Search Results - "Clore, G.Marius"

Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA by Cai, Mengli, Huang, Ying, Ghirlando, Rodolfo, Wilson, Katherine L., Craigie, Robert, Clore, G.Marius

“…The nuclear envelope proteins LAP2, emerin and MAN1 share a conserved ∼40‐residue ‘LEM’ motif. Loss of emerin causes Emery–Dreifuss muscular dystrophy. We have…”
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Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA by Braddock, Demetrios T., Baber, James L., Levens, David, Clore, G. Marius

“…To elucidate the basis of sequence‐specific single‐stranded (ss) DNA recognition by K homology (KH) domains, we have solved the solution structure of a complex…”
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A Robust Method for Determining the Magnitude of the Fully Asymmetric Alignment Tensor of Oriented Macromolecules in the Absence of Structural Information by Clore, G.Marius, Gronenborn, Angela M., Bax, Ad

“…It has recently been shown that the degree of alignment of macromolecules in an aqueous dilute liquid crystalline medium of bicelles is sufficient to permit…”
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The VMD-XPLOR Visualization Package for NMR Structure Refinement by Schwieters, Charles D., Clore, G.Marius

“…In this paper we present the VMD-XPLOR package combining the XPLOR refinement program and the VMD visualization program and including extensions for use in the…”
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Improvements and Extensions in the Conformational Database Potential for the Refinement of NMR and X-ray Structures of Proteins and Nucleic Acids by Kuszewski, John, Gronenborn, Angela M., Clore, G.Marius

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Theoretical and computational advances in biomolecular NMR spectroscopy by Clore, G.Marius, Schwieters, Charles D

“…Recent developments in experimental and computational aspects of NMR spectroscopy have had a significant impact on the accuracy and speed of macromolecular…”
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Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors by Huang, Kai, Louis, John M., Donaldson, Logan, Lim, Fei-Ling, Sharrocks, Andrew D., Clore, G. Marius

“…The solution structure of the 33 kDa complex between the dimeric DNA‐binding core domain of the transcription factor MEF2A (residues 1–85) and a 20mer DNA…”
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Visualization of the Phosphorylated Active Site Loop of the Cytoplasmic B Domain of the Mannitol Transporter IIMannitol of the Escherichia coli Phosphotransferase System by NMR Spectroscopy and Residual Dipolar Couplings by Suh, Jeong-Yong, Tang, Chun, Cai, Mengli, Clore, G.Marius

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The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin by Qin, J, Clore, G M, Gronenborn, A M

“…Thioredoxin is a ubiquitous protein and is involved in a variety of fundamental biological functions. Its active site is conserved and has two redox active…”
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Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations by Nilges, Michael, Clore, G.Marius, Gronenborn, Angela M.

“…A new hybrid distance space-real space method for determining three-dimensional structures of proteins on the basis of interproton distance restraints is…”
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Structural comparisons among the short-chain helical cytokines by Rozwarski, D A, Gronenborn, A M, Clore, G M, Bazan, J F, Bohm, A, Wlodawer, A, Hatada, M, Karplus, P A

“…Cytokines and growth factors are soluble proteins that regulate the development and activities of many cell types. One group of these proteins have structures…”
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Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy by Schmidt, Thomas, Wälti, Marielle A., Baber, James L., Hustedt, Eric J., Clore, G. Marius

“…Current distance measurements between spin‐labels on multimeric protonated proteins using double electron–electron resonance (DEER) EPR spectroscopy are…”
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Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy by Clore, G M, Robien, M A, Gronenborn, A M

“…The effects of the number, precision and accuracy of interproton distance restraints, of direct refinement against nuclear Overhauser enhancement (NOE)…”
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Targeting a Dark Excited State of HIV‐1 Nucleocapsid by Antiretroviral Thioesters Revealed by NMR Spectroscopy by Deshmukh, Lalit, Tugarinov, Vitali, Appella, Daniel H., Clore, G. Marius

“…HIV‐1 nucleocapsid (NCp7) is a two Cys2HisCys zinc knuckle (N‐Zn and C‐Zn) protein that plays a key role in viral replication. NCp7 conformational dynamics is…”
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Quantitative Resolution of Monomer-Dimer Populations by Inversion Modulated DEER EPR Spectroscopy by Schmidt, Thomas, Ghirlando, Rodolfo, Baber, James, Clore, G. Marius

“…A simple method, based on inversion modulated double electron–electron resonance electron paramagnetic resonance (DEER EPR) spectroscopy, is presented for…”
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Dependence of Distance Distributions Derived from Double Electron-Electron Resonance Pulsed EPR Spectroscopy on Pulse-Sequence Time by Baber, James L., Louis, John M., Clore, G. Marius

“…Pulsed double electron–electron resonance (DEER) provides pairwise P(r) distance distributions in doubly spin labeled proteins. We report that in protonated…”
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Molecular Basis for Synergistic Transcriptional Activation by Oct1 and Sox2 Revealed from the Solution Structure of the 42-kDa Oct1·Sox2·Hoxb1-DNA Ternary Transcription Factor Complex by Williams, David C., Cai, Mengli, Clore, G.Marius

“…The Oct and Sox transcription factors control many different aspects of neural development and embryogenesis, often binding to adjacent sites on DNA, and…”
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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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Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by Wang, Guangshun, Louis, John M., Sondej, Melissa, Seok, Yeong-Jae, Peterkofsky, Alan, Clore, G.Marius

“…The solution structure of the second protein–protein complex of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system, that between…”
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Investigation of the Structure and Dynamics of the Capsid-Spacer Peptide 1-Nucleocapsid Fragment of the HIV-1 Gag Polyprotein by Solution NMR Spectroscopy by Deshmukh, Lalit, Ghirlando, Rodolfo, Clore, G. Marius

“…Structural studies of HIV‐1 Gag, the primary structural polyprotein involved in retroviral assembly, have been challenging, owing to its flexibility and…”
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