal area.
    Keywords: EARTH RESOURCES AND REMOTE SENSING
    Type: JPL, Summaries of the 4th Annual JPL Airborne Geoscience Workshop. Volume 3: AIRSAR Workshop; p 81-84
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  • 8
    Publication Date: 2013-08-31
    Description: Point source measurements (e.g. sun photometer data, weather station observations) are often used to constrain radiative transfer models such as MODTRAN/LOWTRAN7 when atmospherically correcting AVIRIS imagery. The basic assumption is that the atmosphere is horizontally homogeneous throughout the entire area. If the target area of interest is isolated a distance away from the point measurement position, the calculated visibility and atmospheric profiles may not be characteristic of the atmosphere over the target. AVIRIS scenes are often rejected when cloud cover exceeds 10%. However, if the cloud cover is determined to be primarily cirrus rather than cumulus, in-water optical properties may still be extracted over open ocean. High altitude cirrus clouds are non-absorbing at 744 nm. If the optical properties of the AVIRIS scene can be determined from the 744 nm band itself, the atmospheric conditions during the overflight may be deduced.
    Keywords: EARTH RESOURCES AND REMOTE SENSING
    Type: Summaries of the 4th Annual JPL Airborne Geoscience Workshop. Volume 1: AVIRIS Workshop; p 185-188
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  • 9
    Publication Date: 2019-06-28
    Description: The NASA and ESA retracking algorithms are compared with an algorithm based upon a combined surface and volume (S/V) scattering model. First, the S/V, NASA, and ESA algorithms were used to retrack over 400,000 altimeter return waveforms from the Greenland and Antarctic ice sheets. The surface elevations from the S/V algorithm were compared with the elevations produced by the NASA and ESA algorithms to determine the relative accuracy of these algorithms when subsurface volume-scattering occurs. The results show that the NASA algorithm produced surface elevations within 35 to 50 cm of the S/V algorithm, while the performance of the ESA algorithm was slightly worse. Next, by analyzing several thousand satellite crossover points from the Antarctic data set, we determined the retracking algorithm that produced the most repeatable surface elevations. The elevations derived from the S/V algorithm had the smallest RMS error for the region of the East Antarctic plateau examined here. The ESA algorithm produced erroneous estimates of elevation change when seasonal variations were present; it measured 0.7 to 1.6-m change in elevation over a 6-month period on the East Antarctic plateau where accumulation rates are only 10 cm/year.
    Keywords: EARTH RESOURCES AND REMOTE SENSING
    Type: NASA-CR-194825 , NAS 1.26:194825
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  • 10
    Publication Date: 2019-06-28
    Description: In this paper, we compare dry-snow extinction coefficients derived from radar altimeter data with brightness temperature data from passive microwave measurements over a portion of the East Antarctic plateau. The comparison between the extinction coefficients and the brightness temperatures shows a strong negative correlation, where the correlation coefficients ranged from -0.87 to -0.95. The extinction coefficient of the dry polar snow decreases with increasing surface elevation, while the average brightness temperature increases with surface elevation. Our analysis shows that the observed trends are related to geographic variations in scattering coefficient of snow, which in turn are controlled by variations in surface temperature and snow accumulation rate. By combining information present in the extinction coefficient and brightness temperature data sets, we develop a model that can be used to obtain quantitative estimates of the accumulation rate of dry polar snow.
    Keywords: EARTH RESOURCES AND REMOTE SENSING
    Type: NASA-CR-194864 , NAS 1.26:194864
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