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  • American Association for the Advancement of Science (AAAS)  (49)
  • International Union of Crystallography  (22)
  • Nature Publishing Group (NPG)  (14)
  • 1
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    Repair of tooth enamel by a biomimetic mineralization frontier ensuring epitaxial growth (2019)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉The regeneration of tooth enamel, the hardest biological tissue, remains a considerable challenge because its complicated and well-aligned apatite structure has not been duplicated artificially. We herein reveal that a rationally designed material composed of calcium phosphate ion clusters can be used to produce a precursor layer to induce the epitaxial crystal growth of enamel apatite, which mimics the biomineralization crystalline-amorphous frontier of hard tissue development in nature. After repair, the damaged enamel can be recovered completely because its hierarchical structure and mechanical properties are identical to those of natural enamel. The suggested phase transformation–based epitaxial growth follows a promising strategy for enamel regeneration and, more generally, for biomimetic reproduction of materials with complicated structure.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Extra strengthening and work hardening in gradient nanotwinned metals (2018)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2018
    Description: 〈p〉Gradient structures exist ubiquitously in nature and are increasingly being introduced in engineering. However, understanding structural gradient–related mechanical behaviors in all gradient structures, including those in engineering materials, has been challenging. We explored the mechanical performance of a gradient nanotwinned structure with highly tunable structural gradients in pure copper. A large structural gradient allows for superior work hardening and strength that can exceed those of the strongest component of the gradient structure. We found through systematic experiments and atomistic simulations that this unusual behavior is afforded by a unique patterning of ultrahigh densities of dislocations in the grain interiors. These observations not only shed light on gradient structures, but may also indicate a promising route for improving the mechanical properties of materials through gradient design.〈/p〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-26
    Description: The Caenorhabditis elegans Bcl-2-like protein CED-9 prevents programmed cell death by antagonizing the Apaf-1-like cell-death activator CED-4. Endogenous CED-9 and CED-4 proteins localized to mitochondria in wild-type embryos, in which most cells survive. By contrast, in embryos in which cells had been induced to die, CED-4 assumed a perinuclear localization. CED-4 translocation induced by the cell-death activator EGL-1 was blocked by a gain-of-function mutation in ced-9 but was not dependent on ced-3 function, suggesting that CED-4 translocation precedes caspase activation and the execution phase of programmed cell death. Thus, a change in the subcellular localization of CED-4 may drive programmed cell death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, F -- Hersh, B M -- Conradt, B -- Zhou, Z -- Riemer, D -- Gruenbaum, Y -- Horvitz, H R -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1485-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biology, 68-425, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10688797" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Animals, Genetically Modified ; *Apoptosis ; Apoptosis Regulatory Proteins ; Caenorhabditis elegans/*cytology/embryology/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Calcium-Binding Proteins/genetics/*metabolism ; *Caspases ; Cysteine Endopeptidases/genetics/metabolism ; Genes, Helminth ; Helminth Proteins/genetics/*metabolism ; Immunohistochemistry ; Mitochondria/metabolism ; Mutation ; Nuclear Envelope/*metabolism ; Phenotype ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-bcl-2 ; Repressor Proteins/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    In search of the first flower: A jurassic angiosperm, archaefructus, from northeast china (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-30
    Description: Angiosperm fruiting axes were discovered from the Upper Jurassic of China. Angiosperms are defined by carpels enclosing ovules, a character demonstrated in this fossil. This feature is lacking in other fossils reported to be earliest angiosperms. The fruits are small follicles formed from conduplicate carpels helically arranged. Adaxial elongate stigmatic crests are conspicuous on each carpel. The basal one-third of the axes bore deciduous organs of uncertain affinities. No scars of subtending floral organs are present to define the individual fertile parts as floral units, but the leaf-like structures subtending each axis define them as flowers. These fruiting axes have primitive characters and characters not considered primitive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun -- Dilcher -- Zheng -- Zhou -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1692-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉G. Sun, Nanjing Institute of Geology and Palaeontology, Academia Sinica, Nanjing 210008, China. D. L. Dilcher, Florida Museum of Natural History, University of Florida, Gainesville, FL 32611, USA. S. Zheng, Shenyang Institute of Geology and Mi.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831557" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    A primitive enantiornithine bird and the origin of feathers (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-09
    Description: A fossil enantiornithine bird, Protopteryx fengningensis gen. et sp. nov., was collected from the Early Cretaceous Yixian Formation of Northern China. It provides fossil evidence of a triosseal canal in early birds. The manus and the alular digit are long, as in Archaeopteryx and Confuciusornis, but are relatively short in other enantiornithines. The alula or bastard wing is attached to an unreduced alular digit. The two central tail feathers are scalelike without branching. This type of feather may suggest that modern feathers evolved through the following stages: (i) elongated scale, (ii) central shaft, (iii) barbs, and finally (iv) barbules and barbicel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, F -- Zhou, Z -- New York, N.Y. -- Science. 2000 Dec 8;290(5498):1955-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Vertebrate Paleontology and Paleoanthropology, Chinese Academy of Sciences, Post Office Box 643, Beijing 100044, China. fuchengzhang@yeah.net〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11110660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; *Birds/anatomy & histology ; Bone and Bones/anatomy & histology ; China ; *Feathers/anatomy & histology ; *Fossils ; Reptiles/anatomy & histology ; Wings, Animal/anatomy & histology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Function of WW domains as phosphoserine- or phosphothreonine-binding modules (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-02-26
    Description: Protein-interacting modules help determine the specificity of signal transduction events, and protein phosphorylation can modulate the assembly of such modules into specific signaling complexes. Although phosphotyrosine-binding modules have been well-characterized, phosphoserine- or phosphothreonine-binding modules have not been described. WW domains are small protein modules found in various proteins that participate in cell signaling or regulation. WW domains of the essential mitotic prolyl isomerase Pin1 and the ubiquitin ligase Nedd4 bound to phosphoproteins, including physiological substrates of enzymes, in a phosphorylation-dependent manner. The Pin1 WW domain functioned as a phosphoserine- or phosphothreonine-binding module, with properties similar to those of SRC homology 2 domains. Phosphoserine- or phosphothreonine-binding activity was required for Pin1 to interact with its substrates in vitro and to perform its essential function in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, P J -- Zhou, X Z -- Shen, M -- Lu, K P -- R01GM56230/GM/NIGMS NIH HHS/ -- R01GM58556/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Feb 26;283(5406):1325-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10037602" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Calcium-Binding Proteins/chemistry/*metabolism ; Cell Cycle Proteins/metabolism ; Endosomal Sorting Complexes Required for Transport ; HeLa Cells ; Humans ; *Ligases ; Peptidylprolyl Isomerase/chemistry/genetics/*metabolism ; Phosphopeptides/metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Phosphoserine/*metabolism ; Phosphothreonine/*metabolism ; Point Mutation ; Signal Transduction ; *Ubiquitin-Protein Ligases ; *cdc25 Phosphatases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: Pin1 is an essential and conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins). In response to their phosphorylation during mitosis, Pin1 binds and regulates members of a highly conserved set of proteins that overlaps with antigens recognized by the mitosis-specific monoclonal antibody MPM-2. Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Both Pin1 and MPM-2 selected similar phosphorylated serine-proline-containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Pin1 preferentially isomerized proline residues preceded by phosphorylated serine or threonine with up to 1300-fold selectivity compared with unphosphorylated peptides. Pin1 may thus regulate mitotic progression by catalyzing sequence-specific and phosphorylation-dependent proline isomerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yaffe, M B -- Schutkowski, M -- Shen, M -- Zhou, X Z -- Stukenberg, P T -- Rahfeld, J U -- Xu, J -- Kuang, J -- Kirschner, M W -- Fischer, G -- Cantley, L C -- Lu, K P -- GM56203/GM/NIGMS NIH HHS/ -- GM56230/GM/NIGMS NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1957-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395400" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/metabolism ; Antibodies, Monoclonal ; Binding Sites ; Carrier Proteins/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; DNA-Binding Proteins/metabolism ; Epitopes ; HeLa Cells ; Heat-Shock Proteins/metabolism ; Humans ; Isomerism ; *Mitosis ; Models, Molecular ; Oligopeptides/chemistry/*metabolism ; Peptide Library ; Peptidylprolyl Isomerase/chemistry/*metabolism ; Phosphoproteins/chemistry/immunology/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Proline/*metabolism ; Protein Conformation ; Recombinant Fusion Proteins/chemistry/metabolism ; Substrate Specificity ; Tacrolimus Binding Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    A population-specific HTR2B stop codon predisposes to severe impulsivity (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-12-24
    Description: Impulsivity, describing action without foresight, is an important feature of several psychiatric diseases, suicidality and violent behaviour. The complex origins of impulsivity hinder identification of the genes influencing it and the diseases with which it is associated. Here we perform exon-focused sequencing of impulsive individuals in a founder population, targeting fourteen genes belonging to the serotonin and dopamine domain. A stop codon in HTR2B was identified that is common (minor allele frequency 〉 1%) but exclusive to Finnish people. Expression of the gene in the human brain was assessed, as well as the molecular functionality of the stop codon, which was associated with psychiatric diseases marked by impulsivity in both population and family-based analyses. Knockout of Htr2b increased impulsive behaviours in mice, indicative of predictive validity. Our study shows the potential for identifying and tracing effects of rare alleles in complex behavioural phenotypes using founder populations, and indicates a role for HTR2B in impulsivity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3183507/" 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/PMC3183507/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bevilacqua, Laura -- Doly, Stephane -- Kaprio, Jaakko -- Yuan, Qiaoping -- Tikkanen, Roope -- Paunio, Tiina -- Zhou, Zhifeng -- Wedenoja, Juho -- Maroteaux, Luc -- Diaz, Silvina -- Belmer, Arnaud -- Hodgkinson, Colin A -- Dell'osso, Liliana -- Suvisaari, Jaana -- Coccaro, Emil -- Rose, Richard J -- Peltonen, Leena -- Virkkunen, Matti -- Goldman, David -- AA-09203/AA/NIAAA NIH HHS/ -- AA-12502/AA/NIAAA NIH HHS/ -- Z01 AA000301-09/Intramural NIH HHS/ -- Z01 AA000301-10/Intramural NIH HHS/ -- Z99 AA999999/Intramural NIH HHS/ -- England -- Nature. 2010 Dec 23;468(7327):1061-6. doi: 10.1038/nature09629.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Neurogenetics, National Institute on Alcohol Abuse and Alcoholism, NIH, Rockville, Maryland 20852, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21179162" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Case-Control Studies ; Cell Line ; Female ; Finland ; Founder Effect ; Gene Expression Regulation ; Gene Knockout Techniques ; Genotype ; Humans ; Impulsive Behavior/*genetics ; Male ; Mental Disorders/genetics ; Mice ; Mice, 129 Strain ; Mice, Knockout ; Pedigree ; Polymorphism, Single Nucleotide/genetics ; Receptor, Serotonin, 5-HT2B/*genetics/*metabolism ; Testosterone/blood/cerebrospinal fluid
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 9
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    A bizarre Jurassic maniraptoran from China with elongate ribbon-like feathers (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-10-25
    Description: Recent coelurosaurian discoveries have greatly enriched our knowledge of the transition from dinosaurs to birds, but all reported taxa close to this transition are from relatively well known coelurosaurian groups. Here we report a new basal avialan, Epidexipteryx hui gen. et sp. nov., from the Middle to Late Jurassic of Inner Mongolia, China. This new species is characterized by an unexpected combination of characters seen in several different theropod groups, particularly the Oviraptorosauria. Phylogenetic analysis shows it to be the sister taxon to Epidendrosaurus, forming a new clade at the base of Avialae. Epidexipteryx also possesses two pairs of elongate ribbon-like tail feathers, and its limbs lack contour feathers for flight. This finding shows that a member of the avialan lineage experimented with integumentary ornamentation as early as the Middle to Late Jurassic, and provides further evidence relating to this aspect of the transition from non-avian theropods to birds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Fucheng -- Zhou, Zhonghe -- Xu, Xing -- Wang, Xiaolin -- Sullivan, Corwin -- England -- Nature. 2008 Oct 23;455(7216):1105-8. doi: 10.1038/nature07447.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Evolutionary Systematics of Vertebrates, Institute of Vertebrate Paleontology and Paleoanthropology, Chinese Academy of Sciences, PO Box 643, Beijing 100044, China. zhangfucheng@ivpp.ac.cn〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18948955" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; China ; Dinosaurs/*anatomy & histology/*classification ; Feathers/*anatomy & histology ; *Fossils ; History, Ancient ; Phylogeny
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 10
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    Genetic variation in human NPY expression affects stress response and emotion (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-04-04
    Description: Understanding inter-individual differences in stress response requires the explanation of genetic influences at multiple phenotypic levels, including complex behaviours and the metabolic responses of brain regions to emotional stimuli. Neuropeptide Y (NPY) is anxiolytic and its release is induced by stress. NPY is abundantly expressed in regions of the limbic system that are implicated in arousal and in the assignment of emotional valences to stimuli and memories. Here we show that haplotype-driven NPY expression predicts brain responses to emotional and stress challenges and also inversely correlates with trait anxiety. NPY haplotypes predicted levels of NPY messenger RNA in post-mortem brain and lymphoblasts, and levels of plasma NPY. Lower haplotype-driven NPY expression predicted higher emotion-induced activation of the amygdala, as well as diminished resiliency as assessed by pain/stress-induced activations of endogenous opioid neurotransmission in various brain regions. A single nucleotide polymorphism (SNP rs16147) located in the promoter region alters NPY expression in vitro and seems to account for more than half of the variation in expression in vivo. These convergent findings are consistent with the function of NPY as an anxiolytic peptide and help to explain inter-individual variation in resiliency to stress, a risk factor for many diseases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2715959/" 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/PMC2715959/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Zhifeng -- Zhu, Guanshan -- Hariri, Ahmad R -- Enoch, Mary-Anne -- Scott, David -- Sinha, Rajita -- Virkkunen, Matti -- Mash, Deborah C -- Lipsky, Robert H -- Hu, Xian-Zhang -- Hodgkinson, Colin A -- Xu, Ke -- Buzas, Beata -- Yuan, Qiaoping -- Shen, Pei-Hong -- Ferrell, Robert E -- Manuck, Stephen B -- Brown, Sarah M -- Hauger, Richard L -- Stohler, Christian S -- Zubieta, Jon-Kar -- Goldman, David -- K01 MH072837/MH/NIMH NIH HHS/ -- K02-DA17232/DA/NIDA NIH HHS/ -- P01 HL040962/HL/NHLBI NIH HHS/ -- P50-DA16556/DA/NIDA NIH HHS/ -- PL1 DA024859/DA/NIDA NIH HHS/ -- PL1 DA024859-02/DA/NIDA NIH HHS/ -- R01 DA 016423/DA/NIDA NIH HHS/ -- R01 DE 15396/DE/NIDCR NIH HHS/ -- R01 HL065137/HL/NHLBI NIH HHS/ -- R01 MH074697/MH/NIMH NIH HHS/ -- R01 MH074697-04A1/MH/NIMH NIH HHS/ -- R01-AA13892/AA/NIAAA NIH HHS/ -- Z01 AA000301-09/Intramural NIH HHS/ -- Z99 AA999999/Intramural NIH HHS/ -- England -- Nature. 2008 Apr 24;452(7190):997-1001. doi: 10.1038/nature06858. Epub 2008 Apr 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Neurogenetics, NIAAA, NIH, Bethesda, Maryland 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18385673" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Anxiety/genetics ; Anxiety Disorders/genetics ; Brain/*metabolism/physiology/physiopathology ; *Emotions ; European Continental Ancestry Group/genetics ; Facial Expression ; Finland/ethnology ; Gene Expression Regulation/*genetics ; Genetic Variation/*genetics ; Haplotypes/genetics ; Humans ; Lymphocytes/metabolism ; Magnetic Resonance Imaging ; Male ; Neuropeptide Y/blood/*genetics ; Opioid Peptides/metabolism ; Pain/genetics ; Polymorphism, Single Nucleotide/genetics ; RNA, Messenger/genetics/metabolism ; Stress, Physiological/*genetics/psychology ; United States/ethnology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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