Kooperativer Bibliotheksverbund

Berlin Brandenburg

and
and

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Type of Medium
Language
Year
  • 1
    In: National Underwriter - Property & Casualty Insurance Edition, Oct 4, 1985, p.30(2)
    Keywords: Life Insurance -- Innovations ; Health Insurance -- Innovations ; Insurance Policies -- Innovations
    ISSN: 0163-8912
    Source: Cengage Learning, Inc.
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Language: English
    In: PLoS ONE, 01 January 2016, Vol.11(2), p.e0148174
    Description: Genetic code redundancy would yield, on the average, the assignment of three codons for each of the natural amino acids. The fact that this number is observed only for incorporating Ile and to stop RNA translation still waits for an overall explanation. Through a Structural Bioinformatics approach, the wealth of information stored in the Protein Data Bank has been used here to look for unambiguous clues to decipher the rationale of standard genetic code (SGC) in assigning from one to six different codons for amino acid translation. Leu and Arg, both protected from translational errors by six codons, offer the clearest clue by appearing as the most abundant amino acids in protein-protein and protein-nucleic acid interfaces. Other SGC hidden messages have been sought by analyzing, in a protein structure framework, the roles of over- and under-protected amino acids.
    Keywords: Sciences (General)
    E-ISSN: 1932-6203
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    In: PLoS ONE, 2016, Vol.11(2)
    Description: Genetic code redundancy would yield, on the average, the assignment of three codons for each of the natural amino acids. The fact that this number is observed only for incorporating Ile and to stop RNA translation still waits for an overall explanation. Through a Structural Bioinformatics approach, the wealth of information stored in the Protein Data Bank has been used here to look for unambiguous clues to decipher the rationale of standard genetic code (SGC) in assigning from one to six different codons for amino acid translation. Leu and Arg, both protected from translational errors by six codons, offer the clearest clue by appearing as the most abundant amino acids in protein-protein and protein-nucleic acid interfaces. Other SGC hidden messages have been sought by analyzing, in a protein structure framework, the roles of over- and under-protected amino acids.
    Keywords: Research Article ; Biology And Life Sciences ; Biology And Life Sciences ; Research And Analysis Methods ; Research And Analysis Methods ; Biology And Life Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Biology And Life Sciences ; Research And Analysis Methods ; Research And Analysis Methods
    E-ISSN: 1932-6203
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 16 July 1999, Vol.96(14), pp.7768-7773
    Description: Monomeric human pancreatic RNase, devoid of any biological activity other than its RNA degrading ability, was engineered into a dimeric protein with a cytotoxic action on mouse and human tumor cells, but lacking any appreciable toxicity on mouse and human normal cells. This dimeric variant of human pancreas RNase selectively sensitizes to apoptotic death cells derived from a human thyroid tumor. Because of its selectivity for tumor cells, and because of its human origin, this protein represents a potentially very attractive, novel tool for anticancer therapy.
    Keywords: Biological sciences -- Biology -- Cytology ; Biological sciences -- Biology -- Cytology ; Physical sciences -- Chemistry -- Chemical compounds ; Biological sciences -- Biology -- Cytology ; Health sciences -- Medical conditions -- Diseases ; Biological sciences -- Biology -- Genetics ; Health sciences -- Medical conditions -- Diseases ; Biological sciences -- Biology -- Cytology ; Physical sciences -- Physics -- Microphysics ; Biological sciences -- Biology -- Cytology
    ISSN: 00278424
    E-ISSN: 10916490
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    In: Oncogene, 2001, Vol.20(48), p.6973
    Description: Thyroid papillary carcinomas are characterized by RET/PTC rearrangements that cause the tyrosine kinase domain of the RET receptor to fuse with N-terminal sequences encoded by heterologous genes. This results in the aberrant expression of a ligand-independent and constitutively active RET kinase. We analysed actin reorganization induced by the RET/PTC1 oncogene in PC Cl 3 rat thyroid epithelial cells. Differently from oncogenes Src, Ras and Raf, RET/PTC1 caused actin filaments to form prominent stress fibers. Moreover, stress fibers were identified in human thyroid papillary carcinoma cell lines harboring RET/PTC1 rearrangements but not in thyroid carcinoma cells negative for RET/PTC rearrangements. RET/MEN 2A, a constitutively active but unrearranged membrane-bound RET oncoprotein, did not induce stress fibers in PC Cl 3 cells. Induction of stress fibers by RET/PTC1 was restricted to thyroid cells; it did not occur in NIH3T3 fibroblasts or MCF7 mammary cells. RET/PTC1-mediated stress fiber formation depended on Rho but not Rac small GTPase activity. In addition, inhibition of Rho, but not of Rac, caused apoptosis of RET/PTC1-expressing thyroid cells. We conclude that Rho is implicated in the actin reorganization and cell survival mediated by the chimeric RET/PTC1 oncogene in thyroid epithelial cells, both phenotypes being cell type- and oncogene type-specific. Oncogene(2001) 20,6973-6982. Keywords: RET, tyrosine-kinase, Rho, Ras, Rac, actin, thyroid, apoptosis
    Keywords: Cellular Signal Transduction -- Genetic Aspects ; Cellular Signal Transduction -- Research ; G Proteins -- Physiological Aspects ; G Proteins -- Genetic Aspects ; G Proteins -- Research ; Proto-oncogenes -- Physiological Aspects ; Proto-oncogenes -- Research ; Thyroid Cancer -- Genetic Aspects ; Thyroid Cancer -- Research;
    ISSN: 0950-9232
    E-ISSN: 14765594
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    In: Oncogene, 2001, Vol.20(5), p.599
    Description: The RET:/PTC3 oncogene arises from the fusion between the N-terminal encoding domain of the RFG:gene and the tyrosine kinase encoding domain of RET:receptor. RET:/PTC3 is very frequent in papillary thyroid carcinomas, especially in children exposed to the Chernobyl accident. We have studied the functional consequences of the RFG-RET:fusion. Here we show that the N-terminal coiled-coil domain of RGF mediates oligomerization and activation of the kinase and of the transforming capability of RET/PTC3. In addition, the RFG coiled-coil domain mediates a physical association between RET/PTC3 and RGF proteins, rendering RFG a bona fide:substrate of RET/PTC3 kinase. Finally, we show that the coiled-coil domain of RGF is essential for the distribution of the RET/PTC3 protein at the membrane/particulate cell compartment level, where also most of the RFG protein is localized. We propose that fusion to the RFG coiled-coil domain provides RET kinase with a scaffold that mediates oligomerization and re-localization of the RET/PTC3 protein, a process that may be crucial for the signalling of this specific RET/PTC variant. Oncogene(2001) 20,599-608. Keywords: tyrosine kinase, transformation, thyroid, coiled coil, dimerization
    Keywords: Oligomers ; Thyroid Diseases ; Particulate Pollutants ; Proteins ; Child Health ; Air Pollution ; Tyrosine;
    ISSN: 0950-9232
    E-ISSN: 14765594
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
  • 8
    Language: English
    In: International Journal of Cancer, 27 November 1995, Vol.63(5), pp.757-760
    Description: We have earlier shown that expression of the human activated Ki‐ras, directed by the rat thyroglobulin (TG) promoter in the thyroid gland of transgenic mice, is able to induce thyroid benign tumors, albeit at low incidence. A likely explanation of our results is that the low levels of exogenous Ki transcripts are not sufficient to induce multifocal tumors in the thyroid gland. We have performed experiments to analyze the effects of a similar construct upon thyroid‐cell proliferation and differentiation. Transfection of FRTL‐5 rat thyroid cells with the human Ki fused to the rat TG promoter is rapidly followed by reduced expression of the differentiation markers thyroglobulin, thyroperoxydase and thyrotropin receptor, but not by fully malignant cell transformation. The data reported support the hypothesis that Ki‐ mRNA levels are critical to the process of complete neoplastic transformation of thyroid epithelial differentiated cells . © 1995 .
    Keywords: Genes, Ras ; Mutation ; Promoter Regions, Genetic ; Thyroglobulin -- Genetics ; Thyroid Gland -- Cytology;
    ISSN: 0020-7136
    E-ISSN: 1097-0215
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    In: National Underwriter-Life & Health Insurance Edition, Nov 16, 1985, p.9(1)
    Keywords: Life Insurance -- Innovations ; Health Insurance -- Innovations ; Employee Benefits -- Economic Aspects
    ISSN: 0028-033X
    Source: Cengage Learning, Inc.
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 10
    Language: English
    In: International Journal of Cancer, 10 February 2002, Vol.97(5), pp.608-614
    Description: A novel human thyroid papillary carcinoma cell line (FB‐2) has been established and characterized. FB‐2 cells harbor the /PTC1 chimeric oncogene in which the kinase domain is fused to the H4 gene. FB‐2 cells neither formed colonies in semisolid media nor induced tumors after heterotransplant into severe combined immunodeficient mice. However, , and genes, which are associated to thyroid cell transformation, were abundantly expressed in FB‐2 cells but not in normal thyroid cells. FB‐2 cells only partially retained the differentiated thyroid phenotype. In fact, the gene, which codes for a transcriptional factor required for thyroid cell differentiation, was expressed, while thyroglobulin, TSH‐receptor and thyroperoxidase genes were not. Moreover, FB‐2 cells produced high levels of interleukin (IL)‐6 and IL‐8. © 2001 Wiley‐Liss, Inc.
    Keywords: Thyroid ; Papillary Carcinoma ; Cell Line ; Rearrangement
    ISSN: 0020-7136
    E-ISSN: 1097-0215
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. Further information can be found on the KOBV privacy pages