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  • Models, Biological  (13)
  • American Association for the Advancement of Science (AAAS)  (13)
  • American Meteorological Society
  • Copernicus
  • 2015-2019
  • 2010-2014  (13)
  • 1955-1959
  • 2012  (13)
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  • 2015-2019
  • 2010-2014  (13)
  • 1955-1959
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  • 1
    Publication Date: 2012-06-23
    Description: Avian A/H5N1 influenza viruses pose a pandemic threat. As few as five amino acid substitutions, or four with reassortment, might be sufficient for mammal-to-mammal transmission through respiratory droplets. From surveillance data, we found that two of these substitutions are common in A/H5N1 viruses, and thus, some viruses might require only three additional substitutions to become transmissible via respiratory droplets between mammals. We used a mathematical model of within-host virus evolution to study factors that could increase and decrease the probability of the remaining substitutions evolving after the virus has infected a mammalian host. These factors, combined with the presence of some of these substitutions in circulating strains, make a virus evolving in nature a potentially serious threat. These results highlight critical areas in which more data are needed for assessing, and potentially averting, this threat.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3426314/" 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/PMC3426314/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, Colin A -- Fonville, Judith M -- Brown, Andre E X -- Burke, David F -- Smith, David L -- James, Sarah L -- Herfst, Sander -- van Boheemen, Sander -- Linster, Martin -- Schrauwen, Eefje J -- Katzelnick, Leah -- Mosterin, Ana -- Kuiken, Thijs -- Maher, Eileen -- Neumann, Gabriele -- Osterhaus, Albert D M E -- Kawaoka, Yoshihiro -- Fouchier, Ron A M -- Smith, Derek J -- DP1 OD000490/OD/NIH HHS/ -- DP1-OD000490-01/OD/NIH HHS/ -- HHSN266200700010C/AI/NIAID NIH HHS/ -- HHSN266200700010C/PHS HHS/ -- R01 AI 069274/AI/NIAID NIH HHS/ -- R56 AI069274/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1541-7. doi: 10.1126/science.1222526.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723414" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Air Microbiology ; Amino Acid Substitution ; Animals ; Birds ; *Evolution, Molecular ; Genetic Fitness ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus/*genetics/metabolism ; High-Throughput Nucleotide Sequencing ; Humans ; Influenza A Virus, H5N1 Subtype/*genetics/*pathogenicity ; Influenza in Birds/virology ; Influenza, Human/immunology/transmission/*virology ; Mammals ; Models, Biological ; Mutation ; Orthomyxoviridae Infections/transmission/*virology ; Probability ; RNA Replicase/*genetics ; Receptors, Virus/metabolism ; Respiratory System/*virology ; Selection, Genetic ; Sialic Acids/metabolism ; Viral Proteins/*genetics
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  • 2
    Publication Date: 2012-02-11
    Description: Apical constriction changes cell shapes, driving critical morphogenetic events, including gastrulation in diverse organisms and neural tube closure in vertebrates. Apical constriction is thought to be triggered by contraction of apical actomyosin networks. We found that apical actomyosin contractions began before cell shape changes in both Caenorhabitis elegans and Drosophila. In C. elegans, actomyosin networks were initially dynamic, contracting and generating cortical tension without substantial shrinking of apical surfaces. Apical cell-cell contact zones and actomyosin only later moved increasingly in concert, with no detectable change in actomyosin dynamics or cortical tension. Thus, apical constriction appears to be triggered not by a change in cortical tension, but by dynamic linking of apical cell-cell contact zones to an already contractile apical cortex.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298882/" 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/PMC3298882/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roh-Johnson, Minna -- Shemer, Gidi -- Higgins, Christopher D -- McClellan, Joseph H -- Werts, Adam D -- Tulu, U Serdar -- Gao, Liang -- Betzig, Eric -- Kiehart, Daniel P -- Goldstein, Bob -- R01 GM033830/GM/NIGMS NIH HHS/ -- R01 GM083071/GM/NIGMS NIH HHS/ -- R01 GM083071-01A1/GM/NIGMS NIH HHS/ -- R01 GM083071-02/GM/NIGMS NIH HHS/ -- R01 GM083071-02S1/GM/NIGMS NIH HHS/ -- R01 GM083071-03/GM/NIGMS NIH HHS/ -- R01 GM083071-04/GM/NIGMS NIH HHS/ -- R01 GM33830/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Mar 9;335(6073):1232-5. doi: 10.1126/science.1217869. Epub 2012 Feb 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22323741" target="_blank"〉PubMed〈/a〉
    Keywords: Actomyosin/chemistry/*physiology ; Animals ; Caenorhabditis elegans/*cytology/*embryology ; Cell Membrane/physiology/ultrastructure ; *Cell Shape ; Computer Simulation ; Cytoskeleton/physiology/ultrastructure ; Drosophila melanogaster/*cytology/*embryology ; Embryo, Nonmammalian/cytology/physiology ; Fluorescence Recovery After Photobleaching ; *Gastrulation ; Intercellular Junctions/physiology/ultrastructure ; Mechanical Phenomena ; Models, Biological ; Morphogenesis ; Myosins/chemistry/physiology
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  • 3
    Publication Date: 2012-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia, S M -- Kolding, J -- Rice, J -- Rochet, M-J -- Zhou, S -- Arimoto, T -- Beyer, J E -- Borges, L -- Bundy, A -- Dunn, D -- Fulton, E A -- Hall, M -- Heino, M -- Law, R -- Makino, M -- Rijnsdorp, A D -- Simard, F -- Smith, A D M -- New York, N.Y. -- Science. 2012 Mar 2;335(6072):1045-7. doi: 10.1126/science.1214594.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Commission on Ecosystem Management, International Union for Conservation of Nature (IUCN-CEM), Fisheries Expert Group, Brussels, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22383833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; Biomass ; Body Size ; *Conservation of Natural Resources ; *Ecosystem ; *Fisheries ; *Fishes ; Models, Biological ; Policy
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  • 4
    Publication Date: 2012-04-14
    Description: The mechanism of ion channel voltage gating-how channels open and close in response to voltage changes-has been debated since Hodgkin and Huxley's seminal discovery that the crux of nerve conduction is ion flow across cellular membranes. Using all-atom molecular dynamics simulations, we show how a voltage-gated potassium channel (KV) switches between activated and deactivated states. On deactivation, pore hydrophobic collapse rapidly halts ion flow. Subsequent voltage-sensing domain (VSD) relaxation, including inward, 15-angstrom S4-helix motion, completes the transition. On activation, outward S4 motion tightens the VSD-pore linker, perturbing linker-S6-helix packing. Fluctuations allow water, then potassium ions, to reenter the pore; linker-S6 repacking stabilizes the open pore. We propose a mechanistic model for the sodium/potassium/calcium voltage-gated ion channel superfamily that reconciles apparently conflicting experimental data.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jensen, Morten O -- Jogini, Vishwanath -- Borhani, David W -- Leffler, Abba E -- Dror, Ron O -- Shaw, David E -- New York, N.Y. -- Science. 2012 Apr 13;336(6078):229-33. doi: 10.1126/science.1216533.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉D E Shaw Research, New York, NY 10036, USA. morten.jensen@DEShawResearch.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22499946" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Hydrophobic and Hydrophilic Interactions ; *Ion Channel Gating ; Kv1.2 Potassium Channel/*chemistry/*metabolism ; Membrane Potentials ; Models, Biological ; Models, Molecular ; Molecular Dynamics Simulation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Shab Potassium Channels/*chemistry/*metabolism
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  • 5
    Publication Date: 2012-03-03
    Description: Although genetic control of morphogenesis is well established, elaboration of complex shapes requires changes in the mechanical properties of cells. In plants, the first visible sign of leaf formation is a bulge on the flank of the shoot apical meristem. Bulging results from local relaxation of cell walls, which causes them to yield to internal hydrostatic pressure. By manipulation of tissue tension in combination with quantitative live imaging and finite-element modeling, we found that the slow-growing area at the shoot tip is substantially strain-stiffened compared with surrounding fast-growing tissue. We propose that strain stiffening limits growth, restricts organ bulging, and contributes to the meristem's functional zonation. Thus, mechanical signals are not just passive readouts of gene action but feed back on morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kierzkowski, Daniel -- Nakayama, Naomi -- Routier-Kierzkowska, Anne-Lise -- Weber, Alain -- Bayer, Emmanuelle -- Schorderet, Martine -- Reinhardt, Didier -- Kuhlemeier, Cris -- Smith, Richard S -- New York, N.Y. -- Science. 2012 Mar 2;335(6072):1096-9. doi: 10.1126/science.1213100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Plant Sciences, University of Bern, Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22383847" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Wall/physiology/ultrastructure ; Elasticity ; Hydrostatic Pressure ; Lycopersicon esculentum/cytology/*growth & development ; Meristem/cytology/*growth & development ; Models, Biological ; *Morphogenesis ; Osmolar Concentration ; Osmotic Pressure ; Plant Shoots/cytology/*growth & development
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  • 6
    Publication Date: 2012-05-19
    Description: Cells promote polarized growth by activation of Rho-family protein Cdc42 at the cell membrane. We combined experiments and modeling to study bipolar growth initiation in fission yeast. Concentrations of a fluorescent marker for active Cdc42, Cdc42 protein, Cdc42-activator Scd1, and scaffold protein Scd2 exhibited anticorrelated fluctuations and oscillations with a 5-minute average period at polarized cell tips. These dynamics indicate competition for active Cdc42 or its regulators and the presence of positive and delayed negative feedbacks. Cdc42 oscillations and spatial distribution were sensitive to the amounts of Cdc42-activator Gef1 and to the activity of Cdc42-dependent kinase Pak1, a negative regulator. Feedbacks regulating Cdc42 oscillations and spatial self-organization appear to provide a flexible mechanism for fission yeast cells to explore polarization states and to control their morphology.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3681419/" 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/PMC3681419/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Das, Maitreyi -- Drake, Tyler -- Wiley, David J -- Buchwald, Peter -- Vavylonis, Dimitrios -- Verde, Fulvia -- 1R01GM095867/GM/NIGMS NIH HHS/ -- R01 GM095867/GM/NIGMS NIH HHS/ -- R21 GM083928/GM/NIGMS NIH HHS/ -- R21GM083928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jul 13;337(6091):239-43. doi: 10.1126/science.1218377. Epub 2012 May 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Pharmacology (R-189), University of Miami Miller School of Medicine, Post Office Box 016189, Miami, FL 33101, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22604726" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Microscopy, Fluorescence ; Models, Biological ; Mutation ; Recombinant Fusion Proteins/metabolism ; Schizosaccharomyces/cytology/*enzymology/genetics/*growth & development ; Schizosaccharomyces pombe Proteins/*metabolism ; cdc42 GTP-Binding Protein/*metabolism ; p21-Activated Kinases/metabolism
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  • 7
    Publication Date: 2012-03-31
    Description: The occurrence and magnitude of disease outbreaks can strongly influence host evolution. In particular, when hosts face a resistance-fecundity trade-off, they might evolve increased resistance to infection during larger epidemics but increased susceptibility during smaller ones. We tested this theoretical prediction by using a zooplankton-yeast host-parasite system in which ecological factors determine epidemic size. Lakes with high productivity and low predation pressure had large yeast epidemics; during these outbreaks, hosts became more resistant to infection. However, with low productivity and high predation, epidemics remained small and hosts evolved increased susceptibility. Thus, by modulating disease outbreaks, ecological context (productivity and predation) shaped host evolution during epidemics. Consequently, anthropogenic alteration of productivity and predation might strongly influence both ecological and evolutionary outcomes of disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duffy, Meghan A -- Ochs, Jessica Housley -- Penczykowski, Rachel M -- Civitello, David J -- Klausmeier, Christopher A -- Hall, Spencer R -- New York, N.Y. -- Science. 2012 Mar 30;335(6076):1636-8. doi: 10.1126/science.1215429.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biology, Georgia Institute of Technology, Atlanta, GA 30332-0230, USA. duffy@gatech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22461614" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Daphnia/*microbiology/*physiology ; *Ecosystem ; Female ; Fishes ; *Host-Pathogen Interactions ; Indiana ; *Lakes ; Male ; Metschnikowia/*pathogenicity ; Models, Biological ; Population Dynamics ; Predatory Behavior ; Reproduction ; Zooplankton/microbiology/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2012-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, Daniel P -- R01 DK045416/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2012 Apr 6;336(6077):42-3. doi: 10.1126/science.1221688.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Diabetes and Obesity Research Center, Sanford-Burnham Medical Research Institute, Orlando, FL 32827, USA. dkelly@sanfordburnham.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22491843" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes, Brown/metabolism ; Adipocytes, White/*metabolism ; Animals ; Energy Metabolism ; *Exercise ; Fibronectins/genetics/*metabolism ; Gene Expression Regulation ; Hormones/*metabolism ; Humans ; Mice ; Models, Biological ; Muscle Fibers, Skeletal/metabolism ; Muscle, Skeletal/*metabolism ; Oxygen Consumption ; Physical Conditioning, Animal ; Physical Endurance ; *Physical Exertion ; Thermogenesis ; Trans-Activators/*metabolism ; Transcription Factors
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  • 9
    Publication Date: 2012-03-03
    Description: Adaptation of cells to environmental changes requires dynamic interactions between metabolic and regulatory networks, but studies typically address only one or a few layers of regulation. For nutritional shifts between two preferred carbon sources of Bacillus subtilis, we combined statistical and model-based data analyses of dynamic transcript, protein, and metabolite abundances and promoter activities. Adaptation to malate was rapid and primarily controlled posttranscriptionally compared with the slow, mainly transcriptionally controlled adaptation to glucose that entailed nearly half of the known transcription regulation network. Interactions across multiple levels of regulation were involved in adaptive changes that could also be achieved by controlling single genes. Our analysis suggests that global trade-offs and evolutionary constraints provide incentives to favor complex control programs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buescher, Joerg Martin -- Liebermeister, Wolfram -- Jules, Matthieu -- Uhr, Markus -- Muntel, Jan -- Botella, Eric -- Hessling, Bernd -- Kleijn, Roelco Jacobus -- Le Chat, Ludovic -- Lecointe, Francois -- Mader, Ulrike -- Nicolas, Pierre -- Piersma, Sjouke -- Rugheimer, Frank -- Becher, Dorte -- Bessieres, Philippe -- Bidnenko, Elena -- Denham, Emma L -- Dervyn, Etienne -- Devine, Kevin M -- Doherty, Geoff -- Drulhe, Samuel -- Felicori, Liza -- Fogg, Mark J -- Goelzer, Anne -- Hansen, Annette -- Harwood, Colin R -- Hecker, Michael -- Hubner, Sebastian -- Hultschig, Claus -- Jarmer, Hanne -- Klipp, Edda -- Leduc, Aurelie -- Lewis, Peter -- Molina, Frank -- Noirot, Philippe -- Peres, Sabine -- Pigeonneau, Nathalie -- Pohl, Susanne -- Rasmussen, Simon -- Rinn, Bernd -- Schaffer, Marc -- Schnidder, Julian -- Schwikowski, Benno -- Van Dijl, Jan Maarten -- Veiga, Patrick -- Walsh, Sean -- Wilkinson, Anthony J -- Stelling, Jorg -- Aymerich, Stephane -- Sauer, Uwe -- New York, N.Y. -- Science. 2012 Mar 2;335(6072):1099-103. doi: 10.1126/science.1206871.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22383848" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; Algorithms ; Bacillus subtilis/*genetics/*metabolism ; Bacterial Proteins/metabolism ; Computer Simulation ; Data Interpretation, Statistical ; Gene Expression Regulation, Bacterial ; *Gene Regulatory Networks ; Genome, Bacterial ; Glucose/*metabolism ; Malates/*metabolism ; Metabolic Networks and Pathways/*genetics ; Metabolome ; Metabolomics ; Models, Biological ; Operon ; Promoter Regions, Genetic ; Transcription Factors/metabolism ; Transcription, Genetic
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  • 10
    Publication Date: 2012-04-14
    Description: Biological systems involving short-range activators and long-range inhibitors can generate complex patterns. Reaction-diffusion models postulate that differences in signaling range are caused by differential diffusivity of inhibitor and activator. Other models suggest that differential clearance underlies different signaling ranges. To test these models, we measured the biophysical properties of the Nodal/Lefty activator/inhibitor system during zebrafish embryogenesis. Analysis of Nodal and Lefty gradients revealed that Nodals have a shorter range than Lefty proteins. Pulse-labeling analysis indicated that Nodals and Leftys have similar clearance kinetics, whereas fluorescence recovery assays revealed that Leftys have a higher effective diffusion coefficient than Nodals. These results indicate that differential diffusivity is the major determinant of the differences in Nodal/Lefty range and provide biophysical support for reaction-diffusion models of activator/inhibitor-mediated patterning.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3525670/" 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/PMC3525670/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, Patrick -- Rogers, Katherine W -- Jordan, Ben M -- Lee, Joon S -- Robson, Drew -- Ramanathan, Sharad -- Schier, Alexander F -- 5R01GM56211/GM/NIGMS NIH HHS/ -- R01 GM056211/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 May 11;336(6082):721-4. doi: 10.1126/science.1221920. Epub 2012 Apr 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA. pmueller@fas.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22499809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastula/*metabolism ; *Body Patterning ; Diffusion ; Embryonic Development ; Fluorescence Recovery After Photobleaching ; Half-Life ; Intracellular Signaling Peptides and Proteins/genetics/*metabolism ; Kinetics ; Left-Right Determination Factors/genetics/*metabolism ; Models, Biological ; Nodal Signaling Ligands/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Zebrafish/*embryology/metabolism ; Zebrafish Proteins/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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