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  • Humans  (93)
  • Life and Medical Sciences  (50)
  • Chemical Engineering  (36)
  • ASTROPHYSICS
  • Lunar and Planetary Science and Exploration
  • 1995-1999  (195)
  • 1950-1954
  • 1996  (195)
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  • 1995-1999  (195)
  • 1950-1954
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  • 11
    Publication Date: 1996-07-26
    Description: The functional mimicry of a protein by an unrelated small molecule has been a formidable challenge. Now, however, the biological activity of a 166-residue hematopoietic growth hormone, erythropoietin (EPO), with its class 1 cytokine receptor has been mimicked by a 20-residue cyclic peptide unrelated in sequence to the natural ligand. The crystal structure at 2.8 A resolution of a complex of this agonist peptide with the extracellular domain of EPO receptor reveals that a peptide dimer induces an almost perfect twofold dimerization of the receptor. The dimer assembly differs from that of the human growth hormone (hGH) receptor complex and suggests that more than one mode of dimerization may be able to induce signal transduction and cell proliferation. The EPO receptor binding site, defined by peptide interaction, corresponds to the smaller functional epitope identified for hGH receptor. Similarly, the EPO mimetic peptide ligand can be considered as a minimal hormone, and suggests the design of nonpeptidic small molecule mimetics for EPO and other cytokines may indeed be achievable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Livnah, O -- Stura, E A -- Johnson, D L -- Middleton, S A -- Mulcahy, L S -- Wrighton, N C -- Dower, W J -- Jolliffe, L K -- Wilson, I A -- GM-49497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):464-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662530" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Drug Design ; Erythropoietin/*chemistry/*metabolism ; Growth Hormone/chemistry/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; *Molecular Mimicry ; Molecular Sequence Data ; Peptides, Cyclic/*chemistry/*metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Erythropoietin/*agonists/chemistry/metabolism ; Receptors, Somatotropin/chemistry/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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  • 12
    Publication Date: 1996-07-26
    Description: Random phage display peptide libraries and affinity selective methods were used to isolate small peptides that bind to and activate the receptor for the cytokine erythropoietin (EPO). In a panel of in vitro biological assays, the peptides act as full agonists and they can also stimulate erythropoiesis in mice. These agonists are represented by a 14- amino acid disulfide-bonded, cyclic peptide with the minimum consensus sequence YXCXXGPXTWXCXP, where X represents positions allowing occupation by several amino acids. The amino acid sequences of these peptides are not found in the primary sequence of EPO. The signaling pathways activated by these peptides appear to be identical to those induced by the natural ligand. This discovery may form the basis for the design of small molecule mimetics of EPO.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wrighton, N C -- Farrell, F X -- Chang, R -- Kashyap, A K -- Barbone, F P -- Mulcahy, L S -- Johnson, D L -- Barrett, R W -- Jolliffe, L K -- Dower, W J -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):458-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymax Research Institute, 4001 Miranda Avenue, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages ; Cell Division/drug effects ; Cell Line ; Cloning, Molecular ; Erythropoiesis/drug effects ; Erythropoietin/chemistry/*metabolism/*pharmacology ; Humans ; Ligands ; Mice ; *Molecular Mimicry ; Molecular Sequence Data ; Mutagenesis ; Peptides, Cyclic/chemistry/*metabolism/*pharmacology ; Phosphorylation ; Protein Structure, Secondary ; Receptors, Erythropoietin/*agonists/chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Transduction ; Solubility ; Tyrosine/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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  • 13
    Publication Date: 1996-06-14
    Description: The basal cell nevus syndrome (BCNS) is characterized by developmental abnormalities and by the postnatal occurrence of cancers, especially basal cell carcinomas (BCCs), the most common human cancer. Heritable mutations in BCNS patients and a somatic mutation in a sporadic BCC were identified in a human homolog of the Drosophila patched (ptc) gene. The ptc gene encodes a transmembrane protein that in Drosophila acts in opposition to the Hedgehog signaling protein, controlling cell fates, patterning, and growth in numerous tissues. The human PTC gene appears to be crucial for proper embryonic development and for tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, R L -- Rothman, A L -- Xie, J -- Goodrich, L V -- Bare, J W -- Bonifas, J M -- Quinn, A G -- Myers, R M -- Cox, D R -- Epstein, E H Jr -- Scott, M P -- AR3995/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1668-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, California 94305-5427, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658145" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Basal Cell Nevus Syndrome/*genetics ; Base Sequence ; Cloning, Molecular ; DNA, Neoplasm ; Drosophila ; *Drosophila Proteins ; Female ; Frameshift Mutation ; *Genes, Tumor Suppressor ; Humans ; Insect Hormones/genetics ; Male ; Membrane Proteins/*genetics ; Middle Aged ; Molecular Sequence Data ; Polymerase Chain Reaction ; Polymorphism, Single-Stranded Conformational ; Protein Conformation ; Receptors, Cell Surface
    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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  • 14
    Publication Date: 2019-07-10
    Description: Remote sensing of surface properties and estimation of clear-sky and surface albedo generally assumes that the albedo depends only on the solar zenith angle. The effects of dew, frost, and precipitation as well as evaporation and wind can lead to some systematic diurnal variability resulting in an asymmetric diurnal cycle of albedo. This paper examines the symmetry of both surface-observed albedos and top-of-the-atmosphere (TOA) albedos derived from satellite data. Broadband and visible surface albedos were measured at the Department of Energy Atmospheric Radiation Measurement (ARM) Program Southern Great Plains Central Facility, at some fields near the ARM site, and over a coniferous forest in eastern Virginia. Surface and wind conditions are available for most cases. GOES-8 satellite radiance data are converted to broadband albedo using bidirectional reflectance functions and an empirical narrowband-to-broadband relationship. The initial results indicate that surface moisture has a significant effect and can change the albedo in the afternoon by 20% relative to its morning counterpart. Such effects may need to be incorporated in mesoscale and even large-scale models of atmospheric processes.
    Keywords: Lunar and Planetary Science and Exploration
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dannemiller, J L -- Babler, T G -- Babler, B L -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):256-7; author reply 258-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8668998" target="_blank"〉PubMed〈/a〉
    Keywords: *Baseball ; Humans ; Mathematics ; Models, Psychological ; *Motion Perception ; *Psychomotor Performance ; Running ; *Space Perception
    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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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-21
    Description: The human beta T cell receptor (TCR) locus, comprising a complex family of genes, has been sequenced. The locus contains two types of coding elements--TCR elements (65 variable gene segments and two clusters of diversity, joining, and constant segments) and eight trypsinogen genes --that constitute 4.6 percent of the DNA. Genome-wide interspersed repeats and locus-specific repeats span 30 and 47 percent, respectively, of the 685-kilobase sequence. A comparison of the germline variable elements with their approximately 300 complementary DNA counterparts reveals marked differential patterns of variable gene expression, the importance of exonuclease activity in generating TCR diversity, and the predominant tendency for only functional variable elements to be present in complementary DNA libraries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowen, L -- Koop, B F -- Hood, L -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1755-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biotechnology, University of Washington, Seattle 98195-7730, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Chromosomes, Human, Pair 7 ; Chromosomes, Human, Pair 9 ; DNA, Complementary/genetics ; Exons ; Genetic Variation ; Humans ; Introns ; Molecular Sequence Data ; *Multigene Family ; Polymorphism, Genetic ; Promoter Regions, Genetic ; Pseudogenes ; RNA Splicing ; Receptors, Antigen, T-Cell, alpha-beta/*genetics ; Repetitive Sequences, Nucleic Acid ; Translocation, Genetic ; Trypsinogen/genetics
    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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  • 17
    Publication Date: 1996-01-19
    Description: About 90 percent of human pancreatic carcinomas show allelic loss at chromosome 18q. To identify candidate tumor suppressor genes on 18q, a panel of pancreatic carcinomas were analyzed for convergent sites of homozygous deletion. Twenty-five of 84 tumors had homozygous deletions at 18q21.1, a site that excludes DCC (a candidate suppressor gene for colorectal cancer) and includes DPC4, a gene similar in sequence to a Drosophila melanogaster gene (Mad) implicated in a transforming growth factor-beta (TGF-beta)-like signaling pathway. Potentially inactivating mutations in DPC4 were identified in six of 27 pancreatic carcinomas that did not have homozygous deletions at 18q21.1. These results identify DPC4 as a candidate tumor suppressor gene whose inactivation may play a role in pancreatic and possibly other human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahn, S A -- Schutte, M -- Hoque, A T -- Moskaluk, C A -- da Costa, L T -- Rozenblum, E -- Weinstein, C L -- Fischer, A -- Yeo, C J -- Hruban, R H -- Kern, S E -- CA62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):350-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553070" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Division ; Chromosome Mapping ; *Chromosomes, Human, Pair 18 ; *DNA-Binding Proteins ; Gene Deletion ; Gene Expression ; *Genes, Tumor Suppressor ; Genetic Markers ; Humans ; Mice ; Molecular Sequence Data ; Mutation ; Neoplasm Transplantation ; Pancreatic Neoplasms/*genetics/pathology ; Proteins/chemistry/*genetics/physiology ; Signal Transduction ; Smad4 Protein ; *Trans-Activators ; Transforming Growth Factor beta/physiology ; Transplantation, Heterologous ; Tumor Cells, Cultured
    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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  • 18
    Publication Date: 1996-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schuler, G D -- Boguski, M S -- Hudson, T J -- Hui, L -- Ma, J -- Castle, A B -- Wu, X -- Silva, J -- Nusbaum, H C -- Birren, B B -- Slonim, D K -- Rozen, S -- Stein, L D -- Page, D -- Lander, E S -- Stewart, E A -- Aggarwal, A -- Bajorek, E -- Brady, S -- Chu, S -- Fang, N -- Hadley, D -- Harris, M -- Hussain, S -- Hudson, J R Jr -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):547-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8928009" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosome Mapping ; DNA, Complementary/genetics ; Gene Expression ; Gene Library ; Genetic Diseases, Inborn/genetics ; Genetic Markers ; *Genome, Human ; *Human Genome Project ; Humans ; RNA, Messenger/genetics ; Sequence Tagged Sites
    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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  • 19
    Publication Date: 1996-11-08
    Description: Tumor necrosis factor receptor-1 (TNFR-1) and CD95 (also called Fas or APO-1) are cytokine receptors that engage the apoptosis pathway through a region of intracellular homology, designated the "death domain." Another death domain-containing member of the TNFR family, death receptor 3 (DR3), was identified and was shown to induce both apoptosis and activation of nuclear factor kappaB. Expression of DR3 appears to be restricted to tissues enriched in lymphocytes. DR3 signal transduction is mediated by a complex of intracellular signaling molecules including TRADD, TRAF2, FADD, and FLICE. Thus, DR3 likely plays a role in regulating lymphocyte homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chinnaiyan, A M -- O'Rourke, K -- Yu, G L -- Lyons, R H -- Garg, M -- Duan, D R -- Xing, L -- Gentz, R -- Ni, J -- Dixit, V M -- GM-07863/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):990-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. Sciences Inc., 9620 Medical Center Driv.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875942" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Antigens, CD95/chemistry/physiology ; *Apoptosis ; Carrier Proteins/metabolism ; Caspase 8 ; Caspase 9 ; *Caspases ; Cloning, Molecular ; Cysteine Endopeptidases/metabolism ; Fas-Associated Death Domain Protein ; Gene Library ; Humans ; Lymphocytes ; Molecular Sequence Data ; NF-kappa B/*physiology ; Organ Specificity ; Proteins/metabolism ; RNA, Messenger/analysis/genetics ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*physiology ; Receptors, Tumor Necrosis Factor, Member 25 ; Sequence Alignment ; *Signal Transduction ; TNF Receptor-Associated Factor 1 ; TNF Receptor-Associated Factor 2 ; Transfection ; Tumor Cells, Cultured
    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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  • 20
    Publication Date: 1996-06-07
    Description: Unprotected receptive anal intercourse is a well-recognized risk factor for infection with human immunodeficiency virus-type 1 (HIV-1). Isolated human case reports have implicated HIV-1 transmission by oral-genital exposure. Adult macaques exposed nontraumatically to cell-free simian immunodeficiency virus (SIV) through the oral route became infected and developed acquired immunodeficiency syndrome (AIDS). The minimal virus dose needed to achieve systemic infection after oral exposure was 6000 times lower than the minimal dose required to achieve systemic infection after rectal exposure. Thus, unprotected receptive oral intercourse, even in the absence of mucosal lesions, should be added to the list of risk behaviors for HIV-1 transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baba, T W -- Trichel, A M -- An, L -- Liska, V -- Martin, L N -- Murphey-Corb, M -- Ruprecht, R M -- R01-AI32330/AI/NIAID NIH HHS/ -- R01-AI34266/AI/NIAID NIH HHS/ -- U01-AI24345/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1486-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Newborn Medicine, Department of Pediatrics, Tufts University School of Medicine, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633242" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Disease Transmission, Infectious ; Gastric Acid/physiology ; HIV Infections/*transmission/virology ; *Hiv-1 ; Humans ; Intestinal Mucosa/virology ; Macaca mulatta ; Mouth Mucosa/*virology ; Rectum/virology ; Risk Factors ; *Sexual Behavior ; Sexual Behavior, Animal ; Simian Acquired Immunodeficiency Syndrome/*transmission/virology ; Simian Immunodeficiency Virus/*physiology ; Tongue/virology ; Viremia
    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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