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  • 1
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    The family naturalist (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-10-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agre, Peter -- England -- Nature. 2010 Oct 14;467(7317):S11. doi: 10.1038/467S11a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20944611" target="_blank"〉PubMed〈/a〉
    Keywords: Aquaporins/metabolism ; Chemistry ; Happiness ; Interdisciplinary Communication ; Mentors ; Neurosciences/trends ; *Nobel Prize ; Peer Review, Research ; Politics ; Public Policy ; Research/standards/trends ; *Research Personnel/psychology/standards
    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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  • 2
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    The scientific diplomat (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agre, Peter -- England -- Nature. 2010 Jan 21;463(7279):281. doi: 10.1038/463281a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20090722" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; *Communication ; Cuba ; Democratic People's Republic of Korea ; History, 21st Century ; *International Cooperation ; International Educational Exchange ; Politics ; *Science/economics/trends ; United States
    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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  • 3
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    Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is an abundant integral membrane protein in mammalian RBCs and renal proximal tubules and belongs to a family of membrane proteins with unknown functions. Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels. Therefore it is likely that CHIP28 is a functional unit of membrane water channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preston, G M -- Carroll, T P -- Guggino, W B -- Agre, P -- DK32753/DK/NIDDK NIH HHS/ -- HL33991/HL/NHLBI NIH HHS/ -- HL48268/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):385-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373524" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquaporin 1 ; *Aquaporins ; Cell Membrane Permeability ; Electric Conductivity ; Erythrocyte Membrane/*metabolism ; Immunoblotting ; Membrane Proteins/chemistry/genetics/*physiology ; Mercuric Chloride/pharmacology ; Molecular Structure ; Oocytes/*metabolism ; Osmolar Concentration ; RNA/genetics ; Thermodynamics ; Transfection ; Water/*metabolism ; Xenopus laevis
    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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  • 4
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    Bridging science and society (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-02-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agre, Peter -- Leshner, Alan I -- New York, N.Y. -- Science. 2010 Feb 19;327(5968):921. doi: 10.1126/science.1188231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20167748" target="_blank"〉PubMed〈/a〉
    Keywords: Attitude ; Consumer Participation ; Culture ; Humans ; Public Opinion ; Religion and Science ; *Science ; Sociology
    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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  • 5
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    Presidential address. Life on the river of science (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agre, Peter -- New York, N.Y. -- Science. 2011 Jan 28;331(6016):416-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21284129" target="_blank"〉PubMed〈/a〉
    Keywords: Aquaporin 1/history ; Chemistry/history ; History, 20th Century ; History, 21st Century ; International Cooperation ; Nobel Prize ; *Science/history ; United States
    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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  • 6
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    Aquaporins and ion conductance (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agre, P -- Lee, M D -- Devidas, S -- Guggino, W B -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1490; author reply 1492.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9045617" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquaporin 1 ; Aquaporin 5 ; *Aquaporins ; Biological Transport/drug effects ; Cations/*metabolism ; Cell Membrane/*metabolism ; Colforsin/*pharmacology ; Ion Channels/genetics/*physiology ; Ion Transport/drug effects ; *Membrane Proteins ; Oocytes ; Patch-Clamp Techniques ; RNA, Complementary ; Water/*metabolism ; Xenopus
    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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  • 7
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    Structural biology. The atomic architecture of a gas channel (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knepper, Mark A -- Agre, Peter -- Z01 HL001285-21/Intramural NIH HHS/ -- Z99 HL999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1573-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Kidney and Electrolyte Metabolism, National Institutes of Health, Bethesda, MD 20892, USA. pagre@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15361612" target="_blank"〉PubMed〈/a〉
    Keywords: Ammonia/*metabolism ; Biological Transport ; Carrier Proteins/metabolism ; Cation Transport Proteins/*chemistry/genetics/metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli/*chemistry/genetics/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Glycoproteins/metabolism ; Humans ; Hydrogen-Ion Concentration ; Kidney Tubules, Collecting/metabolism ; Lipid Bilayers/metabolism ; Liver/metabolism ; Membrane Glycoproteins/metabolism ; *Membrane Transport Proteins ; Models, Molecular ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Quaternary Ammonium Compounds/metabolism ; Rh-Hr Blood-Group System/metabolism
    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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  • 8
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    Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-09
    Description: The gene aquaporin-1 encodes channel-forming integral protein (CHIP), a member of a large family of water transporters found throughout nature. Three rare individuals were identified who do not express CHIP-associated Colton blood group antigens and whose red cells exhibit low osmotic water permeabilities. Genomic DNA analyses demonstrated that two individuals were homozygous for different nonsense mutations (exon deletion or frameshift), and the third had a missense mutation encoding a nonfunctioning CHIP molecule. Surprisingly, none of the three suffers any apparent clinical consequence, which raises questions about the physiological importance of CHIP and implies that other mechanisms may compensate for its absence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preston, G M -- Smith, B L -- Zeidel, M L -- Moulds, J J -- Agre, P -- DK32753/DK/NIDDK NIH HHS/ -- HL33991/HL/NHLBI NIH HHS/ -- HL48268/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1585-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7521540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquaporin 1 ; *Aquaporins ; Base Sequence ; Blood Group Antigens ; Cell Membrane Permeability ; Erythrocyte Membrane/chemistry/physiology ; Exons ; Female ; Homozygote ; Humans ; Ion Channels/blood/*genetics/urine ; Kidney Tubules/chemistry ; Molecular Sequence Data ; Mutation ; Oocytes ; Phenotype ; Polymerase Chain Reaction ; Xenopus
    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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  • 9
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    Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-17
    Description: Both C/EBP and GCN4 are sequence-specific DNA binding proteins that control gene expression. Recent evidence implicates C/EBP as a transcriptional regulator of genes involved in lipid and carbohydrate metabolism. The C/EBP protein binds avidly to the dyad symmetric sequence 5'-ATTGCGCAAT-3'; GCN4 regulates the transcription of genes that control amino acid biosynthesis in yeast, and binds avidly to the dyad symmetric sequence 5'-ATGA(G/C)TCAT-3'. Both C/EBP and GCN4 bind DNA via the same structural motif. This motif has been predicted to be bipartite, consisting of a dimerization interface termed the "leucine zipper" and a DNA contact surface termed the "basic region." Specificity of DNA binding has been predicted to be imparted by the basic region. As a test of this hypothesis, recombinant proteins were created wherein the basic regions and leucine zippers of GCN4 and C/EBP were reciprocally exchanged. In both of the recombinant polypeptides, DNA binding specificity is shown to track with the basic region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agre, P -- Johnson, P F -- McKnight, S L -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):922-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2530632" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; CCAAT-Enhancer-Binding Proteins ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Deoxyribonuclease I ; Escherichia coli/genetics ; Fungal Proteins/genetics/*metabolism ; Genes, Fungal ; Genes, Regulator ; Molecular Sequence Data ; Neurospora crassa/genetics ; Nuclear Proteins/genetics/*metabolism ; Nucleotide Mapping ; *Protein Kinases ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/genetics/*metabolism
    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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  • 10
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    The Israeli-Palestinian Science Organization (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wiesel, Torsten -- Agre, Peter -- Arrow, Kenneth J -- Atiyah, Michael -- Brezin, Edouard -- Charfi, Faouzia Farida -- Cohen-Tanoudji, Claude -- Daar, Abdallah -- Jacob, Francois -- Kahneman, Daniel -- Lee, Yuan Tseh -- Nicolaisen, Ida -- Nusseibeh, Sari -- Reuter, Harald -- Shoham, Yoav -- Sulston, John -- Walzer, Michael -- Yaari, Menahem -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):39.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204624" 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
    Published by American Association for the Advancement of Science (AAAS)
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