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  • Amino Acid Sequence  (43)
  • American Association for the Advancement of Science (AAAS)  (43)
  • American Geophysical Union (AGU)
  • 2015-2019
  • 1985-1989  (43)
  • 1945-1949
  • 1986  (43)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (43)
  • American Geophysical Union (AGU)
Years
  • 2015-2019
  • 1985-1989  (43)
  • 1945-1949
Year
  • 1
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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
    Publication Date: 1986-11-07
    Description: 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〉
    Keywords: 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
    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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    Cell surface molecule associated with lymphocyte homing is a ubiquitinated branched-chain glycoprotein (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-02-21
    Description: Partial amino acid sequence analysis of a purified lymphocyte homing receptor demonstrates the presence of two amino termini, one of which corresponds precisely to the amino terminus of ubiquitin. This observation extends the province of this conserved polypeptide to the cell surface and leads to a proposed model of the receptor complex as a core polypeptide modified by glycosylation and ubiquitination. Independent antibodies to ubiquitin serve to identify additional cell surface species, an indication that ubiquitination of cell surface proteins may be more general. It is proposed that functional binding of lymphocytes to lymph node high endothelial venules might involve the ubiquitinated region of the receptor; if true, cell surface ubiquitin could play a more general role in cell-cell interaction and adhesion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siegelman, M -- Bond, M W -- Gallatin, W M -- St John, T -- Smith, H T -- Fried, V A -- Weissman, I L -- AI 19512/AI/NIAID NIH HHS/ -- CA 09151/CA/NCI NIH HHS/ -- GM 31461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):823-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003913" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cell Movement ; Endothelium/metabolism ; Glycoproteins/metabolism/*physiology ; Glycoside Hydrolases/metabolism ; High Mobility Group Proteins/*metabolism ; Lymphocytes/*physiology ; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase ; Membrane Proteins/metabolism/*physiology ; Mice ; Molecular Weight ; Protein Processing, Post-Translational ; Receptors, Cell Surface/metabolism/*physiology ; Ubiquitins/immunology/*metabolism
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  • 3
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    Crystal structure analysis of deamino-oxytocin: conformational flexibility and receptor binding (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-02
    Description: Two crystal structures of deamino-oxytocin have been determined at better than 1.1A resolution from isomorphous replacement and anomalous scattering x-ray measurements. In each of two crystal forms there are two closely related conformers with disulfide bridges of different chirality, which may be important in receptor recognition and activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wood, S P -- Tickle, I J -- Treharne, A M -- Pitts, J E -- Mascarenhas, Y -- Li, J Y -- Husain, J -- Cooper, S -- Blundell, T L -- Hruby, V J -- AM-10080/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 May 2;232(4750):633-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Dimethyl Sulfoxide ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Oxytocin/*analogs & derivatives/metabolism ; Protein Conformation ; Receptors, Angiotensin/*metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Oxytocin ; X-Ray Diffraction
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  • 4
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    Deletion in cysteine-rich region of LDL receptor impedes transport to cell surface in WHHL rabbit (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-06-06
    Description: The Watanabe heritable hyperlipidemic (WHHL) rabbit, an animal with familial hypercholesterolemia, produces a mutant receptor for plasma low-density lipoprotein (LDL) that is not transported to the cell surface at a normal rate. Cloning and sequencing of complementary DNA's from normal and WHHL rabbits, shows that this defect arises from an in-frame deletion of 12 nucleotides that eliminates four amino acids from the cysteine-rich ligand binding domain of the LDL receptor. A similar mutation, detected by S1 nuclease mapping of LDL receptor messenger RNA, occurred in a patient with familial hypercholesterolemia whose receptor also fails to be transported to the cell surface. These findings suggest that animal cells may have fail-safe mechanisms that prevent the surface expression of improperly folded proteins with unpaired or improperly bonded cysteine residues.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451858/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451858/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamoto, T -- Bishop, R W -- Brown, M S -- Goldstein, J L -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1230-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3010466" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport ; *Chromosome Deletion ; Cloning, Molecular ; Cysteine/genetics ; Dna ; DNA Restriction Enzymes ; Genes ; Humans ; Hyperlipoproteinemia Type II/*genetics ; Mutation ; RNA, Messenger ; Rabbits ; Receptors, LDL/*genetics
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  • 5
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    T-cell recognition of Ia molecules selectively altered by a single amino acid substitution (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-17
    Description: T lymphocytes recognize foreign antigen together with allele-specific determinants on membrane-bound class I and class II (Ia) gene products of the major histocompatibility complex. To identify amino acids of class II molecules critical to this recognition process, the genes encoding the beta chains of the I-Ak molecule were cloned from a wild-type B-cell hybridoma and from an immunoselected variant subline showing distinct serological and T-cell stimulatory properties. Nucleotide sequencing and DNA-mediated gene transfer established that a single base transition (G----A) encoding a change from glutamic acid to lysine at position 67 in the I-Ak beta molecule accounted for all the observed phenotypic changes of the variant cells. These results confirm the importance of residues 62 to 78 in the amino terminal domain of I-A beta for class II-restricted T-cell recognition of antigen and demonstrate the ability of a single substitution in this region to alter this recognition event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, M A -- Glimcher, L A -- Nielsen, E A -- Paul, W E -- Germain, R N -- New York, N.Y. -- Science. 1986 Jan 17;231(4735):255-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3484558" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/immunology ; Base Sequence ; Cloning, Molecular ; Histocompatibility Antigens Class II/*immunology ; Humans ; Hybridomas/immunology ; Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C ; T-Lymphocytes/*immunology
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  • 6
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    A yeast gene that is essential for release from glucose repression encodes a protein kinase (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-09-12
    Description: The SNF1 gene plays a central role in carbon catabolite repression in the yeast Saccharomyces cerevisiae, namely that SNF1 function is required for expression of glucose-repressible genes. The nucleotide sequence of the cloned SNF1 gene was determined, and the predicted amino acid sequence shows that SNF1 encodes a 72,040-dalton polypeptide that has significant homology to the conserved catalytic domain of mammalian protein kinases. Specific antisera were prepared and used to identify the SNF1 protein. The protein was shown to transfer phosphate from adenosine triphosphate to serine and threonine residues in an in vitro autophosphorylation reaction. These findings indicate that SNF1 encodes a protein kinase and suggest that protein phosphorylation plays a critical role in regulation by carbon catabolite repression in eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celenza, J L -- Carlson, M -- GM34095/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 12;233(4769):1175-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Enzyme Repression ; Genes ; Glucose/*metabolism ; Phosphorylation ; Protein Kinases/biosynthesis/*genetics ; Saccharomyces cerevisiae/enzymology/*genetics
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  • 7
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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
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  • 8
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    Separation of DNA binding from the transcription-activating function of a eukaryotic regulatory protein (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-02-14
    Description: The yeast GAL4 protein (881 amino acids) binds to specific DNA sites upstream of target genes and activates transcription. Derivatives of this protein bearing as few as 74 amino terminal residues bind to these sites but fail to activate transcription. When appropriately positioned in front of a gene these derivatives act as repressors. These and related findings support the idea that GAL4 activates transcription by touching other DNA-bound proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keegan, L -- Gill, G -- Ptashne, M -- GM07598/GM/NIGMS NIH HHS/ -- GM32308/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 14;231(4739):699-704.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3080805" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Fungal/genetics/metabolism ; DNA, Recombinant ; DNA-Binding Proteins/*genetics/metabolism ; Fungal Proteins/genetics ; Galactose ; Gene Expression Regulation ; Repressor Proteins/genetics ; Saccharomyces cerevisiae/*genetics ; Transcription Factors/*genetics/metabolism ; *Transcription, Genetic ; beta-Galactosidase/genetics
    Print ISSN: 0036-8075
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  • 9
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    On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-21
    Description: Structural data are now available for comparing a penicillin target enzyme, the D-alanyl-D-alanine-peptidase from Streptomyces R61, with a penicillin-hydrolyzing enzyme, the beta-lactamase from Bacillus licheniformis 749/C. Although the two enzymes have distinct catalytic properties and lack relatedness in their overall amino acid sequences except near the active-site serine, the significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Dideberg, O -- Charlier, P -- Wery, J P -- Libert, M -- Moews, P C -- Knox, J R -- Duez, C -- Fraipont, C -- Joris, B -- 10RRO1955-01/RR/NCRR NIH HHS/ -- AI-10925/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 21;231(4744):1429-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3082007" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillus cereus/enzymology ; Binding Sites ; Carboxypeptidases/genetics/*metabolism ; Molecular Weight ; *Penicillin Resistance ; Protein Conformation ; *Serine-Type D-Ala-D-Ala Carboxypeptidase ; Streptomyces/enzymology ; X-Ray Diffraction ; beta-Lactamases/genetics/*metabolism
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  • 10
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    Thyrotropin-releasing hormone precursor: characterization in rat brain (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-10
    Description: To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic lambda gt11 library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lechan, R M -- Wu, P -- Jackson, I M -- Wolf, H -- Cooperman, S -- Mandel, G -- Goodman, R H -- AM 34540/AM/NIADDK NIH HHS/ -- CA 37370/CA/NCI NIH HHS/ -- P30 AM 39428/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):159-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*physiology ; DNA/genetics ; Hypothalamus/physiology ; Molecular Weight ; Protein Precursors/genetics/*physiology ; Pyrrolidonecarboxylic Acid/analogs & derivatives ; Rats ; Rats, Inbred Strains ; Thyrotropin-Releasing Hormone/genetics/*physiology
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  • 11
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    Active human-yeast chimeric phosphoglycerate kinases engineered by domain interchange (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: Phosphoglycerate kinase (PGK) is a monomeric protein composed of two domains of approximately equal size, connected by a hinge. Substrate-induced conformational change results in the closure of the active site cleft, which is situated between these two domains. In a study of the relations between structure and function of this enzyme, two interspecies hybrids were constructed, each composed of one domain from the human enzyme and one domain from the yeast enzyme. Despite a 35% difference in the amino acid composition between human and yeast PGK, catalytic properties of the hybrid enzymes are very similar to those of the parental proteins. This result demonstrates that the evolutionary substitutions within these two distantly related molecules do not significantly affect formation of the active site cleft, mechanism of domain closure, or enzyme activity itself.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mas, M T -- Chen, C Y -- Hitzeman, R A -- Riggs, A D -- R01 GM31263/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):788-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526552" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; *Chimera ; *Genes ; *Genes, Fungal ; Genetic Engineering ; Humans ; Kinetics ; Models, Molecular ; Phosphoglycerate Kinase/*genetics/metabolism ; Plasmids ; Protein Conformation ; Protein Multimerization ; Saccharomyces cerevisiae/enzymology/*genetics
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  • 12
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    Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-03
    Description: A sulfated, myotropic neuropeptide termed leucosulfakinin (Glu-Gln-Phe-Glu-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-NH2) was isolated from head extracts of the cockroach Leucophaea maderae. The peptide exhibits sequence homology with the hormonally active portion of the vertebrate hormones human gastrin II and cholecystokinin, suggesting that these peptides are evolutionarily related. Six of the 11 amino acid residues (55 percent) are identical to those in gastrin II. In addition, the intestinal myotropic action of leucosulfakinin is analogous to that of gastrin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nachman, R J -- Holman, G M -- Haddon, W F -- Ling, N -- New York, N.Y. -- Science. 1986 Oct 3;234(4772):71-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3749893" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aplysia ; Brachyura ; Cholecystokinin/genetics ; Cockroaches ; Gastrins/genetics ; Humans ; Insect Hormones/genetics/*isolation & purification/physiology ; Muscle Contraction/drug effects ; Nerve Tissue Proteins/genetics/*isolation & purification/physiology ; *Neuropeptides ; Sequence Homology, Nucleic Acid
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  • 13
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    Nucleotide sequence of SRV-1, a type D simian acquired immune deficiency syndrome retrovirus (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-28
    Description: Simian acquired immune deficiency syndrome (SAIDS) in the macaque genus of monkeys at the California Primate Research Center is apparently caused by infection by a type D retrovirus. The complete nucleotide sequence (8173 base pairs) of a molecular clone of the prototype SAIDS virus isolate, SRV-1, reveals a typical retrovirus structure with long terminal repeats (346 base pairs) and open reading frames for the gag (663 codons), pol (867 codons), and env (605 codons) genes. SRV-1 also has a separate open reading frame of 314 codons between the gag and pol genes that defines the viral protease gene (prt) and a short open reading frame of unknown significance downstream from the env gene. The SRV-1 protease region shows a high degree of homology to its counterpart in the hamster intracisternal A-type particle genome; both these protease genes are about twice as long as the analogous region of other retroviruses. SRV-1 has no notable similarity in either genetic organization or sequence to the human AIDS retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Power, M D -- Marx, P A -- Bryant, M L -- Gardner, M B -- Barr, P J -- Luciw, P A -- AI20573/AI/NIAID NIH HHS/ -- CA37467/CA/NCI NIH HHS/ -- RR00169/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1567-72.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006247" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology/*veterinary ; Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA Restriction Enzymes/metabolism ; Genes, Viral ; Macaca/*microbiology ; Peptide Hydrolases/genetics ; Retroviridae/*genetics ; Retroviridae Proteins/genetics ; Sequence Homology, Nucleic Acid
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  • 14
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    Trying to crack the second half of the genetic code (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-09-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1037-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3738524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Collagen/genetics ; *Genetic Code ; Humans ; *Protein Conformation ; Protein Denaturation ; Protein Processing, Post-Translational ; Structure-Activity Relationship ; X-Ray Diffraction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Molecular genetics of human color vision: the genes encoding blue, green, and red pigments (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-11
    Description: Human color vision is based on three light-sensitive pigments. The isolation and sequencing of genomic and complementary DNA clones that encode the apoproteins of these three pigments are described. The deduced amino acid sequences show 41 +/- 1 percent identity with rhodopsin. The red and green pigments show 96 percent mutual identity but only 43 percent identity with the blue pigment. Green pigment genes vary in number among color-normal individuals and, together with a single red pigment gene, are proposed to reside in a head-to-tail tandem array within the X chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nathans, J -- Thomas, D -- Hogness, D S -- New York, N.Y. -- Science. 1986 Apr 11;232(4747):193-202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2937147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cebidae ; Cercopithecidae ; Color ; Color Perception/*physiology ; DNA/metabolism ; Drosophila melanogaster ; Eye Proteins/genetics/physiology ; *Genes ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Photoreceptor Cells/physiology ; RNA, Messenger/genetics ; Retinal Pigments/*genetics ; Retinaldehyde/physiology ; Rhodopsin/genetics ; Rod Opsins ; X Chromosome
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  • 16
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    Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-28
    Description: Adhesive interactions of the platelet surface with plasma proteins such as fibrinogen and fibronectin play an important role in thrombosis and hemostasis. The binding of both of these proteins to platelets is inhibited by synthetic peptides containing the sequence Arg-Gly-Asp, which corresponds to the cell adhesion site in fibronectin and is also present in the alpha chain of fibrinogen. An affinity matrix made of an insolubilized heptapeptide containing the Arg-Gly-Asp sequence selectively binds the platelet membrane glycoprotein IIb/IIIa from detergent extracts of platelets. When incorporated into liposome membranes, the isolated protein confers to the liposomes the ability to bind to surfaces coated with fibrinogen, fibronectin, and vitronectin but not to surfaces coated with thrombospondin or albumin. This platelet receptor is related to the previously identified fibronectin and vitronectin receptors in that it recognizes an Arg-Gly-Asp sequence but differs from the other receptors in its wider specificity toward various adhesive proteins. These results establish the existence of a family of adhesion receptors that recognize the sequence Arg-Gly-Asp.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pytela, R -- Pierschbacher, M D -- Ginsberg, M H -- Plow, E F -- Ruoslahti, E -- CA38352/CA/NCI NIH HHS/ -- HL26838/HL/NHLBI NIH HHS/ -- HL28235/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1559-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2420006" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blood Platelets/*physiology ; *Cell Adhesion ; Fibrinogen/metabolism ; Fibronectins/metabolism ; Glycoproteins/*metabolism ; Humans ; Membrane Proteins/*metabolism ; Oligopeptides/*metabolism ; Platelet Membrane Glycoproteins ; Receptors, Cell Surface/*metabolism ; Structure-Activity Relationship ; Thrombospondins ; Vitronectin
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  • 17
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    Isolation and sequence of L3T4 complementary DNA clones: expression in T cells and brain (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-31
    Description: T lymphocytes express on their surface not only a specific receptor for antigen and major histocompatibility complex proteins, but also a number of additional glycoproteins that are thought to play accessory roles in the processes of recognition and signal transduction. L3T4 is one such T-cell surface protein that is expressed on most mouse thymocytes and on mature mouse T cells that recognize class II (Ia) major histocompatibility complex proteins. Such cells are predominantly of the helper/inducer phenotype. In this study, complementary DNA clones encoding L3T4 were isolated and sequenced. The predicted protein sequence shows that L3T4 is a member of the immunoglobulin gene superfamily. It is encoded by a single gene that does not require rearrangement prior to expression. Although the protein has not previously been demonstrated on nonhematopoietic cells, two messenger RNA species specific for L3T4 are found in brain. The minor species comigrates with the L3T4 transcript in T cells, whereas the major species is 1 kilobase smaller.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tourvieille, B -- Gorman, S D -- Field, E H -- Hunkapiller, T -- Parnes, J R -- 1 F32 CA07877-01/CA/NCI NIH HHS/ -- AI11313/AI/NIAID NIH HHS/ -- GM34991/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):610-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3094146" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Differentiation, T-Lymphocyte ; Antigens, Surface/genetics/*isolation & purification ; Base Sequence ; Brain/*metabolism ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Humans ; Mice ; Mice, Inbred C57BL ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Sequence Homology, Nucleic Acid ; T-Lymphocytes/*immunology/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    Solid phase synthesis (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merrifield, B -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):341-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961484" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; In Vitro Techniques ; Methods ; Nucleotides/*chemical synthesis ; Peptide Fragments/metabolism ; Peptides/*chemical synthesis ; Ribonuclease, Pancreatic/chemical synthesis/metabolism ; Structure-Activity Relationship
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  • 19
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    Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-07-18
    Description: A human complementary DNA whose protein product is considered to be the major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, and Gerstmann-Straussler syndrome has been identified and characterized. The extensive homology of this gene sequence to the hamster PrP 27- to 30-kilodalton prion protein complementary DNA clone, and its existence as a single copy in the human genome, leads to the conclusion that this is the human prion gene. This human prion gene has been mapped to human chromosome 20, negating a direct link between the prion protein and Down's syndrome or the amyloid of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liao, Y C -- Lebo, R V -- Clawson, G A -- Smuckler, E A -- CA 21141/CA/NCI NIH HHS/ -- CA 40145/CA/NCI NIH HHS/ -- KO4 CA 01003/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):364-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014653" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, 19-20 ; Chromosomes, Human, 21-22 and Y ; *Cloning, Molecular ; Creutzfeldt-Jakob Syndrome/genetics/microbiology ; Cricetinae ; DNA/*analysis ; DNA Restriction Enzymes/metabolism ; Humans ; Prions/*genetics ; Viral Proteins/analysis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Three-dimensional structure of the adenovirus major coat protein hexon (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-30
    Description: The three-dimensional crystal structure of the adenovirus major coat protein is presented. Adenovirus type 2 hexon, at 967 residues, is now the longest polypeptide whose structure has been determined crystallographically. Taken with our model for hexon packing, which positions the 240 trimeric hexons in the capsid, the structure defines 60% of the protein within the 150 X 10(6) dalton virion. The assembly provides the first details of a DNA-containing animal virus that is 20 times larger than the spherical RNA viruses previously described. Unexpectedly, the hexon subunit contains two similar beta-barrels whose topology is identical to those of the spherical RNA viruses, but whose architectural role in adenovirus is very different. The hexon structure reveals several distinctive features related to its function as a stable protective coat, and shows that the type-specific immunological determinants are restricted to the virion surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, M M -- White, J L -- Grutter, M G -- Burnett, R M -- AI 17270/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 May 30;232(4754):1148-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3704642" target="_blank"〉PubMed〈/a〉
    Keywords: *Adenoviridae/genetics/ultrastructure ; Amino Acid Sequence ; *Capsid/genetics/ultrastructure ; *Capsid Proteins ; Protein Conformation ; RNA Viruses/ultrastructure ; X-Ray Diffraction
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  • 21
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    Expression cloning of a lymphocyte homing receptor cDNA: ubiquitin is the reactive species (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-02-21
    Description: The lymphocyte cell surface receptor for the high endothelial venules (HEV's) of peripheral lymph nodes is specifically recognized by the monoclonal antibody MEL-14. Three independent complementary DNA (cDNA) clones, each of which encodes the protein ubiquitin, were detected by virtue of the expression of the MEL-14 antigenic determinant on cDNA-beta-galactosidase bacterial fusion proteins. The antigenic determinant defined by MEL-14 resides in the carboxyl terminal 13-amino-acid proteolytic peptide of ubiquitin, but is undetected in intact undenatured ubiquitin and other cellular ubiquitinated proteins. Antisera and monoclonal antibodies to ubiquitin determinants bind to the surface of both HEV-receptor positive and negative cell lines. The MEL-14-identified cDNA clones hydridize to RNA transcripts that encode tandemly repeated ubiquitins. Sequence analysis of these polyubiquitin cDNA's does not identify a leader sequence for export to the cell surface. The expression of the MEL-14 epitope of ubiquitin depends upon its local environment. The steady-state levels of expression of the ubiquitin messenger RNA's do not correlate with either the tissue derivation of the RNA or the expression of the lymphocyte HEV receptor. Regulation of the expression of the HEV receptor is not likely to reflect the transcriptional control of ubiquitin genes, but rather to reflect control of the expression of the HEV core polypeptide or its level or form of ubiquitination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St John, T -- Gallatin, W M -- Siegelman, M -- Smith, H T -- Fried, V A -- Weissman, I L -- AI19512/AI/NIAID NIH HHS/ -- CA 09151/CA/NCI NIH HHS/ -- GM 31461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):845-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003914" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology ; Antibody Specificity ; Base Sequence ; Cloning, Molecular ; Endothelium/metabolism ; Gene Expression Regulation ; High Mobility Group Proteins/*genetics ; Lymphatic System/metabolism ; Lymphocytes/*physiology ; Mice ; Receptors, Cell Surface/*genetics/immunology/metabolism ; Ubiquitins/*genetics/immunology/metabolism
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  • 22
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    Trypanosoma cruzi infection inhibited by peptides modeled from a fibronectin cell attachment domain (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-31
    Description: The mechanism by which Trypanosoma cruzi, the protozoan parasite that causes Chagas' disease, becomes attached to mammalian cells is not well understood. Fibronectin is thought to participate in the attachment, and in this study the region of fibronectin that interacts with the surface receptors of T. cruzi trypomastigotes was investigated by testing the binding of the amino acid sequence Arg-Gly-Asp-Ser, corresponding to the cell attachment site of fibronectin to T. cruzi trypomastigotes. Peptides with the sequence Arg-Gly-Asp-Ser, but not Arg-Phe-Asp-Ser, Arg-Phe-Asp-Ser-Ala-Ala-Arg-Phe-Asp, Ser-Lys-Pro, Glu-Ser-Gly, or Ala-Lys-Thr-Lys-Pro, bound to the parasite surface and inhibited cell invasion by the pathogen. Monoclonal antibodies to the cell attachment domain of fibronectin also inhibited cell infection by the parasite. The immunization of BALB/c mice with tetanus toxoid-conjugated peptide induced a significant protection against T. cruzi. The data support the notion that the sequence Arg-Gly-Asp-Ser of cell surface fibronectin acts as a recognition site for attachment of the parasites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ouaissi, M A -- Cornette, J -- Afchain, D -- Capron, A -- Gras-Masse, H -- Tartar, A -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):603-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3094145" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Chagas Disease/parasitology/*prevention & control ; Fibronectins/immunology/*physiology ; Mice ; Mice, Inbred BALB C ; Peptides/*therapeutic use ; Trypanocidal Agents/*therapeutic use ; Trypanosoma cruzi/drug effects
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  • 23
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    The oncogenic activation of human p21ras by a novel mechanism (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-08
    Description: Single amino acid changes were introduced into normal (non-oncogenic) and activated forms of the human H-ras protein at a position (residue 116) proposed on structural grounds to represent a contact site with guanine nucleotides. Substitutions at this site could significantly reduce the ability of both forms to bind and hydrolyze guanosine 5'-triphosphate; these substitutions, however, did not necessarily diminish the transforming capacity of activated derivatives. One substitution that severely impairs these functions activated the transforming potential of the otherwise normal polypeptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walter, M -- Clark, S G -- Levinson, A D -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):649-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3487832" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Transformation, Neoplastic/metabolism ; DNA/genetics ; Guanosine Triphosphate/metabolism ; Humans ; Neoplasm Proteins/*genetics/metabolism ; Oncogene Protein p21(ras) ; *Oncogenes
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  • 24
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    Pertussis toxin gene: nucleotide sequence and genetic organization (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-06-06
    Description: The current pertussis vaccines, although efficacious, in some instances produce undesirable side effects. Molecular engineering of pertussis toxin, the major protective antigen, could provide a safer, new generation of vaccines against whooping cough. As a first critical step in the development of such a vaccine, the complete nucleotide sequence of the pertussis toxin gene was determined and the amino acid sequences of the individual subunits were deduced. All five subunits are coded by closely linked cistrons. A promoter-like structure was found in the 5'-flanking region, suggesting that the toxin is expressed through a polycistronic messenger RNA. The order of the cistrons is S1, S2, S4, S5, and S3. All subunits contain signal peptides of variable length. The calculated molecular weights of the mature subunits are 26,024 for S1, 21,924 for S2, 21,873 for S3, 12,058 for S4, and 11,013 for S5. Subunits S2 and S3 share 70% amino acid homology and 75% nucleotide homology. Subunit S1 contains two regions of eight amino acids homologous to analogous regions in the A subunit of both cholera and Escherichia coli heat labile toxins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Locht, C -- Keith, J M -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1258-64.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3704651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Genes ; Molecular Weight ; *Pertussis Toxin ; Virulence Factors, Bordetella/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 25
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    The complete primary structure of protein kinase C--the major phorbol ester receptor (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-22
    Description: Protein kinase C, the major phorbol ester receptor, was purified from bovine brain and through the use of oligonucleotide probes based on partial amino acid sequence, complementary DNA clones were derived from bovine brain complementary DNA libraries. Thus, the complete amino acid sequence of bovine protein kinase C was determined, revealing a domain structure. At the amino terminal is a cysteine-rich domain with an internal duplication; a putative calcium-binding domain follows, and there is at the carboxyl terminal a domain that shows substantial homology, but not identity, to sequences of other protein kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parker, P J -- Coussens, L -- Totty, N -- Rhee, L -- Young, S -- Chen, E -- Stabel, S -- Waterfield, M D -- Ullrich, A -- New York, N.Y. -- Science. 1986 Aug 22;233(4766):853-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/metabolism ; *Caenorhabditis elegans Proteins ; Carrier Proteins ; Cattle ; Dna ; Models, Chemical ; Protein Biosynthesis ; *Protein Kinase C/isolation & purification ; RNA, Messenger/metabolism ; *Receptors, Drug ; *Receptors, Immunologic
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  • 26
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    Structure and diversity of the human T-cell receptor beta-chain variable region genes (1986)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1986-08-22
    Description: In order to characterize the variability of the expressed human T-cell receptor (TCR) beta-chain repertoire and contrast this variability to the known murine beta-chain repertoire, 15 independent complementary DNA (cDNA) clones containing TCR beta-chain variable region (V beta) genes were isolated from a human tonsil cDNA library. The nucleotide and derived amino acid sequences of these 15 V beta genes were analyzed together with 7 previously defined sequences. Fifteen different human V beta genes could be identified from 22 independent sequences. By means of DNA hybridization and sequence homology comparisons, it was possible to group these 15 genes into ten distinct V beta subfamilies, each containing from one to seven members. Minimal polymorphism was noted between individuals, except in multimember subfamilies. The amino acid sequences of these genes contain conserved amino acids that are also shared by murine TCR V beta genes and immunoglobulins; no features were found that distinguish human V beta genes from their murine counterparts. Evaluation of secondary structure showed that maximum variability coincides with generally hydrophilic portions of the amino acid sequence, while specific hydrophobic regions were conserved in all V beta genes examined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tillinghast, J P -- Behlke, M A -- Loh, D Y -- 2-T32-AI00112/AI/NIAID NIH HHS/ -- GM 07200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 22;233(4766):879-83.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755549" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Dna ; Genes ; Humans ; Nucleic Acid Hybridization ; Polymorphism, Genetic ; Receptors, Antigen, T-Cell/*genetics
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  • 27
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    The product of the human c-erbB-2 gene: a 185-kilodalton glycoprotein with tyrosine kinase activity (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-06-27
    Description: Antibodies were raised against a synthetic peptide corresponding to 14 amino acid residues at the COOH-terminus of a protein deduced from the human c-erbB-2 nucleotide sequence. These antibodies immunoprecipitated a 185-kilodalton glycoprotein from MKN-7 adenocarcinoma cells. Incubation of the immunoprecipitates with (gamma-32P)ATP resulted in the phosphorylation of this protein on tyrosine residues. These results indicate that the human c-erbB-2 gene product is the 185-kilodalton glycoprotein that is associated with tyrosine kinase activity. Although the c-erbB-2 protein was predicted to encode a protein very similar to epidermal growth factor (EGF) receptor, EGF did not stimulate this kinase activity either in vivo or in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akiyama, T -- Sudo, C -- Ogawara, H -- Toyoshima, K -- Yamamoto, T -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1644-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3012781" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Epidermal Growth Factor/metabolism ; *Genes ; Glycoproteins/genetics/isolation & purification/*metabolism ; HeLa Cells/metabolism ; Humans ; Molecular Weight ; Oncogenes ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism
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  • 28
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    URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-31
    Description: The polypeptide encoded in URF6, the last unassigned reading frame of human mitochondrial DNA, has been identified with antibodies to peptides predicted from the DNA sequence. Antibodies prepared against highly purified respiratory chain NADH dehydrogenase from beef heart or against the cytoplasmically synthesized 49-kilodalton iron-sulfur subunit isolated from this enzyme complex, when added to a deoxycholate or a Triton X-100 mitochondrial lysate of HeLa cells, specifically precipitated the URF6 product together with the six other URF products previously identified as subunits of NADH dehydrogenase. These results strongly point to the URF6 product as being another subunit of this enzyme complex. Thus, almost 60% of the protein coding capacity of mammalian mitochondrial DNA is utilized for the assembly of the first enzyme complex of the respiratory chain. The absence of such information in yeast mitochondrial DNA dramatizes the variability in gene content of different mitochondrial genomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chomyn, A -- Cleeter, M W -- Ragan, C I -- Riley, M -- Doolittle, R F -- Attardi, G -- GM-11726/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):614-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3764430" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cytochrome Reductases/*genetics ; DNA/*genetics/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Eukaryota/genetics ; Fungi/genetics ; HeLa Cells/metabolism ; Humans ; Mitochondria/enzymology ; NADH Dehydrogenase/*genetics ; Sequence Homology, Nucleic Acid
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    The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: Predictions of the structures of the antigen-binding domains of an antibody, recorded before its experimental structure determination and tested subsequently, were based on comparative analysis of known antibody structures or on conformational energy calculations. The framework, the relative positions of the hypervariable regions, and the folds of four of the hypervariable loops were predicted correctly. This portion includes all residues in contact with the antigen, in this case hen egg white lysozyme, implying that the main chain conformation of the antibody combining site does not change upon ligation. The conformations of three residues in each of the other two hypervariable loops are different in the predicted models and the experimental structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chothia, C -- Lesk, A M -- Levitt, M -- Amit, A G -- Mariuzza, R A -- Phillips, S E -- Poljak, R J -- GM25435/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):755-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3090684" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; *Antigen-Antibody Complex ; Chickens ; Egg White ; Female ; Immunoglobulin Fab Fragments ; *Immunoglobulin G ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; Immunoglobulin Variable Region ; Models, Molecular ; Muramidase/immunology ; Protein Conformation
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  • 30
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    Molecular cloning of the chicken progesterone receptor (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: To define the functional domains of the progesterone receptor required for gene regulation, complementary DNA (cDNA) clones encoding the chicken progesterone receptor have been isolated from a chicken oviduct lambda gt11 cDNA expression library. Positive clones expressed antigenic determinants that cross-reacted with six monospecific antibodies derived from two independent sources. A 36-amino acid peptide sequence obtained by microsequencing of purified progesterone receptor was encoded by nucleotide sequences in the longest cDNA clone. Analysis of the amino acid sequence of the progesterone receptor deduced from the cDNA clones revealed a cysteine-rich region that was homologous to a region found in the estrogen and glucocorticoid receptors and to the avian erythroblastosis virus gag-erb-A fusion protein. Northern blot analysis with chicken progesterone receptor cDNA's indicated the existence of at least three messenger RNA species. These messages were found only in oviduct and could be induced by estrogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conneely, O M -- Sullivan, W P -- Toft, D O -- Birnbaumer, M -- Cook, R G -- Maxwell, B L -- Zarucki-Schulz, T -- Greene, G L -- Schrader, W T -- O'Malley, B W -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):767-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2426779" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Base Sequence ; Chickens ; *Cloning, Molecular ; Cross Reactions ; DNA/*metabolism ; Epitopes/analysis ; Female ; *Genes ; Humans ; Nucleic Acid Hybridization ; Oviducts/metabolism ; RNA, Messenger/genetics ; Receptors, Progesterone/*genetics ; Species Specificity
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  • 31
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    Modification of the active site of alkaline phosphatase by site-directed mutagenesis (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-10
    Description: The catalytically essential amino acid in the active site of bacterial alkaline phosphatase (Ser-102) has been replaced with a cysteine by site-directed mutagenesis. The resulting thiol enzyme catalyzes the hydrolysis of a variety of phosphate monoesters. The rate-determining step of hydrolysis, however, is no longer the same for catalysis when the active protein nucleophile is changed from the hydroxyl of serine to the thiol of cysteine. Unlike the steady-state kinetics of native alkaline phosphatase, those of the mutant show sensitivity to the leaving group of the phosphate ester.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, S S -- Bock, S C -- Rokita, S E -- Kaiser, E T -- AM 07122-02/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):145-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3510454" target="_blank"〉PubMed〈/a〉
    Keywords: *2,4-Dinitrophenol/*analogs & derivatives ; Alkaline Phosphatase/*genetics/metabolism ; Amino Acid Sequence ; Binding Sites ; DNA/genetics ; Dinitrophenols/metabolism ; Escherichia coli/enzymology/genetics ; Kinetics ; Mutation ; Nitrophenols/metabolism ; Organophosphates/metabolism ; Organophosphorus Compounds/metabolism ; Plasmids
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 32
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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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    Structure, antigenic determinants of some clinically important insect allergens: chironomid hemoglobins (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-07-18
    Description: Determination of the molecular structure and properties of allergens that elicit severe immediate-type hypersensitivity diseases in humans and a knowledge of the structure of their antibody-binding sites should provide new insight into the pathogenetic mechanisms of allergic diseases. Monomeric and homodimeric hemoglobins (CTT I to X) have been identified as potent allergenic components of Chironomidae, a family of Diptera. Immunologic investigations of peptides of three of these hemoglobins (CTT IV, CTT VI, and CTT VIII) showed that human antibodies of the E and G classes recognize at least two different sites within each molecule. Individual hemoglobin peptides were aligned with homologous regions of chironomid hemoglobin CTT III, whose tertiary structure has been determined by x-ray analysis at a resolution of 1.4 angstroms. The antigenic site CTT IV(91 to 101) showed the following characteristics: (i) seven polar or hydroxylated amino acids, from a total of eleven, occupying predominantly superficial regions; (ii) the property of linkage to other molecules by hydrogen bonds or solvent clusters; and (iii) high thermal mobility factors. In contrast, peptide CTT IV(102 to 108), which does not bind human antibodies, contained no polar amino acids and had low thermal mobility factors. These results support the idea that the antigenicity of clinically relevant proteins is related to regions with a predominance of polar amino acids and with low energy barriers between different conformations, which allow high flexibility, including site-specific adaptation in antibody binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baur, X -- Aschauer, H -- Mazur, G -- Dewair, M -- Prelicz, H -- Steigemann, W -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):351-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425431" target="_blank"〉PubMed〈/a〉
    Keywords: Allergens/*immunology ; Amino Acid Sequence ; Animals ; Chironomidae/*immunology ; Diptera/*immunology ; Epitopes/*analysis ; Hemoglobins/analysis/*immunology ; Larva/analysis ; Molecular Conformation ; Peptide Fragments/analysis ; Temperature
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    Automated chemical synthesis of a protein growth factor for hemopoietic cells, interleukin-3 (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-10
    Description: Interleukin-3 (IL-3), a protein of 140 amino acids, was chemically synthesized by means of an automated peptide synthesizer and was shown to have the biological activities attributed to native IL-3. Assays of synthetic analogues established that an amino terminal fragment has detectable IL-3 activity, but that the stable tertiary structure of the complete molecule was required for full activity. The results demonstrate that automated peptide synthesis can be applied to the study of the structure and function of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark-Lewis, I -- Aebersold, R -- Ziltener, H -- Schrader, J W -- Hood, L E -- Kent, S B -- R01-CA38684-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):134-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079915" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Chromatography, High Pressure Liquid ; Electrophoresis, Polyacrylamide Gel ; Interleukin-3 ; Lymphokines/*chemical synthesis/pharmacology ; Mast Cells/drug effects ; Megakaryocytes/drug effects ; Mice ; Protein Conformation ; Structure-Activity Relationship
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  • 35
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    Uroporphyrinogen decarboxylase structural mutant (Gly281----Glu) in a case of porphyria (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-07
    Description: Uroporphyrinogen decarboxylase deficiency in man is responsible for familial porphyria cutanea tarda and hepatoerythropoietic porphyria. A recent study of a family with hepatoerythropoietic porphyria showed that the enzyme defect resulted from rapid degradation of the protein in vivo. Cloning and sequencing of a complementary DNA for the mutated gene revealed that the mutation was due to the replacement of a glycine residue by a glutamic acid residue at position 281. This base change leads to a protein that is very rapidly degraded in the presence of cell lysate. Characterization of the mutation will allow comparison of this defect in a homozygous patient with defects in other patients with familial porphyria cutanea tarda.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Verneuil, H -- Grandchamp, B -- Beaumont, C -- Picat, C -- Nordmann, Y -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):732-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775362" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carboxy-Lyases/*genetics ; Cloning, Molecular ; DNA/genetics ; Humans ; Liver Diseases/genetics ; Mutation ; Porphyrias/*genetics ; Skin Diseases/genetics ; Structure-Activity Relationship ; Uroporphyrinogen Decarboxylase/deficiency/*genetics/metabolism
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    Genetic variation in HTLV-III/LAV over time in patients with AIDS or at risk for AIDS (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-06-20
    Description: In a study of genetic variation in the AIDS virus, HTLV-III/LAV, sequential virus isolates from persistently infected individuals were examined by Southern blot genomic analysis, molecular cloning, and nucleotide sequencing. Four to six virus isolates were obtained from each of three individuals over a 1-year or 2-year period. Changes were detected throughout the viral genomes and consisted of isolated and clustered nucleotide point mutations as well as short deletions or insertions. Results from genomic restriction mapping and nucleotide sequence comparisons indicated that viruses isolated sequentially had evolved in parallel from a common progenitor virus. The rate of evolution of HTLV-III/LAV was estimated to be at least 10(-3) nucleotide substitutions per site per year for the env gene and 10(-4) for the gag gene, values a millionfold greater than for most DNA genomes. Despite this relatively rapid rate of sequence divergence, virus isolates from any one patient were all much more related to each other than to viruses from other individuals. In view of the substantial heterogeneity among most independent HTLV-III/LAV isolates, the repeated isolation from a given individual of only highly related viruses raises the possibility that some type of interference mechanism may prevent simultaneous infection by more than one major genotypic form of the virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahn, B H -- Shaw, G M -- Taylor, M E -- Redfield, R R -- Markham, P D -- Salahuddin, S Z -- Wong-Staal, F -- Gallo, R C -- Parks, E S -- Parks, W P -- AI 23616-01/AI/NIAID NIH HHS/ -- AI 23854-01/AI/NIAID NIH HHS/ -- P30 CA 13148/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 20;232(4757):1548-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3012778" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Amino Acid Sequence ; Base Sequence ; Chromosome Deletion ; DNA Restriction Enzymes ; DNA Transposable Elements ; Deltaretrovirus/*genetics/isolation & purification ; *Genetic Variation ; Humans ; Mutation ; Nucleic Acid Hybridization ; Risk
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  • 37
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    Identification of a missense mutation in the factor VIII gene of a mild hemophiliac (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-06-13
    Description: DNA probes derived from the cloned factor VIII gene can be used to detect mutations in the factor VIII gene of hemophiliacs. DNA hybridization analysis led to the identification of two contrasting point mutations in the same codon. In a severe hemophiliac with no detectable factor VIII activity, the normal arginine codon (number 2307) is converted to a stop codon, while in a mild hemophiliac with 10 percent of normal activity, this same codon is converted to glutamine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gitschier, J -- Wood, W I -- Shuman, M A -- Lawn, R M -- New York, N.Y. -- Science. 1986 Jun 13;232(4756):1415-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3012775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Restriction Enzymes ; Factor VIII/*genetics/metabolism ; Hemophilia A/*genetics ; Humans ; Metabolic Clearance Rate ; Mutation
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    Sequence and expression of human estrogen receptor complementary DNA (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-07
    Description: The mechanism by which the estrogen receptor and other steroid hormone receptors regulate gene expression in eukaryotic cells is not well understood. In this study, a complementary DNA clone containing the entire translated portion of the messenger RNA for the estrogen receptor from MCF-7 human breast cancer cells was sequenced and then expressed in Chinese hamster ovary (CHO-K1) cells to give a functional protein. An open reading frame of 1785 nucleotides in the complementary DNA corresponded to a polypeptide of 595 amino acids and a molecular weight of 66,200, which is in good agreement with published molecular weight values of 65,000 to 70,000 for the estrogen receptor. Homogenates of transformed Chinese hamster ovary cells containing a protein that bound [3H]estradiol and sedimented as a 4S complex in salt-containing sucrose gradients and as an 8 to 9S complex in the absence of salt. Interaction of this receptor-[3H]estradiol complex with a monoclonal antibody that is specific for primate ER confirms the identity of the expressed complementary DNA as human estrogen receptor. Amino acid sequence comparisons revealed significant regional homology among the human estrogen receptor, the human glucocorticoid receptor, and the putative v-erbA oncogene product. This suggests that steroid receptor genes and the avian erythroblastosis viral oncogene are derived from a common primordial gene. The homologous region, which is rich in cysteine, lysine, and arginine, may represent the DNA-binding domain of these proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greene, G L -- Gilna, P -- Waterfield, M -- Baker, A -- Hort, Y -- Shine, J -- CA-02897/CA/NCI NIH HHS/ -- HD17103/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 7;231(4742):1150-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3753802" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Antibodies, Monoclonal ; Base Sequence ; Cells, Cultured ; Cloning, Molecular ; DNA/*metabolism ; Female ; Humans ; Molecular Weight ; Receptors, Estrogen/*genetics ; Transformation, Genetic
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    Molecular cloning and expression of neuroleukin, a neurotrophic factor for spinal and sensory neurons (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-31
    Description: A novel 56,000-dalton growth factor found in mouse salivary gland was purified, molecularly cloned, and expressed in monkey COS cells. The protein is a neurotrophic factor and also, surprisingly, a lymphokine product of lectin-stimulated T cells. The factor was therefore named neuroleukin. Neuroleukin promotes the survival in culture of a subpopulation of embryonic spinal neurons that probably includes skeletal motor neurons. Neuroleukin also supports the survival of cultured sensory neurons that are insensitive to nerve growth factor, but has no effect on sympathetic or parasympathetic neurons. The amino acid sequence of neuroleukin is partly homologous to a highly conserved region of the external envelope protein of HTLV-III/LAV, the retrovirus that causes acquired immune deficiency syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gurney, M E -- Heinrich, S P -- Lee, M R -- Yin, H S -- 5PO1 NS-21442/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):566-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3764429" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Chick Embryo ; Cloning, Molecular ; DNA/genetics ; Glucose-6-Phosphate Isomerase ; Growth Substances/genetics/*physiology ; Lymphokines/genetics/*physiology ; Male ; Mice ; Mice, Inbred BALB C ; Motor Neurons/drug effects ; Muscles/innervation ; Nerve Growth Factors/genetics/isolation & purification/*physiology ; Neurons/drug effects ; Neurons, Afferent/drug effects ; Salivary Glands/metabolism ; Spinal Cord/cytology
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    A novel human gene closely related to the abl proto-oncogene (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: A DNA sequence related to the abl proto-oncogene was identified in human placenta. Molecular cloning and nucleotide sequence analysis revealed two putative exons whose predicted amino acid sequence was most homologous to the corresponding sequences of c-abl and v-abl but was related to other tyrosine kinase genes as well. The new sequence was localized by in situ hybridization and somatic cell genetic analysis to human chromosome 1q24-25, which differs from the location of any previously identified tyrosine kinase gene. The detection of a novel 12-kb transcript by this gene in human normal and tumor cells establishes it as a new member of the tyrosine kinase family that is closely related to but distinct from c-abl.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kruh, G D -- King, C R -- Kraus, M H -- Popescu, N C -- Amsbaugh, S C -- McBride, W O -- Aaronson, S A -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1545-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3787260" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 1 ; Cloning, Molecular ; DNA/*genetics ; Exons ; Humans ; Nucleic Acid Hybridization ; *Oncogenes ; Placenta/analysis ; Protein-Tyrosine Kinases/*genetics
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    Identification of paramyosin as schistosome antigen recognized by intradermally vaccinated mice (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-31
    Description: Mice immunized intradermally with extracts of Schistosoma mansoni in combination with the adjuvant BCG are significantly protected against subsequent infection with living larval forms of the parasite. Remarkably, these vaccinated animals produce antibodies predominantly against a single parasite protein of molecular weight 97 kilodaltons (Sm-97). A complementary DNA that encodes about half of the Sm-97 molecule has now been cloned and sequenced. Analysis of the deduced amino acid sequence reveals a protein containing periodic repeats of hydrophobic amino acids characteristic of an alpha-helical coiled-coil structure. The deduced amino acid composition of the cloned gene and several properties of the native protein are similar to that of paramyosin, an alpha-helical protein that forms the core for myosin filaments in invertebrate muscle. Paramyosin was isolated from Schistosoma mansoni adult worms and antibodies to Sm-97 were shown to react with this molecule as well as with a known paramyosin from molluscan muscle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanar, D E -- Pearce, E J -- James, S L -- Sher, A -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):593-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3094144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Helminth/genetics/*immunology ; Base Sequence ; Schistosoma mansoni/*immunology ; Schistosomiasis mansoni/immunology/prevention & control ; Tropomyosin/genetics/*immunology ; *Vaccination
    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 (AAAS)
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  • 42
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    Structure-activity studies of interleukin-2 (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-17
    Description: The critical role of interleukin-2 (IL-2) in immune response heightens the need to know its structure in order to understand its activity. New computer-assisted predictive methods for the assignment of secondary structure together with a method to predict the tertiary structure of a protein from data on its primary sequence and secondary structure were applied to IL-2. This method generated four topological families of structures, of which the most plausible is a right-handed fourfold alpha-helical bundle. Members of this family were shown to be compatible with existing structural data on disulfide bridges and monoclonal antibody binding for IL-2. Experimental estimates of secondary structure from circular dichroism and site-directed mutagenesis data support the model. A region likely to be important in IL-2 binding to its receptor was identified as residues Leu36, Met38, Leu40, Phe42, Phe44, and Met46.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, F E -- Kosen, P A -- Kuntz, I D -- Epstein, L B -- Ciardelli, T L -- Smith, K A -- CA27903/CA/NCI NIH HHS/ -- GM34197/GM/NIGMS NIH HHS/ -- MOJ JD17001/PHS HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Oct 17;234(4774):349-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3489989" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Computer Simulation ; Humans ; *Interleukin-2/genetics/physiology ; Mice ; Models, Molecular ; Structure-Activity Relationship
    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 (AAAS)
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  • 43
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    A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-28
    Description: The DNA of the HTLV-III/LAV group of retroviruses contains certain additional open reading frames that are not found in typical avian or mammalian retroviruses. The role of these sequences in encoding for gene products that may be related to pathogenesis remains to be resolved. An open reading frame whose 5' end overlaps with the pol gene, but is unrelated to the env gene, has been observed in HTLV-III/LAV and visna virus, both cytopathic mammalian retroviruses. Evidence presented here shows that this open reading frame is a bona fide coding sequence of HTLV-III/LAV and that its product, a protein with a molecular weight of 23,000, induces antibody production in the natural course of infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, T H -- Coligan, J E -- Allan, J S -- McLane, M F -- Groopman, J E -- Essex, M -- CA 18216/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- ST 32 CA 9382/ST/OHS HRSA HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1546-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006243" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*genetics ; Deltaretrovirus/*genetics/immunology ; *Genes, Viral ; Molecular Weight ; Retroviridae Proteins/*genetics/immunology
    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 (AAAS)
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