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  • Chemistry  (3)
  • *Gene Expression Regulation, Neoplastic  (1)
  • I.V. glucose tolerance test (IVGTT); familial Mediterranean fever  (1)
  • Keratinocytes/metabolism  (1)
  • nitric oxide
  • 1995-1999  (5)
  • 1925-1929
  • 1900-1904
  • 1997  (5)
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  • 1995-1999  (5)
  • 1925-1929
  • 1900-1904
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  • 1
    Publication Date: 1997-05-02
    Description: Mutations in the tumor suppressor gene PATCHED (PTC) are found in human patients with the basal cell nevus syndrome, a disease causing developmental defects and tumors, including basal cell carcinomas. Gene regulatory relationships defined in the fruit fly Drosophila suggest that overproduction of Sonic hedgehog (SHH), the ligand for PTC, will mimic loss of ptc function. It is shown here that transgenic mice overexpressing SHH in the skin develop many features of basal cell nevus syndrome, demonstrating that SHH is sufficient to induce basal cell carcinomas in mice. These data suggest that SHH may have a role in human tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oro, A E -- Higgins, K M -- Hu, Z -- Bonifas, J M -- Epstein, E H Jr -- Scott, M P -- AR39959/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 2;276(5313):817-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Dermatology, Stanford University School of Medicine, Stanford, CA 94305-5427, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9115210" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Basal Cell Nevus Syndrome/*genetics/metabolism/pathology ; Carcinoma, Basal Cell/*genetics/metabolism/pathology ; Embryo, Mammalian ; *Gene Expression Regulation, Neoplastic ; Hedgehog Proteins ; Humans ; Intracellular Signaling Peptides and Proteins ; Keratinocytes/metabolism ; Male ; Membrane Proteins/genetics/metabolism ; Mice ; Mice, SCID ; Mice, Transgenic ; Mutation ; Neoplasm Transplantation ; Protein Biosynthesis ; Proteins/*genetics/metabolism ; Receptors, Cell Surface ; Skin/pathology ; Skin Neoplasms/*genetics/metabolism/pathology ; Skin Transplantation ; *Trans-Activators
    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
    ISSN: 1432-1041
    Keywords: Key words Colchicine ; I.V. glucose tolerance test (IVGTT); familial Mediterranean fever ; oral glucose tolerance test (OGTT)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Abstract Objective: To investigate a long-term colchicine treatment in inhibiting normal release of insulin, in response to a glucose load. Setting: The Heller Institute of Medical Research, Sheba Medical Center, Tel-Hashomer. Patients: Thirty-one familial Mediterranean fever (FMF) patients, treated continuously with colchicine (1.0–2.0 mg · day–1) for 2–13 years. Methods: A standard oral glucose tolerance test (OGTT) was performed to study the effect of long-term colchicine treatment on glucose-induced insulin response. An intravenous glucose tolerance test (IVGTT) was then performed on randomly chosen FMF patients (n = 9) and age-matched controls (n = 5). Glucose was administered 30 min after intravenous colchicine (2 mg) infusion. The sum of 1st- and 3rd-min insulin levels served as an index of early-phase insulin release. Results: Based on the Office Guide to Diagnosis of Glucose Intolerance [13], one subject exhibited impaired glucose tolerance and two others had abnormal dynamics of glucose during the test but normal values at 120 min. Insulin values were normal in all participants. No significant differences were found in maximal glucose and insulin concentration, nor in the insulin release index between FMF colchicine-treated and healthy controls. Conclusions: Based on these findings, no impairment in glucose dynamics could be demonstrated in chronically colchicine treated patients, compared to untreated controls.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0935-9648
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0947-6539
    Keywords: electron transfer ; magnetic properties ; metalloporphryins ; polymers ; spin density ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: [MnIIITtBuPP]+[C4(CN)6].- · 5PhMe [MnIIITtBuPP = meso-tetrakis-(4′-tert-butylphenyl)porphinatomanganese(III)] has been prepared and structurally and magnetically characterized. The uniform, linear-chain (1-D) coordination polymer comprises alternating cations and anions. The bond lengths in planar ion [C4(CN)6].-]'- are 1.377(10) (CC-CC), 1.418(7) (C-CCC), 1.414 (C-CN), 1.457 (C-CNMn), 1.150 (C≡N), and 1.134 Å (C = NMn). The Mn-N-C angle is 172.3(4)°, and the intrachain Mn  -  Mn separation is 10.685 Å. Each [C4(CN)6].-]' unit is bonded to two MnIII atoms through the interior nitrogen atoms in a trans-μ2-N-σ manner with N-Mn bond lengths of 2.353 Å. The ṽCN absorptions are at 2217 (w, br) and 2190 (m) cm-1. Above 50 K the magnetic susceptibility of [MnIIITtBuPP]+[C4(CN)6].- can be fitted to the Curie-Weiss expression, χ∝1(T - θ), with an effective θ of -13 K. This is consistent with weak antiferromagnetic coupling, which is in contrast to the effective θ of +67 K for the uniform chain [MnIIIOEP]+[C4(CN)6].- [OEP = octaethylporphinato]. Here, the [C4(CN)6].-'- units are bonded to the MnIII centers through endo CN nitrogen atoms in a similar trans-μ2 manner. Density functional theory MO calculations reveal that the spin density of the CN nitrogen atom bound to [MnIIITtBuPP]+ (0.019 μBÅ-3) is significantly lower than that of the N atom bound to [MnIIIOEP]+ (0.102 μBÅ-3). This is consistent with the reduced spin coupling observed for [MnIIITtBuPP]+[C4(CN)6].-with respect to [MnIIITtBuPP]+[C4(CN)6].-, as evidenced by the lower θ value. The different orientations of the [C4(CN)6].- units - almost perpendicular (84.72°) for [MnIIITtBuPP]+[C4(CN)6].- and substantially tilted (32.1°) for [MnIIIOEP]+ [C4(CN)6].- may also contribute to the poorer overlap and weaker spin coupling. Hence, binding between sites with large spin densities is needed to stabilize strong ferromagnetic coupling.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0173-0835
    Keywords: Cervical carcinoma ; Two-dimensional polyacrylamide gel electrophoresis ; Mass spectrometry ; Immobilized pH gradient ; Cytokine ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two-dimensional (2-D) polyacrylamide gel electrophoresis combined with mass spectrometry is a powerful combination of technologies that allows high resolution separation of proteins and their rapid identification. Immobilized pH gradient (IPG) first-dimensional gels have several advantages over carrier ampholyte isoelectric focusing, including a high degree of reproducibility, good protein spot resolution, and a selection of pH range. Here we demonstrate the utility and efficacy of combining IPG 2-D gel electrophoresis with mass spectrometry to identify interferon-γ- (IFN) and tumor necrosis factor (TNF)-regulated proteins in ME-180 cervical carcinoma cells. Three cytokine-regulated proteins have been identified, using imidazole-zinc-stained preparative IPG 2-D gels and in-gel tryptic digestion followed by matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry for determination of peptide masses and sequences: (1) triosephosphate isomerase, a glycolytic pathway enzyme, (2) proteasome subunit C3, which is important in protein degradation, and (3) Ran, a GTP-binding protein important in cell cycle regulation, protein import into the nucleus, and RNA export from the nucleus.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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