Peter B. Berget
Carnegie Mellon University
25 Papers
299 Citations
Peter B. Berget is an academic researcher from Carnegie Mellon University. The author has contributed to research in topics: Gene & Cyanine. The author has an hindex of 17, co-authored 25 publications. Previous affiliations of Peter B. Berget include University of the Sciences & University UCINF.
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Papers
Fluorogen-activating single-chain antibodies for imaging cell surface proteins
Christopher Szent-Gyorgyi,Brigitte F. Schmidt,Yehuda Creeger,Gregory W. Fisher,Kelly L Zakel,Sally A. Adler,James A. J. Fitzpatrick,Carol A. Woolford,Qi Yan,Kalin V. Vasilev,Peter B. Berget,Marcel P. Bruchez,Jonathan W. Jarvik,Alan S. Waggoner +13 more
TL;DR: The development of protein reporters that generate fluorescence from otherwise dark molecules (fluorogens) is reported, isolated by screening a library of human single-chain antibodies using derivatives of thiazole orange and malachite green.
A rainbow of fluoromodules: a promiscuous scFv protein binds to and activates a diverse set of fluorogenic cyanine dyes.
Hayriye Ozhalici-Unal,Crystal Lee Pow,Sarah A. Marks,Lawrence D. Jesper,Gloria L. Silva,Nathaniel I. Shank,Elizabeth W. Jones,James M. Burnette,Peter B. Berget,Bruce A. Armitage +9 more
TL;DR: One of these FAPs exhibits considerable promiscuity, binding with high affinity to several other fluorogenic cyanine dyes with emission wavelengths covering most of the visible and near-IR regions of the spectrum, significantly expands the number and wavelength range of scFv-based fluoromodules.
Enhanced photostability of genetically encodable fluoromodules based on fluorogenic cyanine dyes and a promiscuous protein partner.
TL;DR: A previously reported promiscuous binding interaction between a single-chain, variable fragment antibody protein and a family of cyanine dyes is exploited to create new protein-dye fluoromodules that exhibit enhanced photostability while retaining high affinity protein- dye binding.
Phage P22 tail protein: gene and amino acid sequence
TL;DR: Comparison of the gene and protein sequences indicates that mature tail protein arises by cleavage of the initiator N-formyl-methionine from the nascent chain.
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STED Nanoscopy in Living Cells Using Fluorogen Activating Proteins
James A. J. Fitzpatrick,Qi Yan,Jochen J. Sieber,Marcus Dyba,Ulf Schwarz,Christopher Szent-Gyorgyi,Carol A. Woolford,Peter B. Berget,Alan S. Waggoner,Marcel P. Bruchez +9 more
TL;DR: It is demonstrated the effectiveness of a genetically encoded Malachite Green binding fluorogen activating protein for live cell stimulated emission depletion nanoscopy (STED) and suggests a resolution of 70nm with the given instrument.
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