Search Results - "Libich, David S."

Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR by Libich, David S, Vitali Tugarinov, G. Marius Clore

“…The prototypical chaperonin GroEL assists protein folding through an ATP-dependent encapsulation mechanism. The details of how GroEL folds proteins remain…”
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Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR by Libich, David S., Fawzi, Nicolas L., Ying, Jinfa, Clore, G. Marius

“…The mechanism whereby the prototypical chaperonin GroEL performs work on substrate proteins has not yet been fully elucidated, hindered by lack of detailed…”
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Enhancing the Conformational Stability of the cl-Par-4 Tumor Suppressor via Site-Directed Mutagenesis by Pandey, Samjhana, Raut, Krishna K, Clark, Andrea M, Baudin, Antoine, Djemri, Lamya, Libich, David S, Ponniah, Komala, Pascal, Steven M

“…Intrinsically disordered proteins play important roles in cell signaling, and dysregulation of these proteins is associated with several diseases. Prostate…”
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Defining function of wild-type and three patient-specific TP53 mutations in a zebrafish model of embryonal rhabdomyosarcoma by Chen, Jiangfei, Baxi, Kunal, Lipsitt, Amanda E, Hensch, Nicole Rae, Wang, Long, Sreenivas, Prethish, Modi, Paulomi, Zhao, Xiang Ru, Baudin, Antoine, Robledo, Daniel G, Bandyopadhyay, Abhik, Sugalski, Aaron, Challa, Anil K, Kurmashev, Dias, Gilbert, Andrea R, Tomlinson, Gail E, Houghton, Peter, Chen, Yidong, Hayes, Madeline N, Chen, Eleanor Y, Libich, David S, Ignatius, Myron S

“…In embryonal rhabdomyosarcoma (ERMS) and generally in sarcomas, the role of wild-type and loss- or gain-of-function mutations remains largely undefined…”
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Reply to Marchenko et al: Flux analysis of GroEL-assisted protein folding/unfolding by Libich, David S., Tugarinov, Vitali, Clore, G. Marius

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Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes by Baudin, Antoine, Moreno-Romero, Alma K., Xu, Xiaoping, Selig, Emily E., Penalva, Luiz O. F., Libich, David S.

“…RNA binding proteins (RBPs) are essential for critical biological processes such as translation regulation and mRNA processing, and misfunctions of these…”
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Order and disorder bound together in SARS-CoV-2 Nsp1 suppress host translation by Libich, David S., Baudin, Antoine

“…In this issue of Structure, Wang et al. investigate the interplay between folded and disordered regions of the SARS-CoV-2 non-structural protein 1 (Nsp1) that…”
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Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis by Harauz, George, Ishiyama, Noboru, Hill, Christopher M.D, Bates, Ian R, Libich, David S, Farès, Christophe

“…The 18.5 kDa isoform of myelin basic protein (MBP) is a major component of the myelin sheath in the central nervous system of higher vertebrates, and a member…”
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Squishy to crusty: Biophysics reveal the molecular details of FUS droplet maturation by Sohn, Erich J, Libich, David S

“…In a recent issue of Nature Chemical Biology, Emmanouilidis et al. (2024) investigate the maturation of biomolecular condensates of FUS and probe the molecular…”
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Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP) by Libich, David S., Harauz, George

“…The stability and secondary structure propensity of recombinant murine 18.5 kDa myelin basic protein (rmMBP, 176 residues) was assessed using circular dichroic…”
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Hijacking the BAF complex: the mechanistic interplay of ARID1A and EWS::FLI1 in Ewing sarcoma by Sohn, Erich J, Libich, David S

“…Ewing sarcoma, an aggressive pediatric cancer, is driven by the EWS::FLI1 fusion protein, which disrupts gene expression by hijacking the BAF chromatin…”
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Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR by Kotler, Samuel A., Tugarinov, Vitali, Schmidt, Thomas, Ceccon, Alberto, Libich, David S., Ghirlando, Rodolfo, Schwieters, Charles D., Clore, G. Marius

“…The N-terminal region of the huntingtin protein, encoded by exon-1, comprises an amphiphilic domain (httNT), a polyglutamine (Q n ) tract, and a proline-rich…”
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Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR by Libich, David S, Tugarinov, Vitali, Ghirlando, Rodolfo, Clore, G. Marius

“…The interaction of two folding intermediate mimetics of the model protein substrate Fyn SH3 with the chaperonin GroEL, a supramolecular foldase/unfoldase…”
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Insights 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 by Johnson, Courtney N., Sojitra, Kandarp A., Sohn, Erich J., Moreno-Romero, Alma K., Baudin, Antoine, Xu, Xiaoping, Mittal, Jeetain, Libich, David S.

“…The FET protein family, comprising FUS, EWS, and TAF15, plays crucial roles in mRNA maturation, transcriptional regulation, and DNA damage response…”
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins by Johnson, Courtney N, Libich, David S

“…Intrinsically disordered proteins and intrinsically disordered regions within proteins make up a large and functionally significant part of the human proteome…”
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Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using ¹³C(methyl)-DEST and lifetime line broadening by Fawzi, Nicolas L, Libich, David S, Ying, Jinfa, Tugarinov, Vitali, Clore, G Marius

“…Many details pertaining to the formation and interactions of protein aggregates associated with neurodegenerative diseases are invisible to conventional…”
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Biochemical and biophysical characterization of the nucleic acid binding properties of the RNA/DNA binding protein EWS by Selig, Emily E., Bhura, Roohi, White, Matthew R., Akula, Shivani, Hoffman, Renee D., Tovar, Carmel N., Xu, Xiaoping, Booth, Rachell E., Libich, David S.

“…EWS is a member of the FET family of RNA/DNA binding proteins that regulate crucial phases of nucleic acid metabolism. EWS comprises an N‐terminal…”
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Promotion of DNA end resection by BRCA1–BARD1 in homologous recombination by Salunkhe, Sameer, Daley, James M., Kaur, Hardeep, Tomimatsu, Nozomi, Xue, Chaoyou, Raina, Vivek B., Jasper, Angela M., Rogers, Cody M., Li, Wenjing, Zhou, Shuo, Mojidra, Rahul, Kwon, Youngho, Fang, Qingming, Ji, Jae-Hoon, Badamchi Shabestari, Aida, Fitzgerald, O’Taveon, Dinh, Hoang, Mukherjee, Bipasha, Habib, Amyn A., Hromas, Robert, Mazin, Alexander V., Wasmuth, Elizabeth V., Olsen, Shaun K., Libich, David S., Zhou, Daohong, Zhao, Weixing, Greene, Eric C., Burma, Sandeep, Sung, Patrick

“…The licensing step of DNA double-strand break repair by homologous recombination entails resection of DNA ends to generate a single-stranded DNA template for…”
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The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy by Tugarinov, Vitali, Libich, David S., Meyer, Virginia, Roche, Julien, Clore, G. Marius

“…The energetic and volumetric properties of a three‐state protein folding system, comprising a metastable triple mutant of the Fyn SH3 domain, have been…”
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Extensive Sampling of the Cavity of the GroEL Nanomachine by Protein Substrates Probed by Paramagnetic Relaxation Enhancement by Wälti, Marielle A, Libich, David S, Clore, G. Marius

“…The chaperonin GroEL is a 800 kDa nanomachine comprising two heptameric rings, each of which encloses a large cavity or folding chamber. The GroEL cycle…”
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