ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • American Institute of Physics (AIP)  (2)
  • Genetics Society of America (GSA)  (1)
  • 1
    facet.materialart.
    Unknown
    Single-molecule detection of proteins with antigen-antibody interaction using resistive-pulse sensing of submicron latex particles (2016)
    American Institute of Physics (AIP)
    Details
    Publication Date: 2016-03-22
    Description: We developed a resistive-pulse sensor with a solid-state pore and measured the latex agglutination of submicron particles induced by antigen-antibody interaction for single-molecule detection of proteins. We fabricated the pore based on numerical simulation to clearly distinguish between monomer and dimer latex particles. By measuring single dimers agglutinated in the single-molecule regime, we detected single human alpha-fetoprotein molecules. Adjusting the initial particle concentration improves the limit of detection (LOD) to 95 fmol/l. We established a theoretical model of the LOD by combining the reaction kinetics and the counting statistics to explain the effect of initial particle concentration on the LOD. The theoretical model shows how to improve the LOD quantitatively. The single-molecule detection studied here indicates the feasibility of implementing a highly sensitive immunoassay by a simple measurement method using resistive-pulse sensing.
    Print ISSN: 0003-6951
    Electronic ISSN: 1077-3118
    Topics: Physics
    Published by American Institute of Physics (AIP)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    Electronic Resource
    Electronic Resource
    Magnetoresistance in magnetite films prepared from aqueous solution at room temperature (2000)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 87 (2000), S. 7127-7129 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Polycrystalline iron oxide films, 0.1–1.1 μm in thickness, are synthesized on glass substrates at room temperature directly from an aqueous solution of FeCl2 by ferrite plating. The films have a single phase spinel structure of mixed solution (Fe3O4)1−x–(γ-Fe2O3)x, as revealed by x-ray diffractometer and conversion electron 57Fe Mössbauer spectroscopy. At room temperature the films exhibit negative magnetoresistance (MR) of ratio ΔR/R=−3.3% to −7.4%, which is ascribed to intergranular tunneling of spin polarized electrons of Fe3O4. The resistivity R of the films is 2.2×100–1.3×103 Ω cm, much higher than that (∼10−2 Ω cm) reported for bulk samples of Fe3O4; R and ΔR/R depend on the plating conditions and, therefore, the composition x in (Fe3O4)1−x–(γ-Fe2O3)x of the samples. © 2000 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.372952
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    facet.materialart.
    Unknown
    Caenorhabditis elegans glp-4 Encodes a Valyl Aminoacyl tRNA Synthetase (2015)
    Genetics Society of America (GSA)
    Details
    Publication Date: 2015-12-10
    Description: Germline stem cell proliferation is necessary to populate the germline with sufficient numbers of cells for gametogenesis and for signaling the soma to control organismal properties such as aging. The Caenorhabditis elegans gene glp-4 was identified by the temperature-sensitive allele bn2 where mutants raised at the restrictive temperature produce adults that are essentially germ cell deficient, containing only a small number of stem cells arrested in the mitotic cycle but otherwise have a morphologically normal soma. We determined that glp-4 encodes a valyl aminoacyl transfer RNA synthetase ( VARS-2 ) and that the probable null phenotype is early larval lethality. Phenotypic analysis indicates glp-4 ( bn2ts ) is partial loss of function in the soma. Structural modeling suggests that bn2 Gly296Asp results in partial loss of function by a novel mechanism: aspartate 296 in the editing pocket induces inappropriate deacylation of correctly charged Val-tRNA val . Intragenic suppressor mutations are predicted to displace aspartate 296 so that it is less able to catalyze inappropriate deacylation. Thus glp-4 ( bn2ts ) likely causes reduced protein translation due to decreased levels of Val-tRNA val . The germline, as a reproductive preservation mechanism during unfavorable conditions, signals the soma for organismal aging, stress and pathogen resistance. glp-4 ( bn2ts ) mutants are widely used to generate germline deficient mutants for organismal studies, under the assumption that the soma is unaffected. As reduced translation has also been demonstrated to alter organismal properties, it is unclear whether changes in aging, stress resistance, etc. observed in glp-4 ( bn2ts ) mutants are the result of germline deficiency or reduced translation.
    Electronic ISSN: 2160-1836
    Topics: Biology
    Published by Genetics Society of America (GSA)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...