Relevant bibliographies by topics / RuvB-like

Contents

  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'RuvB-like'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 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 'RuvB-like.'

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 "RuvB-like"

1

Kanemaki, Masato, Yumiko Kurokawa, Toru Matsu-ura, et al. "TIP49b, a New RuvB-like DNA Helicase, Is Included in a Complex Together with Another RuvB-like DNA Helicase, TIP49a." Journal of Biological Chemistry 274, no. 32 (1999): 22437–44. http://dx.doi.org/10.1074/jbc.274.32.22437.

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

Qiu, Xiao-Bo, Yi-Ling Lin, Kelly C. Thome, et al. "An Eukaryotic RuvB-like Protein (RUVBL1) Essential for Growth." Journal of Biological Chemistry 273, no. 43 (1998): 27786–93. http://dx.doi.org/10.1074/jbc.273.43.27786.

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

Kakugawa, Satoshi, Masayuki Shimojima, Gabriele Neumann, Hideo Goto, and Yoshihiro Kawaoka. "RuvB-Like Protein 2 Is a Suppressor of Influenza A Virus Polymerases." Journal of Virology 83, no. 13 (2009): 6429–34. http://dx.doi.org/10.1128/jvi.00293-09.

Full text
Abstract:
ABSTRACT In pro- and eukaryotic cells, RuvB-like protein 2 (RBL2) resolves Holliday junction recombination intermediates. Here, we identified RBL2 as a suppressor of influenza A virus replication. Human RBL2 appears to interfere with the oligomerization of the viral nucleoprotein, a critical step in the assembly of viral replication complexes.
APA, Harvard, Vancouver, ISO, and other styles
4

Rodríguez, Carlos F., and Oscar Llorca. "RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes." Cells 9, no. 5 (2020): 1139. http://dx.doi.org/10.3390/cells9051139.

Full text
Abstract:
The Rvb1-Rvb2-Tah1-Pih1 (R2TP) complex is a co-chaperone complex that works together with HSP90 in the activation and assembly of several macromolecular complexes, including RNA polymerase II (Pol II) and complexes of the phosphatidylinositol-3-kinase-like family of kinases (PIKKs), such as mTORC1 and ATR/ATRIP. R2TP is made of four subunits: RuvB-like protein 1 (RUVBL1) and RuvB-like 2 (RUVBL2) AAA-type ATPases, RNA polymerase II-associated protein 3 (RPAP3), and the Protein interacting with Hsp90 1 (PIH1) domain-containing protein 1 (PIH1D1). R2TP associates with other proteins as part of a
APA, Harvard, Vancouver, ISO, and other styles
5

Gospodinov, Anastas, and Boyka Anachkova. "Lack of Effect of RuvB-Like Proteins on DNA Damage Signaling Activation." Zeitschrift für Naturforschung C 65, no. 1-2 (2010): 148–52. http://dx.doi.org/10.1515/znc-2010-1-223.

Full text
Abstract:
Ataxia telangiectasia mutated (ATM) kinase is a central player in cellular response to DNA damage. Phosphorylation of the histone H2AX by ATM is required for the accumulation of repair proteins at the sites of double-strand breaks. Recently, it was reported that the histone acetyltransferase Tat interactive protein-60 (TIP60) is required to acetylate ATM prior to its activation. The RuvB-like proteins TIP48 and TIP49 are known to be necessary for the assembly and functional activity of the TIP60 acetyltransferase complex. In the present communication, we investigated the requirements of TIP48
APA, Harvard, Vancouver, ISO, and other styles
6

Magalska, Adriana, Anna Katharina Schellhaus, Daniel Moreno-Andrés, et al. "RuvB-like ATPases Function in Chromatin Decondensation at the End of Mitosis." Developmental Cell 31, no. 3 (2014): 305–18. http://dx.doi.org/10.1016/j.devcel.2014.09.001.

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

Niewiarowski, Andrew, Alison S. Bradley, Jayesh Gor, Adam R. McKay, Stephen J. Perkins, and Irina R. Tsaneva. "Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes." Biochemical Journal 429, no. 1 (2010): 113–25. http://dx.doi.org/10.1042/bj20100489.

Full text
Abstract:
The two closely related eukaryotic AAA+ proteins (ATPases associated with various cellular activities), RuvBL1 (RuvB-like 1) and RuvBL2, are essential components of large multi-protein complexes involved in diverse cellular processes. Although the molecular mechanisms of RuvBL1 and RuvBL2 function remain unknown, oligomerization is likely to be important for their function together or individually, and different oligomeric forms might underpin different functions. Several experimental approaches were used to investigate the molecular architecture of the RuvBL1–RuvBL2 complex and the role of th
APA, Harvard, Vancouver, ISO, and other styles
8

Mu, Xin, Yajing Fu, Yiping Zhu, et al. "HIV-1 Exploits the Host Factor RuvB-like 2 to Balance Viral Protein Expression." Cell Host & Microbe 18, no. 2 (2015): 233–42. http://dx.doi.org/10.1016/j.chom.2015.06.018.

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

Makino, Yasutaka, Masato Kanemaki, Yumiko Kurokawa, Takehiko Koji, and Taka-aki Tamura. "A Rat RuvB-like Protein, TIP49a, Is a Germ Cell-enriched Novel DNA Helicase." Journal of Biological Chemistry 274, no. 22 (1999): 15329–35. http://dx.doi.org/10.1074/jbc.274.22.15329.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Gorynia, Sabine, Pedro M. Matias, Susana Gonçalves, et al. "Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1." Acta Crystallographica Section F Structural Biology and Crystallization Communications 62, no. 1 (2005): 61–66. http://dx.doi.org/10.1107/s1744309105041400.

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

Dissertations / Theses on the topic "RuvB-like"

1

Papin, Christophe. "Mécanisme moléculaire de l'hélicase AAA+ TIP49B." Toulouse 3, 2008. http://thesesups.ups-tlse.fr/819/.

Full text
Abstract:
Le déroulement des molécules d'acide nucléique est un mécanisme nécessaire à tous les processus génétiques fondamentaux comme la réplication, la réparation, la recombinaison, la transcription, la synthèse des ribosomes, le remodelage de la chromatine ou encore la maturation des ARN. Dans chacun de ces processus, le déroulement des duplex d'ADN et/ou ARN est catalysé par des enzymes connues sous le nom d'hélicase. Par leur fonction, les hélicases sont essentielles dans tous les aspects du métabolisme des acides nucléiques, et sont ubiquitaires, puisqu'elles ont été identifiées chez les procaryo
APA, Harvard, Vancouver, ISO, and other styles
2

Bradley, A. S. "Insights into the molecular mechanism of replication fork rescue by RuvAB and the putative role of the bacterial RuvB-like protein RarA and its human homologue WRNIP1." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/17976/.

Full text
Abstract:
The RuvAB(C) proteins promote branch migration and resolution of Holliday junctions (HJs) which form during homologous recombination and upon reversal of stalled replication forks. In addition to the function of RuvAB to process HJs formed at stalled forks, RuvAB have recently been shown to be required to reverse stalled replication forks into HJs (chicken foot structures) in certain E. coli replication mutants in vivo (Baharoglu et al., 2008). We introduced two mutations in RuvA which disrupted interactions between tetramers and used the new mutant (RuvA2KaP) to investigate RuvAB function at
APA, Harvard, Vancouver, ISO, and other styles
3

Hsiao, Chung-Jen, and 蕭崇仁. "Biochemical Characterization of RuvB-like DNA Helicases in Arabidopsis thaliana." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/09816533661341023957.

Full text
Abstract:
碩士<br>國立中興大學<br>生物科技學研究所<br>103<br>RuvBL1/RuvBL2 (RuvB-like) proteins are two ATP-dependent DNA helicase highly conserved in eukaryote from yeast to human. They present in various protein and nucleoprotein complexes which play roles in cellular processes including replication, transcription, chromatin remodeling, DNA repair, etc. Acting as indispensable enzymes and playing critical roles in major pathways closely linked to cancer, RuvBLs were heavily studied in human but much less in plant. We aim to characterize their roles firstly via biochemical analysis. Unlike yeast and human, Arabidopsis
APA, Harvard, Vancouver, ISO, and other styles
4

Li, You-Xian, and 李宥賢. "Molecular and Functional Characterization of RuvB-like DNA Helicases in Arabidopsis thaliana." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/3f23q9.

Full text
Abstract:
碩士<br>國立中興大學<br>生物科技學研究所<br>104<br>RuvB-like helicases (RuvBLs) are ATP-dependent DNA helicases which participate in DNA duplication, transcription, repairing, and chromatin remodeling. Constituted by RuvBL1 and RuvBL2, RuvBLs form dodecameric from two stacked heterohexamer. As RuvBLs involved in cancer-related processes and were essential for survivals of various organisms, they were heavily studied in mammalian cells but remained almost uninvestigated in plants. Arabidopsis contain one type I (RuvBL1) but two type II (RuvBL2-3/2-5) RuvBLs. According to the eFP browser transcriptome data, Ruv
APA, Harvard, Vancouver, ISO, and other styles
5

Chuang, Tsung-Hsien, and 莊宗憲. "Characterization of RuvB-like DNA helicases of Arabidopsis thaliana co-expressed in E. coli." Thesis, 2017. http://ndltd.ncl.edu.tw/handle/83146880118133039788.

Full text
Abstract:
碩士<br>國立中興大學<br>生物科技學研究所<br>105<br>RuvB-like 1 (RuvBL1) and RuvB-like 2 (RuvBL2) are members of the superfamily 6 (SF6) helicase that contain core AAA+ (ATPase associated with various cellular activities) domain for coupling chemical energy provided by ATP hydrolysis. The SF6 helicases were found to form hexamer or doubled hexamers with alternated RuvBL1 and RuvBL2. They are present in various protein and nucleoprotein complexes and play important roles in cellular processes including activities unrelated to DNA. Although RuvBLs are essential for viability in yeast, nematode, fruit fly, and ar
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'RuvB-like' 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