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  • American Association for the Advancement of Science (AAAS)  (16)
  • 2005-2009  (9)
  • 1980-1984  (7)
  • 1935-1939
  • 1
    Publication Date: 2006-03-25
    Description: Traditionally the dispersion of particles in polymeric materials has proven difficult and frequently results in phase separation and agglomeration. We show that thermodynamically stable dispersion of nanoparticles into a polymeric liquid is enhanced for systems where the radius of gyration of the linear polymer is greater than the radius of the nanoparticle. Dispersed nanoparticles swell the linear polymer chains, resulting in a polymer radius of gyration that grows with the nanoparticle volume fraction. It is proposed that this entropically unfavorable process is offset by an enthalpy gain due to an increase in molecular contacts at dispersed nanoparticle surfaces as compared with the surfaces of phase-separated nanoparticles. Even when the dispersed state is thermodynamically stable, it may be inaccessible unless the correct processing strategy is adopted, which is particularly important for the case of fullerene dispersion into linear polymers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackay, Michael E -- Tuteja, Anish -- Duxbury, Phillip M -- Hawker, Craig J -- Van Horn, Brooke -- Guan, Zhibin -- Chen, Guanghui -- Krishnan, R S -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1740-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering and Materials Science, Michigan State University, East Lansing, MI 48824, USA. mackay@msu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556836" target="_blank"〉PubMed〈/a〉
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2007-02-03
    Description: Intense femtosecond laser excitation can produce transient states of matter that would otherwise be inaccessible to laboratory investigation. At high excitation densities, the interatomic forces that bind solids and determine many of their properties can be substantially altered. Here, we present the detailed mapping of the carrier density-dependent interatomic potential of bismuth approaching a solid-solid phase transition. Our experiments combine stroboscopic techniques that use a high-brightness linear electron accelerator-based x-ray source with pulse-by-pulse timing reconstruction for femtosecond resolution, allowing quantitative characterization of the interatomic potential energy surface of the highly excited solid.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fritz, D M -- Reis, D A -- Adams, B -- Akre, R A -- Arthur, J -- Blome, C -- Bucksbaum, P H -- Cavalieri, A L -- Engemann, S -- Fahy, S -- Falcone, R W -- Fuoss, P H -- Gaffney, K J -- George, M J -- Hajdu, J -- Hertlein, M P -- Hillyard, P B -- Horn-von Hoegen, M -- Kammler, M -- Kaspar, J -- Kienberger, R -- Krejcik, P -- Lee, S H -- Lindenberg, A M -- McFarland, B -- Meyer, D -- Montagne, T -- Murray, E D -- Nelson, A J -- Nicoul, M -- Pahl, R -- Rudati, J -- Schlarb, H -- Siddons, D P -- Sokolowski-Tinten, K -- Tschentscher, Th -- von der Linde, D -- Hastings, J B -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):633-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Frontiers in Optical Coherent and Ultrafast Science (FOCUS) Center, Departments of Physics and Applied Physics Program, University of Michigan, Ann Arbor, MI 48109, USA. dmfritz@slac.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272718" target="_blank"〉PubMed〈/a〉
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  • 3
    Publication Date: 2009-06-27
    Description: Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2764269/" 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/PMC2764269/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Horn, Wade D -- Kim, Hak-Jun -- Ellis, Charles D -- Hadziselimovic, Arina -- Sulistijo, Endah S -- Karra, Murthy D -- Tian, Changlin -- Sonnichsen, Frank D -- Sanders, Charles R -- R01 GM047485/GM/NIGMS NIH HHS/ -- R01 GM047485-17/GM/NIGMS NIH HHS/ -- R01 GM47485/GM/NIGMS NIH HHS/ -- T32 NS007491/NS/NINDS NIH HHS/ -- T32 NS007491-09/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2009 Jun 26;324(5935):1726-9. doi: 10.1126/science.1171716.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19556511" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Biocatalysis ; Catalytic Domain ; Cell Membrane/enzymology ; Diacylglycerol Kinase/*chemistry/metabolism ; Escherichia coli/*enzymology ; Escherichia coli Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Protein Folding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 4
    Publication Date: 2005-07-16
    Description: Leishmania species cause a spectrum of human diseases in tropical and subtropical regions of the world. We have sequenced the 36 chromosomes of the 32.8-megabase haploid genome of Leishmania major (Friedlin strain) and predict 911 RNA genes, 39 pseudogenes, and 8272 protein-coding genes, of which 36% can be ascribed a putative function. These include genes involved in host-pathogen interactions, such as proteolytic enzymes, and extensive machinery for synthesis of complex surface glycoconjugates. The organization of protein-coding genes into long, strand-specific, polycistronic clusters and lack of general transcription factors in the L. major, Trypanosoma brucei, and Trypanosoma cruzi (Tritryp) genomes suggest that the mechanisms regulating RNA polymerase II-directed transcription are distinct from those operating in other eukaryotes, although the trypanosomatids appear capable of chromatin remodeling. Abundant RNA-binding proteins are encoded in the Tritryp genomes, consistent with active posttranscriptional regulation of gene expression.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1470643/" 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/PMC1470643/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivens, Alasdair C -- Peacock, Christopher S -- Worthey, Elizabeth A -- Murphy, Lee -- Aggarwal, Gautam -- Berriman, Matthew -- Sisk, Ellen -- Rajandream, Marie-Adele -- Adlem, Ellen -- Aert, Rita -- Anupama, Atashi -- Apostolou, Zina -- Attipoe, Philip -- Bason, Nathalie -- Bauser, Christopher -- Beck, Alfred -- Beverley, Stephen M -- Bianchettin, Gabriella -- Borzym, Katja -- Bothe, Gordana -- Bruschi, Carlo V -- Collins, Matt -- Cadag, Eithon -- Ciarloni, Laura -- Clayton, Christine -- Coulson, Richard M R -- Cronin, Ann -- Cruz, Angela K -- Davies, Robert M -- De Gaudenzi, Javier -- Dobson, Deborah E -- Duesterhoeft, Andreas -- Fazelina, Gholam -- Fosker, Nigel -- Frasch, Alberto Carlos -- Fraser, Audrey -- Fuchs, Monika -- Gabel, Claudia -- Goble, Arlette -- Goffeau, Andre -- Harris, David -- Hertz-Fowler, Christiane -- Hilbert, Helmut -- Horn, David -- Huang, Yiting -- Klages, Sven -- Knights, Andrew -- Kube, Michael -- Larke, Natasha -- Litvin, Lyudmila -- Lord, Angela -- Louie, Tin -- Marra, Marco -- Masuy, David -- Matthews, Keith -- Michaeli, Shulamit -- Mottram, Jeremy C -- Muller-Auer, Silke -- Munden, Heather -- Nelson, Siri -- Norbertczak, Halina -- Oliver, Karen -- O'neil, Susan -- Pentony, Martin -- Pohl, Thomas M -- Price, Claire -- Purnelle, Benedicte -- Quail, Michael A -- Rabbinowitsch, Ester -- Reinhardt, Richard -- Rieger, Michael -- Rinta, Joel -- Robben, Johan -- Robertson, Laura -- Ruiz, Jeronimo C -- Rutter, Simon -- Saunders, David -- Schafer, Melanie -- Schein, Jacquie -- Schwartz, David C -- Seeger, Kathy -- Seyler, Amber -- Sharp, Sarah -- Shin, Heesun -- Sivam, Dhileep -- Squares, Rob -- Squares, Steve -- Tosato, Valentina -- Vogt, Christy -- Volckaert, Guido -- Wambutt, Rolf -- Warren, Tim -- Wedler, Holger -- Woodward, John -- Zhou, Shiguo -- Zimmermann, Wolfgang -- Smith, Deborah F -- Blackwell, Jenefer M -- Stuart, Kenneth D -- Barrell, Bart -- Myler, Peter J -- R01 AI040599/AI/NIAID NIH HHS/ -- R01 AI053667/AI/NIAID NIH HHS/ -- U01 AI040599/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):436-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire CB10 1SA, UK. alicat@sanger.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020728" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/genetics/metabolism ; Gene Expression Regulation ; Genes, Protozoan ; Genes, rRNA ; *Genome, Protozoan ; Glycoconjugates/biosynthesis/metabolism ; Leishmania major/chemistry/*genetics/metabolism ; Leishmaniasis, Cutaneous/parasitology ; Lipid Metabolism ; Membrane Proteins/biosynthesis/chemistry/genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Protein Biosynthesis ; Protein Processing, Post-Translational ; Protozoan Proteins/biosynthesis/chemistry/genetics/metabolism ; RNA Processing, Post-Transcriptional ; RNA Splicing ; RNA, Protozoan/genetics/metabolism ; *Sequence Analysis, DNA ; Transcription, Genetic
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  • 5
    Publication Date: 2005-07-16
    Description: Whole-genome sequencing of the protozoan pathogen Trypanosoma cruzi revealed that the diploid genome contains a predicted 22,570 proteins encoded by genes, of which 12,570 represent allelic pairs. Over 50% of the genome consists of repeated sequences, such as retrotransposons and genes for large families of surface molecules, which include trans-sialidases, mucins, gp63s, and a large novel family (〉1300 copies) of mucin-associated surface protein (MASP) genes. Analyses of the T. cruzi, T. brucei, and Leishmania major (Tritryp) genomes imply differences from other eukaryotes in DNA repair and initiation of replication and reflect their unusual mitochondrial DNA. Although the Tritryp lack several classes of signaling molecules, their kinomes contain a large and diverse set of protein kinases and phosphatases; their size and diversity imply previously unknown interactions and regulatory processes, which may be targets for intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉El-Sayed, Najib M -- Myler, Peter J -- Bartholomeu, Daniella C -- Nilsson, Daniel -- Aggarwal, Gautam -- Tran, Anh-Nhi -- Ghedin, Elodie -- Worthey, Elizabeth A -- Delcher, Arthur L -- Blandin, Gaelle -- Westenberger, Scott J -- Caler, Elisabet -- Cerqueira, Gustavo C -- Branche, Carole -- Haas, Brian -- Anupama, Atashi -- Arner, Erik -- Aslund, Lena -- Attipoe, Philip -- Bontempi, Esteban -- Bringaud, Frederic -- Burton, Peter -- Cadag, Eithon -- Campbell, David A -- Carrington, Mark -- Crabtree, Jonathan -- Darban, Hamid -- da Silveira, Jose Franco -- de Jong, Pieter -- Edwards, Kimberly -- Englund, Paul T -- Fazelina, Gholam -- Feldblyum, Tamara -- Ferella, Marcela -- Frasch, Alberto Carlos -- Gull, Keith -- Horn, David -- Hou, Lihua -- Huang, Yiting -- Kindlund, Ellen -- Klingbeil, Michele -- Kluge, Sindy -- Koo, Hean -- Lacerda, Daniela -- Levin, Mariano J -- Lorenzi, Hernan -- Louie, Tin -- Machado, Carlos Renato -- McCulloch, Richard -- McKenna, Alan -- Mizuno, Yumi -- Mottram, Jeremy C -- Nelson, Siri -- Ochaya, Stephen -- Osoegawa, Kazutoyo -- Pai, Grace -- Parsons, Marilyn -- Pentony, Martin -- Pettersson, Ulf -- Pop, Mihai -- Ramirez, Jose Luis -- Rinta, Joel -- Robertson, Laura -- Salzberg, Steven L -- Sanchez, Daniel O -- Seyler, Amber -- Sharma, Reuben -- Shetty, Jyoti -- Simpson, Anjana J -- Sisk, Ellen -- Tammi, Martti T -- Tarleton, Rick -- Teixeira, Santuza -- Van Aken, Susan -- Vogt, Christy -- Ward, Pauline N -- Wickstead, Bill -- Wortman, Jennifer -- White, Owen -- Fraser, Claire M -- Stuart, Kenneth D -- Andersson, Bjorn -- AI045039/AI/NIAID NIH HHS/ -- AI45038/AI/NIAID NIH HHS/ -- AI45061/AI/NIAID NIH HHS/ -- R01 AI031077/AI/NIAID NIH HHS/ -- R01 AI031077-11/AI/NIAID NIH HHS/ -- U01 AI045038/AI/NIAID NIH HHS/ -- U01 AI045039/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):409-15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Parasite Genomics, Institute for Genomic Research, Rockville, MD 20850, USA. nelsayed@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020725" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chagas Disease/drug therapy/parasitology ; DNA Repair ; DNA Replication ; DNA, Mitochondrial/genetics ; DNA, Protozoan/genetics ; Genes, Protozoan ; *Genome, Protozoan ; Humans ; Meiosis ; Membrane Proteins/chemistry/genetics/physiology ; Multigene Family ; Protozoan Proteins/chemistry/*genetics/physiology ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroelements ; *Sequence Analysis, DNA ; Signal Transduction ; Telomere/genetics ; Trypanocidal Agents/pharmacology/therapeutic use ; Trypanosoma cruzi/chemistry/*genetics/physiology
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  • 6
    Publication Date: 2006-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gazzaniga, Michael S -- Van Horn, John D -- Bloom, Floyd -- Shepherd, Gordon M -- Raichle, Marcus -- Jones, Edward -- New York, N.Y. -- Science. 2006 Jan 13;311(5758):176.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16410506" target="_blank"〉PubMed〈/a〉
    Keywords: Medical Informatics/*trends ; National Institutes of Health (U.S.) ; Neurosciences/*trends ; United States
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  • 7
    Publication Date: 2006-08-19
    Description: We describe the synthesis of bilayer graphene thin films deposited on insulating silicon carbide and report the characterization of their electronic band structure using angle-resolved photoemission. By selectively adjusting the carrier concentration in each layer, changes in the Coulomb potential led to control of the gap between valence and conduction bands. This control over the band structure suggests the potential application of bilayer graphene to switching functions in atomic-scale electronic devices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohta, Taisuke -- Bostwick, Aaron -- Seyller, Thomas -- Horn, Karsten -- Rotenberg, Eli -- New York, N.Y. -- Science. 2006 Aug 18;313(5789):951-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Advanced Light Source, Lawrence Berkeley National Laboratory, One Cyclotron Road, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917057" target="_blank"〉PubMed〈/a〉
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  • 8
    Publication Date: 2007-01-20
    Description: Despite evidence pointing to a ubiquitous tendency of human minds to wander, little is known about the neural operations that support this core component of human cognition. Using both thought sampling and brain imaging, the current investigation demonstrated that mind-wandering is associated with activity in a default network of cortical regions that are active when the brain is "at rest." In addition, individuals' reports of the tendency of their minds to wander were correlated with activity in this network.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1821121/" 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/PMC1821121/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mason, Malia F -- Norton, Michael I -- Van Horn, John D -- Wegner, Daniel M -- Grafton, Scott T -- Macrae, C Neil -- MH49127/MH/NIMH NIH HHS/ -- R01 NS033504/NS/NINDS NIH HHS/ -- R01 NS050614/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):393-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychological and Brain Sciences, Dartmouth College, Hanover, NH 03755, USA. malia@nmr.mgh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17234951" target="_blank"〉PubMed〈/a〉
    Keywords: Attention ; Brain Mapping ; Cerebral Cortex/*physiology ; Cognition ; Fantasy ; Female ; Humans ; Magnetic Resonance Imaging ; Male ; Nerve Net/physiology ; Thinking/*physiology
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  • 9
    Publication Date: 2009-10-17
    Description: Chondroitin sulfate proteoglycans (CSPGs) present a barrier to axon regeneration. However, no specific receptor for the inhibitory effect of CSPGs has been identified. We showed that a transmembrane protein tyrosine phosphatase, PTPsigma, binds with high affinity to neural CSPGs. Binding involves the chondroitin sulfate chains and a specific site on the first immunoglobulin-like domain of PTPsigma. In culture, PTPsigma(-/-) neurons show reduced inhibition by CSPG. A PTPsigma fusion protein probe can detect cognate ligands that are up-regulated specifically at neural lesion sites. After spinal cord injury, PTPsigma gene disruption enhanced the ability of axons to penetrate regions containing CSPG. These results indicate that PTPsigma can act as a receptor for CSPGs and may provide new therapeutic approaches to neural regeneration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811318/" 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/PMC2811318/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shen, Yingjie -- Tenney, Alan P -- Busch, Sarah A -- Horn, Kevin P -- Cuascut, Fernando X -- Liu, Kai -- He, Zhigang -- Silver, Jerry -- Flanagan, John G -- R01 EY011559/EY/NEI NIH HHS/ -- R01 NS025713/NS/NINDS NIH HHS/ -- R37 HD029417/HD/NICHD NIH HHS/ -- R37 NS025713/NS/NINDS NIH HHS/ -- R37 NS025713-22/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2009 Oct 23;326(5952):592-6. doi: 10.1126/science.1178310. Epub 2009 Oct 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19833921" target="_blank"〉PubMed〈/a〉
    Keywords: Aggrecans/metabolism ; Animals ; Astrocytes/metabolism ; Axons/physiology ; Binding Sites ; Cells, Cultured ; Chondroitin Sulfate Proteoglycans/chemistry/*metabolism ; Chondroitin Sulfates/metabolism ; Female ; Ganglia, Spinal/cytology/metabolism ; Ligands ; Mice ; *Nerve Regeneration ; Nerve Tissue Proteins/chemistry/*metabolism ; Neurites/physiology ; Neurons/*physiology ; Protein Binding ; Protein Interaction Domains and Motifs ; Proteoglycans/chemistry/*metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class ; 2/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Spinal Cord/metabolism/pathology ; Spinal Cord Injuries/*metabolism/pathology/physiopathology
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-09-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horn, J M -- New York, N.Y. -- Science. 1981 Sep 4;213(4512):1145.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17741106" target="_blank"〉PubMed〈/a〉
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