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  • Articles  (10)
  • Molecular Weight  (10)
  • American Association for the Advancement of Science (AAAS)  (10)
  • American Geophysical Union
  • Blackwell Publishing Ltd
  • 1985-1989  (10)
  • 1980-1984
  • 1970-1974
  • 1986  (10)
Collection
  • Articles  (10)
Source
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (10)
  • American Geophysical Union
  • Blackwell Publishing Ltd
Years
  • 1985-1989  (10)
  • 1980-1984
  • 1970-1974
Year
Journal
Topic
  • 1
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    Propolypeptide of von Willebrand factor circulates in blood and is identical to von Willebrand antigen II (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-23
    Description: The generally mild bleeding disorder of von Willebrand disease is associated with abnormalities of two distinct plasma proteins, the large multimeric von Willebrand factor (vWF), which mediates platelet adhesion, and von Willebrand antigen II (vW AgII), which is of unknown function. The two proteins were found to have a common biosynthetic origin in endothelial cells and megakaryocytes, which explains their simultaneous absence in the severe form of this hereditary disease. Shared amino acid sequences from a 100-kilodalton plasma glycoprotein and from vW AgII are identical to amino acid sequences predicted from a complementary DNA clone encoding the 5' end of vWF. In addition, these proteins have identical molecular weights and immunologic cross reactivities. Monoclonal antibodies prepared against both proteins recognize epitopes on the pro-vWF subunit and on a 100-kilodalton protein that are not present on the mature vWF subunit in endothelial cell lysates. In contrast, polyclonal antibodies against vWF recognize both pro-vWF and vWF subunits. Thus, the 100-kilodalton plasma glycoprotein and vW AgII are identical proteins and represent an extremely large propolypeptide that is first cleaved from pro-vWF during intracellular processing and then released into plasma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fay, P J -- Kawai, Y -- Wagner, D D -- Ginsburg, D -- Bonthron, D -- Ohlsson-Wilhelm, B M -- Chavin, S I -- Abraham, G N -- Handin, R I -- Orkin, S H -- HL-30616/HL/NHLBI NIH HHS/ -- HL-34050/HL/NHLBI NIH HHS/ -- HL-34787/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 23;232(4753):995-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3486471" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens/immunology/*metabolism ; Blood Proteins/immunology/metabolism ; Endothelium/metabolism ; Humans ; Molecular Weight ; Peptide Fragments/analysis ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; von Willebrand Factor/*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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  • 2
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    Studies of the human c-myb gene and its product in human acute leukemias (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-07-18
    Description: The myb gene is the transforming oncogene of the avian myeloblastosis virus (AMV); its normal cellular homolog, c-myb, is conserved across a broad span of evolution. In humans, c-myb is expressed in malignant hematopoietic cell lines and in primary hematopoietic tumors. Partial complementary DNA clones were generated from blast cells of patients with acute myelogenous leukemia. The sequences of the clones were compared to the c-myb of other species, as well as the v-myb of AMV. In addition, the carboxyl terminal region of human c-myb was placed in an expression vector to obtain protein for the generation of antiserum, which was used to identify the human c-myb gene product. Like v-myb, this protein was found within the nucleus of leukemic cells where it was associated with the nuclear matrix. These studies provide further evidence that c-myb might be involved in human leukemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slamon, D J -- Boone, T C -- Murdock, D C -- Keith, D E -- Press, M F -- Larson, R A -- Souza, L M -- CA36827/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):347-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014652" target="_blank"〉PubMed〈/a〉
    Keywords: *Aspartate Carbamoyltransferase ; Avian Leukosis Virus/*genetics ; Avian Myeloblastosis Virus/*genetics ; Base Sequence ; *Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) ; Cell Line ; Cloning, Molecular ; DNA/analysis ; DNA Restriction Enzymes/metabolism ; *Dihydroorotase ; Escherichia coli/genetics ; Hematopoietic Stem Cells/microbiology ; Humans ; Leukemia, Myeloid, Acute/*genetics ; Molecular Weight ; *Multienzyme Complexes ; *Oncogenes ; Proteins/analysis
    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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    Antiserum to a synthetic peptide recognizes the HTLV-III envelope glycoprotein (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-28
    Description: In a study performed to determine which regions of the human T-cell lymphotrophic virus type III (HTLV-III) may represent vaccine candidates to prevent the acquired immune deficiency syndrome (AIDS), a synthetic peptide corresponding to amino acid sequence 735 to 752 of the precursor envelope glycoprotein of HTLV-III was used to immunize rabbits. The resulting rabbit antiserum to the synthetic peptide specifically recognized the precursor envelope glycoprotein (gp160) of HTLV-III. Human sera positive for antibody to HTLV-III reacted with this peptide. These findings indicate that synthetic peptides can be used to induce an immune response directed against a native envelope glycoprotein epitope of HTLV-III. The data are discussed in terms of using synthetic peptides to identify antigenic determinants involved in the induction of protective immunity and possibly as vaccine candidates against the etiologic agent of AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kennedy, R C -- Henkel, R D -- Pauletti, D -- Allan, J S -- Lee, T H -- Essex, M -- Dreesman, G R -- N0I-HL-23505/HL/NHLBI NIH HHS/ -- R23-AI-22307-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1556-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006246" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/*immunology ; Antibody Specificity ; Antigens, Viral/*immunology ; Deltaretrovirus/*immunology ; Humans ; Molecular Weight ; Peptides/chemical synthesis/*immunology ; Rabbits ; Solubility ; 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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  • 4
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    HTLV-III/LAV-neutralizing antibodies to an E. coli-produced fragment of the virus envelope (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-12
    Description: Immunization with either an Escherichia coli recombinant segment of the human T-cell lymphotropic virus (HTLV-III/LAV) envelope protein (gp 120) or with deglycosylated gp 120 envelope protein produced antibodies that neutralize HTLV-III/LAV infection in vitro. Virus neutralization titers of these antisera were equivalent to those obtained with purified native gp120 as immunogen. This localizes at least one class of neutralizing epitopes to the carboxyl-terminal half of the molecule. In addition, native gp120 prevented HTLV-III/LAV--mediated cell fusion, whereas the recombinant gp120 fragment did not. This shows that although glycosylation is not required for induction of neutralizing antibodies, it may be important for interaction with CD4, the virus receptor. A segment of the HTLV-III/LAV envelope produced in E. coli may be an important ingredient of a vaccine for acquired immune deficiency syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Putney, S D -- Matthews, T J -- Robey, W G -- Lynn, D L -- Robert-Guroff, M -- Mueller, W T -- Langlois, A J -- Ghrayeb, J -- Petteway, S R Jr -- Weinhold, K J -- 1PO1-CA43447-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 12;234(4782):1392-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2431482" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Viral/*immunology ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Epitopes/analysis ; Escherichia coli/*genetics ; HIV Antibodies ; Humans ; Immunization ; Molecular Weight ; Receptors, Virus/metabolism ; Recombinant Proteins/immunology ; Viral Envelope Proteins/genetics/*immunology
    Print ISSN: 0036-8075
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  • 5
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    Transition state analogs as ligands for affinity purification of juvenile hormone esterase (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-09-05
    Description: Insect juvenile hormones are metabolized in numerous species of caterpillars by low abundance, highly specific esterases. Because of their role in regulating and possibly disrupting juvenile hormone titer and thus insect metamorphosis, they are of interest to developmental biologists as well as scientists interested in selective insect control. However, the enzymes have defied attempts to purify and characterize them. Juvenile hormone esterase activity can be inhibited by a variety of 3-substituted 1,1,1-trifluoropropanone sulfides. These apparent transition state analogs were used as ligands and eluting agents to purify juvenile hormone esterase from four insect species from 500-fold to over 1000-fold in high yield. After elution from the affinity column, the enzymes were radiolabeled with paraoxon and analyzed by electrophoresis, and the results demonstrate a high degree of purity. Transition state analogs may be useful for the affinity purification of other enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abdel-Aal, Y A -- Hammock, B D -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1073-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3738525" target="_blank"〉PubMed〈/a〉
    Keywords: Acetone/*analogs & derivatives ; Animals ; Carboxylic Ester Hydrolases/antagonists & inhibitors/*isolation & purification ; Chromatography, Affinity/*methods ; Fluorine ; Hemolymph/enzymology ; Juvenile Hormones/*metabolism ; Ligands ; Molecular Weight ; Moths ; Paraoxon/pharmacology
    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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    A neuronal antigen in the brains of Alzheimer patients (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-02
    Description: A monoclonal antibody was prepared against pooled homogenates of brain tissue from patients with Alzheimer's disease. This antibody recognizes an antigen present in much higher concentration in certain brain regions of Alzheimer patients than in normal brain. The antigen appears to be a protein present in neurons involved in the formation of neuritic plaques and neurofibrillary tangles, and in some morphologically normal neurons in sections from Alzheimer brains. Partial purification and Western blot analysis revealed the antigen from Alzheimer brain to be a single protein with a molecular weight of 68,000. Application of the same purification procedure to normal brain tissue results in the detection of small amounts of a protein of lower molecular weight.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolozin, B L -- Pruchnicki, A -- Dickson, D W -- Davies, P -- CA13330/CA/NCI NIH HHS/ -- T32 GM7288/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 May 2;232(4750):648-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3083509" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*immunology ; Antibodies, Monoclonal/immunology ; Antigens/immunology/isolation & purification ; Brain/cytology/*immunology ; Cerebral Cortex/cytology/immunology ; Choline O-Acetyltransferase/immunology ; Chromatography, Gel ; Enzyme-Linked Immunosorbent Assay ; Hippocampus/cytology/immunology ; Humans ; Intermediate Filaments/immunology ; Microtubule-Associated Proteins/immunology ; Molecular Weight ; Nerve Tissue Proteins/immunology/isolation & purification ; Neurons/immunology ; tau Proteins
    Print ISSN: 0036-8075
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  • 7
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    The ninth component of complement and the pore-forming protein (perforin 1) from cytotoxic T cells: structural, immunological, and functional similarities (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-07-11
    Description: The ninth component of complement (C9) and the pore-forming protein (PFP or perforin) from cytotoxic T lymphocytes polymerize to tubular lesions having an internal diameter of 100 A and 160 A, respectively, when bound to lipid bilayers. Polymerized C9, assembled by slow spontaneous or rapid Zn2+-induced polymerization, and polyperforin, which is assembled only in the presence of Ca2+, constitute large aqueous pores that are stable, nonselective for solutes, and insensitive to changes of membrane potential. Monospecific polyclonal antibodies to purified C9 and PFP show cross-reactivity, suggesting structural homology between the two molecules. The structural and functional homologies between these two killer molecules imply an active role for pore formation during cell lysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, J D -- Cohn, Z A -- Podack, E R -- AI070127/AI/NIAID NIH HHS/ -- AI18525/AI/NIAID NIH HHS/ -- CA3019/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):184-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425429" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Centrifugation, Isopycnic ; Complement C9/*immunology/physiology ; Cross Reactions ; Humans ; Ion Channels/physiology ; *Membrane Glycoproteins ; Membrane Proteins/*immunology/physiology ; Mice ; Molecular Weight ; Perforin ; Pore Forming Cytotoxic Proteins ; T-Lymphocytes, Cytotoxic/*physiology ; Zinc/physiology
    Print ISSN: 0036-8075
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  • 8
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    Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-14
    Description: Interleukin-2 (IL-2) binds to both high- and low-affinity classes of IL-2 receptors on activated T lymphocytes. Only the high-affinity receptors are involved in receptor-mediated endocytosis and normally transduce the mitogenic signals of IL-2; however, the structural features distinguishing the high- and low-affinity receptors are unknown. When 125I-labeled IL-2 was chemically cross-linked to activated human T lymphocytes, two major bands were identified. First, as predicted, a 68- to 72-kilodalton band, consisting of IL-2 (15.5 kilodaltons) cross-linked to the IL-2 receptor (55 kilodaltons), was observed. Second, an unpredicted 85- to 92-kilodalton moiety was detected. This band was not present when IL-2 was cross-linked to transfected C127 cells, which exclusively express low-affinity receptors. The data presented are most consistent with the existence of a 70- to 77-kilodalton glycoprotein subunit (p70) which, upon associating with the 55-kilodalton low-affinity receptor (p55), transforms it into a high-affinity site. It is proposed that p55 and p70 be referred to as the alpha and beta subunits, respectively, of the high-affinity IL-2 receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharon, M -- Klausner, R D -- Cullen, B R -- Chizzonite, R -- Leonard, W J -- New York, N.Y. -- Science. 1986 Nov 14;234(4778):859-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3095922" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; *Cross-Linking Reagents ; Humans ; Immunosorbent Techniques ; Interleukin-2/metabolism ; Leukemia, Lymphoid/metabolism ; Lymphocyte Activation ; Mice ; Molecular Weight ; Receptors, Immunologic/*metabolism ; Receptors, Interleukin-2 ; Succinimides ; T-Lymphocytes/metabolism
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  • 9
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    Separation of large DNA molecules by contour-clamped homogeneous electric fields (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: Electric fields can be manipulated by a method in which multiple electrodes are arranged along a closed contour and clamped to predetermined electric potentials. This method may be applied to a broad range of problems in the separation of macromolecules by gel electrophoresis. DNA molecules as large as 2 megabases can be well separated with a contour-clamped homogeneous electric field alternating between two orientations 120 degrees apart. The pattern of separation is independent of position in the gel, which is an advantage over previous methods. DNA less than 50 kilobases can be separated without distortion even at high voltage with a nonalternating contour-clamped homogeneous field. Decreased band broadening in DNA less than 200 bases can be achieved with a contour-clamped inhomogeneous field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chu, G -- Vollrath, D -- Davis, R W -- GM21891-12/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1582-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3538420" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*isolation & purification ; DNA, Fungal/isolation & purification ; Electricity ; Electrodes ; Electrophoresis/methods ; Molecular Weight ; Saccharomyces cerevisiae/genetics
    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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    Characterization of T cell receptor gamma chain expression in a subset of murine thymocytes (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-12
    Description: While much information exists about the structure and function of the clonally distributed T cell receptor (TCR) alpha beta heterodimer, little is known about the gamma protein, the product of a third rearranging TCR gene. An antiserum to a carboxyl-terminal peptide common to several of the murine gamma chain constant regions and a monoclonal antibody to the murine T3 complex were used to identify products of this TCR gene family in a subpopulation of Lyt2-, L3T4- thymocytes. This subpopulation does not express TCR alpha or full-length TCR beta messenger RNA. The gamma chain is a 35-kilodalton (kD) protein that is disulfide-bonded to a 45-kD partner and is associated with the T3 complex. Analysis of the glycosylation pattern of this thymic gamma chain revealed that the major variable region gamma (V gamma) gene transcribed in activated peripheral T cells is absent from this subpopulation. The cells that bear this second T cell receptor may therefore represent a distinct lineage differentiating within the thymus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lew, A M -- Pardoll, D M -- Maloy, W L -- Fowlkes, B J -- Kruisbeek, A -- Cheng, S F -- Germain, R N -- Bluestone, J A -- Schwartz, R H -- Coligan, J E -- New York, N.Y. -- Science. 1986 Dec 12;234(4782):1401-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3787252" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Disulfides/analysis ; Electrophoresis, Polyacrylamide Gel ; Glycosylation ; Macromolecular Substances ; Mice ; Molecular Weight ; RNA, Messenger/metabolism ; Receptors, Antigen, T-Cell/*biosynthesis/genetics ; Structure-Activity Relationship ; Thymus Gland/*metabolism
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