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  • 1
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    Control of a mucosal challenge and prevention of AIDS by a multiprotein DNA/MVA vaccine (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-08
    Description: Heterologous prime/boost regimens have the potential for raising high levels of immune responses. Here we report that DNA priming followed by a recombinant modified vaccinia Ankara (rMVA) booster controlled a highly pathogenic immunodeficiency virus challenge in a rhesus macaque model. Both the DNA and rMVA components of the vaccine expressed multiple immunodeficiency virus proteins. Two DNA inoculations at 0 and 8 weeks and a single rMVA booster at 24 weeks effectively controlled an intrarectal challenge administered 7 months after the booster. These findings provide hope that a relatively simple multiprotein DNA/MVA vaccine can help to control the acquired immune deficiency syndrome epidemic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amara, R R -- Villinger, F -- Altman, J D -- Lydy, S L -- O'Neil, S P -- Staprans, S I -- Montefiori, D C -- Xu, Y -- Herndon, J G -- Wyatt, L S -- Candido, M A -- Kozyr, N L -- Earl, P L -- Smith, J M -- Ma, H L -- Grimm, B D -- Hulsey, M L -- Miller, J -- McClure, H M -- McNicholl, J M -- Moss, B -- Robinson, H L -- P01 AI 43045/AI/NIAID NIH HHS/ -- P30 DA 12121/DA/NIDA NIH HHS/ -- P51 RR000165/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2001 Apr 6;292(5514):69-74.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center and Yerkes Regional Primate Research Center, Emory University, Atlanta, GA 30329, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11393868" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/administration & dosage/*immunology ; Acquired Immunodeficiency Syndrome/immunology/*prevention & control/virology ; Animals ; Antibodies, Viral/blood/immunology ; CD4-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/immunology ; Germinal Center/immunology ; HIV Antibodies/blood/immunology ; HIV-1/genetics/immunology/physiology ; Immunity, Mucosal ; Immunization, Secondary ; Immunologic Memory ; Interferon-gamma/biosynthesis ; Lymph Nodes/immunology ; Macaca mulatta ; SAIDS Vaccines/administration & dosage/immunology ; Simian Acquired Immunodeficiency Syndrome/immunology/prevention & ; control/virology ; Simian Immunodeficiency Virus/genetics/immunology/physiology ; T-Lymphocytes/immunology ; Vaccines, DNA/administration & dosage/*immunology ; Vaccines, Synthetic/administration & dosage/immunology ; Vaccinia virus/immunology ; Viral Load
    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
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    A single amino acid interchange yields reciprocal CTL specificities for HIV-1 gp160 (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-10-06
    Description: For the IIIB isolate of human immunodeficiency virus type-1 (HIV-1), the immunodominant determinant of the envelope protein gp160 for cytotoxic T lymphocytes (CTLs) of H-2d mice is in a region of high sequence variability among HIV-1 isolates. The general requirements for CTL recognition of peptide antigens and the relation of recognition requirements to the natural variation in sequence of the HIV were investigated. For this purpose, a CTL line specific for the homologous segment of the envelope from the MN isolate of HIV-1 and restricted by the same class I major histocompatibility (MHC) molecule (Dd) as the IIIB-specific CTLs was raised from mice immunized with MN-env-recombinant vaccinia virus. The IIIB-specific and MN-specific CTLs were completely non-cross-reactive. Reciprocal exchange of a single amino acid between the two peptide sequences, which differed in 6 of 15 residues, led to a complete reversal of the specificity of the peptides in sensitizing targets, such that the IIIB-specific CTLs lysed targets exposed to the singly substituted MN peptide and vice versa. These data indicate the importance of single residues in defining peptide epitopic specificity and have implications for both the effect of immune pressure on selection of viral mutants and the design of effective vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, H -- Merli, S -- Putney, S D -- Houghten, R -- Moss, B -- Germain, R N -- Berzofsky, J A -- New York, N.Y. -- Science. 1989 Oct 6;246(4926):118-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Metabolism Branch, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2789433" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Genes, MHC Class I ; HIV Envelope Protein gp160 ; HIV-1/*immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Molecular Sequence Data ; Retroviridae Proteins/*immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Viral Envelope Proteins/*immunology
    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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    Vaccinia virus: a tool for research and vaccine development (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: Vaccinia virus is no longer needed for smallpox immunization, but now serves as a useful vector for expressing genes within the cytoplasm of eukaryotic cells. As a research tool, recombinant vaccinia viruses are used to synthesize biologically active proteins and analyze structure-function relations, determine the targets of humoral- and cell-mediated immunity, and investigate the immune responses needed for protection against specific infectious diseases. When more data on safety and efficacy are available, recombinant vaccinia and related poxviruses may be candidates for live vaccines and for cancer immunotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moss, B -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1662-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047875" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteriophages/genetics ; Gene Expression ; Genetic Engineering/methods ; *Genetic Vectors ; Humans ; Recombinant Proteins ; *Vaccines, Synthetic ; *Vaccinia virus/genetics/immunology
    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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    Immunobiology and pathogenesis of hepatocellular injury in hepatitis B virus transgenic mice (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-04-20
    Description: The role of the immune response to hepatitis B virus (HBV)-encoded antigens in the pathogenesis of liver cell injury has not been defined because of the absence of appropriate experimental models. HBV envelope transgenic mice were used to show that HBV-encoded antigens are expressed at the hepatocyte surface in a form recognizable by major histocompatibility complex (MHC) class I-restricted, CD8+ cytotoxic T lymphocytes specific for a dominant T cell epitope within the major envelope polypeptide and by envelope-specific antibodies. Both interactions led to the death of the hepatocyte in vivo, providing direct evidence that hepatocellular injury in human HBV infection may also be immunologically mediated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moriyama, T -- Guilhot, S -- Klopchin, K -- Moss, B -- Pinkert, C A -- Palmiter, R D -- Brinster, R L -- Kanagawa, O -- Chisari, F V -- CA34635/CA/NCI NIH HHS/ -- CA38635/CA/NCI NIH HHS/ -- CA40489/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Apr 20;248(4953):361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1691527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line, Transformed ; Cytotoxicity, Immunologic ; Epitopes/immunology ; Hepatitis B/*immunology ; Hepatitis B Surface Antigens/genetics/*immunology ; Histocompatibility Antigens Class I/immunology ; Liver/*immunology ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Simian virus 40 ; T-Lymphocytes, Cytotoxic/immunology ; T-Lymphocytes, Regulatory/immunology ; 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
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    Induction of Plasmodium falciparum transmission-blocking antibodies by recombinant vaccinia virus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: Many candidate antigens of malaria vaccines have limited immunological recognition. One exception is Pfs25, a cysteine-rich, 25-kilodalton sexual stage surface protein of Plasmodium falciparum. Pfs25 is a target of monoclonal antibodies that block transmission of malaria from vertebrate host to mosquito vector. The surface of mammalian cells infected with a recombinant vaccinia virus that expressed Pfs25 specifically bound transmission-blocking monoclonal antibodies. Furthermore, major histocompatibility complex-disparate congenic mouse strains immunized with recombinant Pfs25 elicited transmission-blocking antibodies, demonstrating that the capacity to develop transmission-blocking antibodies is not genetically restricted in mice. Live recombinant viruses may provide an inexpensive, easily administered alternative to subunit vaccines prepared from purified recombinant proteins to block transmission of malaria in developing countries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaslow, D C -- Isaacs, S N -- Quakyi, I A -- Gwadz, R W -- Moss, B -- Keister, D B -- New York, N.Y. -- Science. 1991 May 31;252(5010):1310-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Malaria Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925544" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/analysis/immunology ; Antibodies, Protozoan/*immunology ; Antigens, Protozoan ; Immunization ; Malaria, Falciparum/*prevention & control ; Mice ; Plasmodium falciparum/*immunology ; Protozoan Proteins/genetics/*immunology ; Recombinant Proteins/immunology ; Transfection ; Vaccinia virus/genetics/*immunology
    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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    Plasmodium knowlesi sporozoite antigen: expression by infectious recombinant vaccinia virus (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: The gene coding for the circumsporozoite antigen of the malaria parasite Plasmodium knowlesi was inserted into the vaccinia virus genome under the control of a defined vaccinia virus promoter. Cells infected with the recombinant virus synthesized polypeptides of 53,000 to 56,000 daltons that reacted with monoclonal antibody against the repeating epitope of the malaria protein. Furthermore, rabbits vaccinated with the recombinant virus produced antibodies that bound specifically to sporozoites. These data provide evidence for expression of a cloned malaria gene in mammalian cells and illustrate the potential of vaccinia virus recombinants as live malaria vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, G L -- Godson, G N -- Nussenzweig, V -- Nussenzweig, R S -- Barnwell, J -- Moss, B -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):397-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6200932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; Antigens, Surface/analysis/*genetics/immunology ; *Cloning, Molecular ; *DNA, Recombinant ; Epitopes/immunology ; Genes ; Genes, Viral ; Genetic Vectors ; Operon ; Plasmodium/*genetics/immunology ; Rabbits ; Vaccination ; Vaccinia virus/*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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  • 7
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    Limited immunological recognition of critical malaria vaccine candidate antigens (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-28
    Description: Current vaccine development strategies for malaria depend on widespread immunological responsiveness to candidate antigens such as the zygote surface antigens and the sporozoite coat protein, the circumsporozoite (CS) protein. Since immunological responsiveness is controlled mainly by genes mapping within the major histocompatibility complex (MHC), the humoral immune response to the zygote surface antigens and the cytotoxic T lymphocyte (CTL) response to the CS protein were examined in MHC-disparate congenic mouse strains. Only two of six strains responded to the 230-kilodalton zygote surface antigen and another two strains responded to the 48/45-kilodalton surface antigen. From two mouse strains, expressing between them five different class I MHC molecules, there was recognition of only a single CTL epitope from the CS protein, which was from a polymorphic segment of the molecule. The restricted CTL response to this protein parallels the restricted antibody response to this protein observed in humans and mice. These findings suggest that subunit malaria vaccines now being developed may be ineffective.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Good, M F -- Miller, L H -- Kumar, S -- Quakyi, I A -- Keister, D -- Adams, J H -- Moss, B -- Berzofsky, J A -- Carter, R -- New York, N.Y. -- Science. 1988 Oct 28;242(4878):574-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2902690" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Protozoan/biosynthesis ; Antigens, Protozoan/*immunology ; Antigens, Surface/genetics/immunology ; CD4-Positive T-Lymphocytes/immunology ; Genes, MHC Class II ; Immunity, Cellular ; Lymphocyte Cooperation ; Malaria/*prevention & control ; Mice ; Plasmodium falciparum/*immunology ; *Protozoan Proteins ; T-Lymphocytes, Cytotoxic/immunology ; Transfection ; Vaccines/*immunology ; Zygote/immunology
    Print ISSN: 0036-8075
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  • 8
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    Vaccinia virus recombinant expressing herpes simplex virus type 1 glycoprotein D prevents latent herpes in mice (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: In humans, herpes simplex virus causes a primary infection and then often a latent ganglionic infection that persists for life. Because these latent infections can recur periodically, vaccines are needed that can protect against both primary and latent herpes simplex infections. Infectious vaccinia virus recombinants that contain the herpes simplex virus type 1 (HSV-1) glycoprotein D gene under control of defined early or late vaccinia virus promoters were constructed. Tissue culture cells infected with these recombinant viruses synthesized a glycosylated protein that had the same mass (60,000 daltons) as the glycoprotein D produced by HSV-1. Immunization of mice with one of these recombinant viruses by intradermal, subcutaneous, or intraperitoneal routes resulted in the production of antibodies that neutralized HSV-1 and protected the mice against subsequent lethal challenge with HSV-1 or HSV-2. Immunization with the recombinant virus also protected the majority of the mice against the development of a latent HSV-1 infection of the trigeminal ganglia. This is the first demonstration that a genetically engineered vaccine can prevent the development of latency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cremer, K J -- Mackett, M -- Wohlenberg, C -- Notkins, A L -- Moss, B -- New York, N.Y. -- Science. 1985 May 10;228(4700):737-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986288" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/immunology ; *Genetic Engineering ; Herpes Simplex/immunology/*prevention & control ; Humans ; Mice ; Mice, Inbred BALB C ; Simplexvirus/genetics/immunology ; Vaccines ; Vaccinia virus/*genetics ; *Viral Envelope Proteins ; Viral Proteins/*genetics/immunology
    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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    Vaccinia virus recombinants: expression of VSV genes and protective immunization of mice and cattle (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-25
    Description: Vesicular stomatitis virus (VSV) causes a contagious disease of horses, cattle, and pigs. When DNA copies of messenger RNA's for the G or N proteins of VSV were linked to a vaccinia virus promoter and inserted into the vaccinia genome, the recombinants retained infectivity and synthesized VSV polypeptides. After intradermal vaccination with live recombinant virus expressing the G protein, mice produced VSV-neutralizing antibodies and were protected against lethal encephalitis upon intravenous challenge with VSV. In cattle, the degree of protection against intradermalingually injected VSV was correlated with the level of neutralizing antibody produced following vaccination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackett, M -- Yilma, T -- Rose, J K -- Moss, B -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):433-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981435" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/analysis ; Cattle ; Cattle Diseases/prevention & control ; *Cloning, Molecular ; DNA, Recombinant ; Genes, Viral ; *Membrane Glycoproteins ; Mice ; Operon ; Stomatitis/prevention & control/veterinary ; Vaccination/veterinary ; Vaccinia virus/*genetics ; Vesicular stomatitis Indiana virus/genetics/*immunology ; *Viral Envelope Proteins ; Viral Proteins/biosynthesis/*immunology ; Viral Vaccines/*immunology ; Virus Diseases/prevention & control/*veterinary
    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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  • 10
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    Construction of synthetic immunogen: use of new T-helper epitope on malaria circumsporozoite protein (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-02-27
    Description: The circumsporozoite (CS) protein of Plasmodium falciparum is the focus of intense efforts to develop an antisporozoite malaria vaccine. Localization of sites for T-cell recognition on this molecule is critical for vaccine design. By using an algorithm designed to predict T-cell sites and a large panel of H-2 congenic mice, a major nonrepetitive T-cell site was located. When a synthetic peptide corresponding to this site was covalently linked to the major B-cell site on the molecule, an immunogen capable of eliciting a high-titer antibody response was formed. This peptide sequence could prime helper T cells for a secondary response to the intact CS protein. The new helper T-cell site is located outside the repetitive region of the CS protein and appears to be the immunodominant T site on the molecule. This approach should be useful in the rational design and construction of vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Good, M F -- Maloy, W L -- Lunde, M N -- Margalit, H -- Cornette, J L -- Smith, G L -- Moss, B -- Miller, L H -- Berzofsky, J A -- New York, N.Y. -- Science. 1987 Feb 27;235(4792):1059-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2434994" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Antigens, Protozoan/immunology ; Antigens, Surface/*immunology ; B-Lymphocytes/immunology ; Epitopes/*immunology ; Mice ; Peptide Fragments/chemical synthesis/*immunology ; Plasmodium falciparum/*immunology ; *Protozoan Proteins ; Receptors, Antigen, B-Cell/immunology ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/immunology ; T-Lymphocytes, Helper-Inducer/*immunology ; Vaccines/immunology
    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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