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  • 1
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    Preclinical screening of histone deacetylase inhibitors combined with ABT-737, rhTRAIL/MD5-1 or 5-azacytidine using syngeneic Vk*MYC multiple myeloma (2013)
    Springer Nature
    Details
    Publication Date: 2013-09-13
    Description: Preclinical screening of histone deacetylase inhibitors combined with ABT-737, rhTRAIL/MD5-1 or 5-azacytidine using syngeneic Vk*MYC multiple myeloma Cell Death and Disease 4, e798 (September 2013). doi:10.1038/cddis.2013.306 Authors: G M Matthews, M Lefebure, M A Doyle, J Shortt, J Ellul, M Chesi, K-M Banks, E Vidacs, D Faulkner, P Atadja, P L Bergsagel & R W Johnstone
    Keywords: multiple myelomahistone deacetylase inhibitorsintrinsic apoptosisextrinsic apoptosisDNA methylation
    Electronic ISSN: 2041-4889
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 2
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    MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-02-05
    Description: p53-binding protein 1 (53BP1) is known to be an important mediator of the DNA damage response, with dimethylation of histone H4 lysine 20 (H4K20me2) critical to the recruitment of 53BP1 to double-strand breaks (DSBs). However, it is not clear how 53BP1 is specifically targeted to the sites of DNA damage, as the overall level of H4K20me2 does not seem to increase following DNA damage. It has been proposed that DNA breaks may cause exposure of methylated H4K20 previously buried within the chromosome; however, experimental evidence for such a model is lacking. Here we found that H4K20 methylation actually increases locally upon the induction of DSBs and that methylation of H4K20 at DSBs is mediated by the histone methyltransferase MMSET (also known as NSD2 or WHSC1) in mammals. Downregulation of MMSET significantly decreases H4K20 methylation at DSBs and the subsequent accumulation of 53BP1. Furthermore, we found that the recruitment of MMSET to DSBs requires the gammaH2AX-MDC1 pathway; specifically, the interaction between the MDC1 BRCT domain and phosphorylated Ser 102 of MMSET. Thus, we propose that a pathway involving gammaH2AX-MDC1-MMSET regulates the induction of H4K20 methylation on histones around DSBs, which, in turn, facilitates 53BP1 recruitment.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064261/" 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/PMC3064261/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pei, Huadong -- Zhang, Lindsey -- Luo, Kuntian -- Qin, Yuxin -- Chesi, Marta -- Fei, Frances -- Bergsagel, P Leif -- Wang, Liewei -- You, Zhongsheng -- Lou, Zhenkun -- CA130996/CA/NCI NIH HHS/ -- CA151329/CA/NCI NIH HHS/ -- R01 AG020686/AG/NIA NIH HHS/ -- R01 AG020686-06A2/AG/NIA NIH HHS/ -- R01 AG020686-07/AG/NIA NIH HHS/ -- R01 CA130996/CA/NCI NIH HHS/ -- R01 CA130996-03/CA/NCI NIH HHS/ -- R01 CA133966/CA/NCI NIH HHS/ -- R01 CA133966-01A2/CA/NCI NIH HHS/ -- R01 CA133966-02/CA/NCI NIH HHS/ -- R01 CA133966-03/CA/NCI NIH HHS/ -- R01 CA136671/CA/NCI NIH HHS/ -- R01 CA136671-02/CA/NCI NIH HHS/ -- R01 CA136671-03/CA/NCI NIH HHS/ -- R01 CA151329/CA/NCI NIH HHS/ -- R01 CA151329-01/CA/NCI NIH HHS/ -- R56 AG020686/AG/NIA NIH HHS/ -- R56 AG020686-06A1/AG/NIA NIH HHS/ -- England -- Nature. 2011 Feb 3;470(7332):124-8. doi: 10.1038/nature09658.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Oncology Research, Mayo Clinic, Rochester, Minnesota 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21293379" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins/metabolism ; Chromatin Immunoprecipitation ; *DNA Breaks, Double-Stranded ; DNA-Binding Proteins/metabolism ; HEK293 Cells ; HeLa Cells ; Histone-Lysine N-Methyltransferase/chemistry/*metabolism ; Histones/*chemistry/*metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/*metabolism ; Lysine/*metabolism ; Methylation ; Nuclear Proteins/chemistry/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Transport ; Protein-Serine-Threonine Kinases/metabolism ; Repressor Proteins/chemistry/*metabolism ; Trans-Activators/chemistry/metabolism ; Tumor Suppressor Proteins/metabolism
    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 structurally distinct human mycoplasma protein that generically blocks antigen-antibody union (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-02-08
    Description: We report the discovery of a broadly reactive antibody-binding protein (Protein M) from human mycoplasma. The crystal structure of the ectodomain of transmembrane Protein M differs from other known protein structures, as does its mechanism of antibody binding. Protein M binds with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the kappa and lambda light chains. Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens. Similar to the other immunoglobulin-binding proteins such as Protein A, Protein M as well as its orthologs in other Mycoplasma species could become invaluable reagents in the antibody field.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3987992/" 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/PMC3987992/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grover, Rajesh K -- Zhu, Xueyong -- Nieusma, Travis -- Jones, Teresa -- Boero, Isabel -- MacLeod, Amanda S -- Mark, Adam -- Niessen, Sherry -- Kim, Helen J -- Kong, Leopold -- Assad-Garcia, Nacyra -- Kwon, Keehwan -- Chesi, Marta -- Smider, Vaughn V -- Salomon, Daniel R -- Jelinek, Diane F -- Kyle, Robert A -- Pyles, Richard B -- Glass, John I -- Ward, Andrew B -- Wilson, Ian A -- Lerner, Richard A -- 5 R21 AI098057-02/AI/NIAID NIH HHS/ -- K08 AR063729/AR/NIAMS NIH HHS/ -- K08 AR063729-01/AR/NIAMS NIH HHS/ -- P41 GM103310/GM/NIGMS NIH HHS/ -- R01 AG020686/AG/NIA NIH HHS/ -- R01 AI042266/AI/NIAID NIH HHS/ -- R21 AI098057/AI/NIAID NIH HHS/ -- RR017573/RR/NCRR NIH HHS/ -- U19 AI06360/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2014 Feb 7;343(6171):656-61. doi: 10.1126/science.1246135.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Biology, The 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/24503852" target="_blank"〉PubMed〈/a〉
    Keywords: Antigen-Antibody Reactions/genetics/*immunology ; Antigens/*immunology ; Bacterial Proteins/chemistry/genetics/*immunology ; Crystallography, X-Ray ; Humans ; Immunoglobulin G/*immunology ; Immunoglobulin Variable Region/*immunology ; Immunoglobulin kappa-Chains/immunology ; Immunoglobulin lambda-Chains/immunology ; Lymphokines/chemistry/genetics/*immunology ; Membrane Proteins/chemistry/genetics/*immunology ; Mycoplasma/*immunology ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/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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  • 4
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    Gross morphology and microstructure of type locality ossicles of Psephophorus polygonus Meyer, 1847 (Testudines, Dermochelyidae) (2013)
    Cambridge University Press
    Details
    Publication Date: 2013-08-15
    Description: Psephophorus polygonus Meyer, 1847, the first fossil leatherback turtle to be named, was described on the basis of shell ossicles from the middle Miocene (MN6–7/8?) of Slovakia. The whereabouts of this material is uncertain but a slab on display at the Naturhistorisches Museum Wien is considered the neotype. We rediscovered further type locality ossicles in four European institutions, re-evaluated their gross morphology and described for the first time their microstructure by comparing them with Dermochelys coriacea , the only living dermochelyid turtle. The gross morphology is congruent with that already described for P. polygonus , but with two significant exceptions: the ridged ossicles of P. polygonus may have a distinctly concave ventral surface as well as a tectiform shape in cross-section. They do not develop the external keel typical of many ossicles of D. coriacea . Both ridged and non-ridged ossicles of P. polygonus are characterized by compact diploe structures with an internal cortex consisting of a coarse fibrous meshwork, whereas the proportionately thinner ossicles of D. coriacea tend to lose the internal cortex, and thus their diploe, during ontogeny. The ossicles of both P. polygonus and D. coriacea differ from those of other lineages of amniotes whose carapace is composed of polygonal ossicles or platelets, in having growth centres situated at the plate centres just interior to the external bone surface and not within the cancellous core or closer to the internal compact layer. The new diagnosis of P. polygonus allows us to preliminarily re-evaluate the taxonomy of some of the Psephophorus- like species. Despite some macro- and micromorphological differences, it seems likely that Psephophorus was as cosmopolitan as extant Dermochelys and had a broadly similar ecology, with a possible difference concerning the dive depth.
    Print ISSN: 0016-7568
    Electronic ISSN: 1469-5081
    Topics: Geosciences
    Published by Cambridge University Press
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  • 5
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    Promiscuous translocations into immunoglobulin heavy chain switch regions in multiple myeloma (1996)
    National Academy of Sciences
    Details
    Publication Date: 1996-11-26
    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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  • 6
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    Preclinical screening of histone deacetylase inhibitors combined with ABT-737, rhTRAIL/MD5-1 or 5-azacytidine using syngeneic Vk*MYC multiple myeloma (2013)
    Springer Nature
    Details
    Publication Date: 2013-09-01
    Electronic ISSN: 2041-4889
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 7
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    Dysregulation of cyclin D1 by translocation into an IgH gamma switch region in two multiple myeloma cell lines [see comments] (1996)
    American Society of Hematology
    Details
    Publication Date: 1996-07-15
    Description: Translocations involving the IgH locus at chromosomal locus 14q32.3 are a common event in many B-cell malignancies. The translocations, which generally occur into JH and switch regions, are mediated by errors in the two developmentally regulated, lymphocyte-specific pathways: VDJ- and switch-mediated recombination. Dysregulation of cyclin D1 by a t(11;14)(q13;q32) translocation occurs in most cases of mantle-cell lymphoma and in approximately 30% of multiple myeloma (MM) tumors in which a 14q32 translocation can be detected. We show here that in two of three myeloma lines that overexpress cyclin D1, there is an 11;14 translocation into a gamma switch region, suggesting an error in switch recombination. By contrast, 11;14 translocations in mantlecell lymphoma are invariably into or near a JH segment, suggesting an error in VDJ recombination. This is consistent with the fact that myeloma cells have undergone lgH switch recombination, whereas mantle-cell lymphoma cells generally have not.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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