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Xiaomin Ni
Researcher at Goethe University Frankfurt
Publications - 22
Citations - 195
Xiaomin Ni is an academic researcher from Goethe University Frankfurt. The author has contributed to research in topics: Biology & Medicine. The author has an hindex of 5, co-authored 17 publications receiving 67 citations. Previous affiliations of Xiaomin Ni include Structural Genomics Consortium.
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Journal ArticleDOI
Targeting cavity-creating p53 cancer mutations with small-molecule stabilizers: the Y220X paradigm
Matthias R. Bauer,Andreas Krämer,Andreas Krämer,Giovanni Settanni,Rhiannon N. Jones,Xiaomin Ni,Xiaomin Ni,Raysa Khan Tareque,Alan R. Fersht,John Spencer,Andreas C. Joerger,Andreas C. Joerger +11 more
TL;DR: The data validate the Y220S and Y220N mutants as druggable targets and provide a framework for the design of Y 220S or Y 220N-specific compounds as well as compounds with dual Y220C/Y220S specificity for use in personalized cancer therapy.
Journal ArticleDOI
The orphan nuclear receptor Nurr1 is responsive to non-steroidal anti-inflammatory drugs
Sabine Willems,Whitney Kilu,Xiaomin Ni,Xiaomin Ni,Apirat Chaikuad,Apirat Chaikuad,Stefan Knapp,Stefan Knapp,Jan Heering,Daniel Merk +9 more
TL;DR: Non-steroidal anti-inflammatory drugs are shown to act as inverse Nurr1 agonists, and their interactions with the NR4A family are characterised.
Journal ArticleDOI
Structural Insights into Plasticity and Discovery of Remdesivir Metabolite GS-441524 Binding in SARS-CoV-2 Macrodomain
Xiaomin Ni,Xiaomin Ni,Martin Schröder,Martin Schröder,Vincent Olieric,M. Sharpe,Victor Hernandez-Olmos,Ewgenij Proschak,Ewgenij Proschak,Daniel Merk,Stefan Knapp,Stefan Knapp,Apirat Chaikuad,Apirat Chaikuad +13 more
TL;DR: The nsP3 macrodomain is a conserved protein interaction module that plays essential regulatory roles in the host immune response by recognizing and removing posttranslational ADP-ribosylation sites during SARS-CoV-2 infection as discussed by the authors.
Journal ArticleDOI
Structural Insights into Interaction Mechanisms of Alternative Piperazine-urea YEATS Domain Binders in MLLT1.
Xiaomin Ni,David Heidenreich,David Heidenreich,Thomas Christott,James M. Bennett,Moses Moustakim,Paul Brennan,Oleg Fedorov,Stefan Knapp,Stefan Knapp,Apirat Chaikuad,Apirat Chaikuad +11 more
TL;DR: Piperazine-urea derivatives are characterized as an acetyl/acyl-lysine mimetic moiety for MLLT1, revealing distinct interaction mechanisms of this chemotype compared to the recently described benzimidazole-amide based inhibitors.
Journal ArticleDOI
Pan-SMARCA/PB1 Bromodomain Inhibitors and Their Role in Regulating Adipogenesis.
Marek Wanior,Marek Wanior,Franziska Preuss,Franziska Preuss,Xiaomin Ni,Xiaomin Ni,Andreas Krämer,Andreas Krämer,Sebastian Mathea,Sebastian Mathea,Tamara Göbel,David Heidenreich,David Heidenreich,Svenja Simonyi,Astrid S. Kahnt,Andreas C. Joerger,Andreas C. Joerger,Stefan Knapp +17 more
TL;DR: Targeted SWI/SNF bromodomain inhibition blocked the expression of key genes during adipogenesis, including the transcription factors PPARγ and C/EBPα, and impaired the differentiation of 3T3-L1 murine fibroblasts into adipocytes.