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  • Articles  (35)
  • Molecular Sequence Data  (32)
  • Cell & Developmental Biology
  • Computational Physics
  • Dynamics, dynamical systems, lattice effects
  • Natural Sciences in General  (35)
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  • Articles  (35)
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  • 1
    Electronic Resource
    Electronic Resource
    Imaging fluid/solid interactions in hydrocarbon reservoir rocks (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 25 (1993), S. 465-473 
    Details
    ISSN: 1059-910X
    Keywords: ESEM ; Liquid hydrocarbons ; Hydrocarbon reservoirs ; Clay minerals ; Chlorite ; Illite/smectite ; Calcite ; Fluid sensitivity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: The environmental scanning electron microscope (ESEM) has been used to image liquid hydrocarbons in sandstones and oil shales. Additionally, the fluid sensitivity of selected clay minerals in hydrocarbon reservoirs was assessed via three case studies: HCl acid sensitivity of authigenic chlorite in sandstone reservoirs, freshwater sensitivity of authigenic illite/smectite in sandstone reservoirs, and bleach sensitivity of a volcanic reservoir containing abundant secondary chlorite/corrensite. The results showed the suitability of using ESEM for imaging liquid hydrocarbon films in hydrocarbon reservoirs and the importance of simulating in situ fluid-rock interactions for hydrocarbon production programmes. In each case, results of the ESEM studies greatly enhanced prediction of reservoir/borehole reactions and, in some cases, contradicted conventional wisdom regarding the outcome of potential engineering solutions. © 1993 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070250518
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  • 2
    Electronic Resource
    Electronic Resource
    Allografts of CNS tissue possess a blood-brain barrier: III. Neuropathological, methodological, and immunological considerations (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 27 (1994), S. 471-494 
    Details
    ISSN: 1059-910X
    Keywords: Transplantation ; Central nervous system ; Endothelium ; Immunology ; Immunohistochemistry ; Blood vessels ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Development of a blood-brain barrier (BBB) within mammalian CNS grafts, placed either intracerebrally or peripherally, has been controversial. Published data from this laboratory have emphasized the presence or the absence of a BBB within solid mammalian tissue or cell suspension grafts is determined intrinsically by the graft and not by the surrounding host parenchyma (e.g., brain, kidney, testis, etc.). Nevertheless, correctly interpreting whether or not a BBB exists within brain grafts is manifested by methodologies employed to answer the question and by ensuing neuropathological and immunological consequences of intracerebral grafting. The present study addresses these issues and suggests misinterpretation for the absence of a BBB in brain grafts can be attributed to: (1) rupture of interendothelial tight junctional complexes in vessels of CNS grafts fixed by perfusion of the host; (2) damage to host vessels and BBB during the intracerebral grafting procedure; (3) graft placement in proximity to inherently permeable vessels (e.g., CNS sites lying outside the BBB) supplying the subarachnoid space/pial surface and circumventricular organs such as the median eminence, area postrema, and choroid plexus; and (4) graft rejection associated with antigen presenting cells and the host immune response. The latter is prevalent in xenogeneic grafts and exists in allogeneic grafts with donor-host mismatch in the major and/or minor histocompatibility complex. CNS grafts between non-immunosuppressed outbred donor and host rats of the same strain (e.g., Sprague Dawley or Wistar rats) can be rejected by the host; these grafts exhibit populations of immuonohistochemically identifiable major histopatibility complex class I+ and class II+ cells (microglia, macrophages, etc.) and CD4+ T-helper and CD8+ T-cytotoxic lymphocytes. PC12 cell suspension grafts placed within the CNS of non-immunosuppressed Sprague Dawley rats are rejected similarly. Donor cells from solid CNS grafts placed intracerebrally and stained immunohistochemically for donor major histocompatibility complex (MHC) class I expression are identified within the host spleen and lymph nodes; these donor MHC expressing cells may initiate the host immune response subsequent to the cells entering the general circulation through host cerebral vessels damaged during graft placement. Rapid healing of damaged cerebral vessels is stimulated with exogenously applied basic fibroblast growth factor, which may prove helpful in reducing the potential entry of donor cells to the host circulation. These results have implication clinically for the intracerebral grafting of human fetal CNS cell suspensions. © 1994 Wiley-Liss, Inc.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070270603
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  • 3
    Electronic Resource
    Electronic Resource
    A method for determining dislocation Burgers' vectors in ice (1986)
    New York, NY : Wiley-Blackwell
    Journal of Electron Microscopy Technique 3 (1986), S. 357-358 
    Details
    ISSN: 0741-0581
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: It is shown that the usual method of Burgers' vector analysis in the Transmission Electron Microscope (TEM) using invisibility criteria is unlikely to succeed for ice. A method is outlined using a novel application of computer-simulated imaging which can be used to perform such an analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1060030308
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  • 4
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    Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-08
    Description: TRAIL (also called Apo2L) belongs to the tumor necrosis factor family, activates rapid apoptosis in tumor cells, and binds to the death-signaling receptor DR4. Two additional TRAIL receptors were identified. The receptor designated death receptor 5 (DR5) contained a cytoplasmic death domain and induced apoptosis much like DR4. The receptor designated decoy receptor 1 (DcR1) displayed properties of a glycophospholipid-anchored cell surface protein. DcR1 acted as a decoy receptor that inhibited TRAIL signaling. Thus, a cell surface mechanism exists for the regulation of cellular responsiveness to pro-apoptotic stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheridan, J P -- Marsters, S A -- Pitti, R M -- Gurney, A -- Skubatch, M -- Baldwin, D -- Ramakrishnan, L -- Gray, C L -- Baker, K -- Wood, W I -- Goddard, A D -- Godowski, P -- Ashkenazi, A -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):818-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, South San Francisco, CA 94080-4918, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9242611" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Apoptosis ; Apoptosis Regulatory Proteins ; Cell Membrane/metabolism ; Cells, Cultured ; GPI-Linked Proteins ; Glycosylphosphatidylinositols/metabolism ; HeLa Cells ; Humans ; Ligands ; Membrane Glycoproteins/*metabolism ; Molecular Sequence Data ; NF-kappa B/metabolism ; Receptors, TNF-Related Apoptosis-Inducing Ligand ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*metabolism ; Signal Transduction ; TNF-Related Apoptosis-Inducing Ligand ; Transfection ; Tumor Cells, Cultured ; Tumor Necrosis Factor Decoy Receptors ; Tumor Necrosis Factor-alpha/*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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  • 5
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    Mapping of DNA instability at the fragile X to a trinucleotide repeat sequence p(CCG)n (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: The sequence of a Pst I restriction fragment was determined that demonstrate instability in fragile X syndrome pedigrees. The region of instability was localized to a trinucleotide repeat p(CCG)n. The sequence flanking this repeat were identical in normal and affected individuals. The breakpoints in two somatic cell hybrids constructed to break at the fragile site also mapped to this repeat sequence. The repeat exhibits instability both when cloned in a nonhomologous host and after amplification by the polymerase chain reaction. These results suggest variation in the trinucleotide repeat copy number as the molecular basis for the instability and possibly the fragile site. This would account for the observed properties of this region in vivo and in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kremer, E J -- Pritchard, M -- Lynch, M -- Yu, S -- Holman, K -- Baker, E -- Warren, S T -- Schlessinger, D -- Sutherland, G R -- Richards, R I -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1711-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cytogenetics and Molecular Genetics, Adelaide Children's Hospital, South Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1675488" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosome Mapping ; Fragile X Syndrome/*genetics ; Humans ; Molecular Sequence Data ; Pedigree ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; Restriction Mapping ; X Chromosome/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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    A multifunctional aqueous channel formed by CFTR (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-27
    Description: The cystic fibrosis gene product (CFTR) is a complex protein that functions as an adenosine 3,5-monophosphate (cAMP)-stimulated ion channel and possibly as a regulator of intracellular processes. In order to determine whether the CFTR molecule contains a functional aqueous pathway, anion, water, and urea transport were measured in Xenopus oocytes expressing CFTR. Cyclic AMP agonists induced a Cl- conductance of 94 microsiemens and an increase in water permeability of 4 x 10(-4) centimeter per second that was inhibited by a Cl- channel blocker and was dependent on anion composition. CFTR has a calculated single channel water conductance of 9 x 10(-13) cubic centimeter per second, suggesting a pore-like aqueous pathway. Oocytes expressing CFTR also showed cAMP-stimulated transport of urea but not the larger solute sucrose. Thus CFTR contains a cAMP-stimulated aqueous pore that can transport anions, water, and small solutes. The results also provide functional evidence for water movement through an ion channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasegawa, H -- Skach, W -- Baker, O -- Calayag, M C -- Lingappa, V -- Verkman, A S -- DK35124/DK/NIDDK NIH HHS/ -- DK43840/DK/NIDDK NIH HHS/ -- HL42368/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Nov 27;258(5087):1477-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143-0532.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Transport/physiology ; Chlorides/metabolism ; Cyclic AMP/physiology ; Cystic Fibrosis Transmembrane Conductance Regulator ; Female ; Humans ; In Vitro Techniques ; Ion Channels/*physiology ; Membrane Proteins/*physiology ; Molecular Sequence Data ; Oocytes ; Urea/metabolism ; Water/metabolism ; Xenopus
    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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    Spacing differentiation in the developing Drosophila eye: a fibrinogen-related lateral inhibitor encoded by scabrous (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-07
    Description: In the development of multicellular organisms a diversity of cell types differentiate at specific positions. Spacing patterns, in which an array of two or more cell types forms from a uniform field of cells, are a common feature of development. Identical precursor cells may adopt different fates because of competition and inhibition between them. Such a pattern in the developing Drosophila eye is the evenly spaced array of R8 cells, around which other cell types are subsequently recruited. Genetic studies suggest that the scabrous mutation disrupts a signal produced by R8 cells that inhibits other cells from also becoming R8 cells. The scabrous locus was cloned, and it appears to encode a secreted protein partly related to the beta and gamma chains of fibrinogen. It is proposed that the sca locus encodes a lateral inhibitor of R8 differentiation. The roles of the Drosophila EGF-receptor homologue (DER) and Notch genes in this process were also investigated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baker, N E -- Mlodzik, M -- Rubin, G M -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1370-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2175046" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Cell Differentiation ; DNA Transposable Elements ; Drosophila/anatomy & histology/*genetics/growth & development ; *Drosophila Proteins ; Eye/anatomy & histology/growth & development ; Fibrinogen/*genetics ; *Glycoproteins ; Humans ; Molecular Sequence Data ; Mosaicism ; *Mutation ; Phenotype ; Proteins/*genetics ; Receptor, Epidermal Growth Factor/genetics ; Sequence Homology, Nucleic Acid
    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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  • 8
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    K+ current diversity is produced by an extended gene family conserved in Drosophila and mouse (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-04
    Description: The Drosophila Shaker gene on the X chromosome has three sister genes, Shal, Shab, and Shaw, which map to the second and third chromosomes. This extended gene family encodes voltage-gated potassium channels with widely varying kinetics (rate of macroscopic current activation and inactivation) and voltage sensitivity of steady-state inactivation. The differences in the currents of the various gene products are greater than the differences produced by alternative splicing of the Shaker gene. In Drosophila, the transient (A current) subtype of the potassium channel (Shaker and Shal) and the delayed-rectifier subtype (Shab and Shaw) are encoded by homologous genes, and there is more than one gene for each subtype of channel. Homologs of Shaker, Shal, Shab, and Shaw are present in mammals; each Drosophila potassium-channel gene may be represented as a multigene subfamily in mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wei, A -- Covarrubias, M -- Butler, A -- Baker, K -- Pak, M -- Salkoff, L -- 1 RO1-NS24785-01/NS/NINDS NIH HHS/ -- GMO 7200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 May 4;248(4955):599-603.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2333511" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Chromosome Mapping ; Drosophila/*genetics ; Drosophila Proteins ; Female ; Membrane Proteins/*genetics/physiology ; Mice/*genetics ; Molecular Sequence Data ; *Multigene Family ; Oocytes/physiology ; Potassium Channels/*physiology ; Sequence Homology, Nucleic Acid ; Shab Potassium Channels ; Transcription, Genetic ; *X Chromosome ; Xenopus
    Print ISSN: 0036-8075
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  • 9
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    Evolutionary history of Salmonella typhi (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-11-25
    Description: For microbial pathogens, phylogeographic differentiation seems to be relatively common. However, the neutral population structure of Salmonella enterica serovar Typhi reflects the continued existence of ubiquitous haplotypes over millennia. In contrast, clinical use of fluoroquinolones has yielded at least 15 independent gyrA mutations within a decade and stimulated clonal expansion of haplotype H58 in Asia and Africa. Yet, antibiotic-sensitive strains and haplotypes other than H58 still persist despite selection for antibiotic resistance. Neutral evolution in Typhi appears to reflect the asymptomatic carrier state, and adaptive evolution depends on the rapid transmission of phenotypic changes through acute infections.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652035/" 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/PMC2652035/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roumagnac, Philippe -- Weill, Francois-Xavier -- Dolecek, Christiane -- Baker, Stephen -- Brisse, Sylvain -- Chinh, Nguyen Tran -- Le, Thi Anh Hong -- Acosta, Camilo J -- Farrar, Jeremy -- Dougan, Gordon -- Achtman, Mark -- 076962/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1301-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Infektionsbiologie, Department of Molecular Biology, Chariteplatz 1, 10117 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124322" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Africa ; Alleles ; Anti-Bacterial Agents/pharmacology/therapeutic use ; Asia ; *Biological Evolution ; Carrier State/*microbiology ; DNA Gyrase/genetics ; Drug Resistance, Bacterial ; Drug Resistance, Multiple, Bacterial ; Fluoroquinolones/pharmacology/therapeutic use ; *Genes, Bacterial ; Genetic Variation ; Haplotypes ; Humans ; Molecular Sequence Data ; Mutation ; Polymorphism, Genetic ; Polymorphism, Single Nucleotide ; Salmonella typhi/drug effects/*genetics ; Selection, Genetic ; Typhoid Fever/drug therapy/*microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 10
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    Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure (2007)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2007-12-08
    Description: Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-beta domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, Hae Joo -- Coulibaly, Fasseli -- Clow, Fiona -- Proft, Thomas -- Baker, Edward N -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1625-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland 1010, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063798" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Asparagine/chemistry ; Chemistry, Physical ; Crystallography, X-Ray ; Fimbriae Proteins/*chemistry ; Fimbriae, Bacterial/*chemistry/ultrastructure ; Hydrogen Bonding ; Lysine/chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Streptococcus pyogenes/*chemistry/metabolism/*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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