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  • 1
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    Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-28
    Description: The protective antigen moiety of anthrax toxin translocates the toxin's enzymic moieties to the cytosol of mammalian cells by a mechanism that depends on its ability to heptamerize and insert into membranes. We identified dominant-negative mutants of protective antigen that co-assemble with the wild-type protein and block its ability to translocate the enzymic moieties across membranes. These mutants strongly inhibited toxin action in cell culture and in an animal intoxication model, suggesting that they could be useful in therapy of anthrax.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sellman, B R -- Mourez, M -- Collier, R J -- 5T32AI07410/AI/NIAID NIH HHS/ -- R37-AI22021/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):695-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11326092" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthrax/*drug therapy ; *Antigens, Bacterial ; Bacterial Toxins/*antagonists & inhibitors/*genetics/metabolism/toxicity ; CHO Cells ; Cell Membrane/metabolism ; Cricetinae ; Endocytosis ; Genes, Dominant ; Male ; *Mutation ; Protein Transport ; Rats ; Rats, Inbred F344 ; Receptors, Peptide/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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    Moribund funding in agricultural research (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robertson, G P -- Barry, P J -- Busta, F F -- Collier, R J -- Keen, N T -- Sederoff, R R -- Simpkins, W W -- Urban, T N -- New York, N.Y. -- Science. 2001 Mar 16;291(5511):2089-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11256402" target="_blank"〉PubMed〈/a〉
    Keywords: *Agriculture ; Research ; *Research Support as Topic ; United States ; United States Department of Agriculture/*economics
    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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    Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-13
    Description: The transmembrane (T) domain of diphtheria toxin has a critical role in the low pH-induced translocation of the catalytic domain (A chain) of the toxin across membranes. Here it is shown that at low pH, addition of proteins in a partly unfolded, molten globule-like conformation converted the T domain from a shallow membrane-inserted form to its transmembrane form. Fluorescence energy transfer demonstrated that molten globule-like proteins bound to the T domain. Thus, the T domain recognizes proteins that are partly unfolded and may function in translocation of the A chain as a transmembrane chaperone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ren, J -- Kachel, K -- Kim, H -- Malenbaum, S E -- Collier, R J -- London, E -- AI 22021/AI/NIAID NIH HHS/ -- GM 39186/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 7;284(5416):955-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10320374" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies/metabolism ; Apoproteins/chemistry/metabolism ; Boron Compounds/immunology/metabolism ; Catalytic Domain ; Diphtheria Toxin/*chemistry/*metabolism ; Energy Transfer ; Fluorescence ; Hydrogen-Ion Concentration ; Lactalbumin/chemistry/metabolism ; Membranes, Artificial ; Myoglobin/chemistry/metabolism ; Peptide Fragments/chemistry/*metabolism ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/chemistry/*metabolism ; Serum Albumin/chemistry/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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  • 4
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    In reply: does diphtheria toxin have nuclease activity? (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, B A -- Blanke, S R -- Murphy, J R -- Pappenheimer, A M Jr -- Collier, R J -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):834-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17759975" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    An open letter to Elias Zerhouni (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, Sidney -- Bassler, Bonnie L -- Beckwith, Jon -- Belfort, Marlene -- Berg, Howard C -- Bloom, Barry -- Brenchley, Jean E -- Campbell, Allan -- Collier, R John -- Connell, Nancy -- Cozzarelli, Nicholas R -- Craig, Nancy L -- Darst, Seth -- Ebright, Richard H -- Elledge, Stephen J -- Falkow, Stanley -- Galan, Jorge E -- Gottesman, Max -- Gourse, Richard -- Grindley, Nigel D F -- Gross, Carol A -- Grossman, Alan -- Hochschild, Ann -- Howe, Martha -- Hurwitz, Jerard -- Isberg, Ralph R -- Kaplan, Samuel -- Kornberg, Arthur -- Kustu, Sydney G -- Landick, Robert C -- Landy, Arthur -- Levy, Stuart B -- Losick, Richard -- Long, Sharon R -- Maloy, Stanley R -- Mekalanos, John J -- Neidhardt, Frederick C -- Pace, Norman R -- Ptashne, Mark -- Roberts, Jeffrey W -- Roth, John R -- Rothman-Denes, Lucia B -- Salyers, Abigail -- Schaechter, Moselio -- Shapiro, Lucy -- Silhavy, Thomas J -- Simon, Melvin I -- Walker, Graham -- Yanofsky, Charles -- Zinder, Norton -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1409-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746409" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Warfare ; *Biomedical Research/economics ; *Bioterrorism ; Financing, Government ; *Microbiology ; *National Institutes of Health (U.S.) ; Peer Review, Research ; Public Health ; *Research Support as Topic ; United States
    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 phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-30
    Description: The protective antigen component of anthrax toxin forms a homoheptameric pore in the endosomal membrane, creating a narrow passageway for the enzymatic components of the toxin to enter the cytosol. We found that, during conversion of the heptameric precursor to the pore, the seven phenylalanine-427 residues converged within the lumen, generating a radially symmetric heptad of solvent-exposed aromatic rings. This "phi-clamp" structure was required for protein translocation and comprised the major conductance-blocking site for hydrophobic drugs and model cations. We conclude that the phi clamp serves a chaperone-like function, interacting with hydrophobic sequences presented by the protein substrate as it unfolds during translocation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1815389/" 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/PMC1815389/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krantz, Bryan A -- Melnyk, Roman A -- Zhang, Sen -- Juris, Stephen J -- Lacy, D Borden -- Wu, Zhengyan -- Finkelstein, Alan -- Collier, R John -- AI022021/AI/NIAID NIH HHS/ -- AI062204/AI/NIAID NIH HHS/ -- F32 AI062204/AI/NIAID NIH HHS/ -- F32 AI062204-01/AI/NIAID NIH HHS/ -- GM29210/GM/NIGMS NIH HHS/ -- R37 AI022021/AI/NIAID NIH HHS/ -- R37 GM029210/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):777-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051798" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Antigens, Bacterial/*chemistry/genetics/*metabolism ; Bacillus anthracis/*chemistry/metabolism ; Bacterial Toxins/*chemistry/genetics/*metabolism ; Binding Sites ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Electron Spin Resonance Spectroscopy ; Endosomes/metabolism ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/metabolism ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Onium Compounds/metabolism ; Organophosphorus Compounds/metabolism ; Phenylalanine/*chemistry ; Protein Conformation ; Protein Folding ; Quaternary Ammonium Compounds/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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  • 7
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    Organization of diphtheria toxin T domain in bilayers: a site-directed spin labeling study (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: The diphtheria toxin transmembrane (T) domain was spin-labeled at consecutive residues in a helical segment, TH9. After binding of the T domain to membranes at low pH, the nitroxide side chains generated by spin labeling were measured with respect to their frequency of collision with polar and nonpolar reagents. The data showed that the helical structure of TH9 in solution is conserved, with one face exposed to water and the other to the hydrophobic interior of the bilayer. Measurement of the depth of the nitroxide side chains from the membrane surfaces revealed an incremental change of about 5 angstroms per turn, which is consistent with a transmembrane orientation of an alpha helix. These results indicate that the helix forms the lining of a transmembrane water-filled channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oh, K J -- Zhan, H -- Cui, C -- Hideg, K -- Collier, R J -- Hubbell, W L -- AI-22021/AI/NIAID NIH HHS/ -- AI-22848/AI/NIAID NIH HHS/ -- EY-05216/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):810-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-7008, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670424" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Diphtheria Toxin/*chemistry/genetics ; Edetic Acid/analogs & derivatives ; Electron Spin Resonance Spectroscopy ; Hydrogen-Ion Concentration ; *Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nickel ; Oxygen ; Phospholipids ; *Protein Structure, Secondary ; *Protein Structure, Tertiary ; Spin Labels
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: In this study, a protein that interacts with sequences encoded by the first exon of the protein kinase Bcr was cloned. The Bcr-associated protein 1 (Bap-1) is a member of the 14-3-3 family of proteins. Bap-1 interacts with full-length c-Bcr and with the chimeric Bcr-Abl tyrosine kinase of Philadelphia chromosome (Ph1)-positive human leukemias. Bap-1 is a substrate for the Bcr serine-threonine kinase and is also phosphorylated on tyrosine by Bcr-Abl but not by c-Abl. Bap-1 may function in the regulation of c-Bcr and may contribute to the transforming activity of Bcr-Abl in vivo. 14-3-3 proteins are essential for cell proliferation and have a role in determining the timing of mitosis in yeast. Through direct binding to sequences present in Bcr and in other proteins implicated in signaling, the mammalian 14-3-3 proteins may link specific signaling protein components to mitogenic and cell-cycle control pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reuther, G W -- Fu, H -- Cripe, L D -- Collier, R J -- Pendergast, A M -- CA61033/CA/NCI NIH HHS/ -- DK01965/DK/NIDDK NIH HHS/ -- GM07184/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):129-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939633" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Animals ; Cell Division ; Cell Line ; Cell Transformation, Neoplastic ; Fusion Proteins, bcr-abl/*metabolism ; Humans ; Mice ; Phosphorylation ; Poly(ADP-ribose) Polymerases/metabolism ; Protein-Tyrosine Kinases/*metabolism ; Proteins/isolation & purification/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-bcr ; Rats ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; *Tyrosine 3-Monooxygenase
    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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  • 9
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    Association of polyomavirus middle tumor antigen with 14-3-3 proteins (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-22
    Description: To carry out its transformation function, the middle tumor antigen (MT) of murine polyomavirus associates with a number of cellular proteins involved in regulation of cell proliferation, including pp60c-Src, phosphatidylinositol 3-kinase, protein phosphatase 2A, Src homologous and collagen protein and growth factor receptor-binding protein 2. Here, two additional MT-associated proteins were identified as members of the 14-3-3 family of proteins. Yeast homologs of 14-3-3 proteins have recently been shown to play a role in the timing of mitosis. Thus, regulation of 14-3-3 protein function by MT may contribute to the development of neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pallas, D C -- Fu, H -- Haehnel, L C -- Weller, W -- Collier, R J -- Roberts, T M -- CA30002/CA/NCI NIH HHS/ -- CA45285/CA/NCI NIH HHS/ -- CA50661/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):535-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036498" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; 3T3 Cells ; Adenosine Diphosphate Ribose/metabolism ; Amino Acid Sequence ; Animals ; Antigens, Polyomavirus Transforming/immunology/*metabolism ; *Cell Division ; Cell Line ; *Cell Transformation, Neoplastic ; *Cell Transformation, Viral ; Humans ; Immune Sera ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/isolation & purification/*metabolism ; Poly(ADP-ribose) Polymerases/metabolism ; Precipitin Tests ; *Tyrosine 3-Monooxygenase
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Interaction of the protein kinase Raf-1 with 14-3-3 proteins (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: Members of a family of highly conserved proteins, termed 14-3-3 proteins, were found by several experimental approaches to associate with Raf-1, a central component of a key signal transduction pathway. Optimal complex formation required the amino-terminal regulatory domain of Raf-1. The association of 14-3-3 proteins and Raf-1 was not substantially affected by the activation state of Raf.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, H -- Xia, K -- Pallas, D C -- Cui, C -- Conroy, K -- Narsimhan, R P -- Mamon, H -- Collier, R J -- Roberts, T M -- AI22021/AI/NIAID NIH HHS/ -- CA57327/CA/NCI NIH HHS/ -- HD24926/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):126-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939632" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; 3T3 Cells ; Animals ; Binding Sites ; Cell Line ; Enzyme Activation ; Humans ; Mice ; Nerve Tissue Proteins/metabolism ; Phosphorylation ; Poly(ADP-ribose) Polymerases/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Proteins/chemistry/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-raf ; *Signal Transduction ; Spodoptera ; *Tyrosine 3-Monooxygenase ; Zinc Fingers
    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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