M
Michael Geralt
Researcher at Scripps Research Institute
Publications - 27
Citations - 5705
Michael Geralt is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Structural genomics & Protein structure. The author has an hindex of 13, co-authored 27 publications receiving 5413 citations. Previous affiliations of Michael Geralt include Scripps Health & Salk Institute for Biological Studies.
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Journal ArticleDOI
Genome-Wide Insertional Mutagenesis of Arabidopsis thaliana
Jose M. Alonso,Anna Stepanova,Thomas J. Leisse,Christopher J. Kim,Huaming Chen,Paul Shinn,Denise K. Stevenson,Justin Zimmerman,Pascual Barajas,Rosa Cheuk,Carmelita Gadrinab,Collen Heller,Albert Jeske,Eric Koesema,Cristina C. Meyers,Holly Parker,Lance Prednis,Yasser Ansari,Nathan Choy,Hashim Deen,Michael Geralt,Nisha Hazari,Emily Hom,Meagan Karnes,Celene Mulholland,Ral Ndubaku,Ian Thomas Schmidt,Plinio Guzmán,Laura Aguilar-Henonin,Markus Schmid,Detlef Weigel,David E. Carter,Trudy Marchand,Eddy Risseeuw,Debra Brogden,Albana Zeko,William L. Crosby,Charles C. Berry,Joseph R. Ecker +38 more
TL;DR: Genome-wide analysis of the distribution of integration events revealed the existence of a large integration site bias at both the chromosome and gene levels, and insertion mutations were identified in genes that are regulated in response to the plant hormone ethylene.
Journal ArticleDOI
Novel β-Barrel Fold in the Nuclear Magnetic Resonance Structure of the Replicase Nonstructural Protein 1 from the Severe Acute Respiratory Syndrome Coronavirus
TL;DR: The nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128 is reported, which represents a novel α/β-fold formed by a mixed parallel/antiparallel six-stranded β-barrel, an α-helix covering one opening of the barrel, and a 310-helIX alongside the barrel.
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The J-UNIO protocol for automated protein structure determination by NMR in solution.
Pedro Serrano,Bill Pedrini,Bill Pedrini,Bill Pedrini,Biswaranjan Mohanty,Biswaranjan Mohanty,Michael Geralt,Torsten Herrmann,Kurt Wüthrich,Kurt Wüthrich +9 more
TL;DR: Applications with proteins from the JCSG target list with sizes up to 150 residues showed that the procedure is highly robust and efficient, and in all instances the correct polypeptide fold was obtained in the first round of automated data analysis and structure calculation.
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Microscale NMR Screening of New Detergents for Membrane Protein Structural Biology
Qinghai Zhang,Reto Horst,Michael Geralt,Xingquan Ma,Wen-Xu Hong,M. G. Finn,Raymond C. Stevens,Kurt Wüthrich +7 more
TL;DR: It is demonstrated that microcoil nuclear magnetic resonance (NMR) technology can be used to screen microscale quantities of membrane proteins for proper folding in samples destined for structural studies.
Journal ArticleDOI
UHM–ULM interactions in the RBM39–U2AF65 splicing-factor complex
Galina A. Stepanyuk,Pedro Serrano,Eigen R. Peralta,Carol L. Farr,Carol L. Farr,Herbert L. Axelrod,Michael Geralt,Debanu Das,Hsiu-Ju Chiu,Lukasz Jaroszewski,Lukasz Jaroszewski,Ashley M. Deacon,Scott A. Lesley,Scott A. Lesley,Marc-André Elsliger,Adam Godzik,Adam Godzik,Ian A. Wilson,Kurt Wüthrich,Daniel R. Salomon,James R. Williamson +20 more
TL;DR: The RBM39-U2AF65 interaction was confirmed by co-immunoprecipitation from human cell extracts, by isothermal titration calorimetry and by NMR chemical shift perturbation experiments with the purified proteins, and this study establishes a structural basis for specific UHM-ULM interactions by splicing factors.