Greehey CCRI Archives

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Nature: Promotion of DNA end resection by BRCA1–BARD1 in homologous recombination (Sung, Libich)

September 12, 2024

Sameer Salunkhe, James M. Daley, Hardeep Kaur, Nozomi Tomimatsu, Chaoyou Xue, Vivek B. Raina, Angela M. Jasper, Cody M. Rogers, Wenjing Li, Shuo Zhou, Rahul Mojidra, Youngho Kwon, Qingming Fang, Jae-Hoon Ji, Aida Badamchi Shabestari, O’Taveon Fitzgeral …


eLife: SERBP1 interacts with PARP1 and is Present in PARylation-Dependent Protein Complexes Regulating Splicing, Cell Division, and Ribosome Biogenesis (Penalva, Libich, et al)

July 3, 2024

Kira Breunig Xiufen Lei Mauro Montalbano Gabriela D. A. Guardia Shiva Ostadrahimi Victoria Alers Adam Kosti Jennifer Chiou Nicole Klein Corina Vinarov Lily Wang Mujia Li Weidan Song W. Lee Kraus David S. Libich Stefano Tiziani Susan T. Weintraub Pedro …


Journal of the American Chemical Society: ights into Molecular Diversity within the FUS/EWS/TAF15 Protein Family: Unraveling Phase Separation of the N-Terminal Low-Complexity Domain from RNA-Binding Protein EWS (Libich Lab)

April 8, 2024

Abstract The FET protein family, comprising FUS, EWS, and TAF15, plays crucial roles in mRNA maturation, transcriptional regulation, and DNA damage response. Clinically, they are linked to Ewing family tumors and neurodegenerative diseases such as amyo …


ELife: Defining function of wild-type and three patient specific TP53 mutations in a zebrafish model of embryonal rhabdomyosarcoma (Ignatius Lab, Houghton Lab, Libich Lab, Chen, Tomlinson)

June 2, 2023

Jiangfei Chen Kunal Baxi Amanda E Lipsitt Nicole Rae Hensch Long Wang Prethish Sreenivas Paulomi Modi Xiang Ru Zhao Antoine Baudin Daniel G Robledo Abhik Bandyopadhyay Aaron Sugalski Anil K Challa Dias Kurmashev Andrea R Gilbert Gail E Tomlinson Peter …


Biomolecules: Enhancing the Conformational Stability of the cl-Par-4 Tumor Suppressor via Site-Directed Mutagenesis (Libich Lab)

May 17, 2023

Samjhana Pandey Krishna K. Raut Andrea M. Clark  Antoine Baudin  Lamya Djemri  David S. Libich  Komala Ponniah Steven M. Pascal Abstract Intrinsically disordered proteins play important roles in cell signaling, and dysregulation of these proteins is as …


Biopolymers: Biochemical and biophysical characterization of the nucleic acid binding properties of the RNA/DNA binding protein EWS

March 21, 2023

Emily E. Selig,  Roohi Bhura,  Matthew R. White,  Shivani Akula,  Renee D. Hoffman,  Carmel N. Tovar,  Xiaoping Xu,  Rachell E. Booth,  David S. Libich Abstract EWS is a member of the FET family of RNA/DNA binding proteins that regulate crucial phases …


BioPhysics Journal: Unraveling the phase separation of EWS low complexity domain using molecular dynamics simulations (Libich Lab)

March 3, 2023

Kandarp A. Sojitra 1, Courtney Johnson 2 3, Erich Sohn 2 3, David Libich 2 3, Jeetain Mittal 1 EWS, an RNA-binding protein, is responsible for gene expression, cell signaling, RNA processing, and transport. It is a member of the FET (FUS, EWS, TAF15) f …


Biomolecular NMR Assignments: The 1H, 15N and 13C resonance assignments of the low-complexity domain from the oncogenic fusion protein EWS-FLI1 (Libich Lab)

January 12, 2022

Courtney N. Johnson, Xiaoping Xu, Stephen P. Holloway & David S. Libich Abstract The RNA-binding protein EWS is a multifunctional protein with roles in the regulation of transcription and RNA splicing. It is one of the FET (FUS, EWS, and TAF15) fam …


Childhood Cancer Q&A: David Libich, PhD

December 1, 2021

Asst Prof. David S. Libich, PhD,and members of his lab. What are some achievements you’ve made in advancing scientific knowledge relevant to childhood cancer research? My lab works on Ewing sarcoma, specifically on how the EWS-FLI1 oncogenic fusion pro …


JoVE: Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins (Libich Lab)

October 13, 2021

Courtney N. Johnson1, David S. Libich1 Abstract Intrinsically disordered proteins and intrinsically disordered regions within proteins make up a large and functionally significant part of the human proteome. The highly flexible nature of these sequence …


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