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  • 1
    In: Business and Economics Journal, 2014, Vol.05(04)
    ISSN: Business and Economics Journal
    E-ISSN: 21516219
    Source: CrossRef
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  • 2
    Language: English
    In: Journal of the American College of Cardiology, 25 December 2012, Vol.60(25), pp.e165-e165
    Description: The echocardiography (A and B, Online Videos 1 and 2) showed a large aorto-pulmonary window (APW, arrow in A) with a broad communication between the aorta (AO) and pulmonary artery (PA), anomalous origin of left pulmonary artery (LPA) from the right pulmonary artery with retrotracheal course (asterisk...
    Keywords: Medicine
    ISSN: 0735-1097
    E-ISSN: 1558-3597
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  • 3
    In: Nature, 2014, Vol.505(7485), p.648
    Keywords: Sciences (General) ; Physics;
    ISSN: 0028-0836
    E-ISSN: 14764687
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  • 4
    In: Journal of Socialomics, 2015, Vol.04(01)
    ISSN: Journal of Socialomics
    E-ISSN: 21670358
    Source: CrossRef
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  • 5
    Language: English
    In: The Journal of Virology, 2011, Vol. 85(11), p.5350
    Description: Recently, we showed that the Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) VP80 protein is essential for the formation of both virion types, budded virus (BV) and occlusion-derived virus (ODV). Deletion of the vp80 gene did not affect assembly of nucleocapsids. However, these nucleocapsids were not able to migrate from the virogenic stroma to the nuclear periphery. In the current paper, we constructed a baculovirus recombinant with enhanced-green fluorescent protein (EGFP)-tagged VP80, allowing visualization of the VP80 distribution pattern during infection. In baculovirus-infected cells, the EGFP-VP80 protein is entirely localized in nuclei, adjacent to the virus-triggered F-actin scaffold that forms a highly organized three-dimensional network connecting the virogenic stroma physically with the nuclear envelope. Interaction between VP80 and host actin was confirmed by coimmunoprecipitation. We further showed that VP80 is associated with the nucleocapsid fraction of both BVs and ODVs, typically at one end of the nucleocapsids. In addition, the presence of sequence motifs with homology to invertebrate paramyosin proteins strongly supports a role for VP80 in the polar transport of nucleocapsids to the periphery of the nucleus on their way to the plasma membrane to form BVs and for assembly in the nuclear periphery to form ODVs for embedding in viral occlusion bodies.
    Keywords: Stroma ; Virions ; Replication ; Infection ; Embedding ; Scaffolds ; Cytoskeleton ; Gene Deletion ; Plasma Membranes ; Homology ; Nuclear Membranes ; Nucleocapsids ; Actin ; Occlusion Bodies ; Cell Migration ; Nuclei ; Nuclear Polyhedrosis Virus ; Autographa Californica ; Baculovirus ; Replication;
    ISSN: 0022-538X
    ISSN: 0022538X
    E-ISSN: 10985514
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  • 6
    Language: English
    In: Nature, 30 January 2014, Vol.505(7485), pp.648-53
    Description: H2A.Z is an essential histone variant implicated in the regulation of key nuclear events. However, the metazoan chaperones responsible for H2A.Z deposition and its removal from chromatin remain unknown. Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone. We show that ANP32E is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). The 1.48 Å resolution crystal structure of the complex formed between the ANP32E-ZID and the H2A.Z/H2B dimer and biochemical data support an underlying molecular mechanism for H2A.Z/H2B eviction from the nucleosome and its stabilization by ANP32E through a specific extension of the H2A.Z carboxy-terminal α-helix. Finally, analysis of H2A.Z localization in ANP32E(-/-) cells by chromatin immunoprecipitation followed by sequencing shows genome-wide enrichment, redistribution and accumulation of H2A.Z at specific chromatin control regions, in particular at enhancers and insulators.
    Keywords: Chromatin -- Chemistry ; Histones -- Metabolism ; Molecular Chaperones -- Metabolism ; Nuclear Proteins -- Metabolism ; Phosphoproteins -- Metabolism
    ISSN: 00280836
    E-ISSN: 1476-4687
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  • 7
    Language: English
    In: Materials Letters, 01 October 2016, Vol.180, pp.280-283
    Description: The twist channel angular pressing (TCAP) technology was recently developed in accordance to the contemporary trend of increasing the efficiency of severe plastic deformation technologies. This study was aimed to analyse structural changes, particularly grain sizes and orientations and textures, in commercial purity aluminium after a single pass TCAP and to put the structure in connection with the strain path. For comparison, another sample processed by two passes equal channel angular pressing (ECAP), Bc route, was analysed. Three independent shear planes affecting the material during a single pass TCAP caused the grains to refine down to the average size of 5.8 µm. The sample after a TCAP pass also exhibited highly developed subgrains. The textures of the samples exhibited differences in preferential orientations and their intensities.
    Keywords: Twist Channel Angular Pressing ; Aluminium ; Texture ; Microstructure ; Electron Microscopy ; Metal Forming and Shaping ; Engineering ; Physics
    ISSN: 0167-577X
    E-ISSN: 1873-4979
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  • 8
    Language: English
    In: Journal of medicinal chemistry, 25 February 2016, Vol.59(4), pp.1545-55
    Description: Histone deacetylase 6 (HDAC6) catalyzes the removal of an acetyl group from lysine residues of several non-histone proteins. Here we report the preparation of thiazole-, oxazole-, and oxadiazole-containing biarylhydroxamic acids by a short synthetic procedure. We identified them as selective HDAC6 inhibitors by investigating the inhibition of recombinant HDAC enzymes and the protein acetylation in cells by Western blotting (tubulin vs histone acetylation). The most active compounds exhibited nanomolar potency and high selectivity for HDAC6. For example, an oxazole hydroxamate inhibits HDAC6 with an IC50 of 59 nM and has a selectivity index of 〉200 against HDAC1 and HDAC8. This is the first report showing that the nature of a heterocycle directly connected to a zinc binding group (ZBG) can be used to modulate subtype selectivity and potency for HDAC6 inhibitors to such an extent. We rationalize the high potency and selectivity of the oxazoles by molecular modeling and docking.
    Keywords: Histone Deacetylase Inhibitors -- Chemistry ; Histone Deacetylases -- Metabolism ; Hydroxamic Acids -- Chemistry ; Oxazoles -- Chemistry
    ISSN: 00222623
    E-ISSN: 1520-4804
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  • 9
    Language: English
    In: BMC Biology, 01 April 2010, Vol.8(1), p.32
    Description: Abstract Tiny marine animals that complete their life cycle in the total absence of light and oxygen are reported by Roberto Danovaro and colleagues in this issue of BMC Biology. These fascinating animals are new members of the phylum Loricifera and possess mitochondria that in electron micrographs...
    Keywords: Biology
    ISSN: 1741-7007
    E-ISSN: 1741-7007
    Source: Directory of Open Access Journals (DOAJ)
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  • 10
    Language: English
    In: Biotechnology and Bioengineering, May 2011, Vol.108(5), pp.1056-1067
    Description: A novel baculovirus‐based protein expression strategy was developed to produce recombinant proteins in insect cells without contaminating baculovirus virions. This novel strategy greatly simplifies the downstream processing of biopharmaceuticals produced in insect cells. The formation of these virions is prevented by deletion of a baculovirus gene essential for virion formation. The deletion is complemented in a transgenic insect cell line in which the baculovirus seed stock is produced. The multicapsid nucleopolyhedrovirus gene was selected for this purpose, as absence of VP80 prevented the formation of budded virus as well as occlusion‐derived virus, while foreign gene expression was not affected. Sf9 insect cells were engineered to functionally complement the deletion in the expression vector virus during seed stock production. The ‐complemented ‐deletion baculovirus seed produced an amount of recombinant protein similar to that produced with conventional baculovirus vectors but without contaminating virions. This novel expression method obviates the need to purify the virions away from the biopharmaceuticals. Bioeng. 2011; 108:1056–1067. © 2010 Wiley Periodicals, Inc.
    Keywords: Baculovirus‐Expression System ; Autographa Californica Mnpv ; Vp80 ; Virus Particles ; Insect Cells ; Biopharmaceuticals
    ISSN: 0006-3592
    E-ISSN: 1097-0290
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