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  • Chemistry
  • Crystallography, X-Ray
  • American Association for the Advancement of Science (AAAS)  (42)
  • 2005-2009  (42)
  • 1995-1999
  • 2005  (42)
Collection
Keywords
Publisher
Years
  • 2005-2009  (42)
  • 1995-1999
Year
  • 1
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    Structural biology. Structural genomics, round 2 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1554-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761136" target="_blank"〉PubMed〈/a〉
    Keywords: Automation ; Biomedical Technology ; Budgets ; Computer Simulation ; Costs and Cost Analysis ; Crystallization ; Crystallography, X-Ray ; *Genomics/economics/instrumentation/methods ; Models, Molecular ; National Institutes of Health (U.S.)/economics ; *Protein Conformation ; Proteins/*chemistry/genetics/isolation & purification ; *Proteomics/economics/instrumentation/methods ; Robotics ; United States
    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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  • 2
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    Structural biology. Flipping lipids: is the third time the charm? (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davidson, Amy L -- Chen, Jue -- New York, N.Y. -- Science. 2005 May 13;308(5724):963-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA. davidson@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890866" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/*metabolism ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Bacterial Proteins/*chemistry/*metabolism ; Cell Membrane/*chemistry ; Crystallography, X-Ray ; Dimerization ; Electron Spin Resonance Spectroscopy ; Escherichia coli/chemistry ; Escherichia coli Proteins/chemistry/metabolism ; Hydrolysis ; Lipid A/metabolism ; Lipid Bilayers ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Salmonella typhimurium/*chemistry ; Spin Labels ; Vanadates/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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  • 3
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    Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors. In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta. gammac is then recruited to the composite surface formed by the IL-2/IL-2Rbeta complex. Consistent with its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21, gammac forms degenerate contacts with IL-2. The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID). This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Xinquan -- Rickert, Mathias -- Garcia, K Christopher -- AI51321/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1159-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Microbiology and Immunology, Stanford University School of Medicine, 299 Campus Drive, Fairchild D319, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293754" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Humans ; Interleukin Receptor Common gamma Subunit ; Interleukin-2/*chemistry/metabolism/therapeutic use ; Interleukin-2 Receptor alpha Subunit ; Interleukin-2 Receptor beta Subunit ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; Receptors, Interleukin/*chemistry/metabolism ; Receptors, Interleukin-2/*chemistry/genetics/metabolism ; Recombinant Proteins/therapeutic use ; Severe Combined Immunodeficiency/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Crystal structure of the malaria vaccine candidate apical membrane antigen 1 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-26
    Description: Apical membrane antigen 1 from Plasmodium is a leading malaria vaccine candidate. The protein is essential for host-cell invasion, but its molecular function is unknown. The crystal structure of the three domains comprising the ectoplasmic region of the antigen from P. vivax, solved at 1.8 angstrom resolution, shows that domains I and II belong to the PAN motif, which defines a superfamily of protein folds implicated in receptor binding. We also mapped the epitope of an invasion-inhibitory monoclonal antibody specific for the P. falciparum ortholog and modeled this to the structure. The location of the epitope and current knowledge on structure-function correlations for PAN domains together suggest a receptor-binding role during invasion in which domain II plays a critical part. These results are likely to aid vaccine and drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizarro, Juan Carlos -- Vulliez-Le Normand, Brigitte -- Chesne-Seck, Marie-Laure -- Collins, Christine R -- Withers-Martinez, Chrislaine -- Hackett, Fiona -- Blackman, Michael J -- Faber, Bart W -- Remarque, Edmond J -- Kocken, Clemens H M -- Thomas, Alan W -- Bentley, Graham A -- MC_U117532063/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):408-11. Epub 2005 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite d'Immunologie Structurale, Centre National de la Recherche Scientifique, URA 2185, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731407" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Protozoan/*chemistry/immunology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Epitope Mapping ; Epitopes ; Heparin/metabolism ; Malaria Vaccines ; Membrane Proteins/*chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Plasmodium falciparum/chemistry/immunology ; Plasmodium vivax/chemistry/*immunology ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protozoan Proteins/*chemistry/immunology ; Recombinant Proteins/chemistry ; Sequence Alignment
    Print ISSN: 0036-8075
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  • 5
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    Structural biology. A ribosomal coup: E. coli at last! (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, Peter B -- New York, N.Y. -- Science. 2005 Nov 4;310(5749):793-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA. peter.moore@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16272105" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry/*ultrastructure ; Escherichia coli Proteins/chemistry ; Models, Molecular ; RNA, Bacterial/chemistry ; RNA, Ribosomal/*chemistry ; Ribosomal Proteins/*chemistry ; Ribosomes/*chemistry/*ultrastructure
    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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    Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: Chlorinated natural products include vancomycin and cryptophycin A. Their biosynthesis involves regioselective chlorination by flavin-dependent halogenases. We report the structural characterization of tryptophan 7-halogenase (PrnA), which regioselectively chlorinates tryptophan. Tryptophan and flavin adenine dinucleotide (FAD) are separated by a 10 angstrom-long tunnel and bound by distinct enzyme modules. The FAD module is conserved in halogenases and is related to flavin-dependent monooxygenases. On the basis of biochemical studies, crystal structures, and by analogy with monooxygenases, we predict that FADH2 reacts with O2 to make peroxyflavin, which is decomposed by Cl-. The resulting HOCl is guided through the tunnel to tryptophan, where it is activated to participate in electrophilic aromatic substitution.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315827/" 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/PMC3315827/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, Changjiang -- Flecks, Silvana -- Unversucht, Susanne -- Haupt, Caroline -- van Pee, Karl-Heinz -- Naismith, James H -- BB/C000080/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BBS/B/14426/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2216-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Biomolecular Sciences, EaStchem, University of St. Andrews, St. Andrews KY16 9ST, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195462" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Chlorides/*metabolism ; Crystallography, X-Ray ; Dimerization ; Flavin-Adenine Dinucleotide/analogs & derivatives/metabolism ; Hydrogen Bonding ; Hypochlorous Acid/metabolism ; Indoles/metabolism ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/*chemistry/isolation & purification/metabolism ; Oxygen/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pseudomonas fluorescens/*enzymology ; Tryptophan/analogs & derivatives/metabolism
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  • 7
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    Structure of SARS coronavirus spike receptor-binding domain complexed with receptor (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-17
    Description: The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Fang -- Li, Wenhui -- Farzan, Michael -- Harrison, Stephen C -- AI061601/AI/NIAID NIH HHS/ -- CA13202/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1864-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166518" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antibodies, Viral/immunology ; Binding Sites ; Carboxypeptidases/*chemistry/metabolism ; Cell Line ; Crystallography, X-Ray ; Disease Outbreaks ; Epitopes ; Glycosylation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/*chemistry/genetics/immunology/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Peptidyl-Dipeptidase A ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*chemistry/metabolism ; SARS Virus/*chemistry/genetics/physiology ; Severe Acute Respiratory Syndrome/transmission/*virology ; Species Specificity ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/*chemistry/genetics/immunology/*metabolism ; Viral Vaccines ; Viverridae/virology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 8
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    Structural insights into the activity of enhancer-binding proteins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: Activators of bacterial sigma54-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic electron microscopy (cryo-EM) a 20 angstrom resolution structure of an activator, phage shock protein F [PspF(1-275)], which is bound to an ATP transition state analog in complex with its basal factor, sigma54. By fitting the crystal structure of PspF(1-275) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma54. Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma54.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2756573/" 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/PMC2756573/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rappas, Mathieu -- Schumacher, Jorg -- Beuron, Fabienne -- Niwa, Hajime -- Bordes, Patricia -- Wigneshweraraj, Sivaramesh -- Keetch, Catherine A -- Robinson, Carol V -- Buck, Martin -- Zhang, Xiaodong -- B17129/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1972-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Imperial College London, London, SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790859" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Cryoelectron Microscopy ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/metabolism ; DNA-Directed RNA Polymerases/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; PII Nitrogen Regulatory Proteins ; *Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Polymerase Sigma 54 ; Sigma Factor/chemistry/metabolism ; Trans-Activators/*chemistry/*metabolism ; Transcription Factors/chemistry/metabolism
    Print ISSN: 0036-8075
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  • 9
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    A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-04
    Description: Fluoroquinolones are gaining increasing importance in the treatment of tuberculosis. The expression of MfpA, a member of the pentapeptide repeat family of proteins from Mycobacterium tuberculosis, causes resistance to ciprofloxacin and sparfloxacin. This protein binds to DNA gyrase and inhibits its activity. Its three-dimensional structure reveals a fold, which we have named the right-handed quadrilateral beta helix, that exhibits size, shape, and electrostatic similarity to B-form DNA. This represents a form of DNA mimicry and explains both its inhibitory effect on DNA gyrase and fluoroquinolone resistance resulting from the protein's expression in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hegde, Subray S -- Vetting, Matthew W -- Roderick, Steven L -- Mitchenall, Lesley A -- Maxwell, Anthony -- Takiff, Howard E -- Blanchard, John S -- AI33696/AI/NIAID NIH HHS/ -- AI60899/AI/NIAID NIH HHS/ -- T32 AI007501/AI/NIAID NIH HHS/ -- T32 AI07501/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1480-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933203" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antitubercular Agents/chemistry/*pharmacology ; Bacterial Proteins/chemistry/*physiology ; Ciprofloxacin/pharmacology ; Crystallography, X-Ray ; DNA Gyrase/metabolism ; DNA, Bacterial/*chemistry ; DNA, Superhelical/chemistry ; *Drug Resistance, Bacterial ; Drug Resistance, Microbial/*physiology ; Enzyme Inhibitors/chemistry ; Escherichia coli/enzymology ; Fluoroquinolones/antagonists & inhibitors/chemistry/*pharmacology ; Models, Molecular ; *Molecular Mimicry ; Molecular Sequence Data ; Monomeric GTP-Binding Proteins ; Mycobacterium tuberculosis/drug effects/*physiology ; Protein Conformation ; Protein Folding ; Structure-Activity Relationship ; Topoisomerase II Inhibitors
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Cyberinfrastructure for e-Science (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-10
    Description: Here we describe the requirements of an e-Infrastructure to enable faster, better, and different scientific research capabilities. We use two application exemplars taken from the United Kingdom's e-Science Programme to illustrate these requirements and make the case for a service-oriented infrastructure. We provide a brief overview of the UK "plug-and-play composable services" vision and the role of semantics in such an e-Infrastructure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hey, Tony -- Trefethen, Anne E -- New York, N.Y. -- Science. 2005 May 6;308(5723):817-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Engineering and Physical Sciences Research Council, Polaris House, North Star Avenue, Swindon SN2 1ET, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879209" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Combinatorial Chemistry Techniques ; *Computational Biology ; *Computer Communication Networks ; *Computing Methodologies ; Databases as Topic ; Graves Disease/genetics ; *Internet ; *Research ; *Software ; Williams Syndrome/genetics
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