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  • 1
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    Ataxia telangiectasia mutated (Atm) and DNA-PKcs kinases have overlapping activities during chromosomal signal joint formation [Immunology] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-02-02
    Description: Lymphocyte antigen receptor gene assembly occurs through the process of V(D)J recombination, which is initiated when the RAG endonuclease introduces DNA DSBs at two recombining gene segments to form broken DNA coding end pairs and signal end pairs. These paired DNA ends are joined by proteins of the nonhomologous end-joining (NHEJ) pathway of DSB repair to form a coding joint and signal joint, respectively. RAG DSBs are generated in G1-phase developing lymphocytes, where they activate the ataxia telangiectasia mutated (Atm) and DNA-PKcs kinases to orchestrate diverse cellular DNA damage responses including DSB repair. Paradoxically, although Atm and DNA-PKcs both function during coding joint formation, Atm appears to be dispensible for signal joint formation; and although some studies have revealed an activity for DNA-PKcs during signal joint formation, others have not. Here we show that Atm and DNA-PKcs have overlapping catalytic activities that are required for chromosomal signal joint formation and for preventing the aberrant resolution of signal ends as potentially oncogenic chromosomal translocations.
    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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  • 2
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    Requirement for Atm in ionizing radiation-induced cell death in the developing central nervous system (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-06
    Description: Ataxia telangiectasia (AT) is characterized by progressive neurodegeneration that results from mutation of the ATM gene. However, neither the normal function of ATM in the nervous system nor the biological basis of the degeneration in AT is known. Resistance to apoptosis in the developing central nervous system (CNS) of Atm-/- mice was observed after ionizing radiation. This lack of death occurred in diverse regions of the CNS, including the cerebellum, which is markedly affected in AT. In wild-type, but not Atm-/- mice, up-regulation of p53 coincided with cell death, suggesting that Atm-dependent apoptosis in the CNS is mediated by p53. Further, p53 null mice showed a similar lack of radiation-induced cell death in the developing nervous system. Atm may function at a developmental survival checkpoint that serves to eliminate neurons with excessive DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzog, K H -- Chong, M J -- Kapsetaki, M -- Morgan, J I -- McKinnon, P J -- CA-21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 May 15;280(5366):1089-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Neurobiology, St. Jude Children's Research Hospital, 332 North Lauderdale, Memphis, TN 38101, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9582124" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Ataxia Telangiectasia Mutated Proteins ; Brain/*cytology/*radiation effects ; Cell Cycle Proteins ; Cerebellum/cytology/radiation effects ; DNA-Binding Proteins ; Genes, p53 ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurons/*cytology/radiation effects ; Phenotype ; *Protein-Serine-Threonine Kinases ; Proteins/genetics/*physiology ; Radiation, Ionizing ; Retina/cytology ; Thymus Gland/cytology/radiation effects ; Tumor Suppressor Protein p53/physiology ; Tumor Suppressor Proteins ; Up-Regulation
    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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  • 3
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    Subtypes of medulloblastoma have distinct developmental origins (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-12-15
    Description: Medulloblastoma encompasses a collection of clinically and molecularly diverse tumour subtypes that together comprise the most common malignant childhood brain tumour. These tumours are thought to arise within the cerebellum, with approximately 25% originating from granule neuron precursor cells (GNPCs) after aberrant activation of the Sonic Hedgehog pathway (hereafter, SHH subtype). The pathological processes that drive heterogeneity among the other medulloblastoma subtypes are not known, hindering the development of much needed new therapies. Here we provide evidence that a discrete subtype of medulloblastoma that contains activating mutations in the WNT pathway effector CTNNB1 (hereafter, WNT subtype) arises outside the cerebellum from cells of the dorsal brainstem. We found that genes marking human WNT-subtype medulloblastomas are more frequently expressed in the lower rhombic lip (LRL) and embryonic dorsal brainstem than in the upper rhombic lip (URL) and developing cerebellum. Magnetic resonance imaging (MRI) and intra-operative reports showed that human WNT-subtype tumours infiltrate the dorsal brainstem, whereas SHH-subtype tumours are located within the cerebellar hemispheres. Activating mutations in Ctnnb1 had little impact on progenitor cell populations in the cerebellum, but caused the abnormal accumulation of cells on the embryonic dorsal brainstem which included aberrantly proliferating Zic1(+) precursor cells. These lesions persisted in all mutant adult mice; moreover, in 15% of cases in which Tp53 was concurrently deleted, they progressed to form medulloblastomas that recapitulated the anatomy and gene expression profiles of human WNT-subtype medulloblastoma. We provide the first evidence, to our knowledge, that subtypes of medulloblastoma have distinct cellular origins. Our data provide an explanation for the marked molecular and clinical differences between SHH- and WNT-subtype medulloblastomas and have profound implications for future research and treatment of this important childhood cancer.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059767/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059767/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibson, Paul -- Tong, Yiai -- Robinson, Giles -- Thompson, Margaret C -- Currle, D Spencer -- Eden, Christopher -- Kranenburg, Tanya A -- Hogg, Twala -- Poppleton, Helen -- Martin, Julie -- Finkelstein, David -- Pounds, Stanley -- Weiss, Aaron -- Patay, Zoltan -- Scoggins, Matthew -- Ogg, Robert -- Pei, Yanxin -- Yang, Zeng-Jie -- Brun, Sonja -- Lee, Youngsoo -- Zindy, Frederique -- Lindsey, Janet C -- Taketo, Makoto M -- Boop, Frederick A -- Sanford, Robert A -- Gajjar, Amar -- Clifford, Steven C -- Roussel, Martine F -- McKinnon, Peter J -- Gutmann, David H -- Ellison, David W -- Wechsler-Reya, Robert -- Gilbertson, Richard J -- 01CA96832/CA/NCI NIH HHS/ -- P01 CA096832/CA/NCI NIH HHS/ -- P01 CA096832-06A18120/CA/NCI NIH HHS/ -- P01 CA096832-078120/CA/NCI NIH HHS/ -- P30CA021765/CA/NCI NIH HHS/ -- R01 CA129541/CA/NCI NIH HHS/ -- R01 CA129541-01/CA/NCI NIH HHS/ -- R01 CA129541-02/CA/NCI NIH HHS/ -- R01 CA129541-03/CA/NCI NIH HHS/ -- R01 CA129541-04/CA/NCI NIH HHS/ -- R01 CA129541-05/CA/NCI NIH HHS/ -- R01 NS037956/NS/NINDS NIH HHS/ -- R01 NS037956-13/NS/NINDS NIH HHS/ -- R01CA129541/CA/NCI NIH HHS/ -- England -- Nature. 2010 Dec 23;468(7327):1095-9. doi: 10.1038/nature09587. Epub 2010 Dec 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Neurobiology, St Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, Tennessee 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21150899" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Stem/*pathology ; Cerebellar Neoplasms/*pathology ; Disease Models, Animal ; Gene Expression Profiling ; Gene Expression Regulation, Neoplastic ; Humans ; Medulloblastoma/*pathology ; Mice ; Mice, Transgenic ; Mutation ; beta Catenin/genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    DNA ligase III is critical for mtDNA integrity but not Xrcc1-mediated nuclear DNA repair (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-03-11
    Description: DNA replication and repair in mammalian cells involves three distinct DNA ligases: ligase I (Lig1), ligase III (Lig3) and ligase IV (Lig4). Lig3 is considered a key ligase during base excision repair because its stability depends upon its nuclear binding partner Xrcc1, a critical factor for this DNA repair pathway. Lig3 is also present in the mitochondria, where its role in mitochondrial DNA (mtDNA) maintenance is independent of Xrcc1 (ref. 4). However, the biological role of Lig3 is unclear as inactivation of murine Lig3 results in early embryonic lethality. Here we report that Lig3 is essential for mtDNA integrity but dispensable for nuclear DNA repair. Inactivation of Lig3 in the mouse nervous system resulted in mtDNA loss leading to profound mitochondrial dysfunction, disruption of cellular homeostasis and incapacitating ataxia. Similarly, inactivation of Lig3 in cardiac muscle resulted in mitochondrial dysfunction and defective heart-pump function leading to heart failure. However, Lig3 inactivation did not result in nuclear DNA repair deficiency, indicating essential DNA repair functions of Xrcc1 can occur in the absence of Lig3. Instead, we found that Lig1 was critical for DNA repair, but acted in a cooperative manner with Lig3. Additionally, Lig3 deficiency did not recapitulate the hallmark features of neural Xrcc1 inactivation such as DNA damage-induced cerebellar interneuron loss, further underscoring functional separation of these DNA repair factors. Therefore, our data reveal that the critical biological role of Lig3 is to maintain mtDNA integrity and not Xrcc1-dependent DNA repair.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079429/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079429/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Yankun -- Katyal, Sachin -- Lee, Youngsoo -- Zhao, Jingfeng -- Rehg, Jerold E -- Russell, Helen R -- McKinnon, Peter J -- CA-21765/CA/NCI NIH HHS/ -- NS-37956/NS/NINDS NIH HHS/ -- P01 CA096832/CA/NCI NIH HHS/ -- P01 CA096832-07/CA/NCI NIH HHS/ -- P30 CA21765/CA/NCI NIH HHS/ -- R01 NS037956/NS/NINDS NIH HHS/ -- R01 NS037956-13/NS/NINDS NIH HHS/ -- England -- Nature. 2011 Mar 10;471(7337):240-4. doi: 10.1038/nature09773.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, St Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21390131" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia/pathology/physiopathology ; Biocatalysis ; Cell Nucleus/*genetics ; Cell Survival ; Cells, Cultured ; DNA Damage ; DNA Ligases/deficiency/genetics/*metabolism ; *DNA Repair ; DNA, Mitochondrial/*metabolism ; DNA-Binding Proteins/deficiency/genetics/*metabolism ; Genes, Essential ; Heart/physiology/physiopathology ; Interneurons/enzymology/pathology ; Mice ; Mitochondria/enzymology/genetics/pathology ; Muscle, Skeletal/enzymology/pathology ; Myocardium/enzymology/pathology ; Nervous System/enzymology/pathology ; Phenotype
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    H2AX prevents CtIP-mediated DNA end resection and aberrant repair in G1-phase lymphocytes (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-12-17
    Description: DNA double-strand breaks (DSBs) are generated by the recombination activating gene (RAG) endonuclease in all developing lymphocytes as they assemble antigen receptor genes. DNA cleavage by RAG occurs only at the G1 phase of the cell cycle and generates two hairpin-sealed DNA (coding) ends that require nucleolytic opening before their repair by classical non-homologous end-joining (NHEJ). Although there are several cellular nucleases that could perform this function, only the Artemis nuclease is able to do so efficiently. Here, in vivo, we show that in murine cells the histone protein H2AX prevents nucleases other than Artemis from processing hairpin-sealed coding ends; in the absence of H2AX, CtIP can efficiently promote the hairpin opening and resection of DNA ends generated by RAG cleavage. This CtIP-mediated resection is inhibited by gamma-H2AX and by MDC-1 (mediator of DNA damage checkpoint 1), which binds to gamma-H2AX in chromatin flanking DNA DSBs. Moreover, the ataxia telangiectasia mutated (ATM) kinase activates antagonistic pathways that modulate this resection. CtIP DNA end resection activity is normally limited to cells at post-replicative stages of the cell cycle, in which it is essential for homology-mediated repair. In G1-phase lymphocytes, DNA ends that are processed by CtIP are not efficiently joined by classical NHEJ and the joints that do form frequently use micro-homologies and show significant chromosomal deletions. Thus, H2AX preserves the structural integrity of broken DNA ends in G1-phase lymphocytes, thereby preventing these DNA ends from accessing repair pathways that promote genomic instability.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3150591/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3150591/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Helmink, Beth A -- Tubbs, Anthony T -- Dorsett, Yair -- Bednarski, Jeffrey J -- Walker, Laura M -- Feng, Zhihui -- Sharma, Girdhar G -- McKinnon, Peter J -- Zhang, Junran -- Bassing, Craig H -- Sleckman, Barry P -- A125195/PHS HHS/ -- AI074953/AI/NIAID NIH HHS/ -- AI47829/AI/NIAID NIH HHS/ -- CA136470/CA/NCI NIH HHS/ -- CA21765/CA/NCI NIH HHS/ -- NS37956/NS/NINDS NIH HHS/ -- P01 CA096832/CA/NCI NIH HHS/ -- P01 CA096832-08/CA/NCI NIH HHS/ -- R01 AI047829/AI/NIAID NIH HHS/ -- R01 AI047829-13/AI/NIAID NIH HHS/ -- R01 AI074953/AI/NIAID NIH HHS/ -- R01 AI074953-04/AI/NIAID NIH HHS/ -- R01 CA136470/CA/NCI NIH HHS/ -- R01 CA136470-04/CA/NCI NIH HHS/ -- R01 NS037956/NS/NINDS NIH HHS/ -- R01 NS037956-12/NS/NINDS NIH HHS/ -- R21 ES019779/ES/NIEHS NIH HHS/ -- R21 ES019779-02/ES/NIEHS NIH HHS/ -- T32 D007499/PHS HHS/ -- England -- Nature. 2011 Jan 13;469(7329):245-9. doi: 10.1038/nature09585. Epub 2010 Dec 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Immunology, Washington University School of Medicine, St Louis, Missouri 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21160476" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; Carrier Proteins/*metabolism ; Cell Cycle Proteins/*metabolism ; Cell Line, Transformed ; Chromatin/metabolism ; *DNA Breaks, Double-Stranded ; *DNA Repair ; DNA-Binding Proteins/metabolism ; Endonucleases ; *G1 Phase ; *Gene Rearrangement, B-Lymphocyte/genetics ; Genomic Instability ; Histones/deficiency/genetics/*metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Lymphocytes/cytology/*metabolism ; Mice ; Nuclear Proteins ; Precursor Cells, B-Lymphoid/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombination, Genetic/genetics ; Substrate Specificity ; Tumor Suppressor Proteins/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    Crucial role for DNA ligase III in mitochondria but not in Xrcc1-dependent repair (2011)
    Nature Publishing Group (NPG)
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    Publication Date: 2011-03-11
    Description: Mammalian cells have three ATP-dependent DNA ligases, which are required for DNA replication and repair. Homologues of ligase I (Lig1) and ligase IV (Lig4) are ubiquitous in Eukarya, whereas ligase III (Lig3), which has nuclear and mitochondrial forms, appears to be restricted to vertebrates. Lig3 is implicated in various DNA repair pathways with its partner protein Xrcc1 (ref. 1). Deletion of Lig3 results in early embryonic lethality in mice, as well as apparent cellular lethality, which has precluded definitive characterization of Lig3 function. Here we used pre-emptive complementation to determine the viability requirement for Lig3 in mammalian cells and its requirement in DNA repair. Various forms of Lig3 were introduced stably into mouse embryonic stem (mES) cells containing a conditional allele of Lig3 that could be deleted with Cre recombinase. With this approach, we find that the mitochondrial, but not nuclear, Lig3 is required for cellular viability. Although the catalytic function of Lig3 is required, the zinc finger (ZnF) and BRCA1 carboxy (C)-terminal-related (BRCT) domains of Lig3 are not. Remarkably, the viability requirement for Lig3 can be circumvented by targeting Lig1 to the mitochondria or expressing Chlorella virus DNA ligase, the minimal eukaryal nick-sealing enzyme, or Escherichia coli LigA, an NAD(+)-dependent ligase. Lig3-null cells are not sensitive to several DNA-damaging agents that sensitize Xrcc1-deficient cells. Our results establish a role for Lig3 in mitochondria, but distinguish it from its interacting protein Xrcc1.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3261757/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3261757/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simsek, Deniz -- Furda, Amy -- Gao, Yankun -- Artus, Jerome -- Brunet, Erika -- Hadjantonakis, Anna-Katerina -- Van Houten, Bennett -- Shuman, Stewart -- McKinnon, Peter J -- Jasin, Maria -- CA21765/CA/NCI NIH HHS/ -- ES019566/ES/NIEHS NIH HHS/ -- GM54668/GM/NIGMS NIH HHS/ -- NS37956/NS/NINDS NIH HHS/ -- P30 CA008748/CA/NCI NIH HHS/ -- R01 ES019566/ES/NIEHS NIH HHS/ -- R01 GM054668/GM/NIGMS NIH HHS/ -- R01 GM054668-12/GM/NIGMS NIH HHS/ -- R01 GM054668-12S1/GM/NIGMS NIH HHS/ -- R01 GM063611/GM/NIGMS NIH HHS/ -- R01 NS037956/NS/NINDS NIH HHS/ -- R01 NS037956-13/NS/NINDS NIH HHS/ -- England -- Nature. 2011 Mar 10;471(7337):245-8. doi: 10.1038/nature09794.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Developmental Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21390132" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biocatalysis ; Cell Survival ; DNA Damage ; DNA Ligases/chemistry/deficiency/genetics/*metabolism ; *DNA Repair ; DNA, Mitochondrial/*metabolism ; DNA-Binding Proteins/*metabolism ; Embryonic Stem Cells/metabolism ; Genes, Essential ; Genetic Complementation Test ; Humans ; Mice ; Mitochondria/*enzymology/*genetics/pathology ; Protein Structure, Tertiary ; Sister Chromatid Exchange/drug effects
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 7
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    Pineal opsin: a nonvisual opsin expressed in chick pineal (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: Pineal opsin (P-opsin), an opsin from chick that is highly expressed in pineal but is not detectable in retina, was cloned by the polymerase chain reaction. It is likely that the P-opsin lineage diverged from the retinal opsins early in opsin evolution. The amino acid sequence of P-opsin is 42 to 46 percent identical to that of the retinal opsins. P-opsin is a seven-membrane spanning, G protein-linked receptor with a Schiff-base lysine in the seventh membrane span and a Schiff-base counterion in the third membrane span. The primary sequence of P-opsin suggests that it will be maximally sensitive to approximately 500-nanometer light and produce a slow and prolonged phototransduction response consistent with the nonvisual function of pineal photoreception.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Max, M -- McKinnon, P J -- Seidenman, K J -- Barrett, R K -- Applebury, M L -- Takahashi, J S -- Margolskee, R F -- EYO8467/EY/NEI NIH HHS/ -- MH10287/MH/NIMH NIH HHS/ -- MH39592/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1502-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878470" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Avian Proteins ; Base Sequence ; Biological Evolution ; Brain Chemistry ; Chickens ; Cloning, Molecular ; Molecular Sequence Data ; Nerve Tissue Proteins/analysis/*chemistry/genetics/physiology ; Pineal Gland/*chemistry ; Protein Structure, Secondary ; RNA, Messenger/analysis ; Retina/chemistry ; Rod Opsins/analysis/*chemistry/genetics/physiology ; Sequence Homology, Amino Acid
    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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  • 8
    Electronic Resource
    Electronic Resource
    Ataxia-telangiectasia: an inherited disorder of ionizing-radiation sensitivity in man (1987)
    Springer
    Human genetics 〈Berlin〉 75 (1987), S. 197-208 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary This review summarizes the current research on the biochemical defect leading to ataxia-telangiectasia (AT). A DNA repair defect has been linked to AT, although the precise defect has not been found. A critical examination of the evidence for and against a DNA repair defect in AT is presented. Consideration of other recent data on AT raises the possibility that AT may not primarily be the result of a DNA repair defect. Therefore, in this review AT is approached as a syndrome which is defective in the ability to respond to ionizing-radiation-type damage, rather than defective in the ability to repair this damage. However, this does not necessarily exclude the potential involvement of a DNA repair defect in some of the genetically distinct subsets present in AT. Other recent anomalies found in AT, including an altered cell cycle and DNA synthesis profile following ionizing-radiation damage, are also assessed. A suggestion to account for the underlying defect in AT, based on the various research reports, is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00281059
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  • 9
    Electronic Resource
    Electronic Resource
    ATM dependent apoptosis in the nervous system (2000)
    Springer
    Apoptosis 5 (2000), S. 523-529 
    Details
    ISSN: 1573-675X
    Keywords: apoptosis ; ATM ; DNA damage ; ionizing radiation ; p53
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Ataxia-telangiectasia is a human syndrome resulting from mutations of the ATM protein kinase that is characterized by radiation sensitivity and neurodegeneration. Although neuroprotective, the molecular details of ATM function in the nervous system are uncertain. However, in the mouse, Atm is essential for ionizing radiation-induced apoptosis in select postmitotic populations of the developing nervous system. Atm-dependent apoptosis in the nervous system also requires p53, consistent with the well-established link of p53 as a major substrate of ATM. Furthermore, the proapoptotic effector Bax is also required for most, but not all, Atm-dependent apoptosis. Therefore, after DNA damage in the developing nervous system, Atm initiates a p53-dependent apoptotic cascade in differentiating neural cells. Together, these data suggest ATM-dependent apoptosis may be important for elimination of neural cells that have accumulated genomic damage during development, thus preventing dysfunction of these cells later in life.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009637512917
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  • 10
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    Robust chromosomal DNA repair via alternative end-joining in the absence of X-ray repair cross-complementing protein 1 (XRCC1) (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-01-30
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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