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  • 1
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    p53-independent role of MDM2 in TGF-beta1 resistance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: Transforming growth factor-beta (TGF-beta) inhibits cell proliferation, and acquisition of TGF-beta resistance has been linked to tumorigenesis. A genetic screen was performed to identify complementary DNAs that abrogated TGF-beta sensitivity in mink lung epithelial cells. Ectopic expression of murine double minute 2 rescued TGF-beta-induced growth arrest in a p53-independent manner by interference with retinoblastoma susceptibility gene product (Rb)/E2F function. In human breast tumor cells, increased MDM2 expression levels correlated with TGF-beta resistance. Thus, MDM2 may confer TGF-beta resistance in a subset of tumors and may promote tumorigenesis by interference with two independent tumor suppressors, p53 and Rb.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, P -- Dong, P -- Dai, K -- Hannon, G J -- Beach, D -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2270-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856953" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/genetics/metabolism/pathology ; *Carrier Proteins ; *Cell Cycle Proteins ; *Cell Division ; Cell Line ; Cell Transformation, Neoplastic ; *DNA-Binding Proteins ; Drug Resistance, Neoplasm ; E2F Transcription Factors ; Gene Expression ; Genes, Retinoblastoma ; Genes, p53 ; Genetic Vectors ; Humans ; Mice ; Mink ; *Nuclear Proteins ; Phosphorylation ; Proto-Oncogene Proteins/genetics/*physiology ; Proto-Oncogene Proteins c-mdm2 ; Retinoblastoma Protein/metabolism ; Retinoblastoma-Binding Protein 1 ; Signal Transduction ; Transcription Factor DP1 ; Transcription Factors/genetics/metabolism ; Transcription, Genetic ; Transforming Growth Factor beta/*pharmacology/physiology ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/*physiology
    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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  • 2
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    MaRX: an approach to genetics in mammalian cells (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hannon, G J -- Sun, P -- Carnero, A -- Xie, L Y -- Maestro, R -- Conklin, D S -- Beach, D -- New York, N.Y. -- Science. 1999 Feb 19;283(5405):1129-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10075573" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cloning, Molecular/*methods ; DNA, Complementary ; Gene Expression ; Gene Library ; Genes, p53 ; Genes, ras ; *Genetic Techniques ; Genetic Vectors ; Mammals ; Phenotype ; Proviruses/genetics ; Retroviridae/genetics ; Transformation, Genetic
    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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  • 3
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    A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-01
    Description: A mutated cyclin-dependent kinase 4 (CDK4) was identified as a tumor-specific antigen recognized by HLA-A2. 1-restricted autologous cytolytic T lymphocytes (CTLs) in a human melanoma. The mutated CDK4 allele was present in autologous cultured melanoma cells and metastasis tissue, but not in the patient's lymphocytes. The mutation, an arginine-to-cysteine exchange at residue 24, was part of the CDK4 peptide recognized by CTLs and prevented binding of the CDK4 inhibitor p16INK4a, but not of p21 or of p27KIP1. The same mutation was found in one additional melanoma among 28 melanomas analyzed. These results suggest that mutation of CDK4 can create a tumor-specific antigen and can disrupt the cell-cycle regulation exerted by the tumor suppressor p16INK4a.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolfel, T -- Hauer, M -- Schneider, J -- Serrano, M -- Wolfel, C -- Klehmann-Hieb, E -- De Plaen, E -- Hankeln, T -- Meyer zum Buschenfelde, K H -- Beach, D -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medizinische Klinik und Poliklinik, Johannes Gutenberg-Universitat, Mainz, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652577" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/metabolism/*pharmacology ; *Cell Cycle Proteins ; Cell Line ; Cloning, Molecular ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p15 ; Cyclin-Dependent Kinase Inhibitor p16 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinase Inhibitor p27 ; *Cyclin-Dependent Kinases ; Cyclins/metabolism/pharmacology ; HLA-A2 Antigen/immunology ; Humans ; Melanoma/enzymology/*immunology ; Microtubule-Associated Proteins/metabolism/pharmacology ; Molecular Sequence Data ; Point Mutation ; Polymerase Chain Reaction ; Protein-Serine-Threonine Kinases/antagonists & ; inhibitors/genetics/*immunology/metabolism ; *Proto-Oncogene Proteins ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins
    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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  • 4
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    CDC25 phosphatases as potential human oncogenes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: Cyclin-dependent kinases (CDKs) are activated by CDC25 phosphatases, which remove inhibitory phosphate from tyrosine and threonine residues. In human cells, CDC25 proteins are encoded by a multigene family, consisting of CDC25A, CDC25B, and CDC25C. In rodent cells, human CDC25A or CDC25B but not CDC25C phosphatases cooperate with either Ha-RASG12V or loss of RB1 in oncogenic focus formation. Such transformants were highly aneuploid, grew in soft agar, and formed high-grade tumors in nude mice. Overexpression of CDC25B was detected in 32 percent of human primary breast cancers tested. The CDC25 phosphatases may contribute to the development of human cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galaktionov, K -- Lee, A K -- Eckstein, J -- Draetta, G -- Meckler, J -- Loda, M -- Beach, D -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1575-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667636" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/genetics ; Cell Cycle Proteins/*genetics ; Cell Division ; *Cell Transformation, Neoplastic ; Cells, Cultured ; Gene Expression ; Genes, Retinoblastoma ; Genes, p53 ; Genes, ras ; Humans ; In Situ Hybridization ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; *Multigene Family ; Neoplasm Transplantation ; *Oncogenes ; Phosphoprotein Phosphatases/*genetics ; Prognosis ; Transfection ; Tumor Cells, Cultured ; cdc25 Phosphatases
    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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  • 5
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    Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-17
    Description: Skeletal muscle differentiation entails the coordination of muscle-specific gene expression and terminal withdrawal from the cell cycle. This cell cycle arrest in the G0 phase requires the retinoblastoma tumor suppressor protein (Rb). The function of Rb is negatively regulated by cyclin-dependent kinases (Cdks), which are controlled by Cdk inhibitors. Expression of MyoD, a skeletal muscle-specific transcriptional regulator, activated the expression of the Cdk inhibitor p21 during differentiation of murine myocytes and in nonmyogenic cells. MyoD-mediated induction of p21 did not require the tumor suppressor protein p53 and correlated with cell cycle withdrawal. Thus, MyoD may induce terminal cell cycle arrest during skeletal muscle differentiation by increasing the expression of p21.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halevy, O -- Novitch, B G -- Spicer, D B -- Skapek, S X -- Rhee, J -- Hannon, G J -- Beach, D -- Lassar, A B -- F32ARO8214-01A1/AR/NIAMS NIH HHS/ -- N01-HD-6-2915/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 17;267(5200):1018-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7863327" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carrier Proteins ; *Cell Cycle ; *Cell Cycle Proteins ; *Cell Differentiation ; Cell Line ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/*antagonists & inhibitors ; Cyclins/*biosynthesis/genetics ; *DNA-Binding Proteins ; E2F Transcription Factors ; G0 Phase ; Humans ; Mice ; Microtubule-Associated Proteins/biosynthesis/genetics ; Muscle, Skeletal/*cytology/metabolism ; MyoD Protein/*physiology ; RNA, Messenger/genetics/metabolism ; Retinoblastoma Protein/physiology ; Retinoblastoma-Binding Protein 1 ; Transcription Factor DP1 ; Transcription Factors/metabolism ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/physiology ; *Tumor Suppressor Proteins
    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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  • 6
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    Inhibition of ras-induced proliferation and cellular transformation by p16INK4 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-13
    Description: The cyclin-dependent kinase 4 (CDK4) regulates progression through the G1 phase of the cell cycle. The activity of CDK4 is controlled by the opposing effects of the D-type cyclin, an activating subunit, and p16INK4, an inhibitory subunit. Ectopic expression of p16INK4 blocked entry into S phase of the cell cycle induced by oncogenic Ha-Ras, and this block was relieved by coexpression of a catalytically inactive CDK4 mutant. Expression of p16INK4 suppressed cellular transformation of primary rat embryo fibroblasts by oncogenic Ha-Ras and Myc, but not by Ha-Ras and E1a. Together, these observations provide direct evidence that p16INK4 can inhibit cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Serrano, M -- Gomez-Lahoz, E -- DePinho, R A -- Beach, D -- Bar-Sagi, D -- CA55360/CA/NCI NIH HHS/ -- EY09300-01/EY/NEI NIH HHS/ -- HD28317-02/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):249-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809631" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/genetics/physiology ; Animals ; Carrier Proteins/genetics/*physiology ; *Cell Division ; *Cell Transformation, Neoplastic ; Cells, Cultured ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p16 ; *Cyclin-Dependent Kinases ; Genes, Reporter ; Genes, Retinoblastoma ; Genes, myc ; Genes, ras ; Plasmids ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; *Proto-Oncogene Proteins ; Rats ; Retinoblastoma Protein/physiology ; S Phase ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; ras Proteins/genetics/*physiology
    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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  • 7
    Electronic Resource
    Electronic Resource
    A mutation in a thioredoxin reductase homolog suppresses p53-induced growth inhibition in the fission yeastSchizosaccharomyces pombe (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 518-529 
    Details
    ISSN: 1617-4623
    Keywords: p53 ; Schizosaccharomyces pombe ; Thioredoxin reductase ; Redox state ; Transcriptional reporter
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A strong growth inhibition is observed when the human p53 tumor suppressor gene product is expressed in the fission yeastSchizosaccharomyces pombe. This growth inhibition is specific for wild-type p53; mutant alleles of p53 derived from human tumors show a greatly decreased ability to inhibit growth. These data suggest that there may be a p53-responsive pathway inS. pombe. To identify elements in this pathway genetically, we isolated a mutant yeast strain in which the growth inhibitory activity of p53 is largely suppressed. In addition, the activity of p53 as a transcription factor is also decreased in this strain. The suppression of p53 activity is not due to a decrease in p53 expression or a failure of p53 to localize to the nucleus. This p53 suppressor mutation is in a novelS. pombe gene with homology to thioredoxin reductase genes, and has been namedtrr1. Strains with a mutation of, or deletion in,trr1 are sensitive to oxidizing agents, suggesting that thetrr1 suppressor mutation causes partial loss oftrr1 function. Since oxidizing agents are able to suppress p53 activity in vitro, thistrr1 mutation may affect the activity of p53 in fission yeast by increasing the oxidation state of the tumor suppressor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172398
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  • 8
    Electronic Resource
    Electronic Resource
    The capacitance of Pt/Pb0.65La0.28Ti0.96O3/Pt structures (1996)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 68 (1996), S. 3043-3045 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The capacitance/voltage characteristics of thin paraelectric lead lanthanum titanate films are measured using platinum electrodes. The films have a maximum capacitance when either a small positive or negative bias voltage is applied. This characteristic is consistent with the electrode interfaces acting as Schottky-like barriers. The voltage at which the capacitance maxima occur increases linearly with film thickness indicating that the film is highly resistive. On the basis of the high apparent film resistance it is proposed that the voltage dependence of the capacitance of the electrode interfaces arises from the ionization of deep level traps within the film and not from depletion layers associated with shallow donor or acceptor states. Application of voltages larger than about 2–3 V results in the disappearance of the capacitance maxima indicating that irreversible changes in the electrode interfaces occur at higher electric fields. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.115571
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  • 9
    Electronic Resource
    Electronic Resource
    A mutation in a thioredoxin reductase homolog suppresses p53-induced growth inhibition in the fission yeast Schizosaccharomyces pombe (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 518-529 
    Details
    ISSN: 1617-4623
    Keywords: Key words p53 ; Schizosaccharomyces pombe ; Thioredoxin reductase ; Redox state ; Transcriptional reporter
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A strong growth inhibition is observed when the human p53 tumor suppressor gene product is expressed in the fission yeast Schizosaccharomyces pombe. This growth inhibition is specific for wild-type p53; mutant alleles of p53 derived from human tumors show a greatly decreased ability to inhibit growth. These data suggest that there may be a p53-responsive pathway in S. pombe. To identify elements in this pathway genetically, we isolated a mutant yeast strain in which the growth inhibitory activity of p53 is largely suppressed. In addition, the activity of p53 as a transcription factor is also decreased in this strain. The suppression of p53 activity is not due to a decrease in p53 expression or a failure of p53 to localize to the nucleus. This p53 suppressor mutation is in a novel S. pombe gene with homology to thioredoxin reductase genes, and has been named trr1. Strains with a mutation of, or deletion in, trr1 are sensitive to oxidizing agents, suggesting that the trr1 suppressor mutation causes partial loss of trr1 function. Since oxidizing agents are able to suppress p53 activity in vitro, this trr1 mutation may affect the activity of p53 in fission yeast by increasing the oxidation state of the tumor suppressor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172398
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  • 10
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    SLP-76 mediates and maintains activation of the Tec family kinase ITK via the T cell antigen receptor-induced association between SLP-76 and ITK (2007)
    National Academy of Sciences
    Details
    Publication Date: 2007-04-09
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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