ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Collection
Language
  • 1
    facet.materialart.
    Unknown
    De Gruyter
    Publication Date: 2023-12-20
    Description: Why is it that human rights are considered inviolable norms of justice at local and global scales although the number of their violations has steadily increased in modern history? On the surface, this paradox seems to be reducible to a straightforward discrepancy between idealism and reality in humanitarian affairs, but Imagining Human Rights complicates the picture by offering interdisciplinary perspectives on the imaginary status of human rights. By that the contributors mean not merely subject to imagination, open to interpretation or far too abstract, but also formative of a social imaginary with emphatic identifications and shared values. From a variety of disciplinary perspectives, they explore critical ways of engaging in rigorous interdisciplinary conversations about the origin and language of human rights, personal dignity, redistributive justice, and international solidarity. Together, they show how and why a careful examination of the intersection between disciplinary investigations is essential for imagining human rights at large. Examples range from the legitimacy of land ownership rights and the inadequacy of human faculty to make sense of mass violence in visual representation to the stewardship of human rights promoters and the genealogy of human rights.
    Keywords: K1-7720 ; PN1-6790 ; B1-5802 ; Justice ; Dignity ; Literature ; Law ; bic Book Industry Communication::L Law
    Language: English
    Format: application/octet-stream
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 2022-05-27
    Description: © The Author(s), 2022. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Hand, K., Phillips, C., Murray, A., Garvin, J., Maize, E., Gibbs, R., Reeves, G., San Martin, A., Tan-Wang, G., Krajewski, J., Hurst, K., Crum, R., Kennedy, B., McElrath, T., Gallon, J., Sabahi, D., Thurman, S., Goldstein, B., Estabrook, P., Lee, S. W., Dooley, J. A., Brinckerhoff, W. B., Edgett, K. S., German, C. R., Hoehler, T. M., Hörst, S. M., Lunine, J. I., Paranicas, C., Nealson, K., Smith, D. E., Templeton, A. S., Russell, M. J., Schmidt, B., Christner, B., Ehlmann, B., Hayes, A., Rhoden, A., Willis, P., Yingst, R. A., Craft, K., Cameron, M. E., Nordheim, T., Pitesky, J., Scully, J., Hofgartner, J., Sell, S. W., Barltrop, K. J., Izraelevitz, J., Brandon, E. J., Seong, J., Jones, J.-P., Pasalic, J., Billings, K. J., Ruiz, J. P., Bugga, R. V., Graham, D., Arenas, L. A., Takeyama, D., Drummond, M., Aghazarian, H., Andersen, A. J., Andersen, K. B., Anderson, E. W., Babuscia, A., Backes, P. G., Bailey, E. S., Balentine, D., Ballard, C. G., Berisford, D. F., Bhandari, P., Blackwood, K., Bolotin, G. S., Bovre, E. A., Bowkett, J., Boykins, K. T., Bramble, M. S., Brice, T. M., Briggs, P., Brinkman, A. P., Brooks, S. M., Buffington, B. B., Burns, B., Cable, M. L., Campagnola, S., Cangahuala, L. A., Carr, G. A., Casani, J. R., Chahat, N. E., Chamberlain-Simon, B. K., Cheng, Y., Chien, S. A., Cook, B. T., Cooper, M., DiNicola, M., Clement, B., Dean, Z., Cullimore, E. A., Curtis, A. G., Croix, J-P. de la, Pasquale, P. Di, Dodd, E. M., Dubord, L. A., Edlund, J. A., Ellyin, R., Emanuel, B., Foster, J. T., Ganino, A. J., Garner, G. J., Gibson, M. T., Gildner, M., Glazebrook, K. J., Greco, M. E., Green, W. M., Hatch, S. J., Hetzel, M. M., Hoey, W. A., Hofmann, A. E., Ionasescu, R., Jain, A., Jasper, J. D., Johannesen, J. R., Johnson, G. K., Jun, I., Katake, A. B., Kim-Castet, S. Y., Kim, D. I., Kim, W., Klonicki, E. F., Kobeissi, B., Kobie, B. D., Kochocki, J., Kokorowski, M., Kosberg, J. A., Kriechbaum, K., Kulkarni, T. P., Lam, R. L., Landau, D. F., Lattimore, M. A., Laubach, S. L., Lawler, C. R., Lim, G., Lin, J. Y., Litwin, T. E., Lo, M. W., Logan, C. A., Maghasoudi, E., Mandrake, L., Marchetti, Y., Marteau, E., Maxwell, K. A., Namee, J. B. Mc, Mcintyre, O., Meacham, M., Melko, J. P., Mueller, J., Muliere, D. A., Mysore, A., Nash, J., Ono, H., Parker, J. M., Perkins, R. C., Petropoulos, A. E., Gaut, A., Gomez, M. Y. Piette, Casillas, R. P., Preudhomme, M., Pyrzak, G., Rapinchuk, J., Ratliff, J. M., Ray, T. L., Roberts, E. T., Roffo, K., Roth, D. C., Russino, J. A., Schmidt, T. M., Schoppers, M. J., Senent, J. S., Serricchio, F., Sheldon, D. J., Shiraishi, L. R., Shirvanian, J., Siegel, K. J., Singh, G., Sirota, A. R., Skulsky, E. D., Stehly, J. S., Strange, N. J., Stevens, S. U., Sunada, E. T., Tepsuporn, S. P., Tosi, L. P. C., Trawny, N., Uchenik, I., Verma, V., Volpe, R. A., Wagner, C. T., Wang, D., Willson, R. G., Wolff, J. L., Wong, A. T., Zimmer, A. K., Sukhatme, K. G., Bago, K. A., Chen, Y., Deardorff, A. M., Kuch, R. S., Lim, C., Syvertson, M. L., Arakaki, G. A., Avila, A., DeBruin, K. J., Frick, A., Harris, J. R., Heverly, M. C., Kawata, J. M., Kim, S.-K., Kipp, D. M., Murphy, J., Smith, M. W., Spaulding, M. D., Thakker, R., Warner, N. Z., Yahnker, C. R., Young, M. E., Magner, T., Adams, D., Bedini, P., Mehr, L., Sheldon, C., Vernon, S., Bailey, V., Briere, M., Butler, M., Davis, A., Ensor, S., Gannon, M., Haapala-Chalk, A., Hartka, T., Holdridge, M., Hong, A., Hunt, J., Iskow, J., Kahler, F., Murray, K., Napolillo, D., Norkus, M., Pfisterer, R., Porter, J., Roth, D., Schwartz, P., Wolfarth, L., Cardiff, E. H., Davis, A., Grob, E. W., Adam, J. R., Betts, E., Norwood, J., Heller, M. M., Voskuilen, T., Sakievich, P., Gray, L., Hansen, D. J., Irick, K. W., Hewson, J. C., Lamb, J., Stacy, S. C., Brotherton, C. M., Tappan, A. S., Benally, D., Thigpen, H., Ortiz, E., Sandoval, D., Ison, A. M., Warren, M., Stromberg, P. G., Thelen, P. M., Blasy, B., Nandy, P., Haddad, A. W., Trujillo, L. B., Wiseley, T. H., Bell, S. A., Teske, N. P., Post, C., Torres-Castro, L., Grosso, C. Wasiolek, M. Science goals and mission architecture of the Europa Lander mission concept. The Planetary Science Journal, 3(1), (2022): 22, https://doi.org/10.3847/psj/ac4493.
    Description: Europa is a premier target for advancing both planetary science and astrobiology, as well as for opening a new window into the burgeoning field of comparative oceanography. The potentially habitable subsurface ocean of Europa may harbor life, and the globally young and comparatively thin ice shell of Europa may contain biosignatures that are readily accessible to a surface lander. Europa's icy shell also offers the opportunity to study tectonics and geologic cycles across a range of mechanisms and compositions. Here we detail the goals and mission architecture of the Europa Lander mission concept, as developed from 2015 through 2020. The science was developed by the 2016 Europa Lander Science Definition Team (SDT), and the mission architecture was developed by the preproject engineering team, in close collaboration with the SDT. In 2017 and 2018, the mission concept passed its mission concept review and delta-mission concept review, respectively. Since that time, the preproject has been advancing the technologies, and developing the hardware and software, needed to retire risks associated with technology, science, cost, and schedule.
    Description: K.P.H., C.B.P., E.M., and all authors affiliated with the Jet Propulsion Laboratory carried out this research at the Jet Propulsion Laboratory, California Institute of Technology, under a contract with the National Aeronautics and Space Administration (grant No. 80NM0018D0004). J.I.L. was the David Baltimore Distinguished Visiting Scientist during the preparation of the SDT report. JPL/Caltech2021.
    Keywords: Europa ; Ocean planets ; Astrobiology ; Biosignatures
    Repository Name: Woods Hole Open Access Server
    Type: Article
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Geostandards and geoanalytical research 11 (1987), S. 0 
    ISSN: 1751-908X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences
    Notes: Nineteen USGS GRSs were analyzed with a Dupont 903-H Moisture Analyzer at 110°C and 1000°C to obtain H2O-and H2O+, and by thermal neutron induced gamma-ray spectrometry to obtain total H2O. The values are compared with the current literature and the two techniques evaluated. Except for QLO-1 by coulometry, no significant differences were obtained when the results were compared to the the literature.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    [S.l.] : Emerald
    Journal of economic studies 30 (2003), S. 605-622 
    ISSN: 0144-3585
    Source: Emerald Fulltext Archive Database 1994-2005
    Topics: Economics
    Notes: This paper provides empirical evidence on the dynamic relationship between inward foreign direct investment (FDI), economic growth and domestic investment in Korea for the period 1985-1999. By employing a vector autoregression model and the innovations accounting techniques, we explore dynamic interactions between inward FDI, domestic investment and output. We find that FDI has some positive effects on economic growth, but its effects seem to be insignificant. On the other hand, economic growth is found to have statistically significant and highly persistent effects on the future level of FDI. Although FDI is exogenous contemporaneously, we find that FDI shows strong dynamic endogeneity to domestic macroeconomic conditions, which has not been uncovered in previous works. Our finding does not support the view that FDI crowds out domestic investment in Korea.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 480-487 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional structure of a tryptophan-containing variant of the IgG-binding B1 domain of protein L has been solved in two crystal forms to 1.7 and 1.8 Å resolution. In one of the crystal forms, the entire N-terminal histidine-tag region was immobilized through the coordination of zinc ions and its structural conformation along with the zinc coordination scheme were determined. However, the ordering of the histidine tag by zinc does not affect the overall structure of the rest of the protein. Structural comparisons of the tryptophan-containing variant with an NMR-derived wild-type structure, which contains a tyrosine at position 47, reveals a common fold, although the overall backbone root-mean-square difference is 1.5 Å. The Y47W substitution only caused local rearrangement of several side chains, the most prominent of which is the rotation of the Tyr34 side chain, resulting in a 6 Å displacement of its hydroxyl group. A small methyl-sized cavity bounded by β-strands 1, 2 and 4 and the α-helix was found in the structures of the Y47W-substituted protein L B1 domain. This cavity may be created as the result of subsequent side-chain rearrangements caused by the Y47W substitution. These high-resolution structures of the tryptophan-containing variant provide a reference frame for the analysis of thermodynamic and kinetic data derived from a series of mutational studies of the protein L B1 domain.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 506-508 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The small 62-residue IgG-binding domain B1 of protein L from Peptostreptococcus magnus (Ppl-B1) has proven to be a simple system for the study of the thermodynamics and kinetics of protein folding. X-ray diffraction studies have been initiated in order to determine how the thermostability, folding and unfolding rates of a series of point mutations spanning Ppl-B1 correlate with the high-resolution structures. To this end, a tryptophan-containing variant of Ppl-B1 (herein known as wild type) and two mutants, Lys61Ala and Val49Ala, have been crystallized. Full data sets have been collected for the wild type and the Lys61Ala and Val49Ala mutants to resolutions of 1.7, 2.3 and 1.8 Å, respectively. Interestingly, all three crystallize using different precipitants and in different space groups. This may be a consequence of the relatively large effects of single-site mutations on surface-charge distribution or structural conformation, which might affect crystal contact sites.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 8
    facet.materialart.
    Unknown
    Menasha, Wis. : Periodicals Archive Online (PAO)
    The Accounting Review. 62:2 (1987:Apr.) 343 
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomedical science 3 (1996), S. 143-158 
    ISSN: 1423-0127
    Keywords: Transforming growth factor-β ; Tumorigenesis ; Mutation ; Tumor suppressor gene ; Receptor ; Microsatellite instability ; Transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Transforming growth factor-β (TGF-β) plays a pivotal role in numerous vital cellular activities, most significantly the regulation of cellular proliferation and differentiation and synthesis of extracellular matrix components. Its ubiquitous presence in different tissues and strict conservation of nucleotide sequence down through the most primitive vertebrate organisms underscore the essential nature of this family of molecules. The effects of TGF-β are mediated by a family of dedicated receptors, the TGF-β types I, II, and III receptors. It is now known that a wide variety of human pathology can be caused by aberrant expression and function of these receptors or their cognate ligands. The coding sequence of the human type II receptor appears to render it uniquely susceptible to DNA replication errors in the course of normal cell division. There are now substantial data suggesting that TGF-β type II receptor should be considered a tumor suppressor gene. High levels of mutation in the TGF-β type II receptor gene have been observed in a wide variety of primarily epithelial malignancies, including colon, gastric, and hepatic cancer. It appears likely that mutation of the TGF-β type II receptor gene represents a very critical step in the pathway of carcinogenesis.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 19 (1998), S. 473-477 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The location of triads within a mammalian skeletal muscle sarcomere has traditionally been defined as ‘at the A-I junction’. We attempted to verify this statement by examining systematically the location of triads within the sarcomere over the physiological range of sarcomere lengths. This study was conducted using intact feline muscle fibres from caudofemoralis – an exclusively fast-twitch muscle from the hindlimb. Our results in intact fibres indicate that the distance between the Z-band and triad (ZT) is relatively constant over the range of sarcomere lengths (SLs) examined in this study (1.8–3.4μm). The slope between ZT and SL was measured to be 0.06 ± 0.01 (r=0.36, p 〈 0.001) while the slope between the M-line to triad distance (MT) and SL was measured to be 0.440.01 (r 〉 0.9, p 〈 0.001). The mean ZT was 0.52 ± 0.07μm, which corresponds to a triad location approximately halfway along the thin filaments. These results do not support the traditional statement regarding triad location. Nor do these results support a similar recent study conducted using chemically skinned muscle fibres from rat extensor digitorum longus (also a homogeneously fast-twitch muscle of the hindlimb), in which a slope of 0.25 was observed between ZT and SL (r 〉 0.9, p 〈 0.01). These results are, however, in qualitative agreement with results using intact fibres from fast-twitch rat semitendinosus. Based upon known morphology, we suggest that the only structure supporting triad position is the SR itself, and that a non-homogeneous distribution of the SR within the sarcomere might be responsible for maintaining triad location near the mid-region of the thin filaments. We also suggest that there might be optimal design reasons for locating the triads at the mid-region of the thin filaments.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...