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Grzegorz Piszczek
Researcher at National Institutes of Health
Publications - 86
Citations - 3221
Grzegorz Piszczek is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Medicine & Protein structure. The author has an hindex of 29, co-authored 75 publications receiving 2600 citations. Previous affiliations of Grzegorz Piszczek include Binghamton University & University of Gdańsk.
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Journal ArticleDOI
High-Precision Isothermal Titration Calorimetry with Automated Peak-Shape Analysis
TL;DR: A method for automated peak assignment based on peak-shape analysis via singular value decomposition in combination with detailed least-squares modeling of local pre- and postinjection baselines is described, which results in improved detection limits for high-affinity or low-enthalpy binding reactions and significantly higher precision of the derived thermodynamic parameters.
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SEDPHAT – A platform for global ITC analysis and global multi-method analysis of molecular interactions
TL;DR: The present communication reviews principles and strategies of global analysis for ITC and its extension to GMMA in SEDPHAT and introduces a new graphical tool for aiding experimental design by surveying the concentration space and generating simulated data sets, which can be subsequently statistically examined for their information content.
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Fixation-resistant photoactivatable fluorescent proteins for CLEM
Maria G Paez-Segala,Mei G Sun,Gleb Shtengel,Sarada Viswanathan,Michelle A. Baird,John J. Macklin,Ronak Patel,John R. Allen,Elizabeth S. Howe,Grzegorz Piszczek,Harald F. Hess,Michael W. Davidson,Yalin Wang,Loren L. Looger +13 more
TL;DR: E engineered variants of the photoconvertible Eos fluorescent protein are reported that fluoresce and photoconverts normally in heavily fixed samples, enabling correlative super-resolution fluorescence imaging and high-quality electron microscopy.
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Senataxin Mutation Reveals How R-Loops Promote Transcription by Blocking DNA Methylation at Gene Promoters
Christopher Grunseich,Isabel X. Wang,Jason A. Watts,Joshua T. Burdick,Robert D. Guber,Zhengwei Zhu,Alan Bruzel,Tyler Lanman,Ke-lian Chen,Alice B. Schindler,Nancy A. Edwards,Abhik Ray-Chaudhury,Jianhua Yao,Tanya J. Lehky,Grzegorz Piszczek,Barbara J. Crain,Kenneth H. Fischbeck,Vivian G. Cheung,Vivian G. Cheung +18 more
TL;DR: Results show that nucleic acid structures, in addition to sequences, influence the binding and activity of regulatory proteins in genome-wide R-loops.
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Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin.
TL;DR: The first crystal structure of TTL is presented, defining the structural scaffold upon which the diverse TTL-like family of tubulin-modifying enzymes is built and possibly modulating the partition oftubulin between monomeric and polymeric forms.