C
Clemens Grimm
Researcher at University of Würzburg
Publications - 39
Citations - 1024
Clemens Grimm is an academic researcher from University of Würzburg. The author has contributed to research in topics: DNA & RNA polymerase. The author has an hindex of 15, co-authored 33 publications receiving 855 citations. Previous affiliations of Clemens Grimm include University of Marburg & Max Planck Society.
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Journal ArticleDOI
Structural basis for LEAFY floral switch function and similarity with helix-turn-helix proteins
Cécile Hamès,Denis Ptchelkine,Clemens Grimm,Emmanuel Thévenon,Edwige Moyroud,Francine C. A. Gérard,Jean-Louis Martiel,Reyes Benlloch,François Parcy,Christoph W. Müller +9 more
TL;DR: The LEAFY (LFY) protein is a key regulator of flower development in angiosperms as mentioned in this paper, and its gradually increased expression governs the sharp floral transition, and LFY subsequently controls the patterning of flower meristems by inducing the expression of floral homeotic genes.
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The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family.
TL;DR: The crystal structure of 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni (3α-HSDH) as well as the structure of its binary complex with NAD+ have been solved at 1.68-Å and 1.95-™ resolution.
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Molecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbt.
Clemens Grimm,Raquel Matos,Nga Ly-Hartig,Ulrich Steuerwald,Doris Lindner,Vladimir Rybin,Jürg Müller,Christoph W. Müller +7 more
TL;DR: dSfmbt and Scm co‐occupy Polycomb response elements of target genes in Drosophila and they strongly synergize in the repression of these target genes, suggesting that the combined action of these two MBT proteins is crucial for Polycomb silencing.
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Structural Basis of Assembly Chaperone- Mediated snRNP Formation
Clemens Grimm,Ashwin Chari,Ashwin Chari,Jann Patrick Pelz,Jochen Kuper,Caroline Kisker,Kay Diederichs,Holger Stark,Hermann Schindelin,Utz Fischer +9 more
TL;DR: The studies reveal how assembly factors facilitate formation of RNA-protein complexes in vivo and reveal a plausible mechanism of pICln elimination and Sm protein activation for snRNA binding.
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ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space
Ashwin Chari,David Haselbach,Jan-Martin Kirves,Juergen Ohmer,Elham Paknia,Niels Fischer,Oleg M. Ganichkin,Vanessa Möller,Jeremiah J. Frye,Georg Petzold,Marc A. Jarvis,Michael Tietzel,Clemens Grimm,Jan-Michael Peters,Brenda A. Schulman,Kai Tittmann,Jürgen Markl,Utz Fischer,Holger Stark +18 more
TL;DR: A generic method that optimizes the stability, homogeneity and solubility of macromolecular complexes by sparse-matrix screening of their thermal unfolding behavior in the presence of various buffers and small molecules is presented.