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  • Articles  (758)
  • 2020-2023
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  • 1995-1999
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  • Articles  (758)
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  • 2020-2023
  • 2020-2020
  • 1995-1999
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  • 1
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    Complete Nucleotide Sequence of Saccharomyces cerevisiae Chromosome VIII (1994)
    American Association for the Advancement of Science
    Details
    Publication Date: 1994-09-30
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science
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  • 2
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    GDNF: a potent survival factor for motoneurons present in peripheral nerve and muscle (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-11
    Description: For survival, embryonic motoneurons in vertebrates depend on as yet undefined neurotrophic factors present in the limb bud. Members of the neurotrophin family are currently the best candidates for such neurotrophic factors, but inactivation of their receptor genes leads to only partial loss of motoneurons, which suggests that other factors are involved. Glial cell line-derived neurotrophic factor (GDNF), originally identified as a trophic factor specific for dopaminergic neurons, was found to be 75-fold more potent than the neurotrophins in supporting the survival of purified embryonic rat motoneurons in culture. GDNF messenger RNA was found in the immediate vicinity of motoneurons during the period of cell death in development. In vivo, GDNF rescues and prevents the atrophy of facial motoneurons that have been deprived of target-derived survival factors by axotomy. GDNF may therefore be a physiological trophic factor for spinal motoneurons. Its potency and specificity in vitro and in vivo also make it a good candidate for treatment of motoneuron disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henderson, C E -- Phillips, H S -- Pollock, R A -- Davies, A M -- Lemeulle, C -- Armanini, M -- Simmons, L -- Moffet, B -- Vandlen, R A -- Simpson LC corrected to Simmons, L -- Koliatsos, V E -- Rosenthal, A -- NS 10580/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1062-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U.382, IBDM, Marseille, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973664" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor ; Cell Death ; Cell Survival/drug effects ; Cells, Cultured ; Ciliary Neurotrophic Factor ; Face/innervation ; Glial Cell Line-Derived Neurotrophic Factor ; Growth Inhibitors/pharmacology ; *Interleukin-6 ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Molecular Sequence Data ; Motor Neurons/*cytology/drug effects ; Muscle Fibers, Skeletal/*metabolism ; Nerve Growth Factors/analysis/biosynthesis/genetics/*pharmacology ; Nerve Tissue Proteins/*analysis/biosynthesis/genetics/*pharmacology ; Neurons, Afferent/cytology/drug effects ; Peripheral Nerves/*metabolism ; RNA, Messenger/analysis/genetics ; Rats ; Schwann Cells/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
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    Structure of the allosteric regulatory enzyme of purine biosynthesis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-03
    Description: Multi-wavelength anomalous diffraction (MAD) has been used to determine the structure of the regulatory enzyme of de novo synthesis of purine nucleotides, glutamine 5-phosphoribosyl-1-pyrophosphate (PRPP) amidotransferase, from Bacillus subtilis. This allosteric enzyme, a 200-kilodalton tetramer, is subject to end product regulation by purine nucleotides. The metalloenzyme from B. subtilis is a paradigm for the higher eukaryotic enzymes, which have been refractory to isolation in stable form. The two folding domains of the polypeptide are correlated with functional domains for glutamine binding and for transfer of ammonia to the substrate PRPP. Eight molecules of the feedback inhibitor adenosine monophosphate (AMP) are bound to the tetrameric enzyme in two types of binding sites: the PRPP catalytic site of each subunit and an unusual regulatory site that is immediately adjacent to each active site but is between subunits. An oxygen-sensitive [4Fe-4S] cluster in each subunit is proposed to regulate protein turnover in vivo and is distant from the catalytic site. Oxygen sensitivity of the cluster is diminished by AMP, which blocks a channel through the protein to the cluster. The structure is representative of both glutamine amidotransferases and phosphoribosyltransferases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, J L -- Zaluzec, E J -- Wery, J P -- Niu, L -- Switzer, R L -- Zalkin, H -- Satow, Y -- DK-42303/DK/NIDDK NIH HHS/ -- GM-24658/GM/NIGMS NIH HHS/ -- R37 DK042303/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1427-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197456" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/metabolism ; Allosteric Regulation ; Amidophosphoribosyltransferase/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Bacillus subtilis/*enzymology ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; Oxygen/pharmacology ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae
    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
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    Association of intestinal peptide transport with a protein related to the cadherin superfamily (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: The first step in oral absorption of many medically important peptide-based drugs is mediated by an intestinal proton-dependent peptide transporter. This transporter facilitates the oral absorption of beta-lactam antibiotics and angiotensin-converting enzyme inhibitors from the intestine into enterocytes lining the luminal wall. A monoclonal antibody that blocked uptake of cephalexin was used to identify and clone a gene that encodes an approximately 92-kilodalton membrane protein that was associated with the acquisition of peptide transport activity by transport-deficient cells. The amino acid sequence deduced from the complementary DNA sequence of the cloned gene indicated that this transport-associated protein shares several conserved structural elements with the cadherin superfamily of calcium-dependent, cell-cell adhesion proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dantzig, A H -- Hoskins, J A -- Tabas, L B -- Bright, S -- Shepard, R L -- Jenkins, I L -- Duckworth, D C -- Sportsman, J R -- Mackensen, D -- Rosteck, P R Jr -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153632" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; CHO Cells ; Cadherins/*chemistry ; Carrier Proteins/*chemistry/genetics/isolation & purification/metabolism ; Cephalexin/*metabolism ; Cloning, Molecular ; Cricetinae ; Glycosylation ; Humans ; Hydrogen-Ion Concentration ; Intestinal Mucosa/*metabolism ; Leucine/analogs & derivatives/metabolism ; *Membrane Transport Proteins ; Mice ; Mice, Inbred A ; Molecular Sequence Data ; Open Reading Frames ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
    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
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    Identification of a peptide recognized by five melanoma-specific human cytotoxic T cell lines (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-29
    Description: Of several thousand peptides presented by the major histocompatibility molecule HLA-A2.1, at least nine are recognized by melanoma-specific cytotoxic T lymphocytes (CTLs). Tandem mass spectrometry was used to identify and to sequence one of these peptide epitopes. Melanoma-specific CTLs had an exceptionally high affinity for this nine-residue peptide, which reconstituted an epitope for CTL lines from each of five different melanoma patients tested. Recognition by multiple CTL lines suggests that this may be a promising candidate for use in peptide-based melanoma vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cox, A L -- Skipper, J -- Chen, Y -- Henderson, R A -- Darrow, T L -- Shabanowitz, J -- Engelhard, V H -- Hunt, D F -- Slingluff, C L Jr -- AI33993/AI/NIAID NIH HHS/ -- CA57653/CA/NCI NIH HHS/ -- GM37537/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):716-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Virginia, Charlottesville 22908.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7513441" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Neoplasm/*immunology ; Chromatography, High Pressure Liquid ; Epitopes/immunology ; HLA-A2 Antigen/immunology ; Humans ; Mass Spectrometry ; Melanoma/*immunology ; Molecular Sequence Data ; Oligopeptides/*immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Tumor Cells, Cultured
    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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  • 6
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    Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-04
    Description: The success of Mycobacterium species as pathogens depends on their ability to maintain an infection inside the phagocytic vacuole of the macrophage. Although the bacteria are reported to modulate maturation of their intracellular vacuoles, the nature of such modifications is unknown. In this study, vacuoles formed around Mycobacterium avium failed to acidify below pH 6.3 to 6.5. Immunoelectron microscopy of infected macrophages and immunoblotting of isolated phagosomes showed that Mycobacterium vacuoles acquire the lysosomal membrane protein LAMP-1, but not the vesicular proton-adenosine triphosphatase (ATPase) responsible for phagosomal acidification. This suggests either a selective inhibition of fusion with proton-ATPase-containing vesicles or a rapid removal of the complex from Mycobacterium phagosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sturgill-Koszycki, S -- Schlesinger, P H -- Chakraborty, P -- Haddix, P L -- Collins, H L -- Fok, A K -- Allen, R D -- Gluck, S L -- Heuser, J -- Russell, D G -- AI26889/AI/NIAID NIH HHS/ -- AI34207/AI/NIAID NIH HHS/ -- AR42370/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):678-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University Medical Center, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303277" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Hydrogen-Ion Concentration ; Leishmania mexicana/physiology ; Lysosome-Associated Membrane Glycoproteins ; Macrophages/metabolism/*microbiology/parasitology/ultrastructure ; Membrane Fusion ; Membrane Glycoproteins/metabolism ; Mice ; Microscopy, Immunoelectron ; Mycobacterium avium/*physiology ; Mycobacterium tuberculosis/physiology ; Phagosomes/metabolism/*microbiology/parasitology/ultrastructure ; Proton-Translocating ATPases/*metabolism ; Vacuoles/metabolism/microbiology/parasitology/ultrastructure
    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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  • 7
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    Lunar laser ranging: a continuing legacy of the apollo program (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-22
    Description: On 21 July 1969, during the first manned lunar mission, Apollo 11, the first retroreflector array was placed on the moon, enabling highly accurate measurements of the Earthmoon separation by means of laser ranging. Lunar laser ranging (LLR) turns the Earthmoon system into a laboratory for a broad range of investigations, including astronomy, lunar science, gravitational physics, geodesy, and geodynamics. Contributions from LLR include the three-orders-of-magnitude improvement in accuracy in the lunar ephemeris, a several-orders-of-magnitude improvement in the measurement of the variations in the moon's rotation, and the verification of the principle of equivalence for massive bodies with unprecedented accuracy. Lunar laser ranging analysis has provided measurements of the Earth's precession, the moon's tidal acceleration, and lunar rotational dissipation. These scientific results, current technological developments, and prospects for the future are discussed here.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickey, J O -- Bender, P L -- Faller, J E -- Newhall, X X -- Ricklefs, R L -- Ries, J G -- Shelus, P J -- Veillet, C -- Whipple, A L -- Wiant, J R -- Williams, J G -- Yoder, C F -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):482-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17781305" target="_blank"〉PubMed〈/a〉
    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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  • 8
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    Ceramic thin-film formation on functionalized interfaces through biomimetic processing (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: Processing routes have been developed for the production of thin ceramic films through precipitation from aqueous solutions. The techniques are based on crystal nucleation and growth onto functionalized interfaces. Surface functionalization routes have been developed by the mimicking of schemes used by organisms to produce complex ceramic composites such as teeth, bones, and shells. High-quality, dense polycrystalline films of oxides, hydroxides, and sulfides have now been prepared from "biomimetic" synthesis techniques. Ceramic films can be synthesized on plastics and other materials at temperatures below 100 degrees C. As a low-temperature process in which water rather than organic solvents is used, this synthesis is environmentally benign. Nanocrystalline ceramics can be produced, sometimes with preferred crystallite orientation. The direct deposition of high-resolution patterned films has also been demonstrated. The process is well suited to the production of organic-inorganic composites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bunker, B C -- Rieke, P C -- Tarasevich, B J -- Campbell, A A -- Fryxell, G E -- Graff, G L -- Song, L -- Liu, J -- Virden, J W -- McVay, G L -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):48-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17778133" target="_blank"〉PubMed〈/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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  • 9
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    Block in nuclear localization of period protein by a second clock mutation, timeless (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-18
    Description: In wild-type Drosophila, the period protein (PER) is found in nuclei of the eyes and brain, and PER immunoreactivity oscillates with a circadian rhythm. The studies described here indicate that the nuclear localization of PER is blocked by timeless (tim), a second chromosome mutation that, like per null mutations, abolishes circadian rhythms. PER fusion proteins without a conserved domain (PAS) and some flanking sequences are nuclear in tim mutants. This suggests that a segment of PER inhibits nuclear localization in tim mutants. The tim gene may have a role in establishing rhythms of PER abundance and nuclear localization in wild-type flies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vosshall, L B -- Price, J L -- Sehgal, A -- Saez, L -- Young, M W -- GM07982-09/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1606-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, National Science Foundation Science and Technology Center for Biological Timing, and Laboratory of Genetics, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128247" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/*genetics ; Cell Nucleus/*metabolism ; Circadian Rhythm/*genetics ; Cytoplasm/metabolism ; Drosophila Proteins ; Drosophila melanogaster/genetics/*metabolism ; Gene Expression ; *Genes, Insect ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Phenotype ; Recombinant Fusion Proteins/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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  • 10
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    Association of Intestinal Peptide Transport with a Protein Related to the Cadherin Superfamily (1994)
    American Association for the Advancement of Science
    Details
    Publication Date: 1994-04-15
    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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