Relevant bibliographies by topics / Dmp53

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Dmp53'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Dmp53.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Dmp53"

1

Chen, Su, Hui-Min Wei, Wen-Wen Lv, Da-Liang Wang, and Fang-Lin Sun. "E2 Ligase dRad6 Regulates DMP53 Turnover inDrosophila." Journal of Biological Chemistry 286, no. 11 (January 4, 2011): 9020–30. http://dx.doi.org/10.1074/jbc.m110.190314.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Bodai, László, Norbert Pardi, Zsuzsanna Újfaludi, Orsolya Bereczki, Orbán Komonyi, Eva Balint, and Imre M. Boros. "Daxx-like Protein ofDrosophilaInteracts with Dmp53 and Affects Longevity andArkmRNA Level." Journal of Biological Chemistry 282, no. 50 (October 12, 2007): 36386–93. http://dx.doi.org/10.1074/jbc.m705547200.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Monk, Adrian C., Helen E. Abud, and Gary R. Hime. "Dmp53 is sequestered to nuclear bodies in spermatogonia of Drosophila melanogaster." Cell and Tissue Research 350, no. 2 (August 12, 2012): 385–94. http://dx.doi.org/10.1007/s00441-012-1479-4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Jassim, O. W. "Dmp53 protects the Drosophila retina during a developmentally regulated DNA damage response." EMBO Journal 22, no. 20 (October 15, 2003): 5622–32. http://dx.doi.org/10.1093/emboj/cdg543.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Bauer, Johannes H., Chengyi Chang, Gina Bae, Siti Nur Sarah Morris, and Stephen L. Helfand. "Dominant-negative Dmp53 extends life span through the dTOR pathway in D. melanogaster." Mechanisms of Ageing and Development 131, no. 3 (March 2010): 193–201. http://dx.doi.org/10.1016/j.mad.2010.01.007.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Bauer, J. H., C. Chang, S. N. S. Morris, S. Hozier, S. Andersen, J. S. Waitzman, and S. L. Helfand. "Expression of dominant-negative Dmp53 in the adult fly brain inhibits insulin signaling." Proceedings of the National Academy of Sciences 104, no. 33 (August 8, 2007): 13355–60. http://dx.doi.org/10.1073/pnas.0706121104.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Colombani, Julien, Cédric Polesello, Filipe Josué, and Nicolas Tapon. "Dmp53 Activates the Hippo Pathway to Promote Cell Death in Response to DNA Damage." Current Biology 16, no. 14 (July 2006): 1453–58. http://dx.doi.org/10.1016/j.cub.2006.05.059.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Ibarra, E. Piedra, J. T. Torres Gregorio, B. G. Ramírez Cruz, M. E. Heres Pulido, L. F. Santos Cruz, and A. Ponciano Gomez. "Transcription levels of Cyp450s, H99, Hsps and Dmp53 in Drosophila melanogaster larvae treated with zearalenona." Toxicology Letters 258 (September 2016): S76—S77. http://dx.doi.org/10.1016/j.toxlet.2016.06.1357.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Merino, Carlos, Enrique Reynaud, Martha Vázquez, and Mario Zurita. "DNA Repair and Transcriptional Effects of Mutations in TFIIH inDrosophila Development." Molecular Biology of the Cell 13, no. 9 (September 2002): 3246–56. http://dx.doi.org/10.1091/mbc.e02-02-0087.

Full text
Abstract:
Mutations in XPB and XPD TFIIH helicases have been related with three hereditary human disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. The dual role of TFIIH in DNA repair and transcription makes it difficult to discern which of the mutant TFIIH phenotypes is due to defects in any of these different processes. We used haywire (hay), theDrosophila XPB homolog, to dissect this problem. Our results show that when hay dosage is affected, the fly shows defects in structures that require high levels of transcription. We found a genetic interaction between hay andcdk7, and we propose that some of these phenotypes are due to transcriptional deficiencies. We also found more apoptotic cells in imaginal discs and in the CNS of hay mutant flies than in wild-type flies. Because this abnormal level of apoptosis was not detected in cdk7 flies, this phenotype could be related to defects in DNA repair. In addition the apoptosis induced by p53 Drosophila homolog (Dmp53) is suppressed in heterozygous hay flies.
APA, Harvard, Vancouver, ISO, and other styles
10

Bauer, Johannes H., Siti Nur Sarah Morris, Chengyi Chang, Thomas Flatt, Jason G. Wood, and Stephen L. Helfand. "dSir2 and Dmp53 interact to mediate aspects of CR-dependent life span extension in D. melanogaster." Aging 1, no. 1 (November 6, 2008): 38–48. http://dx.doi.org/10.18632/aging.100001.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Dmp53"

1

Morey, Ramonell Marta. "Selenoproteïnes i estrès oxidatiu a "Drosophila": regulació negativa de la via Ras/MAPK i activació de l'apoptosi." Doctoral thesis, Universitat de Barcelona, 2003. http://hdl.handle.net/10803/1852.

Full text
Abstract:
La tesi doctoral "Selenoproteïnes i estrès oxidatiu a Drosophila: regulació negativa de la via Ras/MAPK i activació de l'apoptosi" està dividida en els següents apartats:

1. La Introducció tracta la temàtica de les selenoproteïnes i els radicals lliures, i presenta el mutant selD[ptuf] de Drosophila melanogaster com a model d'estudi. Les selenoproteïnes són proteïnes que es caracteritzen per la presencia de Seleni en forma de l'aminoàcid selenocisteïna (Sec). Les selenoproteïnes identificades de les quals es coneix la seva funció actuen com antioxidants protegint les cèl·lules de l'acció nociva dels radicals lliures. Els radicals lliures són la conseqüència del metabolisme aeròbic i per tant es generen constantment. Si bé en determinades situacions els radicals lliures tenen una funció fisiològica, també són nocius per la cèl·lules que han desenvolupat mecanismes de defensa entre els que destaquen les selenoproteïnes. La mutació selD[ptuf] és una mutació nul·la en un element de la ruta de biosíntesi de les selenoproteïnes. Així el mutant selD[ptuf] no té selenoproteïnes i acumula radicals lliures el que el converteix en un model perfecte per a l'estudi dels efectes de l'estrès oxidatiu durant el desenvolupament.

2. Objectius. Els objectius concrets d'aquests tesi doctoral han estat:
- estudiar la relació entre les selenoproteïnes i la via de transducció del senyal Ras/MAPK
- analitzar quina o quines vies apoptòtiques s'engeguen en resposta a una situació d'estrès oxidatiu
- identificar selenoproteïnes concretes que poguessin explicar els fenotips observats

3. L'apartat de Resultats està dividit en tres capítols:
- Capítol 1: En aquest capítol es mostra com l'increment de radicals lliures causat per la mutació selD[ptuf] regula negativament la via Ras/MAPK (Morey et al., 2001 Dev Biol 238:145-156). També es demostra que el mutant és sensible a situacions d'estrès oxidatiu (Morey et al., 2003 FEBS Lett 534:111-114).
- Capítol 2: En aquest capítol es mostra com l'increment de radicals lliures causat per la mutació indueix apoptosi a través de la via Dmp53/Rpr (Morey et al., enviat a J. Cell Sci)
- Capítol 3: En aquest capítol es presenta la identificació dues noves selenoproteïnes: dselM i dselG (Castellano et al., 2001 EMBO Rep. 2: 697-702), les quals podrien ser les responsables dels fenotips observats .

4. L'apartat de Discussió està dividit en cinc seccions cada una de les quals prosa una funció del gen selD.
- La mutació selD[ptuf] genera una situació d'estrès oxidatiu.
- Importància de les selenoproteïnes de Drosophila en el control de ROS
- L'increment de ROS modula negativament la via Ras/MAPK
- L'increment de ROS activa l'apoptosi a través de la via Dmp53/Rpr
- Una visió integrada: defectes en proliferació i activació de l'apoptosi en el mutant selD[ptuf]

5. Conclusions. D'aquest treball se n'extreuen les següents conclusions:
- El gen selD modula la via Ras/MAPK a través de la síntesi de selenoproteïnes i la seva funció antioxidant
- L'increment de radicals lliures causat per la mutació selD[ptuf] engega l'apoptosi majoritàriament a través de la via depenent de caspases Dmp53/Rpr.
- A part de la selenoproteïna Sps2, Drosophila té dues altres selenoproteïnes: dselG i dselM.
APA, Harvard, Vancouver, ISO, and other styles
2

Rakgotho, Patrick Mpho. "Identification of proteins that interact with DWNN domain of SNAMA a member of a novel protein superfamily." Thesis, 2008. http://hdl.handle.net/10539/5784.

Full text
Abstract:
SNAMA is a 142 kDa Drosophila melanogaster protein, which consists of the uncharacterized conserved domain with no name (DWNN), zinc and RING finger-like motifs. The primary structure of SNAMA suggests that it might play an important role in cell cycle regulation and apoptosis. Previous studies revealed that homozygous SNAMA mutants underwent ectopic apoptosis which resulted in recessive lethality. SNAMA orthologues such P2P-R, PACT and RBBP6 are involved in cell cycle regulation, whereas Mpe1 is involved in mRNA processing. The aim of this study was to map out the role of SNAMA by isolating proteins which interact with it. DWNN was inserted into pGEX6P-2, phylexzeo plasmid (bait) and the Drosophila 0-12 hours cDNA library inserted in pJG4-5 (prey). The bait and the prey plasmid were used to transform appropriate yeast cells to probe for interacting proteins in yeast two hybrid assays, whereas the pGEX6P-2 was used for heterologous overexpression of DWNN in E. coli. Immunoprecipitation assays were also carried out with the crude protein extract from embryos, adult wild type, SNAMA mutant flies and the overexpressed protein using antibodies against SNAMA, Drosophila p53 Human DWNN and GST. The hybrid assay did not produce any interactors. Some of the proteins obtained from the immunoprecipitations were isolated and sequenced. The proteins identified were hsp82, Hsp70 and CG2985-PA. Data obtained from the immunoprecipitations suggest that SNAMA like Dmp53 might be involved in cell cycle regulation.
APA, Harvard, Vancouver, ISO, and other styles
3

Nweke, Ekene Emmanuel. "Temporal expression of Dmp53 and SNAMA isoforms and their relation to genotoxic stress." Thesis, 2015. http://hdl.handle.net/10539/18574.

Full text
Abstract:
A dissertation submitted to the Faculty of Science, University of the Witwatersrand, in fulfilment of the requirements for the degree of Master of Science. Johannesburg, 2015.
RBBP6 is an E3 Ubiquitin ligase protein with a U-box motif. It interacts with p53 and Rb and is linked to several cellular functions. SNAMA is the Drosophila RBBP6 homolog, but is less characterized than its vertebrate counterparts. Gene expression studies on Drosophila have a potential to advance the knowledge on molecular mechanism underlying genotoxic stress. Previous studies have shown that SNAMA plays a critical role as an apoptosis suppressor and possibly in responses to genotoxic stress. The molecular basis for this is, however, unknown. Initially, two isoforms were identified by bioinformatics and one (Snama A) experimentally as well. Here, we confirm experimentally the existence of the second isoform (Snama B). We also show that these are differentially expressed during development and when the organism undergoes genotoxic stress. Total RNA samples were used to demonstrate gene expression by using Reverse Transcriptase Polymerase Chain Reaction. Using samples collected at different stages of development and from adult flies treated with the DNA damaging agent, irinotecan, it is shown that these isoforms are differentially expressed throughout development and upon genotoxic stress. This knowledge may help to understand the functional role SNAMA plays in normal physiology and in response to genotoxic stress. Furthermore, the results show that SNAMA is involved in a potentially beneficial intervention whereby the glycolytic pathway is bypassed by the addition of methyl pyruvate.
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Dmp53"

1

Ayad, Shirley, Ray Boot-Handford, Martin J. Humphries, Karl E. Kadler, and Adrian Shuttleworth. "Dentine sialoprotein DMP3." In The Extracellular Matrix FactsBook, 131–32. Elsevier, 1998. http://dx.doi.org/10.1016/b978-012068911-8.50127-5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Dmp53' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography