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  • 1
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    Lasting emotions promote hyperarousal [Psychological and Cognitive Sciences] (2016)
    National Academy of Sciences
    Details
    Publication Date: 2016-03-02
    Description: The mechanisms underlying hyperarousal, the key symptom of insomnia, have remained elusive, hampering cause-targeted treatment. Recently, restless rapid-eye-movement (REM) sleep emerged as a robust signature of sleep in insomnia. Given the role of REM sleep in emotion regulation, we hypothesized that restless REM sleep could interfere with the overnight resolution...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    DNA double-strand breaks activate a multi-functional genetic program in developing lymphocytes (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-10-14
    Description: DNA double-strand breaks are generated by genotoxic agents and by cellular endonucleases as intermediates of several important physiological processes. The cellular response to genotoxic DNA breaks includes the activation of transcriptional programs known primarily to regulate cell-cycle checkpoints and cell survival. DNA double-strand breaks are generated in all developing lymphocytes during the assembly of antigen receptor genes, a process that is essential for normal lymphocyte development. Here we show that in murine lymphocytes these physiological DNA breaks activate a broad transcriptional program. This program transcends the canonical DNA double-strand break response and includes many genes that regulate diverse cellular processes important for lymphocyte development. Moreover, the expression of several of these genes is regulated similarly in response to genotoxic DNA damage. Thus, physiological DNA double-strand breaks provide cues that can regulate cell-type-specific processes not directly involved in maintaining the integrity of the genome, and genotoxic DNA breaks could disrupt normal cellular functions by corrupting these processes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605662/" 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/PMC2605662/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bredemeyer, Andrea L -- Helmink, Beth A -- Innes, Cynthia L -- Calderon, Boris -- McGinnis, Lisa M -- Mahowald, Grace K -- Gapud, Eric J -- Walker, Laura M -- Collins, Jennifer B -- Weaver, Brian K -- Mandik-Nayak, Laura -- Schreiber, Robert D -- Allen, Paul M -- May, Michael J -- Paules, Richard S -- Bassing, Craig H -- Sleckman, Barry P -- R01 AI047829/AI/NIAID NIH HHS/ -- R01 AI047829-09/AI/NIAID NIH HHS/ -- R01 CA125195/CA/NCI NIH HHS/ -- R01 CA125195-02/CA/NCI NIH HHS/ -- England -- Nature. 2008 Dec 11;456(7223):819-23. doi: 10.1038/nature07392. Epub 2008 Oct 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18849970" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; B-Lymphocytes/drug effects/*metabolism ; Cell Cycle Proteins/drug effects ; Cell Line ; *DNA Breaks, Double-Stranded ; DNA-Binding Proteins/drug effects ; Enzyme Inhibitors/pharmacology ; Gene Expression Profiling ; Gene Expression Regulation, Developmental/drug effects/*genetics ; Homeodomain Proteins/metabolism ; Mice ; Mice, Knockout ; Mice, SCID ; NF-kappa B/metabolism ; Protein-Serine-Threonine Kinases/drug effects ; Tumor Suppressor Proteins/drug effects
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-10-15
    Description: The HIV envelope (Env) protein gp120 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly neutralizing antibodies appear to interact directly with the HIV glycan coat. Crystal structures of antigen-binding fragments (Fabs) PGT 127 and 128 with Man(9) at 1.65 and 1.29 angstrom resolution, respectively, and glycan binding data delineate a specific high mannose-binding site. Fab PGT 128 complexed with a fully glycosylated gp120 outer domain at 3.25 angstroms reveals that the antibody penetrates the glycan shield and recognizes two conserved glycans as well as a short beta-strand segment of the gp120 V3 loop, accounting for its high binding affinity and broad specificity. Furthermore, our data suggest that the high neutralization potency of PGT 127 and 128 immunoglobulin Gs may be mediated by cross-linking Env trimers on the viral surface.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3280215/" 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/PMC3280215/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pejchal, Robert -- Doores, Katie J -- Walker, Laura M -- Khayat, Reza -- Huang, Po-Ssu -- Wang, Sheng-Kai -- Stanfield, Robyn L -- Julien, Jean-Philippe -- Ramos, Alejandra -- Crispin, Max -- Depetris, Rafael -- Katpally, Umesh -- Marozsan, Andre -- Cupo, Albert -- Maloveste, Sebastien -- Liu, Yan -- McBride, Ryan -- Ito, Yukishige -- Sanders, Rogier W -- Ogohara, Cassandra -- Paulson, James C -- Feizi, Ten -- Scanlan, Christopher N -- Wong, Chi-Huey -- Moore, John P -- Olson, William C -- Ward, Andrew B -- Poignard, Pascal -- Schief, William R -- Burton, Dennis R -- Wilson, Ian A -- AI082362/AI/NIAID NIH HHS/ -- AI33292/AI/NIAID NIH HHS/ -- AI74372/AI/NIAID NIH HHS/ -- AI84817/AI/NIAID NIH HHS/ -- F32 AI074372-03/AI/NIAID NIH HHS/ -- HFE-224662/Canadian Institutes of Health Research/Canada -- P01 AI082362/AI/NIAID NIH HHS/ -- P01 AI082362-03/AI/NIAID NIH HHS/ -- P01 AI082362-04/AI/NIAID NIH HHS/ -- P41RR001209/RR/NCRR NIH HHS/ -- R01 AI033292/AI/NIAID NIH HHS/ -- R01 AI033292-14/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- R01 AI084817-04/AI/NIAID NIH HHS/ -- RR017573/RR/NCRR NIH HHS/ -- U01 CA128416/CA/NCI NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Nov 25;334(6059):1097-103. doi: 10.1126/science.1213256. Epub 2011 Oct 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Skaggs Institute for Chemical Biology and International AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center, nhe Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21998254" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Neutralizing/chemistry/genetics/*immunology/metabolism ; Antibody Specificity ; Binding Sites, Antibody ; Carbohydrate Conformation ; Cell Line ; Crystallography, X-Ray ; Disaccharides/chemistry/metabolism ; Epitopes ; Glycosylation ; HIV Antibodies/chemistry/genetics/*immunology/*metabolism ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV-1/*immunology/physiology ; Humans ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/chemistry/immunology/metabolism ; Mannose/chemistry/immunology/metabolism ; Mannosides/chemistry/metabolism ; Models, Molecular ; Mutation ; Oligosaccharides/chemistry/*immunology/metabolism ; Polysaccharides/chemistry/*immunology/*metabolism ; Protein Conformation ; Protein Structure, Tertiary
    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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  • 4
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    Broad neutralization coverage of HIV by multiple highly potent antibodies (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-08-19
    Description: Broadly neutralizing antibodies against highly variable viral pathogens are much sought after to treat or protect against global circulating viruses. Here we probed the neutralizing antibody repertoires of four human immunodeficiency virus (HIV)-infected donors with remarkably broad and potent neutralizing responses and rescued 17 new monoclonal antibodies that neutralize broadly across clades. Many of the new monoclonal antibodies are almost tenfold more potent than the recently described PG9, PG16 and VRC01 broadly neutralizing monoclonal antibodies and 100-fold more potent than the original prototype HIV broadly neutralizing monoclonal antibodies. The monoclonal antibodies largely recapitulate the neutralization breadth found in the corresponding donor serum and many recognize novel epitopes on envelope (Env) glycoprotein gp120, illuminating new targets for vaccine design. Analysis of neutralization by the full complement of anti-HIV broadly neutralizing monoclonal antibodies now available reveals that certain combinations of antibodies should offer markedly more favourable coverage of the enormous diversity of global circulating viruses than others and these combinations might be sought in active or passive immunization regimes. Overall, the isolation of multiple HIV broadly neutralizing monoclonal antibodies from several donors that, in aggregate, provide broad coverage at low concentrations is a highly positive indicator for the eventual design of an effective antibody-based HIV vaccine.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3393110/" 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/PMC3393110/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walker, Laura M -- Huber, Michael -- Doores, Katie J -- Falkowska, Emilia -- Pejchal, Robert -- Julien, Jean-Philippe -- Wang, Sheng-Kai -- Ramos, Alejandra -- Chan-Hui, Po-Ying -- Moyle, Matthew -- Mitcham, Jennifer L -- Hammond, Phillip W -- Olsen, Ole A -- Phung, Pham -- Fling, Steven -- Wong, Chi-Huey -- Phogat, Sanjay -- Wrin, Terri -- Simek, Melissa D -- Protocol G Principal Investigators -- Koff, Wayne C -- Wilson, Ian A -- Burton, Dennis R -- Poignard, Pascal -- R01 AI033292/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Sep 22;477(7365):466-70. doi: 10.1038/nature10373.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Microbial Science and IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21849977" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/biosynthesis/immunology ; Antibodies, Monoclonal/immunology ; Antibodies, Neutralizing/*immunology ; Cell Line ; Epitope Mapping ; Epitopes/chemistry/immunology ; Glycoproteins/chemistry/immunology ; Glycosylation ; HEK293 Cells ; HIV/*classification/*immunology/isolation & purification ; HIV Antibodies/*immunology ; HIV Infections/immunology/therapy ; Human Immunodeficiency Virus Proteins/chemistry/immunology ; Humans ; Immune Sera/blood/immunology ; Molecular Sequence Data ; Neutralization Tests
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9 (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-11-25
    Description: Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody neutralization, and are themselves protected by extraordinary sequence diversity and N-linked glycosylation. Human antibodies such as PG9 nonetheless engage V1/V2 and neutralize 80% of HIV-1 isolates. Here we report the structure of V1/V2 in complex with PG9. V1/V2 forms a four-stranded beta-sheet domain, in which sequence diversity and glycosylation are largely segregated to strand-connecting loops. PG9 recognition involves electrostatic, sequence-independent and glycan interactions: the latter account for over half the interactive surface but are of sufficiently weak affinity to avoid autoreactivity. The structures of V1/V2-directed antibodies CH04 and PGT145 indicate that they share a common mode of glycan penetration by extended anionic loops. In addition to structurally defining V1/V2, the results thus identify a paradigm of antibody recognition for highly glycosylated antigens, which-with PG9-involves a site of vulnerability comprising just two glycans and a strand.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3406929/" 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/PMC3406929/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McLellan, Jason S -- Pancera, Marie -- Carrico, Chris -- Gorman, Jason -- Julien, Jean-Philippe -- Khayat, Reza -- Louder, Robert -- Pejchal, Robert -- Sastry, Mallika -- Dai, Kaifan -- O'Dell, Sijy -- Patel, Nikita -- Shahzad-ul-Hussan, Syed -- Yang, Yongping -- Zhang, Baoshan -- Zhou, Tongqing -- Zhu, Jiang -- Boyington, Jeffrey C -- Chuang, Gwo-Yu -- Diwanji, Devan -- Georgiev, Ivelin -- Kwon, Young Do -- Lee, Doyung -- Louder, Mark K -- Moquin, Stephanie -- Schmidt, Stephen D -- Yang, Zhi-Yong -- Bonsignori, Mattia -- Crump, John A -- Kapiga, Saidi H -- Sam, Noel E -- Haynes, Barton F -- Burton, Dennis R -- Koff, Wayne C -- Walker, Laura M -- Phogat, Sanjay -- Wyatt, Richard -- Orwenyo, Jared -- Wang, Lai-Xi -- Arthos, James -- Bewley, Carole A -- Mascola, John R -- Nabel, Gary J -- Schief, William R -- Ward, Andrew B -- Wilson, Ian A -- Kwong, Peter D -- R01 AI033292/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- RR017573/RR/NCRR NIH HHS/ -- Canadian Institutes of Health Research/Canada -- Intramural NIH HHS/ -- England -- Nature. 2011 Nov 23;480(7377):336-43. doi: 10.1038/nature10696.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22113616" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/chemistry/immunology ; Amino Acid Motifs ; Amino Acid Sequence ; Antibodies, Neutralizing/chemistry/*immunology ; Antibody Affinity/immunology ; Antibody Specificity/*immunology ; Antigen-Antibody Complex/chemistry/immunology ; Binding Sites, Antibody/immunology ; Conserved Sequence ; Crystallography, X-Ray ; Epitopes/chemistry/immunology ; Glycopeptides/chemistry/immunology ; Glycosylation ; HIV Antibodies/chemistry/*immunology ; HIV Envelope Protein gp120/*chemistry/*immunology ; HIV-1/*chemistry/*immunology ; Hydrogen Bonding ; Immune Evasion ; Models, Molecular ; Molecular Sequence Data ; Polysaccharides/chemistry/immunology ; Protein Structure, Quaternary ; Protein Structure, Tertiary
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    H2AX prevents CtIP-mediated DNA end resection and aberrant repair in G1-phase lymphocytes (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-12-17
    Description: DNA double-strand breaks (DSBs) are generated by the recombination activating gene (RAG) endonuclease in all developing lymphocytes as they assemble antigen receptor genes. DNA cleavage by RAG occurs only at the G1 phase of the cell cycle and generates two hairpin-sealed DNA (coding) ends that require nucleolytic opening before their repair by classical non-homologous end-joining (NHEJ). Although there are several cellular nucleases that could perform this function, only the Artemis nuclease is able to do so efficiently. Here, in vivo, we show that in murine cells the histone protein H2AX prevents nucleases other than Artemis from processing hairpin-sealed coding ends; in the absence of H2AX, CtIP can efficiently promote the hairpin opening and resection of DNA ends generated by RAG cleavage. This CtIP-mediated resection is inhibited by gamma-H2AX and by MDC-1 (mediator of DNA damage checkpoint 1), which binds to gamma-H2AX in chromatin flanking DNA DSBs. Moreover, the ataxia telangiectasia mutated (ATM) kinase activates antagonistic pathways that modulate this resection. CtIP DNA end resection activity is normally limited to cells at post-replicative stages of the cell cycle, in which it is essential for homology-mediated repair. In G1-phase lymphocytes, DNA ends that are processed by CtIP are not efficiently joined by classical NHEJ and the joints that do form frequently use micro-homologies and show significant chromosomal deletions. Thus, H2AX preserves the structural integrity of broken DNA ends in G1-phase lymphocytes, thereby preventing these DNA ends from accessing repair pathways that promote genomic instability.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3150591/" 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/PMC3150591/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Helmink, Beth A -- Tubbs, Anthony T -- Dorsett, Yair -- Bednarski, Jeffrey J -- Walker, Laura M -- Feng, Zhihui -- Sharma, Girdhar G -- McKinnon, Peter J -- Zhang, Junran -- Bassing, Craig H -- Sleckman, Barry P -- A125195/PHS HHS/ -- AI074953/AI/NIAID NIH HHS/ -- AI47829/AI/NIAID NIH HHS/ -- CA136470/CA/NCI NIH HHS/ -- CA21765/CA/NCI NIH HHS/ -- NS37956/NS/NINDS NIH HHS/ -- P01 CA096832/CA/NCI NIH HHS/ -- P01 CA096832-08/CA/NCI NIH HHS/ -- R01 AI047829/AI/NIAID NIH HHS/ -- R01 AI047829-13/AI/NIAID NIH HHS/ -- R01 AI074953/AI/NIAID NIH HHS/ -- R01 AI074953-04/AI/NIAID NIH HHS/ -- R01 CA136470/CA/NCI NIH HHS/ -- R01 CA136470-04/CA/NCI NIH HHS/ -- R01 NS037956/NS/NINDS NIH HHS/ -- R01 NS037956-12/NS/NINDS NIH HHS/ -- R21 ES019779/ES/NIEHS NIH HHS/ -- R21 ES019779-02/ES/NIEHS NIH HHS/ -- T32 D007499/PHS HHS/ -- England -- Nature. 2011 Jan 13;469(7329):245-9. doi: 10.1038/nature09585. Epub 2010 Dec 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Immunology, Washington University School of Medicine, St Louis, Missouri 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21160476" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; Carrier Proteins/*metabolism ; Cell Cycle Proteins/*metabolism ; Cell Line, Transformed ; Chromatin/metabolism ; *DNA Breaks, Double-Stranded ; *DNA Repair ; DNA-Binding Proteins/metabolism ; Endonucleases ; *G1 Phase ; *Gene Rearrangement, B-Lymphocyte/genetics ; Genomic Instability ; Histones/deficiency/genetics/*metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Lymphocytes/cytology/*metabolism ; Mice ; Nuclear Proteins ; Precursor Cells, B-Lymphoid/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombination, Genetic/genetics ; Substrate Specificity ; Tumor Suppressor Proteins/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 7
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    Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-09-05
    Description: Broadly neutralizing antibodies (bNAbs), which develop over time in some HIV-1-infected individuals, define critical epitopes for HIV vaccine design. Using a systematic approach, we have examined neutralization breadth in the sera of about 1800 HIV-1-infected individuals, primarily infected with non-clade B viruses, and have selected donors for monoclonal antibody (mAb) generation. We then used a high-throughput neutralization screen of antibody-containing culture supernatants from about 30,000 activated memory B cells from a clade A-infected African donor to isolate two potent mAbs that target a broadly neutralizing epitope. This epitope is preferentially expressed on trimeric Envelope protein and spans conserved regions of variable loops of the gp120 subunit. The results provide a framework for the design of new vaccine candidates for the elicitation of bNAb responses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3335270/" 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/PMC3335270/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walker, Laura M -- Phogat, Sanjay K -- Chan-Hui, Po-Ying -- Wagner, Denise -- Phung, Pham -- Goss, Julie L -- Wrin, Terri -- Simek, Melissa D -- Fling, Steven -- Mitcham, Jennifer L -- Lehrman, Jennifer K -- Priddy, Frances H -- Olsen, Ole A -- Frey, Steven M -- Hammond, Phillip W -- Protocol G Principal Investigators -- Kaminsky, Stephen -- Zamb, Timothy -- Moyle, Matthew -- Koff, Wayne C -- Poignard, Pascal -- Burton, Dennis R -- AI33292/AI/NIAID NIH HHS/ -- MC_U950097145/Medical Research Council/United Kingdom -- R01 AI033292/AI/NIAID NIH HHS/ -- R01 AI033292-18/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2009 Oct 9;326(5950):285-9. doi: 10.1126/science.1178746. Epub 2009 Sep 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Microbial Science and IAVI Neutralizing Antibody Center, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19729618" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/*immunology ; Africa South of the Sahara ; Antibodies, Monoclonal/*immunology ; B-Lymphocyte Subsets/immunology ; Epitopes/immunology ; HIV Antibodies/biosynthesis/*immunology ; HIV Envelope Protein gp120/chemistry/*immunology ; HIV Envelope Protein gp41/immunology ; HIV Infections/*immunology ; HIV-1/*immunology ; Humans ; Immunologic Memory ; Lymphocyte Activation ; Neutralization Tests ; Peptide Fragments/immunology ; Protein Multimerization ; Recombinant Proteins/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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  • 8
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    Isolation of potent neutralizing antibodies from a survivor of the 2014 Ebola virus outbreak (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-02-26
    Description: Antibodies targeting the Ebola virus surface glycoprotein (EBOV GP) are implicated in protection against lethal disease, but the characteristics of the human antibody response to EBOV GP remain poorly understood. We isolated and characterized 349 GP-specific monoclonal antibodies (mAbs) from the peripheral B cells of a convalescent donor who survived the 2014 EBOV Zaire outbreak. Remarkably, 77% of the mAbs neutralize live EBOV, and several mAbs exhibit unprecedented potency. Structures of selected mAbs in complex with GP reveal a site of vulnerability located in the GP stalk region proximal to the viral membrane. Neutralizing antibodies targeting this site show potent therapeutic efficacy against lethal EBOV challenge in mice. The results provide a framework for the design of new EBOV vaccine candidates and immunotherapies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bornholdt, Zachary A -- Turner, Hannah L -- Murin, Charles D -- Li, Wen -- Sok, Devin -- Souders, Colby A -- Piper, Ashley E -- Goff, Arthur -- Shamblin, Joshua D -- Wollen, Suzanne E -- Sprague, Thomas R -- Fusco, Marnie L -- Pommert, Kathleen B J -- Cavacini, Lisa A -- Smith, Heidi L -- Klempner, Mark -- Reimann, Keith A -- Krauland, Eric -- Gerngross, Tillman U -- Wittrup, Karl D -- Saphire, Erica Ollmann -- Burton, Dennis R -- Glass, Pamela J -- Ward, Andrew B -- Walker, Laura M -- R01AI067927/AI/NIAID NIH HHS/ -- U19AI109762/AI/NIAID NIH HHS/ -- UM1AI100663/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2016 Mar 4;351(6277):1078-83. doi: 10.1126/science.aad5788. Epub 2016 Feb 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA. ; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. ; Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. ; Adimab, Lebanon, NH 03766, USA. ; MassBiologics, University of Massachusetts Medical School, Boston, MA 02126, USA. ; U.S. Army Medical Research Institute of Infectious Diseases, Frederick, MD 21702, USA. ; Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA. Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology, and Harvard University, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26912366" 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
    Published by American Association for the Advancement of Science (AAAS)
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  • 9
    Electronic Resource
    Electronic Resource
    Microfilament distribution in protonemata of the mossCeratodon (1995)
    Springer
    Protoplasma 189 (1995), S. 229-237 
    Details
    ISSN: 1615-6102
    Keywords: Ceratodon ; Protonema ; Confocal laser scanning microscopy ; Microfilament ; Actin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Microfilaments were visualized in dark-grown protonemata of the mossCeratodon to assess their possible role in tip growth and gravitropism. The relative effectiveness of rhodamine phalloidin (with or without MBS) and of immunofluorescence (using the C4 antibody) was evaluated for actin localization in the same cell type. Using immunofluorescence, microfilaments were primarily in an axial orientation within the apical cell. However, a more complex network of microfilaments was observed using rhodamine phalloidin after MBS pretreatment, especially when viewed by confocal laser scanning microscopy. This method revealed a rich three dimensional network of fine microfilaments throughout the apical cell, including the extreme apex. Although there were numerous internal microfilaments, peripheral microfilaments were more abundant. No major redistribution of microfilaments was detected after gravistimulation. The combination of MBS, rhodamine phalloidin, and confocal laser scanning microscopy preserves and reveals microfilaments remarkably well and documents perhaps the most extensive F-actin network visualized to date in any tip-growing cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01280177
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  • 10
    Electronic Resource
    Electronic Resource
    Ultrastructural analysis of cell component distribution in the apical cell ofCeratodon protonemata (1995)
    Springer
    Protoplasma 189 (1995), S. 238-248 
    Details
    ISSN: 1615-6102
    Keywords: Tip growth ; Stereology ; Protonemata ; Moss ; Ceratodon
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A distinctive feature of tip-growing plant cells is that cell components are distributed differentially along the length of the cell, although most ultrastructural analyses have been qualitative. The longitudinal distribution of cell components was studied both qualitatively and quantitatively in the apical cell of dark-grown protonemata of the mossCeratodon. The first 35 μm of the apical cell was analyzed stereologically using transmission electron microscopy. There were four types of distributions along the cell's axis, three of them differential: (1) tubular endoplasmic reticulum was evenly distributed, (2) cisternal endoplasmic reticulum and Golgi vesicles were distributed in a tip-to-base gradient, (3) plastids, vacuoles, and Golgi stacks were enriched in specific areas, although the locations of the enrichments varied, and (4) mitochondria were excluded in the tipmost 5 μm and evenly distributed throughout the remaining 30 μm. This study provides one of the most comprehensive quantitative, ultrastructural analyses of the distribution of cell components in the apex of any tip-growing plant cell. The finding that almost every component had its own spatial arrangement demonstrates the complexity of the organization and regulation of the distribution of components in tip-growing cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01280178
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