R
Raimund J. Ober
Researcher at Texas A&M University
Publications - 219
Citations - 8686
Raimund J. Ober is an academic researcher from Texas A&M University. The author has contributed to research in topics: Estimation theory & Multifocal plane microscopy. The author has an hindex of 43, co-authored 219 publications receiving 7830 citations. Previous affiliations of Raimund J. Ober include University of Texas at Dallas & University of Texas at Austin.
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Journal ArticleDOI
Localization Accuracy in Single-Molecule Microscopy
TL;DR: Using Monte Carlo simulations it is shown that estimation algorithms can come close to attaining the limit given in the expression and explicit quantitative results are provided to show how the limit of the localization accuracy is reduced by factors such as pixelation of the detector and noise sources in the detection system.
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Differences in promiscuity for antibody-FcRn interactions across species: implications for therapeutic antibodies.
TL;DR: An extensive analysis of the interaction of the human or mouse forms of FcRn with IgG from various species using surface plasmon resonance shows that in contrast to mouse F cRn, human Fc Rn is surprisingly stringent in its binding specificity for IgG derived from different species.
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Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels.
TL;DR: It is shown that an IgG whose Fc region was engineered to bind with higher affinity and reduced pH dependence to FcRn potently inhibits Fc Rn-IgG interactions and induces a rapid decrease of IgG levels in mice.
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Increasing the serum persistence of an IgG fragment by random mutagenesis.
Victor Ghetie,Serguei Popov,Jozef Borvak,Caius G. Radu,Diana Matesoi,Corneliu Medesan,Raimund J. Ober,E. Sally Ward +7 more
TL;DR: The results provide support for the involvement of FcRn in the home-ostasis of serum IgGs in mice and suggest that this approach has implications for increasing the serum persistence of therapeutic antibodies.
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Visualizing the Site and Dynamics of IgG Salvage by the MHC Class I-Related Receptor, FcRn
TL;DR: It is shown that segregation of FcRn-IgG complexes from unbound IgG occurs in the sorting endosome, and the pathways taken by F cRn and the transferrin receptor overlap, despite distinct mechanisms of ligand uptake.