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  • 1
    Publication Date: 2011-07-06
    Description: Author(s): Q.-C. Sun, S. N. Baker, A. D. Christianson, and J. L. Musfeldt Phonons are exquisitely sensitive to finite length scale effects because they are intimately connected to charge, structure, and magnetism, and a quantitative analysis of their behavior can reveal microscopic aspects of spin-lattice interaction. To investigate these effects in a model correlated oxi... [Phys. Rev. B 84, 014301] Published Tue Jul 05, 2011
    Keywords: Dynamics, dynamical systems, lattice effects
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 2
    Publication Date: 2012-09-21
    Description: Author(s): Christopher H. Baker, Donald A. Jordan, and Pamela M. Norris The continuous wavelet transform is employed to analyze the dynamics and time-dependent energy distribution of phonon wave-packet propagation and scattering in molecular dynamics simulations. The equations of the one-dimensional continuous wavelet transform are presented and then discretized for imp... [Phys. Rev. B 86, 104306] Published Thu Sep 20, 2012
    Keywords: Dynamics, dynamical systems, lattice effects
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 3
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    Nature Publishing Group (NPG)
    Publication Date: 2010-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baker, Monya -- England -- Nature. 2010 Aug 26;466(7310):1137-40. doi: 10.1038/4661137a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20740018" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Culture Techniques/instrumentation ; *Computer Systems ; Humans ; Microscopy/*instrumentation/methods/trends
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
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    Nature Publishing Group (NPG)
    Publication Date: 2010-06-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baker, Monya -- England -- Nature. 2010 Jun 10;465(7299):823-6. doi: 10.1038/465823a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20535212" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Computational Biology ; Computer Simulation ; Cryoelectron Microscopy ; Crystallization ; Crystallography, X-Ray ; Drug Design ; Humans ; Lipid Bilayers/chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Membrane Proteins/*chemistry/isolation & purification/*metabolism ; Membranes, Artificial ; *Models, Molecular ; Movement ; Protein Conformation ; Receptors, G-Protein-Coupled/chemistry/isolation & purification/metabolism ; Solubility ; Structure-Activity Relationship
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    Nature Publishing Group (NPG)
    Publication Date: 2010-04-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baker, Monya -- England -- Nature. 2010 Apr 22;464(7292):1225. doi: 10.1038/4641225b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20414309" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drug Carriers ; Drug Delivery Systems/*methods ; Gene Knockdown Techniques/methods/*trends ; Humans ; Nanoparticles/administration & dosage/analysis ; Organ Specificity ; *RNA Interference ; RNA, Small Interfering/administration & dosage/*pharmacology/*therapeutic use
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
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    Nature Publishing Group (NPG)
    Publication Date: 2010-02-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baker, Monya -- England -- Nature. 2010 Feb 18;463(7283):979. doi: 10.1038/463979a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20164932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Models, Animal ; Molecular Imaging/instrumentation/*methods ; Whole Body Imaging/instrumentation/*methods
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 7
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    Nature Publishing Group (NPG)
    Publication Date: 2010-04-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baker, Monya -- England -- Nature. 2010 Apr 22;464(7292):1225-8. doi: 10.1038/4641225a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20414308" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Clinical Trials as Topic ; Drug Carriers/administration & dosage/economics/metabolism/pharmacokinetics ; Drug Delivery Systems/economics/*methods ; Gene Knockdown Techniques/economics/*methods ; Humans ; MicroRNAs/genetics/pharmacology/therapeutic use ; Nanoparticles/administration & dosage/analysis ; Oligoribonucleotides/administration & ; dosage/chemistry/pharmacokinetics/therapeutic use ; Organ Specificity ; *RNA Interference ; RNA, Small Interfering/*administration & ; dosage/genetics/*pharmacokinetics/therapeutic use
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
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    Nature Publishing Group (NPG)
    Publication Date: 2010-02-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baker, Monya -- England -- Nature. 2010 Feb 18;463(7283):977-80. doi: 10.1038/463977a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20164931" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Fluorescence ; Life ; Luminescent Measurements/methods ; Magnetic Resonance Imaging ; Mice ; *Models, Animal ; Molecular Imaging/economics/instrumentation/*methods ; Positron-Emission Tomography ; Tomography, Emission-Computed, Single-Photon ; Whole Body Imaging/economics/instrumentation/*methods ; X-Rays
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2010-07-09
    Description: Vertebrate embryos are characterized by an elongated antero-posterior (AP) body axis, which forms by progressive cell deposition from a posterior growth zone in the embryo. Here, we used tissue ablation in the chicken embryo to demonstrate that the caudal presomitic mesoderm (PSM) has a key role in axis elongation. Using time-lapse microscopy, we analysed the movements of fluorescently labelled cells in the PSM during embryo elongation, which revealed a clear posterior-to-anterior gradient of cell motility and directionality in the PSM. We tracked the movement of the PSM extracellular matrix in parallel with the labelled cells and subtracted the extracellular matrix movement from the global motion of cells. After subtraction, cell motility remained graded but lacked directionality, indicating that the posterior cell movements associated with axis elongation in the PSM are not intrinsic but reflect tissue deformation. The gradient of cell motion along the PSM parallels the fibroblast growth factor (FGF)/mitogen-activated protein kinase (MAPK) gradient, which has been implicated in the control of cell motility in this tissue. Both FGF signalling gain- and loss-of-function experiments lead to disruption of the motility gradient and a slowing down of axis elongation. Furthermore, embryos treated with cell movement inhibitors (blebbistatin or RhoK inhibitor), but not cell cycle inhibitors, show a slower axis elongation rate. We propose that the gradient of random cell motility downstream of FGF signalling in the PSM controls posterior elongation in the amniote embryo. Our data indicate that tissue elongation is an emergent property that arises from the collective regulation of graded, random cell motion rather than by the regulation of directionality of individual cellular movements.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3118990/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3118990/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benazeraf, Bertrand -- Francois, Paul -- Baker, Ruth E -- Denans, Nicolas -- Little, Charles D -- Pourquie, Olivier -- R01 GM076692/GM/NIGMS NIH HHS/ -- R01 GM076692-06/GM/NIGMS NIH HHS/ -- R01 HD043158-01/HD/NICHD NIH HHS/ -- R02 HD043158/HD/NICHD NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2010 Jul 8;466(7303):248-52. doi: 10.1038/nature09151.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Kansas City, Missouri 64110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20613841" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Movement/*physiology ; Cell Proliferation ; Chemotaxis ; Chick Embryo/*cytology/*embryology/metabolism ; Fibroblast Growth Factors/*metabolism ; Neurons/cytology/metabolism ; Receptors, Fibroblast Growth Factor/genetics/metabolism ; Signal Transduction ; Xenopus
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2010-11-19
    Description: Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tuned to perform diverse biochemical functions. The absence of a consensus sequence that defines functional cysteines in proteins has hindered their discovery and characterization. Here we describe a proteomics method to profile quantitatively the intrinsic reactivity of cysteine residues en masse directly in native biological systems. Hyper-reactivity was a rare feature among cysteines and it was found to specify a wide range of activities, including nucleophilic and reductive catalysis and sites of oxidative modification. Hyper-reactive cysteines were identified in several proteins of uncharacterized function, including a residue conserved across eukaryotic phylogeny that we show is required for yeast viability and is involved in iron-sulphur protein biogenesis. We also demonstrate that quantitative reactivity profiling can form the basis for screening and functional assignment of cysteines in computationally designed proteins, where it discriminated catalytically active from inactive cysteine hydrolase designs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3058684/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3058684/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weerapana, Eranthie -- Wang, Chu -- Simon, Gabriel M -- Richter, Florian -- Khare, Sagar -- Dillon, Myles B D -- Bachovchin, Daniel A -- Mowen, Kerri -- Baker, David -- Cravatt, Benjamin F -- CA087660/CA/NCI NIH HHS/ -- MH084512/MH/NIMH NIH HHS/ -- R01 CA087660/CA/NCI NIH HHS/ -- R01 CA087660-09/CA/NCI NIH HHS/ -- R01 GM085117/GM/NIGMS NIH HHS/ -- R01 GM090294/GM/NIGMS NIH HHS/ -- R01 GM090294-02/GM/NIGMS NIH HHS/ -- R37 CA087660/CA/NCI NIH HHS/ -- R37 CA087660-10/CA/NCI NIH HHS/ -- U54 MH084512/MH/NIMH NIH HHS/ -- U54 MH084512-030004/MH/NIMH NIH HHS/ -- England -- Nature. 2010 Dec 9;468(7325):790-5. doi: 10.1038/nature09472. Epub 2010 Nov 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21085121" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biocatalysis ; Cell Line, Tumor ; Conserved Sequence ; Cysteine/analysis/*metabolism ; Humans ; Hydrolases/chemistry/metabolism ; Iron-Sulfur Proteins/biosynthesis ; Liver/metabolism ; Mice ; Myocardium/metabolism ; Nuclear Proteins/chemistry/metabolism ; Oxidation-Reduction ; Protein Engineering ; Protein Hydrolysates ; Protein-Arginine N-Methyltransferases/chemistry/metabolism ; Proteins/*chemistry/*metabolism ; Proteome/*chemistry/*metabolism ; Proteomics/methods ; Repressor Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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