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  • Transcription, Genetic  (65)
  • American Association for the Advancement of Science (AAAS)  (65)
  • American Chemical Society
  • International Union of Crystallography (IUCr)
  • 1985-1989  (52)
  • 1980-1984  (13)
  • 1945-1949
Sammlung
Schlagwörter
Verlag/Herausgeber
  • American Association for the Advancement of Science (AAAS)  (65)
  • American Chemical Society
  • International Union of Crystallography (IUCr)
Erscheinungszeitraum
Jahr
  • 11
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    Structural heterogeneity and functional domains of murine immunoglobulin G Fc receptors (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1986-11-07
    Beschreibung: Binding of antibodies to effector cells by way of receptors to their constant regions (Fc receptors) is central to the pathway that leads to clearance of antigens by the immune system. The structure and function of this important class of receptors on immune cells is addressed through the molecular characterization of Fc receptors (FcR) specific for the murine immunoglobulin G isotype. Structural diversity is encoded by two genes that by alternative splicing result in expression of molecules with highly conserved extracellular domains and different transmembrane and intracytoplasmic domains. The proteins encoded by these genes are members of the immunoglobulin supergene family, most homologous to the major histocompatibility complex molecule E beta. Functional reconstitution of ligand binding by transfection of individual FcR genes demonstrates that the requirements for ligand binding are encoded in a single gene. These studies demonstrate the molecular basis for the functional heterogeneity of FcR's, accounting for the possible transduction of different signals in response to a single ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravetch, J V -- Luster, A D -- Weinshank, R -- Kochan, J -- Pavlovec, A -- Portnoy, D A -- Hulmes, J -- Pan, Y C -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- GM 36306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):718-25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2946078" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Base Sequence ; DNA/genetics ; Gene Expression Regulation ; Histocompatibility Antigens Class II/genetics ; Immunoglobulin G ; Lymphocytes/*physiology ; Macrophages/*physiology ; Membrane Proteins ; Mice ; Protein Conformation ; *Receptors, Fc/genetics ; Receptors, IgG ; Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 12
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    Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1987-02-20
    Beschreibung: Four clones were isolated from an adult human brain complementary DNA library with an oligonucleotide probe corresponding to the first 20 amino acids of the beta peptide of brain amyloid from Alzheimer's disease. The open reading frame of the sequenced clone coded for 97 amino acids, including the known amino acid sequence of this polypeptide. The 3.5-kilobase messenger RNA was detected in mammalian brains and human thymus. The gene is highly conserved in evolution and has been mapped to human chromosome 21.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldgaber, D -- Lerman, M I -- McBride, O W -- Saffiotti, U -- Gajdusek, D C -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):877-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3810169" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alzheimer Disease/*genetics ; Amino Acid Sequence ; Amyloid/*genetics ; *Chromosomes, Human, Pair 21 ; Cloning, Molecular ; DNA/genetics ; Humans ; Protein Conformation ; RNA, Messenger/genetics ; Solubility ; Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 13
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    In vivo uncoating and efficient expression of foreign mRNAs packaged in TMV-like particles (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1987-05-29
    Beschreibung: The ribonucleocapsids of many plant viruses are extremely stable. The protein coat protects the RNA genome against degradation during the accumulation and spread of progeny virions. Chimeric single-stranded RNA molecules were transcribed in vitro from recombinant plasmids and later encapsidated, in vitro, into ribonucleoprotein particles (pseudoviruses) 60 nanometers long that resembled tobacco mosaic virus. Transcripts encoding an assayable enzyme, chloramphenicol acetyltransferase (CAT), were packaged into pseudovirus particles to assess the utility of this single-stranded RNA delivery system in a wide range of cell types. In all cases, packaged CAT messenger RNA was uncoated and transiently expressed. Significantly higher levels of CAT activity were detected with packaged than with naked CAT messenger RNA after inoculation of plant protoplasts in the presence of polyethylene glycol or abrasive inoculation of intact leaf surfaces. Structural events that lead to the uncoating and expression of CAT messenger RNA showed no cell specificity. This observation may support the view that the comparatively restricted host range of a true plant virus results from events that occur later during the infection cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallie, D R -- Sleat, D E -- Watts, J W -- Turner, P C -- Wilson, T M -- New York, N.Y. -- Science. 1987 May 29;236(4805):1122-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3472350" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acetyltransferases/genetics ; Chloramphenicol O-Acetyltransferase ; Fabaceae/microbiology ; Genetic Engineering/*methods ; Plants, Medicinal ; Plants, Toxic ; Protoplasts/microbiology ; RNA, Messenger/*genetics ; Tobacco/microbiology ; *Tobacco Mosaic Virus ; Transcription, Genetic ; Virus Diseases/microbiology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 14
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    Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-05-13
    Beschreibung: The biosynthetic rates for both the transferrin receptor (TfR) and ferritin are regulated by iron. An iron-responsive element (IRE) in the 5' untranslated portion of the ferritin messenger RNA (mRNA) mediates iron-dependent control of its translation. In this report the 3' untranslated region of the mRNA for the human TfR was shown to be necessary and sufficient for iron-dependent control of mRNA levels. Deletion studies identified a 678-nucleotide fragment of the TfR complementary DNA that is critical for this iron regulation. Five potential stem-loops that resemble the ferritin IRE are contained within the region critical for TfR regulation. Each of two of the five TfR elements was independently inserted into the 5' untranslated region of an indicator gene transcript. In this location they conferred iron regulation of translation. Thus, an mRNA element has been implicated in the mediation of distinct regulatory phenomena dependent on the context of the element within the transcript.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Casey, J L -- Hentze, M W -- Koeller, D M -- Caughman, S W -- Rouault, T A -- Klausner, R D -- Harford, J B -- New York, N.Y. -- Science. 1988 May 13;240(4854):924-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2452485" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Base Sequence ; DNA/genetics ; DNA, Recombinant ; Ferritins/biosynthesis/*genetics ; Growth Hormone/genetics ; Humans ; Iron/*pharmacology ; Mice ; Plasmids ; Protein Biosynthesis/*drug effects ; RNA/*genetics ; RNA, Messenger/*genetics ; Receptors, Transferrin/biosynthesis/*genetics ; *Regulatory Sequences, Nucleic Acid ; Transcription, Genetic ; Transfection ; Transformation, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 15
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    Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1987-02-20
    Beschreibung: The amyloid beta protein has been identified as an important component of both cerebrovascular amyloid and amyloid plaques of Alzheimer's disease and Down syndrome. A complementary DNA for the beta protein suggests that it derives from a larger protein expressed in a variety of tissues. Overexpression of the gene in brain tissue from fetuses with Down syndrome (trisomy 21) can be explained by dosage since the locus encoding the beta protein maps to chromosome 21. Regional localization of this gene by both physical and genetic mapping places it in the vicinity of the genetic defect causing the inherited form of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanzi, R E -- Gusella, J F -- Watkins, P C -- Bruns, G A -- St George-Hyslop, P -- Van Keuren, M L -- Patterson, D -- Pagan, S -- Kurnit, D M -- Neve, R L -- AG00029/AG/NIA NIH HHS/ -- HD10658/HD/NICHD NIH HHS/ -- HD20118/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):880-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2949367" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alzheimer Disease/*genetics ; Amino Acid Sequence ; Amyloid/*genetics ; Amyloidosis/genetics ; Brain/physiopathology ; Chromosome Mapping ; *Chromosomes, Human, Pair 21 ; DNA/genetics ; Down Syndrome/genetics ; Gene Expression Regulation ; Genetic Linkage ; Humans ; RNA, Messenger/genetics ; Tissue Distribution ; Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 16
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    The 3' splice site of pre-messenger RNA is recognized by a small nuclear ribonucleoprotein (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1985-12-20
    Beschreibung: A component present in splicing extracts selectively binds the 3' splice site of a precursor messenger RNA (pre-mRNA) transcript of a human beta-globin gene. Since this component can be immunoprecipitated by either autoantibodies of the Sm class or antibodies specifically directed against trimethylguanosine, it is a small nuclear ribonucleoprotein (snRNP). Its interaction with the 3' splice site occurs rapidly even at 0 degrees C, does not require adenosine triphosphate, and is altered by certain mutations in the 3' splice site region. Binding is surprisingly insensitive to treatment of the extract with micrococcal nuclease. The U5 particle is the only abundant Sm snRNP with a capped 5' end that is equally resistant to micrococcal nuclease. This suggests that, in addition to the U1 and U2 snRNP's, U5 snRNP's participate in pre-mRNA splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chabot, B -- Black, D L -- LeMaster, D M -- Steitz, J A -- GM-26154/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1344-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2933810" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Binding Sites ; Globins/genetics ; Humans ; Nucleic Acid Conformation ; Nucleic Acid Precursors/*genetics/metabolism ; Protein Binding ; RNA Precursors ; *RNA Splicing ; RNA, Messenger/*genetics/metabolism ; Ribonucleoproteins/*genetics/metabolism ; Ribonucleoproteins, Small Nuclear ; Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 17
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    The x gene is essential for HTLV replication (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1985-07-05
    Beschreibung: The human T-cell leukemia viruses (HTLV) are associated with T-cell malignancies in man and will transform normal human T cells in vitro. The mechanism of malignant transformation by HTLV is unknown but appears to be distinct from that of other classes of retroviruses, which induce malignant transformation through viral or cellular oncogenes. Recently a new gene, termed x, was identified in HTLV. This gene has been hypothesized to be the transforming gene of HTLV because of its conservation within the HTLV class of retroviruses. By in vitro mutagenesis of the HTLV-II x gene, it is now demonstrated that the presence of a functional x gene product is necessary for efficient HTLV transcription. Therefore, these studies provide direct evidence for an important function of the x gene in HTLV replication. The functional analogies between the x gene and transcriptional regulatory genes of some DNA viruses suggest that these viruses share similar mechanisms for cellular transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, I S -- Slamon, D J -- Rosenblatt, J D -- Shah, N P -- Quan, S G -- Wachsman, W -- CA 09297/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):54-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990037" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Base Sequence ; Deltaretrovirus/*genetics/growth & development ; Genes, Viral ; Humans ; Mutation ; RNA, Viral/*biosynthesis ; Transcription, Genetic ; *Virus Replication
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 18
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    Amyloid protein precursor messenger RNAs: differential expression in Alzheimer's disease (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-08-26
    Beschreibung: In situ hybridization was used to assess total amyloid protein precursor (APP) messenger RNA and the subset of APP mRNA containing the Kunitz protease inhibitor (KPI) insert in 11 Alzheimer's disease (AD) and 7 control brains. In AD, a significant twofold increase was observed in total APP mRNA in nucleus basalis and locus ceruleus neurons but not in hippocampal subicular neurons, neurons of the basis pontis, or occipital cortical neurons. The increase in total APP mRNA in locus ceruleus and nucleus basalis neurons was due exclusively to an increase in APP mRNA lacking the KPI domain. These findings suggest that increased production of APP lacking the KPI domain in nucleus basalis and locus ceruleus neurons may play an important role in the deposition of cerebral amyloid that occurs in AD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palmert, M R -- Golde, T E -- Cohen, M L -- Kovacs, D M -- Tanzi, R E -- Gusella, J F -- Usiak, M F -- Younkin, L H -- Younkin, S G -- 5T32GM07250/GM/NIGMS NIH HHS/ -- AG06656/AG/NIA NIH HHS/ -- MH43444/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1080-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University, School of Medicine, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2457949" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alzheimer Disease/*genetics ; Amyloid/*genetics ; Bacteriophage lambda/genetics ; Brain/metabolism ; Cerebral Cortex/metabolism ; *Gene Expression Regulation ; Humans ; Locus Coeruleus/metabolism ; Neurons/metabolism ; Nucleic Acid Hybridization ; Operator Regions, Genetic ; Plasmids ; Protein Precursors/*genetics ; RNA/genetics ; RNA, Complementary ; RNA, Messenger/*genetics/metabolism ; Repressor Proteins/metabolism ; Transcription, Genetic ; Trypsin Inhibitors/genetics
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 19
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    The effect of histone gene deletions on chromatin structure in Saccharomyces cerevisiae (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-11-04
    Beschreibung: As a way of studying nucleosome assembly and maintenance in Saccharomyces cerevisiae, mutants bearing deletions or duplications of the genes encoding histones H2A and H2B were analyzed. Previous genetic analysis had shown that only one of these mutants exhibited dramatic and pleiotropic phenotypes. This mutant was also the only one that contained disrupted chromatin, suggesting that the original phenotypes were attributable to alterations in chromosome structure. The chromatin disruption in the mutant, however, did not extend over the entire genome, but rather was localized to specific regions. Thus, while the arrangement of nucleosomes over the HIS4 and GAL1 genes, the telomeres, and the long terminal repeats (delta sequences) of Ty retrotransposons appeared essentially normal, nucleosomes over the CYH2 and UBI4 genes and the centromere of chromosome III were dramatically disrupted. The observation that the mutant exhibited localized chromatin disruptions implies that the assembly or maintenance of nucleosomes differs over different parts of the yeast genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norris, D -- Dunn, B -- Osley, M A -- GM40118/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 4;242(4879):759-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2847314" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Centromere/ultrastructure ; Chromatin/physiology/*ultrastructure ; Chromosome Deletion ; DNA Transposable Elements ; Galactose ; Gene Expression Regulation ; Genes, Fungal ; Histidine ; Histones/*genetics ; Mutation ; Phenotype ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae/genetics/*ultrastructure ; Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 20
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    Human ribosomal RNA genes: orientation of the tandem array and conservation of the 5' end (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1988-01-01
    Beschreibung: The multiple copies of the human ribosomal RNA genes (rDNA) are arranged as tandem repeat clusters that map to the middle of the short arms of chromosomes 13, 14, 15, 21, and 22. Concerted evolution of the gene family is thought to be mediated by interchromosomal recombination between rDNA repeat units, but such events would also result in conservation of the sequences distal to the rDNA on these five pairs of chromosomes. To test this possibility, a DNA fragment spanning the junction between rDNA and distal flanking sequence has been cloned and characterized. Restriction maps, sequence data, and gene mapping studies demonstrate that (i) the rRNA genes are transcribed in a telomere-to-centromere direction, (ii) the 5' end of the cluster and the adjacent non-rDNA sequences are conserved on the five pairs of chromosomes, and (iii) the 5' end of the cluster is positioned about 3.7 kb upstream from the transcription initiation site of the first repeat unit. The data support a model of concerted evolution by interchromosomal recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worton, R G -- Sutherland, J -- Sylvester, J E -- Willard, H F -- Bodrug, S -- Dube, I -- Duff, C -- Kean, V -- Ray, P N -- Schmickel, R D -- HD-13506/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 1;239(4835):64-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics Department, Hospital for Sick Children, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3336775" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Biological Evolution ; Chromosomes, Human, Pair 13 ; Chromosomes, Human, Pair 14 ; Chromosomes, Human, Pair 15 ; Chromosomes, Human, Pair 21 ; Chromosomes, Human, Pair 22 ; Cloning, Molecular ; DNA, Ribosomal/*genetics ; Genes ; Humans ; RNA, Ribosomal/*genetics ; Sequence Homology, Nucleic Acid ; Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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