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  • Articles  (630)
  • Humans  (586)
  • Analytical Chemistry and Spectroscopy
  • General Chemistry
  • Theoretical, Physical and Computational Chemistry
  • 1995-1999  (630)
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  • Articles  (630)
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  • 1995-1999  (630)
  • 1945-1949
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  • 1
    Electronic Resource
    Electronic Resource
    Perception of shape from shading in chimpanzees (Pan troglodytes) and humans (Homo sapiens) (1998)
    Springer
    Animal cognition 1 (1998), S. 25-35 
    Details
    ISSN: 1435-9456
    Keywords: Key words Shape from shading ; Visual search ; Texture segregation ; Chimpanzees ; Humans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The perception of shape from shading was tested in two chimpanzees (Pan troglodytes) and five humans (Homo sapiens), using visual search tasks. Subjects were required to select and touch an odd item (target) from among uniform distractors. Humans found the target faster when shading was vertical than when it was horizontal, consistent with results of previous research. Both chimpanzees showed the opposite pattern: they found the target faster when shading was horizontal. The same difference in response was found in texture segregation tasks. This difference between the species could not be explained by head rotation or head shift parallel to the surface of the monitor. Furthermore, when the shaded shape was changed from a circle to a square, or the shading type was changed from gradual to stepwise, the difference in performance between vertical and horizontal shading disappeared in chimpanzees, but persisted in humans. These results suggest that chimpanzees process shading information in a different way from humans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100710050004
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  • 2
    Electronic Resource
    Electronic Resource
    The binding of biotin analogues by streptavidin: A Raman spectroscopic study (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 197-208 
    Details
    ISSN: 1075-4261
    Keywords: Raman spectroscopy ; protein-ligand interactions ; streptavidin complexes ; biotin analogues ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Raman spectra of anhydrous complexes of streptavidin (Strep) with biotin (Bio) and some Bio analogues [Biotin methyl ester (MEBio), desthiobiotin (DEBio), 2′-iminobiotin (IMBio), and diaminobiotin (DABio)] were recorded. The vibrational results indicate that the interaction with some of these ligands is able to modify the overall structure of the protein and this binding results in a decrease in the βsheet content and an increase in the α-helix content. To further confirm the conformational changes of the protein structure due to Bio analogue binding, the curve-fitting analysis of the amide I Raman band of neat Strep and of the complexes were performed. The intensity ratio of the components due to the β-sheet and α-helix conformations decreased in the Strep-MEBio, Strep-IMBio (pH 11), and Strep-Bio systems, whereas in all the other systems the changes were not significant. This behavior differs from that of Avi bound to the same ligands and suggests that Strep and Avi differ in their binding selectivity. A good correlation was found between the secondary structure percentages of the Avi and of the Strep complexes and ΔG°. On the basis of this linear relationship, the vibrational results allow for an acceptable evaluation of the dissociation constants of the Strep complexes, not previously reported in the literature. The present results indicate a correlation between the type of interaction and the effects of the protein-substrate bonding on the overall structure of the proteins. The amino acid residues in the binding site appear to be positioned in a such a way as to provide a precise fit of Bio. Even slight change in the substrate structure causes a weakness in the strength of the binding. The vibrational results confirm that both the imidazolidinone and the thiophan rings are important in the Strep-Bio interactions, but the former is more responsible for the high affinity of the binding. One of the Tyr residues is hydrogen bound with the ureido ring and another Tyr could be involved in the binding pocket. Trp residues do not directly bind the ligand and probably stabilize other binding site residues which in turn interact directly with Bio. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 197-208, 1998
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  • 3
    Electronic Resource
    Electronic Resource
    Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 209-216 
    Details
    ISSN: 1075-4261
    Keywords: high pressure ; FTIR spectroscopy ; bovine pancreatic trypsin inhibitor ; hydrogen-deuterium exchange ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Fourier transform infrared (FTIR) spectroscopy combined with resolution enhancement techniques, second-derivative and difference spectroscopies, have been used to characterize pressure-induced changes in the structural rearrangements of bovine pancreatic trypsin inhibitor (BPTI) in D2O solution at 25.0°C. According to the observed changes in the amide I′ band up to 550 MPa, the secondary structure elements of BPTI, such as the α-helix, 310-helix, β-sheet, and β-turn, are scarcely rearranged except for the loop structure of residues of 9-17 and 36-43. The polypeptide backbone is not extensively unfolded up to 550 MPa. The minor pressure-induced structural rearrangements are completely reversible. A further increase in pressure above 1000 MPa associated with the precipitation of BPTI in D2O buffer solution induces the partial structural rearrangements of the α-helix, β-turn and/or 310-helix, and β-sheet. The polypeptide backbone of BPTI is not fully unfolded even above 1000 MPa. Most of the protected backbone amide protons involved in the β-sheet remain intact in the pressure range where BPTI is not precipitated, while those involved in the α-helix and β-turn and/or 310-helix are exchanged with solvent deuterons. The protected backbone amide protons located near the surface regions are more easily exchanged with solvent deuterons by application of high pressure than those involved in the core. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 209-216, 1998
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  • 4
    Electronic Resource
    Electronic Resource
    Vibrational study of phosphate modes in GDP and GTP and their interaction with magnesium in aqueous solution (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 219-227 
    Details
    ISSN: 1075-4261
    Keywords: guanosine 5′-diphosphate ; guanosine 5′-triphosphate ; magnesium ; vibrational spectroscopy ; Raman spectroscopy ; FTIR ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Raman and infrared spectra were examined for guanosine 5′-diphosphate (GDP) and guanosine 5′-triphosphate (GTP) in aqueous solution. The vibrational modes were assigned on the basis of isotopic frequency shifts and relative intensities in the Raman and infrared spectra. The observed frequency shifts on 18O isotope labeling made it possible to identify the bands from each phosphate group (α, β, γ). Frequency shifts were observed as Mg2+ complexes with GDP and GTP. The results suggested that Mg2+ binds to GDP in a bidentate manner to the α, β P · · O bonds and in a tridentate manner to the α, β and γ P · · O bonds of Mg·GTP. The results indicate that structure of Mg2+ coordinated to GTP in aqueous solution differs somewhat to that found for Mg·ATP. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 219-227, 1998
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  • 5
    Electronic Resource
    Electronic Resource
    Two-dimensional mid-IR and near-IR correlation spectra of ribonuclease A: Using overtones and combination modes to monitor changes in secondary structure (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S19 
    Details
    ISSN: 1075-4261
    Keywords: near-IR ; protein folding ; denaturation ; ribonuclease A ; overtone and combination bands ; 2-dimensional correlation analysis ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: We introduce near-IR spectroscopy as an ancillary tool for monitoring structural changes of proteins in aqueous solution using ribonuclease A (RNase A) as a model protein. The thermal unfolding of RNase A results in clear spectral changes in the near-IR and the mid-IR regions. In the near-IR the most pronounced changes are observed in the spectral region between 4820 and 4940 cm-1. The strong N—H combination band found at 4867 cm-1 in the spectrum of native RNase A shifts to 4878 cm-1 upon thermal unfolding. Hydrogen-deuterium exchange experiments that validate the N—H character of this mode can also be used to estimate the number of unexchanged amide protons after exposure to D2O. The transition profiles and temperatures derived from the temperature dependence of the N—H combination mode were found to be practically identical with those derived from the temperature dependence of the C=O amide I band in the mid-IR region, demonstrating that the near-IR region can be used as a conformation-sensitive monitor for the thermally induced unfolding of proteins in H2O solution. A 2-dimensional correlation analysis was applied to the mid-IR and near-IR spectra of RNase A to establish correlations between IR bands in both regions. The correlation analysis demonstrates that the thermal unfolding of RNase A is not a completely cooperative process; rather it begins with some changes in β-sheet structure, followed by the loss of α-helical structures, and then ending with the unfolding of the remaining β-sheets. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S19-S29, 1998
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  • 6
    Electronic Resource
    Electronic Resource
    13C- and 57Fe-NMR studies of the Fe—C—O unit of heme proteins and synthetic model compounds in solution: Comparison with IR vibrational frequencies and X-ray structural data (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S57 
    Details
    ISSN: 1075-4261
    Keywords: 13C-NMR ; 57Fe-NMR ; ν(C—O) stretching vibration ; ν(Fe—C) stretching vibration ; heme proteins ; heme models ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: 13C- and 57Fe-NMR spectra of several carbon monoxide hemoprotein models with varying polar and steric effects of the distal organic superstructure, constraints of the proximal side, and solvent polarity are reported. The 13C shieldings of heme models cover a 4.0 ppm range that is extended to 7.0 ppm when several hemoglobin CO and myoglobin CO species at different pHs are included. Both heme models and heme proteins obey a similar excellent linear δ(13C) versus ν(C—O) relationship that is primarily due to modulation of π backbonding from Fe dπ to the CO π* orbital by the distal pocket polar interactions. There is no direct correlation between δ(13C) and Fe—C—O geometry. The poor monotonic relation between δ(13C) and ν(Fe—C) indicates that the iron-carbon π bonding is not a primary factor influencing δ(13C) and δ(57Fe). The δ(57Fe) was found to be extremely sensitive to deformation of the porphyrin geometry, and increased shielding by more than 600 ppm with increased ruffling was observed for various heme models of known X-ray structures. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S57-S69, 1998
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  • 7
    Electronic Resource
    Electronic Resource
    Conformation and interactions of the packaged double-stranded DNA genome of bacteriophage T7 (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S47 
    Details
    ISSN: 1075-4261
    Keywords: nucleic acid ; conformation ; Raman spectroscopy ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The structure of the packaged double-stranded DNA genome of bacteriophage T7 was compared to that of unpackaged T7 DNA using digital difference Raman spectroscopy. Spectral data were obtained at 25°C from native T7 virus (100 mg/mL), empty T7 capsids (50 mg/mL), and purified T7 DNA (40 mg/mL) in buffer containing 200 mM NaCl, 10 mM MgCl2, and 10 mM Tris at pH 7.5. At these conditions, the local conformation of T7 DNA was not affected by packaging. Specifically, the local B-form secondary structure of unpackaged T7 DNA, including furanose C2′-endo pucker, anti glycosyl torsion, Watson-Crick base pairing, and base stacking, were essentially fully (〉98%) retained when the genome was condensed within the viral capsid. However, the average electrostatic environment of T7 DNA phosphates was altered dramatically by packaging as revealed by large perturbations in the Raman bands associated with localized vibrations of the DNA phosphate groups. The change in the phosphate environment was attributed to Mg2+ ions that were packaged with the genomic DNA, and the observed Raman perturbations of genomic DNA were equivalent to those generated by a 50-100-fold increase in Mg2+ concentration in aqueous phosphodiester model compounds. The T7 data were qualitatively and quantitatively similar to those observed previously for packaged DNA of bacteriophage P22 and imply that genomic DNAs of T7 and P22 are both organized in a similar fashion within their respective capsids. The results show that the condensed genome does not contain kinks or folds that would disrupt the local B conformation by more than 2%. The present findings are discussed in relation to previously proposed models for condensation and organization of double-stranded and single-stranded viral DNA. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S47-S56, 1998
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of soybean seed coat peroxidase: Resonance Raman evidence for a structure-based classification of plant peroxidases (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 355-364 
    Details
    ISSN: 1075-4261
    Keywords: peroxidases ; quantum-mixed spin ; fluoride and hydroxyl complexes ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Electronic absorption and resonance Raman spectra of ferric and ferrous forms of a peroxidase from soybean seed coat (SBP) at neutral and alkaline pH values together with the spectra of the ferric-fluoride complex are reported. At neutral pH a quantum mechanically mixed spin state, resulting from the admixture of intermediate spin, S = 3/2, and high spin, S = 5/2, configurations, has been identified which coexists with five- and six-coordinate high-spin hemes. A complete conversion to a fluoride-ligated six-coordinate high-spin and a hydroxy-ligated six-coordinate low-spin heme are observed at acid pH in the presence of fluoride and at alkaline pH, respectively. The spectral features suggest that both the fluoride and hydroxo ligands are stabilized by hydrogen-bond interactions with the distal Arg residue and through a water molecule with the distal His residue. The ferrous form shows a single ν(Fe - Im) at 246 cm-1 at neutral pH. The data indicate that SBP shares many characteristics with peroxidases belonging to class III of the “plant peroxidase” superfamily. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 355-364, 1998
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  • 9
    Electronic Resource
    Electronic Resource
    Resonance Raman spectroscopic study of the caa3 oxidase from Thermus thermophilus (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 365-377 
    Details
    ISSN: 1075-4261
    Keywords: resonance Raman ; Thermus thermophilus ; oxidase ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The terminal caa3 oxidase of Thermus thermophilus has been studied by resonance Raman spectroscopy. Using different excitation wavelengths in the Soret band region, it was possible to disentangle the resonance Raman spectra of the fully oxidized and fully reduced state in terms of the component spectra of the individual hemes a, a3, and c. For the heme a and a3 groups, the spectra reveal only minor differences compared to those of beef heart cytochrome c oxidase attributable to subtle modifications of the heme environment. These differences are not more pronounced than those between the oxidases from beef heart and Paracoccus denitrificans confirming the view that this oxidase of Th. thermophilus is a typical member of the aa3 oxidase superfamily. The heme c component spectra display far-reaching similarities with those of c-type cytochromes which serve as mobile electron carriers in the respiratory chain. These results imply that caa3 oxidase represents an integrated version of the noncovalent redox complex between cytochrome c and cytochrome c oxidase in higher organisms. On the other hand, the structural changes of cytochrome c in the noncovalent complex have no counterpart in the heme c component of the caa3 oxidase indicating a specific cytochrome c binding site for the mitochondrial enzyme. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 365-377, 1998
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  • 10
    Electronic Resource
    Electronic Resource
    Applications of Raman spectroscopy to ophthalmology: Spectroscopic characterization of disposable soft contact lenses (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 413-419 
    Details
    ISSN: 1075-4261
    Keywords: disposable soft contact lenses ; biocompatibility ; Raman spectroscopy ; hydrogels ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Disposable soft contact lenses based on HEMA-MAA hydrogels are examined using Raman and ATR/FTIR vibrational spectroscopies and thermal analysis. The main factors dealing with physical, chemical, and biological biocompatibility are evaluated in relation to those of long-wear soft contact lenses with the aim of individuating the most biocompatible lens. The Raman spectra of HEMA-MAA lenses show that some biocompatibility factors are affected by environmental conditions and, in particular, by changes in pH and ionic strength values. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 413-419, 1998
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  • 11
    Electronic Resource
    Electronic Resource
    Chemiluminescence accompanying oxidation of bopindolol (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 229-233 
    Details
    ISSN: 1075-4261
    Keywords: bopindolol ; luminescence ; oxygen radicals ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The oxidation of bopindolol using the Co-ethylenediaminetetraacetic acid (EDTA) + H2O2 system was investigated by spectrophotometric, chemiluminescence, and fluorescence methods. The effects of oxygen free radicals scavengers and 1O2 quenchers on the light emission were measured. The obtained results show the electronically excited products of the bopindolol degradation are involved in the oxidation process. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 229-233, 1998
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  • 12
    Electronic Resource
    Electronic Resource
    Insight into externally bound 5,10,15,20-tetrakis(2-N-methylpyridyl)porphyrinatopalladium(II), PdP(2), with B-form DNA duplexes poly(G-C)2, poly(A-T)2, and CT DNA by using combined MCD, CD, and optical data (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 341-352 
    Details
    ISSN: 1075-4261
    Keywords: metalloporphyrin ; nucleic acid ; outside binding ; CD ; MCD ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The Soret (B0) region of free and externally DNA-bound 5,10,15,20-tetrakis(2-N-methylpyridyl)porphyrinatopalladium(II), PdP(2), was investigated by electronic magnetic circular dichroism (MCD), natural circular dichroism (CD), and optical (UV-visible) absorption spectroscopies. We conclude that four-coordinate, “thick” PdP(2) binds to the exterior of each of poly(A-T)2 and calf thymus DNA (CT DNA) by two distinctly different AT-specific minor and major groove modes, with site 5′TA3′ being favored for both modes. The minor groove mode involves an edge-on orientation of PdP(2), for which porphyrin electric dipole transition moments (edtms) μx (most perturbed direction of the bound porphyrin) and μy (least perturbed direction) have approximate orientation angles of α/β/β′ = ∼ 90°/0°/0° and ∼ 45°/0°/90°, respectively. Major groove binding is by a face-on mode, which results in the porphyrin plane being approximately parallel to the helix axis, such that νx (most perturbed direction) and μy (least perturbed direction) have approximate orientation angles of α/β/β′ = ∼ 45°/180°/90° and ∼ 45°/180°/270°, respectively. The Soret MCD and optical band alterations upon binding (i.e., sign retention of the tetragonal, genuine MCD (+) A-term on becoming the (+) pseudo-A-term of similar amplitude and small DNA-induced optical red (Δλ) and hypochromic (H) shifts) are all consistent with exterior binding perturbations of the porphyrin's pπ MOs (1a1u3a2u 4eg) by the A and T bases of each polymer being weaker than caused by intercalation. Furthermore, that the (+) A-term of PdP(2) retains the (+) sign upon binding informs that the 4eg splitting, or ΔLUMO, is less than the energy separation |1a1u-3a2u|, or ΔHOMO. For the third system, PdP(2)/poly(G-C)2, the B0 CD spectrum has two extremely weak (+) and (-) CD bands at higher and lower energy, respectively, indicating that weak outside binding (wob) interactions are taking place between the cationic porphyrin and the electron-rich phosphate backbone of this rigid polymer. The composite of our CD, MCD, and optical data are suggestive of a face-on mode at the GC major groove. Band parameter extraction is performed on the Soret CD and MCD bands of each of the three bound systems, and it is determined that (1) very little spatial rotation of molecular charge is induced during CD excitation and (2) the excited state angular momentum, 〈Lj〉, changes very little upon binding of PdP(2) to each duplex. These findings are also consistent with each PdP(2)/B-DNA interaction not being very strong. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 341-352, 1998
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  • 13
    Electronic Resource
    Electronic Resource
    Fluorescent properties of amino acids labeled with ortho-aminobenzoic acid (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 395-402 
    Details
    ISSN: 1075-4261
    Keywords: ortho-aminobenzoylamino acids ; fluorescence ; protease ; peptide ; peptide synthesis ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: ortho-Aminobenzoic acid (Abz) has been used as a convenient fluorescent donor group in internally quenched fluorescent peptides, which are employed as substrates for several proteolytic enzymes. As Abz is usually bound to the N-amino terminal of these peptides, it is of interest to investigate the Abz group fluorescent properties bound to different amino acids. We report in this article the optical absorption and fluorescent properties, in aqueous media, of Abz bound to the α-amino group of Ala, Gly, Leu, Ile, Val, Pro, Phe, Arg, Glu, Met, Asn, Tyr, and Trp, with monomethyl-amidated α-carboxyl group. In order to explore the origin of the drastic reduction of Abz attached to Nα amino group of prolyl-peptides, we also examined the fluorescence properties of Abz-NHCH3, Abz-N(CH3)2, and Abz-pyrrolidine. Molecular dynamics simulation and NMR data indicated a lack of periplanarity of the Abz-dimethylamide, which could be the origin of low fluorescence quantum yield of Abz-prolyl-peptides. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 395-402, 1998
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  • 14
    Electronic Resource
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    Surface structure of human mucin using X-ray photoelectron spectroscopy (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 257-266 
    Details
    ISSN: 1075-4261
    Keywords: X-ray photoelectron spectroscopy ; surface analysis ; MUC1 mucin ; structure ; glycosylation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: X-ray photoelectron spectroscopy (XPS) is a surface sensitive analytical technique that measures the binding energy of electrons in atoms and molecules on the surface of a material. XPS was used to determine the distribution of the oligosaccharide side chains in the glycoprotein, MUC1 mucin. Low-resolution XPS spectra provided elemental composition of MUC1 mucin (fully glycosylated), mucin polypeptide (nonglycosylated), and carbohydrates found in mucin. The nitrogen content of MUC1 mucin was determined to be intermediate between the mucin polypeptide and the carbohydrates. Assuming a uniform distribution of carbohydrate on MUC1 mucin, the average thickness of the carbohydrate layer was calculated to be 4.9 nm using the low-resolution N 1s signals. High-resolution XPS spectra give detailed information about the chemical bonding of the surface molecules. Calculations based on the high-resolution O 1s spectra showed a carbohydrate thickness of 6.6 nm. These experimentally determined values agree reasonably well with an estimated 5 nm of carbohydrate thickness from a simple model which assume that the core protein is a rodlike molecule approximately 5 nm in diameter. Although the carbohydrate coating on the MUC1 mucin appears to be thick enough to cover the core protein entirely, fully glycosylated breast milk MUC1 mucin is susceptible to proteolytic digestion without removal of any oligosaccharide side chain, suggesting areas of exposed core protein. A possible explanation is that the oligosaccharide side chains may form patches of carbohydrate along the core protein with regions of exposed core protein. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 257-266, 1998
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  • 15
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    FTIR characterization of heterocycles lumazine and violapterin in solution: Effects of solvent on anionic forms (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 235-256 
    Details
    ISSN: 1075-4261
    Keywords: pterins ; FTIR ; vibrational analysis ; solvent effects ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Fourier transform infrared (FTIR) spectra have been obtained from solution samples of the heterocycles uracil, lumazine, and violapterin and reveal interpretable carbonyl stretching frequencies. Spectra of conjugate bases of lumazine and violapterin demonstrate decreases in these carbonyl stretching frequencies upon ionization. Based on isotopic shifts from amide deuterated analogs, semiempirical QCFF/PI calculations were used to assign the vibrational frequencies in the region 1100-1800 cm-1 observed from samples in dimethylsulfoxide (DMSO) and aqueous solutions to specific normal modes. The observed deuterium shifts and the calculations suggest that, in some cases, N - H bending motions are coupled to the C=O stretching motions of the pyrimidine ring. These data suggest that for lumazine anions a change in solvent can significantly change the mixing of the N - H bending and C=O stretching vibrational motions. This implies that vibrational analysis for lumazine species in relatively noninteracting media like nonpolar solvents, mulls or pellets cannot necessarily be transferred to the system when it is dissolved in a polar, hydrogen-bonding solvent such as water. Although other explanations can be offered, our vibrational analysis suggests that the changes in normal mode composition of the predominantly C=O stretching vibrations of lumazine anion on going from dimethylsulfoxide to water solution are consistent with a change in the predominant tautomer of the heterocycle. This change appears to correspond to a shifting of the location of the remaining acidic proton to a different ring nitrogen atom. This interpretation is of interest in view of recent ab initio calculations which suggest that proton shifts may occur during the hydroxylation of lumazine as mediated by the enzyme xanthine oxidase. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 235-256, 1998
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  • 16
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    Fourier transform infrared spectroscopy as a probe for the study of the hydration of lipid self-assemblies. II. Water binding versus phase transitions (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 281-294 
    Details
    ISSN: 1075-4261
    Keywords: phosphatidylcholines ; dioleoylphosphatidylethanolamine ; mixed-chain phospholipids ; unsaturation ; hydration ; FTIR spectroscopy ; lyotropic phase transitions ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The gradual hydration of phospholipid films can be effectively probed by Fourier transform infrared (FTIR) spectroscopy (cf. part I of this series). The hydration-induced changes observed for lipid IR-absorption bands are probably composed of contributions arising from the effects of both the direct binding of water molecules and the thereby caused conformational changes and phase transitions in the lipid molecules and assemblies, respectively. In this article, an attempt is made to attribute some of the more indicative spectroscopic results to these molecular and supermolecular processes with a view to separating their individual contributions to the relevant spectroscopic data. This is done by considering a series of suitable PLs consisting of the palmitoyl and oleoyl lecithins, DPPC, DOPC, POPC, and OPPC, and one cephalin, DOPE. This choice of PCs and DOPE means that at room temperature and different degrees of hydration, several phase states including lamellar gel and liquid crystalline as well as certain nonlamellar phases are covered. The separation of the water-binding and phase-transition contributions to the FTIR-spectroscopic data, we believe, is clearly demonstrated by interpreting the hydration-dependent wavenumber shifts of the νC=O band of the PCs. Carbonyl groups are affected to a more significant degree for lipids arrayed in the Lα phase than in the gel phase. A number of spectral features reveal the lyotropically triggered chain-melting transition as well as other structural rearrangements of PCs. This is discussed in detail and demonstrates the excellent sensitivity of the FTIR methodology for the study of such systems. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 281-294, 1998
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    Surface-enhanced Raman scattering and fluorescence spectroscopy reveal molecular interactions of all-trans retinoic acid and RARγ ligand-binding domain (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 297-302 
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    ISSN: 1075-4261
    Keywords: Fourier-transform surface-enhanced Raman scattering ; all-trans retinoic acid ; retinoic acid receptor ; silver colloids ; fluorescence ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Surface-enhanced Raman scattering and fluorescence were used to investigate the interactions of all-trans retinoic acid with the gamma-type retinoic acid receptor. Raman data revealed a significant attenuation in intensity of the bands originating from the retinoic acid polyenic chain upon receptor binding, with the spectrum being dominantly that of the β-ionone ring. Fluorescence measurements supported the hydrophobic character of the ligand binding. These novel spectroscopic results are fully consistent with the published X-ray crystallographic data and suggest that these techniques may be valuable additional tools to characterize the interactions of agonists and antagonists with residues in the ligand-binding pockets of retinoid receptor homo- and heterodimers. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 297-302, 1998
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    Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I from Lucina pectinata (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 311-326 
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    ISSN: 1075-4261
    Keywords: heme vinyl groups ; hemoglobin I ; hydrogen sulfide ; Lucina pectinata ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Hemoglobin I (HbI) from the claim Lucina pectinata is a unique heme protein that binds and transfers hydrogen sulfide (H2S) to a symbiotic bacteria. The metcyano, metaquo, carbon monoxy, oxy, and deoxy complexes of HbI were studied by resonance Raman (RR) spectroscopy, and the metcyano and carbon monoxy complexes were also studied by 1H-NMR. The results indicate a unique orientation of the heme 2-vinyl group relative to other heme proteins. The RR spectra of the HbICO, metHbICN, metHbIH2O, HbIO2 and deoxyHbI heme derivatives show a band at 1621 cm-1 and a shoulder at 1626 cm-1, indicative of an out-of-plane position for one of the vinyls relative to the other one. Spin-lattice relaxation properties of protons in the metHbICN complex also suggest a unique orientation for the heme 2-vinyl group of HbI. The longitudinal relaxation time (T1) for the 2-Hα, 2-Hβc, and Hβt protons are 120 ms, 115 ms, and 135 ms, respectively. The data from both techniques suggest an out-of-plane and trans-oriented 2-vinyl group, and an in-plane and cis-oriented 4-vinyl group for the low-spin complexes of HbI. These results imply that the electron withdrawing character of the out-of-plane vinyl group contributes to the stability of the heme Fe+3 oxidation state, facilitates the binding of the H2S ligand, and promotes the stability of this ferric H2S complex. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 311-326, 1998
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    Understanding heme cavity structure of peroxidases: Comparison of electronic absorption and resonance Raman spectra with crystallographic results (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S3 
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    ISSN: 1075-4261
    Keywords: charge-transfer (CT1) band ; vinyl conjugation ; peroxidases ; heme cavity ; heme ligands ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Electronic absorption and resonance Raman spectra of various peroxidases and selected site-directed mutants are reported. These results and the X-ray crystal structure data are critically analyzed and underline the differences that exist between the crystal and solution states. The effect of the vinyl conjugation on the electronic absorption maxima and the influence of the ligand nature on the wavelength of the charge-transfer (CT1) band are shown to be useful probes of subtle interactions in the heme pocket. The spectroscopic differences observed between the three classes of peroxidases are discussed in terms of their structural diversity. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S3-S17, 1998
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    Molecular dynamics simulations of biomembrane models (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S41 
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    ISSN: 1075-4261
    Keywords: molecular force fields ; molecular dynamics simulations ; biomembranes ; phospholipids ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: A molecular force field dedicated to molecular dynamics simulation of biomembranes was developed. It was parameterized on model compounds related to phospholipids and was able to reproduce at the same time structures, energies, and vibrational spectra. Cross terms in the potential energy function were introduced by solving the redundancy problem among internal coordinates. This force field was used in the 400-ps molecular dynamics simulation of a hydrated bilayer in the gel and liquid crystal phases. The conformational properties of the polar head groups were in particular agreement with the experimental observations using Raman scattering. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S41-S46, 1998
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    Characterization of island films as surface-enhanced Raman spectroscopy substrates for detecting low antitumor drug concentrations at single cell level (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S71 
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    ISSN: 1075-4261
    Keywords: surface-enhanced Raman spectroscopy ; gold and silver island films ; silver colloids ; dimethylcrocetin ; single living cell ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Gold and silver vacuum-deposited island films were characterized by studying deposition variables such as film thickness, evaporation rate, and substrate temperature. For both metals, these parameters were correlated with the surface-enhanced Raman spectroscopy (SERS) effect and an increase in film thickness and low evaporation rates were shown to upshift the wavelength at maximum optical density (λmax) and increase the optical density of the substrates. In contrast, pre- and postdeposition annealing of gold films led to the formation of substrates that exhibited a downshift of λmax. Our spectral data also indicated that silver films are substrates that are more suited for SERS applications where high frequency visible excitations are used. Measurements on gold films classified them into two groups: thin Au films (10-50 Å) well adapted for red excitations and thicker ones that are operative in the near infrared. SERS results, which were obtained from a single HL60 cell treated with micromolar drug quantities, placed on thin gold island films indicated that these island films could be future promising substrates for SERS imaging at the cellular level. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S71-S78, 1998
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    Predictions of protein secondary structures using factor analysis on Fourier transform infrared spectra: Effect of Fourier self-deconvolution of the amide I and amide II bands (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 93-106 
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    ISSN: 1075-4261
    Keywords: protein secondary structure ; FTIR spectroscopy ; Fourier self-deconvolution ; factor analysis ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Fourier self-deconvolution (FSD) was performed on protein amide I and II Fourier transform infrared (FTIR) spectra to test if the resultant increased band shape variation would lead to improvements in protein secondary structure prediction with our factor analysis based restricted multiple regression (RMR) methods. FTIR spectra of 23 proteins dissolved in H2O were measured and normalized to a constant amide I peak absorbance. The deconvolved spectra were renormalized by area so that the deconvolved spectra sets had the same area as before. Principal component analysis of the deconvolved spectra sets was carried out, which was followed by a selective multiple linear regression (RMR) analysis of the principal component loadings with regard to the fractional components (FC) of secondary structure. As compared to analyses based on the original spectra set, helix and sheet predictions were not noticeably improved by FSD; but, if a very large number of component spectra (16) were retained in the pool to select which loadings to be used in the RMR optimization, better predictions of turn and “other” resulted. The prediction quality varied depending on the deconvolution parameters used. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 93-106, 1998
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    Evidence for global mobility in the premelting of a polynucleotide from temperature-dependent Raman optical activity (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 107-111 
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    ISSN: 1075-4261
    Keywords: conformational mobility ; nucleic acid dynamics ; Raman optical activity ; RNA ; temperature dependence ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The backscattered Raman and Raman optical activity (ROA) spectra of poly(rA)-poly(rU) at 20°C and 45°C in buffered aqueous solution between 650 and 1750 cm-1 are reported. Although the intensity of the majority of the Raman bands increase by varying amounts as the temperature is raised in accordance with the well-known hypochromic effect, the reverse effect is found for the ROA signals which we attribute to thermal accessibility of a greater number of distinct conformations leading to cancellation of ROA signals. The difference ROA spectrum obtained by subtracting the spectrum recorded at 45°C from that recorded at 20°C displays a very similar sign pattern to those at both 20°C and 45°C throughout the spectral region examined. This indicates that the same average structure is maintained in this temperature range and that the thermal fluctuations are correlated through the bases, the glycosidic link, the sugar ring, and the phosphate backbone of both strands. These results indicate that ROA may be a useful new probe of the dynamics of nucleic acid in solution. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 107-111, 1998
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    FT-Raman investigation of alkaloids in the liana Ancistrocladus heyneanus (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 113-120 
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    ISSN: 1075-4261
    Keywords: FT-Raman spectroscopy ; micro-Raman technique ; Ancistrocladus heyneanus ; naphthylisoquinoline alkaloids ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The applicability of the micro-FT-Raman technique for studying alkaloids in vitro and for observing alkaloids in plant cells is demonstrated. This technique is examined using fresh plant material of Ancistrocladus heyneanus, a tropical liana known to produce pharmacologically interesting naphthylisoquinoline alkaloids as secondary metabolites. It will be shown that it is possible to localize and identify some of these alkaloids in different parts of the plant by means of Raman microspectroscopic studies. Data on the in situ structure and the spatial distribution can be obtained, which could provide information about the biosynthesis of the alkaloids in the plant. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 113-120, 1998
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    Amphotericin B toxicity as related to the formation of oxidatively modified low-density lipoproteins (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 135-144 
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    ISSN: 1075-4261
    Keywords: amphotericin B ; low-density lipoprotein ; oxidation ; toxicity ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The effect of amphotericin B on the oxidation and degradation of low- and high-density lipoproteins was investigated by UV-vis spectroscopy, electron microscopy, electrophoresis, and size-exclusion chromatography. Two formulations of the drug were used: the commercial Fungizone and a new, less toxic, liposomal formulation, AmBisome. It was shown that Fungizone strongly enhanced the oxidative deformation of low-density lipoprotein structure while AmBisome did not bind to this lipoprotein fraction and did not affect its oxidation. It was shown that amphotericin B contained in Fungizone extracted cholesterol from low-density lipoproteins which sensitized them to oxidation. Both formulations of amphotericin B studied here did not bind to high-density lipoprotein and did not affect the process of its oxidation. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 135-144, 1998
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    Chlorophyll and pheophytin derivatives in geochemical transformation pathways: A surface-enhanced resonance Raman spectroscopic study (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 147-159 
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    ISSN: 1075-4261
    Keywords: protected surface-enhanced resonance Raman spectroscopy ; chlorophyll transformation products ; pheophytins ; geochemical transformations ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Protected surface-enhanced resonance Raman spectroscopy (PSERRS) has been used to study a number of chlorophyll transformation products that have been suggested as intermediates in the so-called Treibs hypothesis which describes the transformation of ancient chlorophyll a (chla) in the biosphere into desoxophylloerythroetioporphyrin (DPEP) found in sedimentary environments. Both Soret- and Qy-resonant PSERR spectra have been recorded, providing two-dimensional structural fingerprints containing a number of bands which enable the presence of specific peripheral substituents to be identified. Some of these marker bands can be assigned directly to vibrational modes of the particular substituents. This has allowed further characterization of the vibrational spectrum of chl a; in particular, a vinyl mode has been identified which previously was thought to be Raman silent. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 147-159, 1998
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    Luminescence and structure of the protonated forms of meso-tetraarylporphyrins in solution (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 121-133 
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    ISSN: 1075-4261
    Keywords: meso-tetraarylporphyrins ; protonated forms ; visible absorption spectra ; luminescence ; radiationless transitions ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: A comparative study of the spectral-luminescent properties (at 293 K and 77 K) of meso-tetrakis(o-tolyl)porphyrin (o-TTP) and meso-tetraphenylporphyrin (TPP), and also meso-tetrakis(n-propyl)porphyrin (TPrP) in nonaqueous acid media has been carried out with the aim to reveal effects associated with the influence of methyl groups which hinder sterically the twist of the phenyl rings enhancing their conjugation with the macrocycle in acid medium. On the basis of the spectral data it is concluded that although the introduction of the methyl groups diminishes this twist of phenyls it does not eliminate it completely (the absorption spectra of protonated o-TTP are intermediate between those of TTP and TPrP). The fluorescence spectra of the protonated forms of o-TTP and TPP at 77 K are approximately mirror-symmetrical to the Q(0-0) and Q(0-1) absorption bands; on the elevation of the temperature up to 293 K the fluorescence and absorption bands broaden, the Stokes shift largely increases, and the mirror symmetry of the spectra disappears, which is indicative of changes in solute-solvent interactions in the S1 state. The analysis of the obtained data on the energetics of photophysical processes leads to the conclusion that the significant role of radiationless deexcitation in the S1 ↝ S0 channel, characteristic of the protonated form of TPP, is retained at 77 K. The introduction of the methyl groups at the ortho positions sharply decreases the corresponding rate constant, so that the S1 ↝ T1 intersystem crossing becomes the main channel of deexcitation. The influence of heavy atoms (the Cl- and Br- anions) on the luminescence of the protonated forms has been investigated. It is shown that, analogous to the case of octaethylporphyrin investigated earlier, in nonaqueous media the protonated species of o-TTP form bis adducts of the dihydrochloride type. Contrary to this, the experiments with meso-tetrakis(p-sulfophenyl)porphyrin (TPPS) in aqueous solutions have shown that the TPPS dications do not add counterions, whereas the influence of Cl- and Br- on fluorescence is realized according to the external heavy-atom effect mechanism. For nonaqueous o-TTP solutions with admixtures of HCl and CF3COOH the short-wavelength fluorescence from the S3 (B1) level has been detected whose unusual peculiarity is its enhancement in passing from 293 K to 77 K. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 121-133, 1998
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    Effect of surface modifiers on the electrode reactions and conformation of cytochrome c3 adsorbed on a silver electrode (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 161-170 
    Details
    ISSN: 1075-4261
    Keywords: surface-enhanced resonance Raman scattering ; SERRS ; cytochrome c3 ; electrode modifiers ; electroreflectance voltammetry ; ER ; 11-mercaptoundecanoic acid ; 4,4′-bipyridine promoters ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Surface-enhanced resonance Raman scattering and electroreflectance voltammetry were used to investigate the effect of electrode surface modification on the structure and redox properties of cytochrome c3 immobilized on Ag surfaces. It is shown that the redox reactions of cytochrome c3 are more reversible at an 11-mercaptoundecanoic acid modified Ag electrode as compared to a bare metal surface. The heme of cytochrome c3 is in a mixed low and high spin state when adsorbed at the bare electrode, whereas only the low spin form is present on the 11-mercaptoundecanoic acid modified electrode, suggesting that the native conformation is maintained in the latter case. The reduction potential is close to that of the most positive macroscopic potential as determined by electroreflectance spectroscopy. In contrast, the reduction potential as determined by SERRS undergoes a large positive shift in the presence of 4,4′-bipyridine, the magnitude of which is dependent upon the concentration of 4,4′-bipyridine. These results indicate that the effect of the cytochrome c3 interaction with the 4,4′-bipyridine-modified surface is significantly different as compared to its interaction with the 11-mercaptoundecaodoic acid modified surface. Moreover, the results emphasize that electrode modifiers can have dramatically different effects on the redox properties of different proteins. It is well known that 4,4′-bipyridine acts as a redox promoter in the case of cytochrome c, whereas no electrochemical or electroreflectance response was observed in the case of cytochrome c3. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 161-170, 1998
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    A spectroscopic study of the hydrogen bonding and π-π stacking interactions of harmane with quinoline (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 185-195 
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    ISSN: 1075-4261
    Keywords: hydrogen bonding ; van der Waals ; betacarbolines ; benzopyridines ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: A spectroscopic (UV-vis, Fourier transform IR, steady state, and time-resolved fluorescence) study of the interactions of the ground and excited singlet states of harmane (1-methyl-9H-pyrido/3,4-b/indole) with quinoline has been carried out in cyclohexane, toluene, and buffered pH = 8.7 aqueous solutions. To analyze how the number of rings in the substrate influences these interactions, pyridine and phenanthridine have also been included in this study. In cyclohexane and toluene 1 : 1 stoichiometric hydrogen-bonded complexes are formed in both the ground and the excited singlet states. As the number of rings of the benzopyridines and the solvent polarity increase hydrogen-bonding interactions weaken and π-π van der Waals interactions become apparent. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 185-195, 1998
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    Raman linear intensity difference of membrane-bound peptides: Indole ring orientations of tryptophans 11 and 13 in the gramicidin A transmembrane channel (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 171-184 
    Details
    ISSN: 1075-4261
    Keywords: ultraviolet resonance Raman spectroscopy ; membrane-bound peptides ; gramicidin A ; ion channel ; tryptophan orientation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: A Raman linear intensity difference (RLID) method has been developed to determine orientations of chromophores in membrane-bound peptides and proteins. The method involves orientation of the peptide or protein in lipid bilayer membranes and measurement of intensity differences between Raman spectra excited with two orthogonal laser polarizations. Analysis of the RLID spectrum is simplified when the chromophore exhibits a vibrational mode for which the Raman band is enhanced through resonance with a single molecular electronic transition. To examine the indole ring orientations of Trp residues in the gramicidin A transmembrane channel, we have prepared analogues of gramicidin A, in which one of four Trp residues is replaced by deuterated Trp (Trp-2,4,5,6,7-d5). Two vibrational Raman bands ωd3 and ωd2 of deuterated Trp have been shown to gain intensity predominantly through resonance with the Bb and La electronic transitions, respectively, when excited at 244 and 257 nm. By examining the RLID spectra of the ωd3 and ωd2 bands of gramicidin A channels oriented in phospholipid bilayer membranes, we have determined the inclination angles of the Bb and La transition moments with respect to the channel axis in the absence and presence of Na+. The orientations of the Trp-11 and Trp-13 indole rings in the gramicidin channel structure have been derived from the inclination angles of the transition moments. The indole rings of Trp-11 and Trp-13, which are known to shift along the channel axis upon binding of Na+, do not reorient during their positional shifts. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 171-184, 1998
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    Fourier transform infrared spectroscopy as a probe for the study of the hydration of lipid self-assemblies. I. Methodology and general phenomena (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 267-280 
    Details
    ISSN: 1075-4261
    Keywords: dipalmitoylphosphatidylcholine ; dioleoylphosphatidylcholine ; mixed-chain phospholipids ; unsaturation ; hydration ; FTIR spectroscopy ; lyotropic phase transition ; chain-melting transition ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: An algorithm for the study of the gradual hydration of phospholipid assemblies by means of Fourier transform infrared (FTIR) spectroscopy is presented. A complete series of diacyl phosphatidylcholines (PCs) including all possible analogues with palmitoyl and oleoyl residues, namely DPPC, DOPC, POPC, and OPPC, was investigated at room temperature. The lipid samples were prepared as cast films probably consisting of aligned multilamellar bilayers. The range of water activities studied in these films was regulated by adsorption via the gas phase corresponding to relative humidities of between 0 and 100%. Analyses of the IR-spectroscopic data have concentrated mainly on determining the amounts of water incorporated by each lipid as well as the hydration-induced response observed for some absorption bands of the different lipids. The water uptake at high relative humidity (RH) increases with the portion of unsaturated acyl chains in the molecular structure of the PCs. Isothermal phase transitions triggered lyotropically have been detected in demonstrating the occurrence of the main transition in POPC and OPPC films at room temperature. Moreover, it appears that both lamellar phases, the gel as well as the liquid-crystalline phase, are not uniform. They seem to comprise an amazingly large span of order/disorder states of the lipid chains generally depending on the degree of hydration. As exemplified by the significant variation in the onset of wavenumber shifts for the PO2- and C=O stretching-vibration modes, obtained as a function of hydration, a sequence of attachment to polar lipid binding sites by water molecules was established for DPPC. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 267-280, 1998
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    Spatially localized ballistic two-photon excitation in scattering mediaThis paper is dedicated to Professor Henryk Z. Wrembel on the occasion of his 70th birthday. (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 303-310 
    Details
    ISSN: 1075-4261
    Keywords: photon migration ; ballistic photons ; two-photon excitation ; fluorescence ; time-resolved fluorescence ; optical tomography ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: We describe spatially localized two-photon excitation in scattering media. Using femtosecond pulses at 770 nm from a Ti : Sapphire laser, we were able to excite fluorophores in capillary tubes under up to 1.5 mm of 0.5% intralipid. Displacement of the laser beam relative to the embedded samples indicates that highly localized excitation was possible with two-photon excitation, whereas one-photon excitation resulted in loss of spatial resolution due to excitation by the diffusely scattered photons. These results indicate that two-photon excitation in the scattering solution is due only to the ballistic photons, a result confirmed by frequency-domain time-resolved measurements. Selective excitation of adjacent embedded samples was found possible for two but not one-photon excitation. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 303-310, 1998
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    Fluorescence and surface-enhanced Raman study of 9-aminoacridine in relation to its aggregation and excimer emission in aqueous solution and on silver surface (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 327-339 
    Details
    ISSN: 1075-4261
    Keywords: 9-aminoacridine ; fluorescence ; SERS ; dimerization ; excimer ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Fluorescence spectroscopy and surface-enhanced Raman spectroscopy (SERS) have been applied to study the aggregation and excimer emission of 9-aminoacridine (9AA) and 9-aminoacridine hydrochloride (9AA-HCl) in aqueous solution and on silver colloids. The effect of the drug concentration, pH, and chloride concentration on these processes has been investigated. The excimer emission of 9AA is connected to the dimerization of this drug in solution: the formation of 9AA dimers is greatly favored when the drug is under the amino form at neutral and acidic pH, while at alkaline pH the imino 9AA form tends to form large-sized aggregates which cannot be excited to render excimer emission. 9AA is adsorbed on the silver surface under two different forms: strongly and weakly attached 9AA, each one corresponding to the different drug tautomers: imino and amino. The interaction of 9AA with silver induces a charge transfer from the adsorbate to the metal leading to a remarkable fluorescence quenching, a basicity decrease of the adsorbed drug and a considerable weakening of the dimer-excimer emission. Furthermore, an attribution of the main Raman features appearing in the SERS spectra has been proposed, providing marker bands for the imino and amino 9AA tautomers, and a mechanism for the molecular dimerization is also suggested. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 327-339, 1998
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    On the use of ultraviolet resonance Raman intensities to elaborate molecular force fields: Application to nucleic acid bases and aromatic amino acid residues models (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 379-393 
    Details
    ISSN: 1075-4261
    Keywords: molecular force field ; resonance Raman intensities ; aromatic amino acids ; nucleic acid bases ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Normal modes analyses for different molecules with biological interest have been performed and checked via the calculation of resonance Raman intensities. For this purpose, molecular orbital calculations were used to determine bond order changes in the lowest-lying electronic transitions. These bond order changes were used to calculate resonance Raman intensities in order to obtain correct vibrational assignments and reliable force fields. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 379-393, 1998
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    Composition, constitution, and interaction of bone with hydroxyapatite coatings determined by FT Raman microscopy (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 403-412 
    Details
    ISSN: 1075-4261
    Keywords: FT Raman microscopy ; qualitative analysis ; bone mineralization ; hydroxyapatite coatings ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: An optimized FT Raman microscope (inverted microscope with high throughput of radiation) was developed that allows minimal sample preparation and Raman spectroscopy without fluorescence. A quantitative determination of the mineralization of bone tissue and hydroxyapatite (HA) coatings of hip and knee prostheses was performed. The lateral resolution reached down to 10 μm. The distribution of the HA content in the coatings investigated was found to be similar all the time. This result was independent of the composition of the coatings and the history of the whole prosthesis. In the immediate vicinity of the prosthesis a large HA content could be observed that decreased to a minimum towards the periphery of the coating and increased at the site of the ongrown bone. For the interface between bone and HA coating a transitional zone was observed at a lateral distance of 30-40 μm to the implant. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 403-412, 1998
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    Special issue on “hot topics” from the ECSBM'97 conference (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S1 
    Details
    ISSN: 1075-4261
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: No abstract.
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    In vitro and in vivo Raman spectroscopy of human skin (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. S31 
    Details
    ISSN: 1075-4261
    Keywords: stratum corneum ; epidermis ; noninvasive ; lipids ; natural moisturizing factor ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Noninvasive techniques that provide detailed information about molecular composition, structure, and interactions are crucial to further our understanding of the relation between skin disease and biochemical changes in the skin, as well as for the development of penetration enhancers for transdermal drug administration. In this study we present in vitro and in vivo Raman spectra of human skin. Using a Raman microspectrometer, in vitro spectra were obtained of thin cross sections of human skin. They provided insight into the molecular composition of different skin layers. Evidence was found for the existence of a large variation in lipid content of the stratum corneum. A simple experimental setup for in vivo confocal Raman microspectroscopy of the skin was developed. In vivo Raman spectra of the stratum corneum were obtained at different positions of the arm and hand of three volunteers. They provided evidence for differences in the concentration of natural moisturizing factor at these positions. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: S31-S39, 1998
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    Oxazole yellow dye interactions with short DNA oligomers of homogeneous base composition and their hybrids (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 17-25 
    Details
    ISSN: 1075-4261
    Keywords: DNA dyes ; single-stranded DNA ; oxazole yellow ; fluorescent dyes ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Interactions between short single-stranded DNA oligomers of homogeneous base composition and the fluorescent probes oxazole yellow (YO) and its homodimer YOYO are described. The oligomers included 15-mers and 30-mers of polydA, polydT, polydG, and polydC. Interactions between the dyes and DNA hybrids formed from complementary homogeneous strands of equal length were also investigated. No interactions were observed between the dyes and the monomeric monophosphate nucleosides A, G, T, or C. The dyes were found to interact much more strongly with the purine oligomers polydA and polydG than with the pyrimidine oligomers polydT and polydC. PolydA of both lengths has strong interactions with YOYO, whereas the polydG 30-mer interacts strongly with monomeric YO. The 15-mers of polydG and polydC of both lengths show little interaction with either dye. Interactions of the dyes with the polydA/polydT and polydG/polydC hybrids tend to be dominated by interactions with polydA and polydG, respectively. Although dye interactions generally were facilitated by hybridization, particularly for polydA/polydT, the interactions were similar to those with the single strands and different from those that have been observed in long double-stranded DNA. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 17-25, 1998
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    Spectroscopic studies of single-stranded DNA ligands and oxazole yellow dyes (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 27-35 
    Details
    ISSN: 1075-4261
    Keywords: DNA dyes ; single-stranded DNA ; oxazole yellow ; fluorescent dyes ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Interactions between short single-stranded DNA ligands and fluorescent DNA indicator dyes were used to investigate binding selectivity of the ligands. Conformational differences among four DNA ligands of different sequence and structure, including two that form a G-quartet and two that do not, were confirmed by circular dichroism spectroscopy. Their interactions with indicator dyes YO-pro-1 iodide (YO) and YOYO-1 iodide (YOYO) were probed using measurements of dye absorbance; induced circular dichroism; and fluorescence spectra, anisotropy, and lifetime. Equilibrium binding constants and stoichiometry were determined as well. Results indicate significant differences among the dye interactions and binding stoichiometries of the four ligands. One of the G-quartet forming ligands, a 20-mer of sequence 5′-GGTTTT-GGTTTTGGTTTTGG-3′, shows distinctly different interactions from the other three ligands, all of which are 15-mers. These studies illustrate the importance of sequence and conformation in determining the binding interactions of short single-stranded DNA. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 27-35, 1998
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    Cancer grading by Fourier transform infrared spectroscopy (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 37-46 
    Details
    ISSN: 1075-4261
    Keywords: FTIR ; cancer prognosis ; cancer grade ; tissue spectroscopy ; lymphoma ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Thirty-nine freeze-dried tissue samples from 17 lymphoid tumors (nine malignant non-Hodgkin's lymphomas) were studied by Fourier transform infrared (FTIR) spectroscopy. The absorbance ratio A1121/A1020 increased, along with the emergence of an absorbance pulse at 1121 cm-1, with increasing clinicopathological grade of malignant lymphoma. An increasing A1121/A1020 ratio from benign to malignant is evident in literature spectra from several different tissues; however, the present study is the first to comment on this effect and to propose it as an index of the cellular RNA/DNA ratio after subtraction of overlapping absorbances, if present, due to collagen or glycogen. Absorbance attributable to collagen increased with lymphoma grade and was greater in benign inflammatory tumors than in low-grade lymphomas. The A1121/A1020 trend observed here may form the basis of a universal cancer-grading parameter to assist with cancer treatment decisions and may also be useful in the analysis of cellular growth perturbation induced by drugs or other therapies. Our spectral findings may potentially be applied to cell clusters and discrete areas of tumor tissue sections using the FTIR microscope, allowing correlation with morphology and a high degree of spatial resolution. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 37-46, 1998
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    Cyanide binding and active site structure in heme-copper oxidases: Normal coordinate analysis of iron-cyanide vibrations of $a^{2+}_3$ CN- complexes of cytochromes ba3 and aa3 (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 1-15 
    Details
    ISSN: 1075-4261
    Keywords: cytochrome ba3 ; cytochrome aa3 ; binuclear site structure ; cyanide ; Raman spectroscopy ; normal coordinates ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The cyanide isotope-sensitive low-frequency vibrations of ferrous cyano complexes of cytochrome a3 are studied for cytochrome ba3 from Thermus thermophilus and cytochrome aa3 from bovine heart. Cyanide complexes of ba3 display three isotope sensitive frequencies at 512, 485, and 473 cm-1. The first is primarily an Fe - C stretching motion, whereas the lower wavenumber modes are bending motions. These iron-cyanide vibrations are independent of the redox levels of the other metal centers in the protein. On the other hand, the fully reduced bovine derivative complexed with cyanide gives rise to a bending vibration at 503 cm-1 and a stretching vibration at 469 cm-1. That is, the ordering of the stretching and bending frequencies is reversed from that of the bacterial protein. These results are analyzed by normal coordinate calculations to obtain comparative models for the binuclear O2 reducing site of the two proteins. We find that the observed frequencies are consistent with a linear Fe - C - N group and larger Fe - C stretching force constant (2.558 mdyn/Å) for ba3 and a slightly bent Fe - C - N group (angle ∼ 170°) and a smaller Fe - C stretching force constant (2.335 mdyn/Å) for aa3. Thus, there are significant differences in the interaction of cyanide with ferrous a3 in the two proteins that are most likely caused by a weaker proximal histidine interaction and stronger peripheral heme electron withdrawing effects in ba3. Possible sources of these protein-induced effects are discussed. Using the analysis developed here, comparison of the FeCN stretching and bending frequencies of the ferrous bovine a3-CN complex to those obtained from the ferric a3-CN complex suggests that upon conversion of the resting to the fully reduced protein, a conformational change occurs that constrains the ligand binding site. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 1-15, 1998
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    Infrared spectroscopy of human tissue. I. Differentiation and maturation of epithelial cells in the human cervix (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 47-53 
    Details
    ISSN: 1075-4261
    Keywords: infrared spectroscopy of human tissue ; basal, parabasal, and superficial layers of cervical squamous epithelium ; cell maturation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Infrared spectral results for the different epithelial layers of human cervical squamous tissue are reported. The layers, representing different cellular maturation stages, exhibit quite different spectral patterns. Thus, infrared spectroscopy presents a powerful tool to monitor cell maturation and differentiation. Furthermore, a detailed understanding of the spectra of the individual layers of tissue permit a proper interpretation of the state of health of cells exfoliated from such tissue. Part II of this series describes the use of the spectral information presented here to interpret the infrared spectra of exfoliated cells. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 47-53, 1998
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    Infrared spectroscopy of human tissue. II. A comparative study of spectra of biopsies of cervical squamous epithelium and of exfoliated cervical cells (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 55-59 
    Details
    ISSN: 1075-4261
    Keywords: infrared spectroscopy of human tissue ; squamous epithelium ; exfoliated cells ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: A comparison of infrared absorption spectra obtained from the different layers of squamous epithelium from the human cervix, and infrared spectra obtained from exfoliated cervical cells, is presented. Infrared spectroscopy has been shown (in part I of this series) to be a sensitive tool to monitor maturation and differentiation of human cervical cells; therefore, this spectroscopic technique provides new insights into the composition and state of health of exfoliated cells. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 55-59, 1998
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    Raman scattering tensors of tyrosine (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 61-71 
    Details
    ISSN: 1075-4261
    Keywords: L-tyrosine ; polarized Raman spectra ; Raman tensor ; ab initio MO calculation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Polarized Raman scattering measurements have been made of a single crystal of L-tyrosine by the use of a Raman microscope with the 488.0-nm exciting beam from an argon ion laser. The L-tyrosine crystal belongs to the space group P212121 (orthorhombic), and Raman scattering intensities corresponding to the aa, bb, cc, ab and ac components of the crystal Raman tensor have been determined for each prominent Raman band. A similar set of measurements has been made of L-tyrosine-d4, in which four hydrogen atoms on the benzene ring are replaced by deuterium atoms. The effects of NH3 → ND3 and OH → OD on the Raman spectrum have also been examined. In addition, depolarization ratios of some bands of L-tyrosine in aqueous solutions of pH 13 and pH 1 were examined. For comparison with these experimental results, on the other hand, ab initio molecular orbital calculations have been made of the normal modes of vibration and their associated polarizability oscillations of the L-tyrosine molecule. On the basis of these experimental data and by referring to the results of the calculations, discussions have been presented on the Raman tensors associated to some Raman bands, including those at 829 cm-1 (benzene ring breathing), 642 cm-1 (benzene ring deformation), and 432 cm-1 (Cα-Cβ-Cγ bending). © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 61-71, 1998
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    FTIR microspectroscopic study of cell types and potential confounding variables in screening for cervical malignancies (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 75-91 
    Details
    ISSN: 1075-4261
    Keywords: FTIR microspectroscopy ; cervical cancer ; leukocytes ; lymphocytes ; erythrocytes ; semen ; mucins ; fibroblasts ; thrombocytes ; bacteria ; nylon ; Candida albicans ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: FTIR microscopy was applied to the analysis of cell types and other variables present in Pap smears to ascertain the limitations of infrared spectroscopy in the diagnosis of cervical cancer and dysplasia. It was found that leukocytes, and in particular lymphocytes, have spectral features in the phophodiester region (1300-900 cm-1) suggestive of what has previously been described as changes indicative of malignancy. Endocervical cells and fibroblasts have similar spectral features to HeLa cells and consequently could also confound diagnosis. The use of ethanol as a fixative and dehydrating agent results in retention of glycogen in cervical cell types and thus minimizes spectral changes in the glycogen region due to sampling technique. Spectra of seminal fluids exhibit strong bands in the phosphodiester/carbohydrate region; however, sperm contamination should be easily detectable by the presence of a distinctive doublet at 981/968 cm-1. Erythrocyte spectra exhibit a reduction in glycogen band intensity, but can be discerned by a relatively low-intensity νs $PO^{-}_{2}$ band. Endocervical mucin spectra exhibit a reduction in glycogen bands and a very pronounced νs $PO^{-}_{2}$ band, which is similar in intensity to the corresponding band in HeLa cells. Thrombocytes have strong bands in the phosphodiester region, but thrombocytes can be discerned from other cell types by the presence of two small broad bands at 980 and 935 cm-1. Candida albicans is characterized by strong bands in the polysaccharide region which could potentially obscure diagnostic bands if C. albicans is present in large numbers. Spectra of bacteria common to the female genital tract, in general, also have strong absorptions in the polysaccharide region; however, bacterial contamination is usually minimal and would not be expected to obscure cervical cell spectra. Nylon threads and bristles from cervical sampling implements produce characteristic IR profiles which allow for easy identification. Given the number of potential confounding variables associated with cervical cytology, a multivariate statistical or neural network analysis would appear to be necessary before the implementation of FTIR technology in clinical laboratories. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 75-91, 1998
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    Metastasis in eggs (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikorski, R -- Peters, R -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1823.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776688" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Vessels/physiology ; Chick Embryo ; *Chorion/blood supply ; Humans ; Metalloendopeptidases/metabolism ; *Neoplasm Metastasis ; Neoplasm Seeding ; *Polymerase Chain Reaction ; Receptors, Cell Surface/metabolism ; Receptors, Urokinase Plasminogen Activator ; 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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    Quantitation of HIV-1-specific cytotoxic T lymphocytes and plasma load of viral RNA (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: Although cytotoxic T lymphocytes (CTLs) are thought to be involved in the control of human immunodeficiency virus-type 1 (HIV-1) infection, it has not been possible to demonstrate a direct relation between CTL activity and plasma RNA viral load. Human leukocyte antigen-peptide tetrameric complexes offer a specific means to directly quantitate circulating CTLs ex vivo. With the use of the tetrameric complexes, a significant inverse correlation was observed between HIV-specific CTL frequency and plasma RNA viral load. In contrast, no significant association was detected between the clearance rate of productively infected cells and frequency of HIV-specific CTLs. These data are consistent with a significant role for HIV-specific CTLs in the control of HIV infection and suggest a considerable cytopathic effect of the virus in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogg, G S -- Jin, X -- Bonhoeffer, S -- Dunbar, P R -- Nowak, M A -- Monard, S -- Segal, J P -- Cao, Y -- Rowland-Jones, S L -- Cerundolo, V -- Hurley, A -- Markowitz, M -- Ho, D D -- Nixon, D F -- McMichael, A J -- MO1-RR00102/RR/NCRR NIH HHS/ -- U01AI41534/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Medicine, Nuffield Department of Medicine, Oxford OX3 9DS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9516110" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/therapeutic use ; CD4 Lymphocyte Count ; Coloring Agents ; Cytopathogenic Effect, Viral ; Cytotoxicity, Immunologic ; Flow Cytometry ; Gene Products, gag ; Gene Products, pol ; HIV Infections/drug therapy/*immunology/*virology ; HIV-1/genetics/*physiology ; HLA-A Antigens ; Humans ; Lymphocyte Count/*methods ; Oligopeptides ; RNA, Viral/*blood ; Sensitivity and Specificity ; T-Lymphocytes, Cytotoxic/*immunology ; Viral Load ; 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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    Which of our genes makes us human? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1432-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9750111" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; *Chromosomes, Human ; Gene Expression ; *Genome ; *Genome, Human ; Hominidae/*genetics ; *Human Characteristics ; Humans ; Mutation ; Pan troglodytes/genetics ; *Sequence Analysis, DNA ; Sialic Acids/chemistry/physiology ; Species Specificity
    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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    Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: The Son of Sevenless (Sos) proteins control receptor-mediated activation of Ras by catalyzing the exchange of guanosine diphosphate for guanosine triphosphate on Ras. The NH2-terminal region of Sos contains a Dbl homology (DH) domain in tandem with a pleckstrin homology (PH) domain. In COS-1 cells, the DH domain of Sos stimulated guanine nucleotide exchange on Rac but not Cdc42 in vitro and in vivo. The tandem DH-PH domain of Sos (DH-PH-Sos) was defective in Rac activation but regained Rac stimulating activity when it was coexpressed with activated Ras. Ras-mediated activation of DH-PH-Sos did not require activation of mitogen-activated protein kinase but it was dependent on activation of phosphoinositide 3-kinase. These results reveal a potential mechanism for coupling of Ras and Rac signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nimnual, A S -- Yatsula, B A -- Bar-Sagi, D -- CA09176/CA/NCI NIH HHS/ -- CA28146/CA/NCI NIH HHS/ -- CA55360/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438849" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Cycle Proteins/metabolism ; Cell Line ; Cell Membrane/ultrastructure ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanine Nucleotide Exchange Factors ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; Membrane Proteins/chemistry/*metabolism ; *Mitogen-Activated Protein Kinases ; Proteins/metabolism ; Proto-Oncogene Proteins ; Recombinant Fusion Proteins/metabolism ; Retroviridae Proteins, Oncogenic/chemistry ; Signal Transduction ; Son of Sevenless Proteins ; Transfection ; cdc42 GTP-Binding Protein ; rac GTP-Binding Proteins ; ras Guanine Nucleotide Exchange Factors ; ras Proteins/*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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    Essential role of CED-4 oligomerization in CED-3 activation and apoptosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: Control of the activation of apoptosis is important both in development and in protection against cancer. In the classic genetic model Caenorhabditis elegans, the pro-apoptotic protein CED-4 activates the CED-3 caspase and is inhibited by the Bcl-2-like protein CED-9. Both processes are mediated by protein-protein interaction. Facilitating the proximity of CED-3 zymogen molecules was found to induce caspase activation and cell death. CED-4 protein oligomerized in cells and in vitro. This oligomerization induced CED-3 proximity and competed with CED-4:CED-9 interaction. Mutations that abolished CED-4 oligomerization inactivated its ability to activate CED-3. Thus, the mechanism of control is that CED-3 in CED-3:CED-4 complexes is activated by CED-4 oligomerization, which is inhibited by binding of CED-9 to CED-4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, X -- Chang, H Y -- Baltimore, D -- CA51462/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1355-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721101" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Apoptosis Regulatory Proteins ; Biopolymers ; *Caenorhabditis elegans Proteins ; Calcium-Binding Proteins/*chemistry/genetics/*metabolism ; *Caspases ; Cell Line ; Chemistry, Physical ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation ; Enzyme Precursors/metabolism ; HeLa Cells ; Helminth Proteins/*chemistry/genetics/*metabolism ; Humans ; Mutation ; Oligopeptides/pharmacology ; Physicochemical Phenomena ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Recombinant Fusion Proteins/metabolism ; Tacrolimus/pharmacology ; Transfection ; bcl-X Protein
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structure and function in the nucleus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: Current evidence suggests that the nucleus has a distinct substructure, albeit one that is dynamic rather than a rigid framework. Viral infection, oncogene expression, and inherited human disorders can each cause profound and specific changes in nuclear organization. This review summarizes recent progress in understanding nuclear organization, highlighting in particular the dynamic aspects of nuclear structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lamond, A I -- Earnshaw, W C -- 073915/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Apr 24;280(5363):547-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, UK. a.i.lamond@dundee.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9554838" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleolus/physiology/ultrastructure ; Cell Nucleus/chemistry/*physiology/*ultrastructure ; Chromatin/physiology ; Chromosomes/physiology ; *Drosophila Proteins ; Euchromatin ; Gene Expression Regulation ; Heterochromatin/physiology ; Humans ; Insect Proteins/chemistry/physiology ; Interphase ; Neoplasm Proteins/chemistry/physiology ; *Nuclear Proteins ; Polycomb Repressive Complex 1 ; Polycomb-Group Proteins ; Repressor Proteins/chemistry/physiology ; Ribonucleoproteins, Small Nuclear/analysis/physiology ; Transcription Factors/chemistry/physiology ; Tumor Suppressor Proteins
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    Anthropologists probe genes, brains at annual meeting (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1998 Apr 17;280(5362):380-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9575083" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthropology, Physical ; Biological Evolution ; Brain/*anatomy & histology ; Computer Simulation ; DNA, Mitochondrial/genetics ; Female ; *Genetics, Population ; *Hinduism/history ; History, Ancient ; Hominidae/*anatomy & histology ; Humans ; India ; Male ; Models, Anatomic ; Y Chromosome/genetics
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    Calibrating the mitochondrial clock (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):28-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9441404" target="_blank"〉PubMed〈/a〉
    Keywords: DNA Fingerprinting ; DNA, Mitochondrial/*genetics ; *Evolution, Molecular ; Forensic Medicine ; Humans ; *Mutation ; Point Mutation ; *Polymorphism, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-25
    Description: The human immunodeficiency virus-type 1 (HIV-1) envelope glycoproteins interact with receptors on the target cell and mediate virus entry by fusing the viral and cell membranes. The structure of the envelope glycoproteins has evolved to fulfill these functions while evading the neutralizing antibody response. An understanding of the viral strategies for immune evasion should guide attempts to improve the immunogenicity of the HIV-1 envelope glycoproteins and, ultimately, aid in HIV-1 vaccine development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wyatt, R -- Sodroski, J -- AI 31783/AI/NIAID NIH HHS/ -- AI 39420/AI/NIAID NIH HHS/ -- AI28691/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1884-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Immunology/AIDS, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9632381" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/chemistry/immunology ; Animals ; Gene Products, env/chemistry/immunology/*physiology ; HIV Antibodies/biosynthesis ; HIV Antigens/immunology ; HIV Envelope Protein gp41/physiology ; HIV Infections/*immunology ; HIV-1/chemistry/immunology/*physiology ; Humans ; Membrane Fusion ; Receptors, HIV/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Anterior cingulate cortex, error detection, and the online monitoring of performance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: An unresolved question in neuroscience and psychology is how the brain monitors performance to regulate behavior. It has been proposed that the anterior cingulate cortex (ACC), on the medial surface of the frontal lobe, contributes to performance monitoring by detecting errors. In this study, event-related functional magnetic resonance imaging was used to examine ACC function. Results confirm that this region shows activity during erroneous responses. However, activity was also observed in the same region during correct responses under conditions of increased response competition. This suggests that the ACC detects conditions under which errors are likely to occur rather than errors themselves.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, C S -- Braver, T S -- Barch, D M -- Botvinick, M M -- Noll, D -- Cohen, J D -- K08MH01306/MH/NIMH NIH HHS/ -- R01MH52864/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1998 May 1;280(5364):747-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Western Psychiatric Institute and Clinic, School of Medicine, University of Pittsburgh, 3811 O'Hara Street, Pittsburgh, PA 15213, USA. cscarter+@pitt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563953" target="_blank"〉PubMed〈/a〉
    Keywords: Brain Mapping ; Cognition/*physiology ; Frontal Lobe/*physiology ; Gyrus Cinguli/*physiology ; Humans ; Magnetic Resonance Imaging
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    New potential for human embryonic stem cells (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gearhart, J -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1061-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Gynecology and Obstetrics, Johns Hopkins Medicine, Baltimore, MD 21287, USA. gearhart@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/*cytology ; *Cell Culture Techniques ; Cell Differentiation ; *Cell Line ; Cell Lineage ; *Embryo Research ; Embryo, Mammalian/*cytology ; Federal Government ; Germ Cells/*cytology ; Government Regulation ; Guidelines as Topic ; Humans ; Major Histocompatibility Complex ; Mice ; Research Support as Topic ; Risk Assessment ; Stem Cell Transplantation ; Stem Cells/*cytology ; Transplantation Immunology ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular basis of T cell inactivation by CTLA-4 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: CTLA-4, a negative regulator of T cell function, was found to associate with the T cell receptor (TCR) complex zeta chain in primary T cells. The association of TCRzeta with CTLA-4, reconstituted in 293 transfectants, was enhanced by p56(lck)-induced tyrosine phosphorylation. Coexpression of the CTLA-4-associated tyrosine phosphatase, SHP-2, resulted in dephosphorylation of TCRzeta bound to CTLA-4 and abolished the p56(lck)-inducible TCRzeta-CTLA-4 interaction. Thus, CTLA-4 inhibits TCR signal transduction by binding to TCRzeta and inhibiting tyrosine phosphorylation after T cell activation. These findings have broad implications for the negative regulation of T cell function and T cell tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K M -- Chuang, E -- Griffin, M -- Khattri, R -- Hong, D K -- Zhang, W -- Straus, D -- Samelson, L E -- Thompson, C B -- Bluestone, J A -- P01 AI35294-6/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2263-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ben May Institute for Cancer Research, and Committee on Immunology, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856951" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigens, CD ; Antigens, Differentiation/*metabolism ; CTLA-4 Antigen ; Cell Line ; Cells, Cultured ; Humans ; *Immunoconjugates ; Intracellular Signaling Peptides and Proteins ; *Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/genetics/metabolism ; Membrane Proteins/*metabolism ; Mice ; Mice, Inbred BALB C ; Models, Immunological ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; SH2 Domain-Containing Protein Tyrosine Phosphatases ; *Signal Transduction ; T-Lymphocytes/*immunology ; Transfection ; src Homology Domains
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    Methylmercury risks (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldman, L R -- Farland, W H -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):640-1; author reply 641.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9471723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Fishes ; *Food Contamination ; Humans ; Maximum Allowable Concentration ; Methylmercury Compounds/*adverse effects ; *Nutrition Policy ; Risk Assessment ; United States ; United States Environmental Protection Agency
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    Chimp research (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leigh, S R -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):47.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9786794" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Humans ; Pan troglodytes/*genetics/*growth & development ; Research
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    Differential use of CREB binding protein-coactivator complexes (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: CREB binding protein (CBP) functions as an essential coactivator of transcription factors that are inhibited by the adenovirus early gene product E1A. Transcriptional activation by the signal transducer and activator of transcription-1 (STAT1) protein requires the C/H3 domain in CBP, which is the primary target of E1A inhibition. Here it was found that the C/H3 domain is not required for retinoic acid receptor (RAR) function, nor is it involved in E1A inhibition. Instead, E1A inhibits RAR function by preventing the assembly of CBP-nuclear receptor coactivator complexes, revealing differences in required CBP domains for transcriptional activation by RAR and STAT1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurokawa, R -- Kalafus, D -- Ogliastro, M H -- Kioussi, C -- Xu, L -- Torchia, J -- Rosenfeld, M G -- Glass, C K -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):700-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular and Molecular Medicine, Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0651, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445474" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/*metabolism/pharmacology ; Animals ; Binding Sites ; CREB-Binding Protein ; Cell Differentiation ; Cell Line ; DNA-Binding Proteins/metabolism ; Histone Acetyltransferases ; Humans ; Mutation ; Nuclear Proteins/chemistry/genetics/*metabolism ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 3 ; Protein Binding ; Receptors, Retinoic Acid/metabolism ; Recombinant Fusion Proteins/metabolism ; STAT1 Transcription Factor ; Trans-Activators/metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Tretinoin/pharmacology
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    The future of long life (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olshansky, S J -- Carnes, B A -- Cassel, C -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1612-3; author reply 1613-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9767025" target="_blank"〉PubMed〈/a〉
    Keywords: Forecasting ; Humans ; Life Expectancy/*trends ; *Longevity ; Mortality/*trends
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    Quantum dot bioconjugates for ultrasensitive nonisotopic detection (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-25
    Description: Highly luminescent semiconductor quantum dots (zinc sulfide-capped cadmium selenide) have been covalently coupled to biomolecules for use in ultrasensitive biological detection. In comparison with organic dyes such as rhodamine, this class of luminescent labels is 20 times as bright, 100 times as stable against photobleaching, and one-third as wide in spectral linewidth. These nanometer-sized conjugates are water-soluble and biocompatible. Quantum dots that were labeled with the protein transferrin underwent receptor-mediated endocytosis in cultured HeLa cells, and those dots that were labeled with immunomolecules recognized specific antibodies or antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, W C -- Nie, S -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):2016-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748158" target="_blank"〉PubMed〈/a〉
    Keywords: *Cadmium Compounds/chemistry ; Endocytosis ; *Fluorescent Antibody Technique ; *Fluorescent Dyes ; HeLa Cells ; Humans ; Luminescence ; Molecular Probe Techniques ; Particle Size ; Receptors, Transferrin/metabolism ; *Selenium Compounds/chemistry ; *Semiconductors ; Solubility ; *Sulfides/chemistry ; Transferrin/metabolism ; *Zinc Compounds/chemistry
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    Triplet-repeat transcripts: a role for DNA in disease (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, R H -- New York, N.Y. -- Science. 1998 May 1;280(5364):696-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Structural Biology, Institute for Molecular Medicine, Albert Einstein College of Medicine, Bronx, NY 10461, USA. rhsinger@aecom.yu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9599147" target="_blank"〉PubMed〈/a〉
    Keywords: CELF1 Protein ; Cell Nucleus/metabolism ; Exons ; Humans ; Models, Genetic ; Myotonic Dystrophy/*genetics/metabolism ; Myotonin-Protein Kinase ; Protein Binding ; Protein-Serine-Threonine Kinases/*genetics ; *RNA Splicing ; RNA, Messenger/*genetics ; RNA-Binding Proteins/genetics/*metabolism ; Ribonucleoproteins/genetics/*metabolism ; Transcription, Genetic ; Transfection ; *Trinucleotide Repeats ; Troponin/genetics ; Troponin T
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    Actin mutations in dilated cardiomyopathy, a heritable form of heart failure (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: To test the hypothesis that actin dysfunction leads to heart failure, patients with hereditary idiopathic dilated cardiomyopathy (IDC) were examined for mutations in the cardiac actin gene (ACTC). Missense mutations in ACTC that cosegregate with IDC were identified in two unrelated families. Both mutations affect universally conserved amino acids in domains of actin that attach to Z bands and intercalated discs. Coupled with previous data showing that dystrophin mutations also cause dilated cardiomyopathy, these results raise the possibility that defective transmission of force in cardiac myocytes is a mechanism underlying heart failure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, T M -- Michels, V V -- Thibodeau, S N -- Tai, Y S -- Keating, M T -- 5-P50-HL-53773/HL/NHLBI NIH HHS/ -- M01-RR00064/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1998 May 1;280(5364):750-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Division of Cardiology, University of Utah Health Sciences Center, Salt Lake City, UT 84112, USA. timo@howard.genetics.utah.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563954" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/chemistry/*genetics/physiology ; Adolescent ; Adult ; Cardiomyopathy, Dilated/*genetics/metabolism/pathology ; Child ; Child, Preschool ; Chromosomes, Human, Pair 15 ; Exons ; Female ; Heart/physiopathology ; Humans ; Male ; *Mutation ; Myocardium/chemistry/pathology ; Pedigree ; Phenotype ; Polymorphism, Single-Stranded Conformational ; Protein Conformation ; Sarcomeres/physiology
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    Outcomes research: measuring the end results of health care (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clancy, C M -- Eisenberg, J M -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):245-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Outcomes and Effectiveness Research, U.S. Department of Health and Human Services, Rockville, MD 20852, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841388" target="_blank"〉PubMed〈/a〉
    Keywords: Activities of Daily Living ; Health Status ; Humans ; *Outcome Assessment (Health Care)/trends ; Patient Satisfaction ; Quality of Life ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A closer look at SNPs suggests difficulties (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1787-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776677" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Ethnic Groups/genetics ; *Genetic Markers ; Genetic Predisposition to Disease ; *Genetic Techniques ; Genetic Variation ; *Genetics, Medical ; *Genome, Human ; Humans ; Point Mutation ; *Polymorphism, Genetic ; Recombination, Genetic
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    Ribozyme-mediated repair of sickle beta-globin mRNAs in erythrocyte precursors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: Sickle cell anemia is the most common heritable hematological disease, yet no curative treatment exists for this disorder. Moreover, the intricacies of globin gene expression have made the development of treatments for hemoglobinopathies based on gene therapy difficult. An alternative genetic approach to sickle cell therapy is based on RNA repair. A trans-splicing group I ribozyme was used to alter mutant beta-globin transcripts in erythrocyte precursors derived from peripheral blood from individuals with sickle cell disease. Sickle beta-globin transcripts were converted into messenger RNAs encoding the anti-sickling protein gamma-globin. These results suggest that RNA repair may become a useful approach in the treatment of genetic disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lan, N -- Howrey, R P -- Lee, S W -- Smith, C A -- Sullenger, B A -- HL57606/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1593-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Genetic and Cellular Therapies, Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616120" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*blood/therapy ; Cloning, Molecular ; Erythroid Precursor Cells/*metabolism ; Exons ; Fetal Blood ; Genetic Therapy ; Globins/*genetics ; Humans ; Mutation ; Polymerase Chain Reaction ; *RNA Splicing ; RNA, Catalytic/genetics/*metabolism ; RNA, Messenger/chemistry/*genetics/metabolism ; Transfection ; Uridine/metabolism
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    Progress in progressive hearing loss (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steel, K P -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1870-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council, Institute of Hearing Research, Nottingham NG7 2RD, UK. karen@ihr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9537904" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Carrier Proteins/genetics/physiology ; Cell Differentiation ; Chromosome Mapping ; Chromosomes, Human, Pair 5/genetics ; Deafness/*genetics ; Dyneins ; Female ; Gene Targeting ; Genes, Dominant ; Hair Cells, Auditory/physiology ; Hearing Loss, Sensorineural/*genetics ; Homeodomain Proteins/*genetics/metabolism ; Humans ; Male ; Mice ; Myosins/genetics/physiology ; Pedigree ; Sequence Deletion ; Transcription Factor Brn-3C ; Transcription Factors/*genetics/metabolism/physiology
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    A possible new partner for telomerase (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1395, 1397.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867637" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Aging ; DNA Repair ; DNA Replication ; DNA-Binding Proteins/metabolism ; Humans ; Poly(ADP-ribose) Polymerase Inhibitors ; Poly(ADP-ribose) Polymerases/chemistry/*metabolism ; Telomerase/antagonists & inhibitors/*metabolism ; Telomere/*metabolism
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    Progress in the development of an HIV-1 vaccine (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-25
    Description: Containment of the acquired immunodeficiency syndrome (AIDS) epidemic will require an effective human immunodeficiency virus type 1 (HIV-1) vaccine. Accumulating evidence suggests that such a vaccine must efficiently elicit an HIV-1-specific cytotoxic T lymphocyte (CTL) response. Nonhuman primate models will continue to provide an important tool for assessing the extent of protective immunity induced by various immunization strategies. Although replication-competent AIDS viruses attenuated for pathogenicity by selective gene deletions have provided protective immunity in nonhuman primate models, the long-term safety of such vaccines in human populations is suspect. Inactivated virus and subunit vaccines have elicited neither CTLs nor antibodies capable of neutralizing a wide array of patient HIV-1 isolates. Considerable effort is now being focused on evaluating live vector-based vaccine and plasmid DNA vaccine approaches for preventing HIV-1 infection both in animal model and human studies. Our growing understanding of the biology of HIV-1 and immune responses to this virus will continue to suggest improved vaccination approaches for exploration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Letvin, N L -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1875-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The author is at Harvard Medical School, Beth Israel Deaconess Medical Center, Boston, MA 02215, USA. nletvin@bidmc.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9632379" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/immunology ; Animals ; Disease Models, Animal ; Genetic Vectors ; HIV Infections/immunology/*prevention & control/therapy/virology ; HIV-1/*immunology/physiology ; Humans ; T-Lymphocytes, Cytotoxic/immunology ; Vaccines, Attenuated/immunology ; Vaccines, DNA/immunology ; Vaccines, Inactivated/immunology ; Vaccines, Synthetic/immunology ; Virus Replication
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    The transcriptional program of sporulation in budding yeast (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: Diploid cells of budding yeast produce haploid cells through the developmental program of sporulation, which consists of meiosis and spore morphogenesis. DNA microarrays containing nearly every yeast gene were used to assay changes in gene expression during sporulation. At least seven distinct temporal patterns of induction were observed. The transcription factor Ndt80 appeared to be important for induction of a large group of genes at the end of meiotic prophase. Consensus sequences known or proposed to be responsible for temporal regulation could be identified solely from analysis of sequences of coordinately expressed genes. The temporal expression pattern provided clues to potential functions of hundreds of previously uncharacterized genes, some of which have vertebrate homologs that may function during gametogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chu, S -- DeRisi, J -- Eisen, M -- Mulholland, J -- Botstein, D -- Brown, P O -- Herskowitz, I -- AI18738/AI/NIAID NIH HHS/ -- GH00450/GH/CGH CDC HHS/ -- GM46406/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):699-705.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784122" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes, Fungal/physiology ; *DNA-Binding Proteins ; Fungal Proteins/genetics/metabolism ; *Gene Expression Regulation, Fungal ; Genes, Fungal ; Genome, Fungal ; Humans ; Meiosis/*genetics ; Morphogenesis ; Organelles/ultrastructure ; Saccharomyces cerevisiae/*genetics/physiology ; *Saccharomyces cerevisiae Proteins ; Spores, Fungal/*genetics/physiology/ultrastructure ; Transcription Factors/genetics/metabolism ; *Transcription, Genetic
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    Mitochondria and apoptosis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: A variety of key events in apoptosis focus on mitochondria, including the release of caspase activators (such as cytochrome c), changes in electron transport, loss of mitochondrial transmembrane potential, altered cellular oxidation-reduction, and participation of pro- and antiapoptotic Bcl-2 family proteins. The different signals that converge on mitochondria to trigger or inhibit these events and their downstream effects delineate several major pathways in physiological cell death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, D R -- Reed, J C -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1309-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉La Jolla Institute for Allergy and Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721092" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cysteine Endopeptidases/metabolism ; Cytochrome c Group/metabolism ; Electron Transport ; Humans ; Intracellular Membranes/metabolism ; Ion Channels/metabolism ; Membrane Potentials ; Mitochondria/*metabolism ; Oxidation-Reduction ; Permeability ; Proto-Oncogene Proteins c-bcl-2/metabolism
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    Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: Protein kinase B (PKB) is activated in response to phosphoinositide 3-kinases and their lipid products phosphatidylinositol 3,4, 5-trisphosphate [PtdIns(3,4,5)P3] and PtdIns(3,4)P2 in the signaling pathways used by a wide variety of growth factors, antigens, and inflammatory stimuli. PKB is a direct target of these lipids, but this regulation is complex. The lipids can bind to the pleckstrin homologous domain of PKB, causing its translocation to the membrane, and also enable upstream, Thr308-directed kinases to phosphorylate and activate PKB. Four isoforms of these PKB kinases were purified from sheep brain. They bound PtdIns(3,4,5)P3 and associated with lipid vesicles containing it. These kinases contain an NH2-terminal catalytic domain and a COOH-terminal pleckstrin homologous domain, and their heterologous expression augments receptor activation of PKB, which suggests they are the primary signal transducers that enable PtdIns(3,4,5)P3 or PtdIns- (3,4)P2 to activate PKB and hence to control signaling pathways regulating cell survival, glucose uptake, and glycogen metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stephens, L -- Anderson, K -- Stokoe, D -- Erdjument-Bromage, H -- Painter, G F -- Holmes, A B -- Gaffney, P R -- Reese, C B -- McCormick, F -- Tempst, P -- Coadwell, J -- Hawkins, P T -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):710-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Inositide Laboratory, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445477" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/enzymology ; Cloning, Molecular ; DNA, Complementary ; Drosophila ; Drosophila Proteins ; Enzyme Activation ; Humans ; Liposomes/metabolism ; Molecular Sequence Data ; Open Reading Frames ; Phosphatidylinositol Phosphates/*metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Protein-Serine-Threonine Kinases/chemistry/genetics/isolation & ; purification/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Recombinant Proteins/metabolism ; Sheep ; *Signal Transduction
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    Human monogamy (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, G A -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1047-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Culture ; Female ; Hominidae/psychology ; Humans ; Male ; *Sexual Behavior ; Sexual Behavior, Animal ; *Sexual Partners
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    Association of malaria parasite population structure, HLA, and immunological antagonism (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: Host-parasite coevolution has been likened to a molecular arms race, with particular parasite genes evolving to evade specific host defenses. Study of the variants of an antigenic epitope of Plasmodium falciparum that induces a cytotoxic T cell response supports this view. In African children with malaria, the variants present are influenced by the presence of a human leukocyte antigen (HLA) type that restricts the immune response to this epitope. The distribution of parasite variants may be further influenced by the ability of cohabiting parasite strains to facilitate each other's survival by down-regulating cellular immune responses, using altered peptide ligand antagonism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilbert, S C -- Plebanski, M -- Gupta, S -- Morris, J -- Cox, M -- Aidoo, M -- Kwiatkowski, D -- Greenwood, B M -- Whittle, H C -- Hill, A V -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1173-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Windmill Road, Oxford OX3 7BN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469800" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Antigens, Protozoan/genetics/*immunology ; Biological Evolution ; Child ; Epitopes ; Evolution, Molecular ; Gambia ; Genes, Protozoan ; Genetic Variation ; HLA-B35 Antigen/*immunology ; Humans ; Ligands ; Malaria, Falciparum/*immunology/parasitology ; Models, Biological ; Plasmodium falciparum/genetics/*immunology ; Protozoan Proteins/genetics/*immunology ; T-Lymphocytes, Cytotoxic/*immunology
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    Stabilization of interleukin-2 mRNA by the c-Jun NH2-terminal kinase pathway (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-25
    Description: Signaling pathways that stabilize interleukin-2 (IL-2) messenger RNA (mRNA) in activated T cells were examined. IL-2 mRNA contains at least two cis elements that mediated its stabilization in response to different signals, including activation of c-Jun amino-terminal kinase (JNK). This response was mediated through a cis element encompassing the 5' untranslated region (UTR) and the beginning of the coding region. IL-2 transcripts lacking this 5' element no longer responded to JNK activation but were still responsive to other signals generated during T cell activation, which were probably sensed through the 3' UTR. Thus, multiple elements within IL-2 mRNA modulate its stability in a combinatorial manner, and the JNK pathway controls turnover as well as synthesis of IL-2 mRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, C Y -- Del Gatto-Konczak, F -- Wu, Z -- Karin, M -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1945-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9632395" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD28/immunology ; Antigens, CD3/immunology ; Calcimycin/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Cyclosporine/pharmacology ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; *Gene Expression Regulation ; Humans ; Imidazoles/pharmacology ; Interleukin-2/*genetics ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Lymphocyte Activation ; MAP Kinase Kinase 1 ; MAP Kinase Kinase 7 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Pyridines/pharmacology ; RNA, Messenger/chemistry/genetics/*metabolism ; Signal Transduction ; T-Lymphocytes/immunology/*metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transgenes ; p38 Mitogen-Activated Protein Kinases
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    Classical conditioning and brain systems: the role of awareness (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-29
    Description: Classical conditioning of the eye-blink response, perhaps the best studied example of associative learning in vertebrates, is relatively automatic and reflexive, and with the standard procedure (simple delay conditioning), it is intact in animals with hippocampal lesions. In delay conditioning, a tone [the conditioned stimulus (CS)] is presented just before an air puff to the eye [the unconditioned stimulus (US)]. The US is then presented, and the two stimuli coterminate. In trace conditioning, a variant of the standard paradigm, a short interval (500 to 1000 ms) is interposed between the offset of the CS and the onset of the US. Animals with hippocampal lesions fail to acquire trace conditioning. Amnesic patients with damage to the hippocampal formation and normal volunteers were tested on two versions of delay conditioning and two versions of trace conditioning and then assessed for the extent to which they became aware of the temporal relationship between the CS and the US. Amnesic patients acquired delay conditioning at a normal rate but failed to acquire trace conditioning. For normal volunteers, awareness was unrelated to successful delay conditioning but was a prerequisite for successful trace conditioning. Trace conditioning is hippocampus dependent because, as in other tasks of declarative memory, conscious knowledge must be acquired across the training session. Trace conditioning may provide a means for studying awareness in nonhuman animals, in the context of current ideas about multiple memory systems and the function of the hippocampus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, R E -- Squire, L R -- 24600/PHS HHS/ -- New York, N.Y. -- Science. 1998 Apr 3;280(5360):77-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9525860" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Amnesia/*physiopathology/psychology ; Awareness/*physiology ; Blinking ; Cerebellum/physiology/physiopathology ; Conditioning, Classical/*physiology ; Female ; Hippocampus/*physiology/physiopathology ; Humans ; Learning/physiology ; Male ; Memory/*physiology ; Middle Aged ; Neocortex/physiology/physiopathology
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    The ethics of AIDS vaccine trials (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zion, D -- New York, N.Y. -- Science. 1998 May 29;280(5368):1329-30; author reply 1330-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9634405" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines ; Acquired Immunodeficiency Syndrome/prevention & control ; Clinical Trials as Topic/*standards ; Controlled Clinical Trials as Topic/*standards ; Developed Countries ; Developing Countries ; *Ethics, Medical ; Humans ; Informed Consent
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    Genetic dissection of a mammalian replicator in the human beta-globin locus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-14
    Description: The timing and localization of DNA replication initiation in mammalian cells are heritable traits, but it is not known whether initiation requires specific DNA sequences. A site-specific recombination strategy was used to show that DNA sequences previously identified as replication initiation sites could initiate replication when transferred to new chromosomal locations. An 8-kilobase DNA sequence encompassing the origin of DNA replication in the human beta-globin locus initiated replication in the simian genome. Specific deletions within the globin origin did not initiate replication in these chromosomal sites. These data suggest that initiation of DNA replication in mammalian cells requires specific sequence information and extend the replicon hypothesis to higher eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aladjem, M I -- Rodewald, L W -- Kolman, J L -- Wahl, G M -- CA48405/CA/NCI NIH HHS/ -- GM51104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 14;281(5379):1005-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, The Salk Institute, San Diego, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9703500" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cercopithecus aethiops ; DNA/genetics ; DNA Nucleotidyltransferases/metabolism ; *DNA Replication ; Gene Targeting ; Globins/*genetics ; Humans ; Integrases/metabolism ; Polymerase Chain Reaction ; *Replication Origin ; S Phase ; Sequence Deletion ; *Viral Proteins
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    Regulation of the proinflammatory effects of Fas ligand (CD95L) (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-30
    Description: Fas ligand (CD95L) inhibits T cell function in immune-privileged organs such as the eye and testis, yet in most tissues CD95L expression induces potent inflammatory responses. With a stably transfected colon carcinoma cell line, CT26-CD95L, the molecular basis for these divergent responses was defined. When injected subcutaneously, rejection of CT26-CD95L was caused by neutrophils activated by CD95L. CT26-CD95L survived in the intraocular space because of the presence of transforming growth factor-beta (TGF-beta), which inhibited neutrophil activation. Providing TGF-beta to subcutaneous sites protected against tumor rejection. Thus, these cytokines together generate a microenvironment that promotes immunologic tolerance, which may aid in the amelioration of allograft rejection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J J -- Sun, Y -- Nabel, G J -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1714-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Michigan Medical Center, Departments of Internal Medicine and Biological Chemistry, 1150 West Medical Center Drive, 4520 Medical Science Research Building I, Ann Arbor, MI 48109-0650, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831564" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anterior Chamber ; Apoptosis ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Cytotoxicity, Immunologic ; Fas Ligand Protein ; Female ; Graft Rejection ; Humans ; Immune Tolerance ; Inflammation/*immunology ; Jurkat Cells ; Membrane Glycoproteins/*physiology ; Mice ; Mice, Inbred BALB C ; *Mitogen-Activated Protein Kinases ; Neoplasm Transplantation ; Neoplasms, Experimental/*immunology/pathology ; *Neutrophil Activation ; Neutrophils/immunology ; Transfection ; Transforming Growth Factor beta/pharmacology ; Tumor Cells, Cultured ; p38 Mitogen-Activated Protein Kinases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    BSE and prions: uncertainties about the agent (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chesebro, B -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):42-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Persistent Virus Diseases, Rocky Mountain Laboratories, Hamilton, MT 59840, USA. bchesebro@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9441410" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/chemistry ; Amyloidosis/metabolism ; Animals ; Cattle ; Creutzfeldt-Jakob Syndrome/epidemiology/*etiology/transmission ; Disease Susceptibility ; Encephalopathy, Bovine Spongiform/epidemiology/*etiology/transmission ; Gene Expression ; Great Britain/epidemiology ; Humans ; Mice ; Mice, Transgenic ; Mutation ; Prion Diseases/*etiology/transmission ; Prions/chemistry/genetics/metabolism/*pathogenicity ; Virus Physiological Phenomena ; Viruses/pathogenicity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 82
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    Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: A large protein complex mediates the phosphorylation of the inhibitor of kappaB (IkappaB), which results in the activation of nuclear factor kappaB (NF-kappaB). Two subunits of this complex, IkappaB kinase alpha (IKKalpha) and IkappaB kinase beta (IKKbeta), are required for NF-kappaB activation. Purified recombinant IKKalpha and IKKbeta expressed in insect cells were used to demonstrate that each protein can directly phosphorylate IkappaB proteins. IKKalpha and IKKbeta were found to form both homodimers and heterodimers. Both IKKalpha and IKKbeta phosphorylated IkappaB bound to NF-kappaB more efficiently than they phosphorylated free IkappaB. This result explains how free IkappaB can accumulate in cells in which IKK is still active and thus can contribute to the termination of NF-kappaB activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zandi, E -- Chen, Y -- Karin, M -- AI 43477/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1360-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Dimerization ; Enzyme Activation ; HeLa Cells ; Helix-Loop-Helix Motifs ; Humans ; I-kappa B Kinase ; Leucine Zippers ; Mutation ; NF-kappa B/antagonists & inhibitors/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Spodoptera ; Transcription Factor RelB ; *Transcription Factors
    Print ISSN: 0036-8075
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  • 83
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    Inducible repair of thymine glycol detected by an ultrasensitive assay for DNA damage (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-06
    Description: An ultrasensitive assay for measuring DNA base damage is described that couples immunochemical recognition with capillary electrophoresis and laser-induced fluorescence detection. The method provides a detection limit of 3 x 10(-21) moles, an improvement of four to five orders of magnitude over current methods. Induction and repair of thymine glycols were studied in irradiated A549 cells (a human lung carcinoma cell line). Exposure of these cells to a low dose of radiation (0.25 Gray) 4 hours before a clinically relevant dose (2 Gray) enhanced removal of thymine glycols after the higher dose. These data provide evidence for an inducible repair response for radiation-induced damage to DNA bases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Le, X C -- Xing, J Z -- Lee, J -- Leadon, S A -- Weinfeld, M -- CA40453/CA/NCI NIH HHS/ -- CA62059/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 May 15;280(5366):1066-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Public Health Sciences, Faculty of Medicine and Oral Health Sciences, University of Alberta, Edmonton, Alberta, T6G 2G3, Canada. xc.le@ualberta.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9582118" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Bromodeoxyuridine/immunology ; *DNA Damage ; *DNA Repair ; DNA, Neoplasm/metabolism/radiation effects ; Dose-Response Relationship, Radiation ; Electrophoresis, Capillary ; Humans ; Radiation, Ionizing ; Thymine/*analogs & derivatives/analysis/immunology/metabolism ; Tumor Cells, Cultured
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  • 84
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    The Bcl-2 protein family: arbiters of cell survival (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-12
    Description: Bcl-2 and related cytoplasmic proteins are key regulators of apoptosis, the cell suicide program critical for development, tissue homeostasis, and protection against pathogens. Those most similar to Bcl-2 promote cell survival by inhibiting adapters needed for activation of the proteases (caspases) that dismantle the cell. More distant relatives instead promote apoptosis, apparently through mechanisms that include displacing the adapters from the pro-survival proteins. Thus, for many but not all apoptotic signals, the balance between these competing activities determines cell fate. Bcl-2 family members are essential for maintenance of major organ systems, and mutations affecting them are implicated in cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adams, J M -- Cory, S -- CA43540/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1322-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Walter and Eliza Institute of Medical Research, Post Office Royal Melbourne Hospital, Victoria 3050, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735050" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Cycle ; *Cell Survival ; Cysteine Endopeptidases/metabolism ; Cytokines/physiology ; Genes, bcl-2 ; Humans ; Neoplasms/etiology/pathology/therapy ; Organelles/physiology ; Proto-Oncogene Proteins c-bcl-2/chemistry/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 85
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    Cell death in us and others (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golstein, P -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1283.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735040" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; *Cell Death ; Cysteine Endopeptidases/metabolism ; Fungi/cytology ; Humans ; Plant Cells
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 86
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    Tobacco: who pays whom? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gori, G B -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1805-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776683" target="_blank"〉PubMed〈/a〉
    Keywords: *Conflict of Interest ; Humans ; Lung Neoplasms/etiology ; *Tobacco Industry ; Tobacco Smoke Pollution/*adverse effects ; United States ; *United States Environmental Protection Agency
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  • 87
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    Early education of the deaf (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adler, H J -- Liebman, J -- Raphael, R M -- Ratnanather, J T -- Steyger, P S -- New York, N.Y. -- Science. 1998 Mar 13;279(5357):1617.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9518371" target="_blank"〉PubMed〈/a〉
    Keywords: Child ; *Correction of Hearing Impairment ; Deafness/*genetics/*rehabilitation/therapy ; *Education of Hearing Disabled ; *Education, Special ; Humans ; Lipreading ; Persons With Hearing Impairments/rehabilitation ; Sign Language ; Speech Therapy
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  • 88
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    Elimination of syphilis in the United States (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St Louis, M E -- Wasserheit, J N -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):353-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for HIV, STD, and TB Prevention, Centers for Disease Control and Prevention, Mailstop E-02, Atlanta, GA 30333, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9705711" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS-Related Opportunistic Infections/prevention & control ; Adult ; African Americans ; Disease Outbreaks ; Female ; Genome, Bacterial ; HIV Infections/transmission ; Humans ; Infant, Newborn ; Male ; Public Health Practice ; Socioeconomic Factors ; Syphilis/complications/epidemiology/*prevention & control ; Syphilis, Congenital/epidemiology ; Treponema pallidum/genetics ; United States/epidemiology
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  • 89
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    Cocaine exposure and children: the meaning of subtle effects (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lester, B M -- LaGasse, L L -- Seifer, R -- U10 DA024119/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):633-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brown University School of Medicine, Providence, RI 02905-2499, USA. barryvlester@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841414" target="_blank"〉PubMed〈/a〉
    Keywords: Child ; Child Language ; Cocaine/*adverse effects ; Cocaine-Related Disorders/therapy ; Cognition Disorders/*chemically induced/prevention & control ; Costs and Cost Analysis ; Education, Special/economics ; Female ; Humans ; Intelligence/*drug effects ; Language Disorders/*chemically induced/prevention & control ; Meta-Analysis as Topic ; Pregnancy ; Pregnancy Complications/therapy ; *Prenatal Exposure Delayed Effects
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  • 90
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    AIDS vaccine development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agosto, M -- Allan, J -- Benson, C -- Berger, E A -- Blumenthal, R -- Burton, D -- Clements, J -- Coffin, J -- Connor, R -- Cullen, B -- Desrosiers, R -- Dimitrov, D -- Doms, R -- Emerman, M -- Feinberg, M -- Fultz, P -- Gerard, C -- Gonsalves, G -- Haase, A -- Haigwood, N -- Hirsch, V -- Ho, D -- Hoxie, J A -- Hu, S L -- Zingale, D -- New York, N.Y. -- Science. 1998 May 8;280(5365):803, 804-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9599148" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/immunology ; Acquired Immunodeficiency Syndrome/prevention & control ; *Clinical Trials as Topic ; HIV Envelope Protein gp120/immunology ; HIV-1/immunology ; Humans ; National Institutes of Health (U.S.) ; United States
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  • 91
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    AIDS vaccine development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, J P -- New York, N.Y. -- Science. 1998 May 8;280(5365):806-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9599149" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/immunology ; Acquired Immunodeficiency Syndrome/immunology/prevention & control ; Animals ; *Clinical Trials as Topic ; HIV/immunology ; HIV Antibodies/biosynthesis/immunology ; Humans ; Immunity, Cellular ; Immunity, Mucosal ; Neutralization Tests
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    More deafness genes (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steel, K P -- Brown, S D -- New York, N.Y. -- Science. 1998 May 29;280(5368):1403.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council, Institute of Hearing Research, University Park, Nottingham NG7 2RD, UK. karen@ihr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9634418" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Animals ; Cilia/physiology ; Deafness/*genetics ; Dyneins ; Extracellular Matrix Proteins/*genetics/physiology ; GPI-Linked Proteins ; Hair Cells, Auditory/physiology/ultrastructure ; Hearing ; Humans ; Membrane Glycoproteins/*genetics/physiology ; Mice ; Mice, Mutant Strains ; Mutation ; Myosin Heavy Chains/genetics/physiology ; Myosins/*genetics/physiology ; Tectorial Membrane/physiology
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  • 93
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    Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: Analysis of the 1,042,519-base pair Chlamydia trachomatis genome revealed unexpected features related to the complex biology of chlamydiae. Although chlamydiae lack many biosynthetic capabilities, they retain functions for performing key steps and interconversions of metabolites obtained from their mammalian host cells. Numerous potential virulence-associated proteins also were characterized. Several eukaryotic chromatin-associated domain proteins were identified, suggesting a eukaryotic-like mechanism for chlamydial nucleoid condensation and decondensation. The phylogenetic mosaic of chlamydial genes, including a large number of genes with phylogenetic origins from eukaryotes, implies a complex evolution for adaptation to obligate intracellular parasitism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stephens, R S -- Kalman, S -- Lammel, C -- Fan, J -- Marathe, R -- Aravind, L -- Mitchell, W -- Olinger, L -- Tatusov, R L -- Zhao, Q -- Koonin, E V -- Davis, R W -- AI 39258/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):754-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Infectious Diseases, University of California, Berkeley, CA 94720, USA. ctgenome@socrates.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784136" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Amino Acid Sequence ; Amino Acids/biosynthesis ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Proteins/chemistry/genetics ; Biological Evolution ; Chlamydia trachomatis/classification/*genetics/metabolism/physiology ; DNA Repair ; Energy Metabolism ; Enzymes/chemistry/genetics ; *Genome, Bacterial ; Humans ; Lipids/biosynthesis ; Molecular Sequence Data ; Peptidoglycan/biosynthesis/genetics ; Phylogeny ; Protein Biosynthesis ; Recombination, Genetic ; *Sequence Analysis, DNA ; Transcription, Genetic ; Transformation, Bacterial ; Virulence
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  • 94
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    Human Genome Project: data quality (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, P -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1115-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9508680" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Simulation ; *Human Genome Project ; Humans ; Quality Control ; Reference Standards ; Sequence Analysis, DNA/*standards
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  • 95
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    How a growth control path takes a wrong turn to cancer (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1438-9, 1441.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9750112" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Animals ; Cadherins/metabolism ; Cell Nucleus/metabolism ; Colorectal Neoplasms/etiology/genetics ; Cytoskeletal Proteins/metabolism ; *Gene Expression Regulation, Neoplastic ; *Genes, APC ; *Genes, myc ; Humans ; Neoplasms/*etiology/genetics ; Proto-Oncogene Proteins/*genetics/physiology ; Proto-Oncogene Proteins c-myc/metabolism ; Signal Transduction ; *Trans-Activators ; Transcription Factors/metabolism ; Wnt Proteins ; *Zebrafish Proteins ; beta Catenin
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  • 96
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    How the genome readies itself for evolution (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1131,1133-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735027" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA Repair ; DNA Transposable Elements ; *Evolution, Molecular ; Exons ; Gene Rearrangement ; *Genome ; Humans ; Micronuclei, Chromosome-Defective/genetics ; Multigene Family ; Mutation ; Plants/genetics ; Repetitive Sequences, Nucleic Acid
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  • 97
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    Kaposi's sarcoma and protection from HIV dementia (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liestael, K -- Goplen, A K -- Dunlop, O -- Bruun, J N -- Maehlen, J -- New York, N.Y. -- Science. 1998 Apr 17;280(5362):361-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9575077" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Dementia Complex/*prevention & control ; AIDS-Related Opportunistic Infections/*immunology/virology ; Chemokines/*metabolism ; Confounding Factors (Epidemiology) ; HIV-1/*metabolism ; Herpesvirus 8, Human/immunology/metabolism ; Humans ; Microglia/metabolism/*virology ; Receptors, CCR3 ; Receptors, Chemokine/metabolism ; Receptors, HIV/metabolism ; Regression Analysis ; Sarcoma, Kaposi/*immunology/virology
    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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  • 98
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    Specific covalent labeling of recombinant protein molecules inside live cells (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-10
    Description: Recombinant proteins containing four cysteines at the i, i + 1, i + 4, and i + 5 positions of an alpha helix were fluorescently labeled in living cells by extracellular administration of 4',5'-bis(1,3, 2-dithioarsolan-2-yl)fluorescein. This designed small ligand is membrane-permeant and nonfluorescent until it binds with high affinity and specificity to the tetracysteine domain. Such in situ labeling adds much less mass than does green fluorescent protein and offers greater versatility in attachment sites as well as potential spectroscopic and chemical properties. This system provides a recipe for slightly modifying a target protein so that it can be singled out from the many other proteins inside live cells and fluorescently stained by small nonfluorescent dye molecules added from outside the cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Griffin, B A -- Adams, S R -- Tsien, R Y -- NS27177/NS/NINDS NIH HHS/ -- T32 CA09523/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 10;281(5374):269-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA 92093-0647, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9657724" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/chemistry/genetics/metabolism ; Cell Membrane Permeability ; Cell Survival ; Cysteine/*chemistry ; Energy Transfer ; Ethylene Glycol ; Fluoresceins/chemical synthesis/chemistry/*metabolism ; Fluorescence ; *Fluorescent Dyes ; Green Fluorescent Proteins ; HeLa Cells ; Humans ; Jurkat Cells ; Ligands ; Luminescent Proteins/chemistry/genetics/metabolism ; Molecular Sequence Data ; Organometallic Compounds/chemical synthesis/chemistry/*metabolism ; Peptides/chemistry/*metabolism ; Protein Structure, Secondary ; Recombinant Proteins/chemistry/*metabolism ; Spectrometry, Fluorescence ; Transfection
    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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  • 99
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    Quantitation of transcription and clonal selection of single living cells with beta-lactamase as reporter (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: Gene expression was visualized in single living mammalian cells with beta-lactamase as a reporter that hydrolyzes a substrate loaded intracellularly as a membrane-permeant ester. Each enzyme molecule changed the fluorescence of many substrate molecules from green to blue by disrupting resonance energy transfer. This wavelength shift was detectable by eye or color film in individual cells containing less than 100 beta-lactamase molecules. The robust change in emission ratio reveals quantitative heterogeneity in real-time gene expression, enables clonal selection by flow cytometry, and forms a basis for high-throughput screening of pharmaceutical candidate drugs in living mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zlokarnik, G -- Negulescu, P A -- Knapp, T E -- Mere, L -- Burres, N -- Feng, L -- Whitney, M -- Roemer, K -- Tsien, R Y -- NS27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):84-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aurora Biosciences, 11010 Torreyana Road, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417030" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Separation/methods ; Clone Cells/*metabolism ; DNA-Binding Proteins/genetics/metabolism ; Drug Evaluation, Preclinical ; Energy Transfer ; Flow Cytometry ; Fluoresceins/metabolism ; Fluorescent Dyes/metabolism ; *Gene Expression ; *Genes, Reporter ; Half-Life ; Humans ; *Lactams ; Muscarinic Agonists/pharmacology ; Muscarinic Antagonists/pharmacology ; NFATC Transcription Factors ; *Nuclear Proteins ; Sensitivity and Specificity ; Spectrometry, Fluorescence ; Transcription Factors/genetics/metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; Umbelliferones/metabolism ; beta-Lactamases/*genetics/metabolism ; beta-Lactams/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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  • 100
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    Unknown
    Mercury in fish (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarkson, T -- Cox, C -- Davidson, P W -- Myers, G J -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):459, 461.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454336" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Child ; *Fishes ; *Food Contamination ; Humans ; Iraq ; Maximum Allowable Concentration ; Methylmercury Compounds/administration & dosage/*adverse effects/analysis ; *Nutrition Policy ; Seychelles ; United States ; United States Environmental Protection Agency ; World Health Organization
    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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