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index medicus (37) 37
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1. Full Text Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
by Xing, Qiong and Shi, Ke and Portaliou, Athina and Rossi, Paolo and Economou, Anastassios and Kalodimos, Charalampos G and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 1773 - 9
The flagellum and the injectisome enable bacterial locomotion and pathogenesis, respectively. These nanomachines assemble and function using a type III... 
CYTOPLASMIC DOMAIN | PROTEIN EXPORT | MECHANISM | RECOGNITION | MULTIDISCIPLINARY SCIENCES | COMPONENTS | SWITCH | FLAGELLUM | APPARATUS | FLHA | DELIVERY | Molecular Chaperones - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Molecular Chaperones - chemistry | Protein Transport | Salmonella typhimurium - metabolism | Cryoelectron Microscopy | Type III Secretion Systems - metabolism | Multiprotein Complexes - metabolism | Multiprotein Complexes - ultrastructure | Multiprotein Complexes - chemistry | Flagella - metabolism | Protein Binding | Bacterial Proteins - metabolism | Protein Conformation | Proteins | Locomotion | Conserved sequence | Pathogenesis | Secretion | Flagellin | Chaperones | Protein transport | Flagella | Substrates | Recognition | Exports
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2. Full Text Gleevec Can Act as an Allosteric Activator of ABL Kinase
by Xie, Tao and Saleh, Tamjeed and Kalodimos, Charalampos G
Biophysical Journal, ISSN 0006-3495, 02/2018, Volume 114, Issue 3, pp. 229a - 229a
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3. Full Text Confirmation for conformational selection
by Jiang, Yajun and Kalodimos, Charalampos G
eLife, ISSN 2050-084X, 02/2018, Volume 7
NMR studies settle part of a long-standing debate about the mechanism used by the Hsp70 chaperone to recognize substrates. 
BIOLOGY | Models, Molecular | Protein Binding | Protein Conformation | Molecular Chaperones | HSP70 Heat-Shock Proteins | Physiological aspects | Heat shock proteins | Substrates (Biochemistry) | Molecular chaperones | Proteins | Hypotheses | Nuclear magnetic resonance--NMR | Spectrum analysis | Amino acids | Hsp70 protein | Binding sites
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4. Full Text Protein activity regulation by conformational entropy
by Tzeng, Shiou-Ru and Kalodimos, Charalampos G
Nature, ISSN 0028-0836, 08/2012, Volume 488, Issue 7410, pp. 236 - 240
How the interplay between protein structure and internal dynamics regulates protein function is poorly understood. Often, ligand binding, post-translational... 
LIGAND-BINDING | MOLECULAR RECOGNITION | DYNAMIC ACTIVATION | NMR-SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | ORDER PARAMETERS | CATABOLITE ACTIVATOR PROTEIN | RELAXATION | RECEPTOR PROTEIN | FREE-ENERGY | Protein Structure, Tertiary | Motion | Models, Molecular | Cyclic AMP Receptor Protein - genetics | Entropy | DNA - metabolism | Cyclic AMP Receptor Protein - metabolism | DNA - chemistry | Cyclic AMP Receptor Protein - chemistry | Time Factors | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Binding Sites | Proteins | Nuclear magnetic resonance spectroscopy | Usage | Research | Structure | Protein binding | Enzymes | Ligands | Experiments | Compensation
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5. Full Text Dynamic activation of an allosteric regulatory protein
by Tzeng, Shiou-Ru and Kalodimos, Charalampos G
Nature, ISSN 0028-0836, 11/2009, Volume 462, Issue 7271, pp. 368 - 372
Allosteric regulation is used as a very efficient mechanism to control protein activity in most biological processes, including signal transduction,... 
CONFORMATIONAL ENTROPY | ANGSTROM RESOLUTION | NMR-SPECTROSCOPY | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | ORDER PARAMETERS | CAMP RECEPTOR PROTEIN | CHEMICAL-EXCHANGE | BINDING PROTEIN | CAP-DNA COMPLEX | ROTATIONAL DIFFUSION | Protein Structure, Tertiary | Cyclic AMP - chemistry | Cyclic AMP Receptor Protein - chemistry | Energy Metabolism | Escherichia coli - metabolism | Models, Molecular | Protein Binding | Escherichia coli Proteins - metabolism | DNA - metabolism | Escherichia coli Proteins - chemistry | Cyclic AMP - metabolism | Cyclic AMP Receptor Protein - metabolism | Usage | Allosteric proteins | Physiological aspects | Nuclear magnetic resonance spectroscopy | Cellular signal transduction | Research | Structure | DNA-ligand interactions | Proteins | Changes | Biochemistry | Entropy | E coli
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6. Recognition and targeting mechanisms by chaperones in flagellum assembly and operation
by Nandish Khanra and Paolo Rossi and Anastassios Economou and Charalampos G Kalodimos
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2016, Volume 113, Issue 35, p. 9798
  The flagellum is a complex bacterial nanomachine that requires the proper assembly of several different proteins for its function. Dedicated chaperones are... 
Proteins | Cytoplasm | Substrates | Binding sites
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7. Full Text NMR illuminates the pathways to ALS
by Xie, Tao and Kalodimos, Charalampos G
eLife, ISSN 2050-084X, 06/2015, Volume 4, Issue JUNE, p. e08679
A combination of NMR techniques is able to explore the structure of short-lived protein conformations. 
DYNAMICS | STATES | CONFORMATION | BIOLOGY | Superoxide Dismutase - chemistry | Humans | Protein Folding - radiation effects | Superoxide Dismutase - metabolism | Proteins | Enzymes | Nuclear magnetic resonance--NMR | Proteomics | Chemical bonds | Amyotrophic lateral sclerosis | Mutation | Protein structure | Equilibrium
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8. Full Text Protein function and allostery: a dynamic relationship
: Protein function and allostery
by Kalodimos, Charalampos G
Annals of the New York Academy of Sciences, ISSN 0077-8923, 07/2012, Volume 1260, Issue 1, pp. 81 - 86
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9. Full Text NMR disentangles a dynamic disaggregase machinery
by Saio, Tomohide and Kalodimos, Charalampos G
Nature Structural and Molecular Biology, ISSN 1545-9993, 05/2013, Volume 20, Issue 4, pp. 409 - 410
The three-dimensional structure of a key complex in chaperone-mediated protein disaggregation, comprising ClpB and DnaK, has been determined using NMR. In... 
MOLECULAR CHAPERONE DNAK | HSP104 | BIOPHYSICS | CLPB | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEASOME | STATE | PROTEINS | BINDING | CELL BIOLOGY | Nuclear Magnetic Resonance, Biomolecular - methods | Endopeptidase Clp | Models, Molecular | Protein Conformation | HSP70 Heat-Shock Proteins - chemistry | Molecular Chaperones - chemistry | Escherichia coli Proteins - chemistry | Heat-Shock Proteins - chemistry | Physiological aspects | Nuclear magnetic resonance spectroscopy | Usage | Research | Molecular chaperones | Structure | Proteins | Nuclear magnetic resonance--NMR | Molecular biology | Crystal structure
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10. Full Text Optimization of ^sup 1^H decoupling eliminates sideband artifacts in 3D TROSY-based triple resonance experiments
by Youlin Xia and Paolo Rossi and Marco Tonelli and Chengdong Huang and Charalampos G Kalodimos and Gianluigi Veglia
Journal of Biomolecular NMR, ISSN 0925-2738, 09/2017, Volume 69, Issue 1, p. 45
TROSY-based triple resonance experiments are essential for protein backbone assignment of large biomolecular systems by solution NMR spectroscopy. In a survey... 
Magnetic resonance spectroscopy | Artifacts | Sidebands | Data analysis | Sensitivity | Decoupling | Spectrometers | Data processing | Resonance | NMR spectroscopy | Experiments | Optimization
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11. Full Text Optimization of 1.sup.H decoupling eliminates sideband artifacts in 3D TROSY-based triple resonance experiments
by Xia, Youlin and Rossi, Paolo and Tonelli, Marco and Huang, Chengdong and Kalodimos, Charalampos G and Veglia, Gianluigi
Journal of Biomolecular NMR, ISSN 0925-2738, 09/2017, Volume 69, Issue 1, p. 45
To access, purchase, authenticate, or subscribe to the full-text of this article, please visit this link: http://dx.doi.org/10.1007/s10858-017-0133-6... 
Analysis | Nuclear magnetic resonance spectroscopy
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12. Full Text Protein dynamics and allostery: an NMR view
by Tzeng, Shiou-Ru and Kalodimos, Charalampos G
Current Opinion in Structural Biology, ISSN 0959-440X, 2011, Volume 21, Issue 1, pp. 62 - 67
Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity... 
CONFORMATIONAL ENTROPY | SIGNAL-TRANSDUCTION | CATALYSIS | INTRINSIC DYNAMICS | ACTIVATION | STRUCTURAL BASIS | PDZ DOMAIN | MOLECULAR RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING | SUBSTRATE RECOGNITION | CELL BIOLOGY | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Proteins - metabolism | Proteins - chemistry | Allosteric Regulation | Humans | Proteins | Analysis | Nuclear magnetic resonance
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13. Full Text Structural basis for protein antiaggregation activity of the trigger factor chaperone
by Saio, Tomohide and Guan, Xiao and Rossi, Paolo and Economou, Anastassios and Kalodimos, Charalampos G
Science, ISSN 0036-8075, 2014, Volume 344, Issue 6184, pp. 597 - 597
Molecular chaperones prevent aggregation and misfolding of proteins, but scarcity of structural data has impeded an understanding of the recognition and... 
NASCENT CHAIN | TRANSLATING RIBOSOMES | MALTOSE-BINDING PROTEIN | MOLECULAR CHAPERONES | ALKALINE-PHOSPHATASE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | IN-VIVO | NEWLY SYNTHESIZED PROTEINS | C-TERMINAL DOMAIN | CHEMICAL-EXCHANGE | Protein Structure, Tertiary | Peptides - chemistry | Protein Structure, Secondary | Molecular Chaperones - chemistry | Protein Folding | Peptidylprolyl Isomerase - chemistry | Intrinsically Disordered Proteins - chemistry | Alkaline Phosphatase - chemistry | Hydrophobic and Hydrophilic Interactions | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Escherichia coli Proteins - chemistry | Binding Sites
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14. Full Text Allosteric inhibition through suppression of transient conformational states
by Tzeng, Shiou-Ru and Kalodimos, Charalampos G
Nature Chemical Biology, ISSN 1552-4450, 07/2013, Volume 9, Issue 7, pp. 462 - 465
The ability to inhibit binding or enzymatic activity is key to preventing aberrant behaviors of proteins. Allosteric inhibition is desirable as it offers... 
RELAXATION DATA | STRUCTURAL BASIS | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PROTEIN-PROTEIN INTERACTIONS | CAMP RECEPTOR PROTEIN | MILLISECOND MOTIONS | CHEMICAL-EXCHANGE | BINDING PROTEIN | ROTATIONAL DIFFUSION | DNA - chemistry | Magnetic Resonance Spectroscopy - methods | Cyclic AMP Receptor Protein - chemistry | Allosteric Site | Escherichia coli - metabolism | Models, Molecular | Protein Binding | Ligands | Protein Conformation | Mutation | Cyclic AMP Receptor Protein - metabolism | Calorimetry - methods | Proteins | Enzymes | Molecular structure | Binding sites
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15. Full Text Protein function and allostery: a dynamic relationship
by Kalodimos, Charalampos G
Annals of the New York Academy of Sciences, ISSN 0077-8923, 07/2012, Volume 1260, Issue 1, pp. 81 - 86
Allostery is a fundamental process by which distant sites within a protein system sense each other. Allosteric regulation is such an efficient mechanism that... 
protein allostery | NMR spectroscopy | protein dynamics | Protein allostery | Protein dynamics | CONFORMATIONAL ENTROPY | KINASE-A | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | CATABOLITE ACTIVATOR PROTEIN | SIGNALING PROTEIN | NEGATIVE COOPERATIVITY | STRUCTURAL BASIS | MOLECULAR RECOGNITION | NMR RELAXATION | BINDING | Proteins - metabolism | Cyclic AMP Receptor Protein - chemistry | Signal Transduction | Allosteric Regulation | Allosteric Site | Models, Molecular | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Proteins - chemistry | Binding Sites | Cyclic AMP Receptor Protein - metabolism | Proteins | Signal transduction | Nuclear magnetic resonance--NMR | Spectroscopy | Dynamics | Signal processing | Catalysis | Gene expression | Metabolism | Dynamical systems
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16. Full Text sup 15^N and ^sup 13^C- SOFAST-HMQC editing enhances 3D-NOESY sensitivity in highly deuterated, selectively [^sup 1^H,^sup 13^C]-labeled proteins
by Paolo Rossi and Youlin Xia and Nandish Khanra and Gianluigi Veglia and Charalampos G Kalodimos
Journal of Biomolecular NMR, ISSN 0925-2738, 12/2016, Volume 66, Issue 4, p. 259
The ongoing NMR method development effort strives for high quality multidimensional data with reduced collection time. Here, we apply 'SOFAST-HMQC' to... 
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17. Full Text 15.sup.N and 13.sup.C- SOFAST-HMQC editing enhances 3D-NOESY sensitivity in highly deuterated, selectively [[.sup.1][H,.sup.13]C]-labeled proteins
by Rossi, Paolo and Xia, Youlin and Khanra, Nandish and Veglia, Gianluigi and Kalodimos, Charalampos G
Journal of Biomolecular NMR, ISSN 0925-2738, 12/2016, Volume 66, Issue 4, p. 259
To access, purchase, authenticate, or subscribe to the full-text of this article, please visit this link: http://dx.doi.org/10.1007/s10858-016-0074-5 
Usage | Magnetization | Data entry
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18. Full Text NMR reveals novel mechanisms of protein activity regulation
by Kalodimos, Charalampos G
Protein Science, ISSN 0961-8368, 05/2011, Volume 20, Issue 5, pp. 773 - 782
NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an... 
allosteric interactions | NMR | protein function | protein regulation | autoinhibition | Protein regulation | Autoinhibition | Allosteric interactions | Protein function | CONFORMATIONAL ENTROPY | ALLOSTERIC REGULATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUPRAMOLECULAR COMPLEXES | MOLECULAR-WEIGHT PROTEINS | SIGNALING PROTEIN | CONTROLS AUTOINHIBITION | TRANSCRIPTION REGULATORS | STRUCTURAL BASIS | CIS-TRANS ISOMERIZATION | PROLINE ISOMERIZATION | Protein Structure, Tertiary | Animals | Magnetic Resonance Spectroscopy - methods | Proteins - metabolism | Models, Chemical | Allosteric Regulation | Humans | Models, Molecular | Protein Binding | Protein Conformation | Proteins - chemistry | Spectrum analysis | Nuclear magnetic resonance--NMR | Review
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