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  • 1
    Electronic Resource
    Electronic Resource
    Reaction of (bromoacetamido)nucleoside affinity labels with ribonuclease A: evidence for steric control of reaction specificity and alkylation rate (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 135-146 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00375a020
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  • 2
    Electronic Resource
    Electronic Resource
    Genetic Testing in the Workplace: Ethical, Legal, and Social Implications (2004)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Public Health 25 (2004), S. 139-153 
    Details
    ISSN: 0163-7525
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine
    Notes: With the completion of the Human Genome Project, it is likely that genetic testing for susceptibility to a wide range of diseases will increase in society. One venue for such increased testing is likely to be the workplace as employers attempt to protect workers from unhealthy gene-environment interactions, improve productivity, and control escalating health care costs. Past and recent examples of genetic testing in the workplace raise serious concerns that such testing could pose a significant threat to workers' privacy, autonomy, and dignity. Thus, defining the ethically, legally, and socially appropriate and inappropriate uses of genetic testing in the workplace presents a major challenge for occupational health professionals in the years ahead.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.publhealth.25.101802.123012
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  • 3
    Electronic Resource
    Electronic Resource
    The High-Risk Occupational Disease Notification and Prevention Act (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 572 (1989), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1989.tb13591.x
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  • 4
    Electronic Resource
    Electronic Resource
    Oncogene proteins as biomarkers in the molecular epidemiology of occupational carcinogenesis (1991)
    Springer
    International archives of occupational and environmental health 63 (1991), S. 1-8 
    Details
    ISSN: 1432-1246
    Keywords: Oncogenes ; Biomarkers ; Molecular epidemiology ; Occupational cancer ; Ras gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The use of oncogene proteins as biomarkers offers a new approach to the molecular epidemiologic evaluation of occupational carcinogenesis. The ras oncogene-encoded p21 protein represents a prototype for this type of study, since it is known to be activated by common occupational carcinogens, is frequently found in human tumors of occupational concern, and, at least in certain instances, appears to be expressed relatively early in the disease process, allowing the possibility of early detection and intervention. Herein, we review our experience with the use of immunologic detection of p21 in cohorts with cancer or at risk for the development of cancer due to their occupational exposures. The results suggest that p21 (particularly when used with other oncoproteins and biomarkers such as PAH-DNA adducts) will indeed be a useful addition to the growing armamentarium of molecular epidemiologic biomarkers in the study of occupational carcinogenic mechanisms and in the detection and prevention of occupational cancers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406190
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  • 5
    Electronic Resource
    Electronic Resource
    Mutant c-Ki-ras p21 protein in chemical carcinogenesis in humans exposed to vinyl chloride (1994)
    Springer
    Cancer causes & control 5 (1994), S. 273-278 
    Details
    ISSN: 1573-7225
    Keywords: Angiosarcoma of the liver ; chemical carcinogenesis ; p21 protein ; ras gene ; serum biomarker ; vinyl chloride
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Mutations inras oncogenes and expression of their encoded p21 protein products are believed to play an important role in carcinogenesis in humans. Detection of mutant p21 proteins in serum may be a useful molecular epidemiologic biomarker with which to study this process, and workers with heavy exposure to vinyl chloride (VC) represent a model population for such study. We studied the occurrence of a specificras mutation (Asp 13 c-Ki-ras) by oligonucleotide hybridization and the expression of the corresponding p21 protein in tumor tissue and serum by immunohistochemistry and immunoblotting with monoclonal antibodies in five individuals with heavy exposure to VC and resultant angiosarcomas of the liver (ASL). Four of five (80 percent) of the cases of ASL were found to contain the mutation and to express the corresponding mutant protein in their tumor tissue and serum. Serum expression of the mutant protein also was examined in nine VC-exposed workers with liver angiomas and 45 VC-exposed workers with no evidence of liver neoplasia; eight of nine (89 percent) of the former and 22 of 45 (49 percent) of the latter were also positive for the mutant p21 in their serum. However, serum immunoblotting results for 28 age-gender-race matched, unexposed controls were all negative. Stratification by years of VC exposure showed a significant linear trend (P〈10−5) for the occurrence of the serum mutant p21 protein with increasing duration of exposure. These results suggest that detection of serum mutant p21 protein can be a valid surrogate forras gene expression at the tissue level. Further, serum mutant p21 may be a useful molecular epidemiologic biomarker for the study of chemical carcinogenesis in humans exposed to VC and possibly for the study of other mutantras-related human cancers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01830248
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  • 6
    Electronic Resource
    Electronic Resource
    An activating amino acid substitution in the c-abl oncogene protein fails to produce a local conformational change (1991)
    Springer
    The protein journal 10 (1991), S. 437-441 
    Details
    ISSN: 1573-4943
    Keywords: Conformational energy ; three-dimensional structure ; amino acid substitution ; c-abl oncogene ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Thebcr-abl chimeric gene of Philadelphia chromosome positive chronic myelogenous leukemias is only weakly transforming. This transformation activity is greatly enhanced by a Lys-for-Glu substitution at position 832 in the c-abl gene, as occurs in the highly transforming v-abl genes. It has been suggested that this mutation results in a significant structural change in the encoded protein product. Using conformational energy analysis, we have determined the allowed low-energy conformations for residues 828–836 of this protein with Lys and Glu at position 832. In both cases, the overwhelmingly preferred conformation for this region is a bend-helix motif. The helix terminates at residue 836, and there are no discernible differences in conformation between the Lys- and Glu-containing sequences. These results suggest that the activating amino acid substitution at position 832 in the c-abl protein product does not produce its effect via a local conformational change.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025258
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  • 7
    Electronic Resource
    Electronic Resource
    Conformation of the transmembrane domain of the c-erbB-2 oncogene-encoded protein in its monomeric and dimeric states (1995)
    Springer
    The protein journal 14 (1995), S. 33-40 
    Details
    ISSN: 1573-4943
    Keywords: c-erbB-2 ; transmembrane domain ; conformational energy analysis ; structurefunction relations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The human c-erbB-2 oncogene is homologous to the ratneu oncogene, both encoding transmembrane growth factor receptors. Overexpression and point mutations in the transmembrane domain of the encoded proteins in both cases have been implicated in cell transformation and carcinogenesis. In the case of theneu protein, it has been proposed that these effects are mediated by conformational preferences for anα-helix in the transmembrane domain, which facilitates receptor dimerization, an important step in the signal transduction process. To examine whether this is the case for c-erbB-2 as well, we have used conformational energy analysis to determine the preferred three-dimensional structures for the transmembrane domain of the c-erbB-2 protein from residues 650 to 668 with Val (nontransforming) and Glu (transforming) at position 659. The global minimum energy conformation for the Val-659 peptide from the normal, nontransforming protein was found to contain several bends, whereas the global minimum energy conformation for Glu-659 peptide from the mutant, transforming protein was found to beα-helical. Thus, the difference in conformational preferences for these transmembrane domains may explain the difference in transforming ability of these proteins. The presence of higher-energyα-helical conformations for the transmembrane domain from the normal Val-659 protein may provide an explanation for the presence of a transforming effect from overexpression of c-erbB-2. In addition, docking of the oncogenic sequences in theirα-helical and bend conformations shows that the all-α-helical dimer is clearly favored energetically over the bend dimer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01902842
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  • 8
    Electronic Resource
    Electronic Resource
    Conformational effects in the p53 protein of mutations induced during chemical carcinogenesis: Molecular dynamic and immunologic analyses (1996)
    Springer
    The protein journal 15 (1996), S. 367-375 
    Details
    ISSN: 1573-4943
    Keywords: p53 ; mutation ; vinyl chloride ; molecular dynamics ; immunohistochemistry ; angiosarcoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The tumor suppressor gene p53 has been identified as the most frequent target of genetic alterations in human cancers. Vinyl chloride, a known human carcinogen that induces the rare sentinel neoplasm angiosarcoma of the liver, has been associated with specific A → T transversions at the first base of codons 249 and 255 of the p53 gene. These mutations result in an Arg→Trp amino acid substitution at residue 249 and an Ile→Phe amino acid substitution at residue 255 in a highly conserved region in the DNA-binding core domain of the p53 protein. To determine the effects of these substitutions on the three-dimensional structure of the p53 protein, we have performed molecular dynamics calculations on this core domain of the wild-type and the Trp-249 and Phe-255 mutants to compute the average structures of each of the three forms. Comparisons of the computed average structures show that both mutants differ substantially from the wild-type structure in certain common, discrete regions. One of these regions (residues 204–217) contains the epitope for the monoclonal antibody PAb240, which is concealed in the wild-type structure but accessible in both mutant structures. In order to confirm this conformational shift, tumor tissue and serum from vinyl chloride-exposed individuals with angiosarcomas of the liver were examined by immunohistochemistry and enzyme-linked immunosorbent assay. Individuals with tumors that contained the p53 mutations were found to have detectable mutant p53 protein in their tumor tissue and serum, whereas individuals with tumors without mutations and normal controls did not.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886863
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  • 9
    Electronic Resource
    Electronic Resource
    Correlation of structure with transforming activity of the P21 proteins with substitutions of L-amino acids for Gly at position 13 (1985)
    Springer
    The protein journal 4 (1985), S. 345-352 
    Details
    ISSN: 1573-4943
    Keywords: conformational energy ; three-dimensional structure ; amino acid substitution ; P21 proteins ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The effects of amino acid substitutions for Gly 13 on the structure of the transforming region (Leu 6-Gly 15) of the P21 proteins have been explored using conformational energy calculations. It has been found that the substitution of Asp for Gly at this position results in a protein capable of transforming cells into malignant ones. Proteins that contain Ser at position 13 (but no other substitutions), however, transform cells with a greatly reduced activity. The transforming peptide with Asp 13 adopts a conformation that is different from the one for the peptide from the normal protein (with Gly 12 and Gly 13) and that may result in expression of a higher energy malignancy-producing form. The Ser-containing peptide adopts as its lowest energy conformation one that is identical to that of the peptide from the normal protein, thus explaining its lack of transforming activity. From analysis of the interactions preventing the Asp 13-containing peptide from adopting the “normal” conformation, it is predicted that substitutions of amino acids with branched side chains atC β, such as Val, Ile, and Thr, should promote cell transformation. This prediction with Val has recently been confirmed in genetic experiments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025175
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  • 10
    Electronic Resource
    Electronic Resource
    Structural effects of amino acid substitutions on the P21 proteins: Evidence for a malignant conformation (1985)
    Springer
    The protein journal 4 (1985), S. 353-362 
    Details
    ISSN: 1573-4943
    Keywords: conformational energy ; three-dimensional structure ; amino acid substitution ; P21 proteins ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The conformational effects of different amino acid substitutions for Gly at position 12 in theras-oncogene-encoded P21 proteins have been investigated using conformational energy calculations. Mutations that cause amino acid substitutions for Gly 12 result in a protein that produces malignant transformation of cells. It had previously been shown that substitution of Val, Lys, or Ser for Gly at position 12 results in a major conformational change, and that the preferred lowest energy structure for each of the substituted peptides is identical. It is now found that substitution for Gly 12 of other amino acids that have widely disparate helix-nucleating potentials and completely different side chains (Asp, Asn, Cys, Phe, Tle, Leu, and Ala) all produce this identical lowest energy conformation. This finding is consistent with the recent results of site-specific mutagenesis experiments showing that P21 proteins containing these amino acids at position 12 all promote malignant transformation of cells and suggests the existence of a “malignancy-causing” conformation for the P21 proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025176
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