Добірка наукової літератури з теми "RecQ4 helicases"
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Статті в журналах з теми "RecQ4 helicases"
Thangavel, Saravanabhavan, Ramiro Mendoza-Maldonado, Erika Tissino, Julia M. Sidorova, Jinhu Yin, Weidong Wang, Raymond J. Monnat, Arturo Falaschi, and Alessandro Vindigni. "Human RECQ1 and RECQ4 Helicases Play Distinct Roles in DNA Replication Initiation." Molecular and Cellular Biology 30, no. 6 (January 11, 2010): 1382–96. http://dx.doi.org/10.1128/mcb.01290-09.
Повний текст джерелаBACHRATI, Csanád Z., and Ian D. HICKSON. "RecQ helicases: suppressors of tumorigenesis and premature aging." Biochemical Journal 374, no. 3 (September 15, 2003): 577–606. http://dx.doi.org/10.1042/bj20030491.
Повний текст джерелаRogers, Cody M., Elsbeth Sanders, Phoebe A. Nguyen, Whitney Smith-Kinnaman, Amber L. Mosley, and Matthew L. Bochman. "The Genetic and Physical Interactomes of the Saccharomyces cerevisiae Hrq1 Helicase." G3: Genes|Genomes|Genetics 10, no. 12 (October 28, 2020): 4347–57. http://dx.doi.org/10.1534/g3.120.401864.
Повний текст джерелаRogers, Cody M., Chun-Ying Lee, Samuel Parkins, Nicholas J. Buehler, Sabine Wenzel, Francisco Martínez-Márquez, Yuichiro Takagi, Sua Myong, and Matthew L. Bochman. "The yeast Hrq1 helicase stimulates Pso2 translesion nuclease activity and thereby promotes DNA interstrand crosslink repair." Journal of Biological Chemistry 295, no. 27 (May 5, 2020): 8945–57. http://dx.doi.org/10.1074/jbc.ra120.013626.
Повний текст джерелаSéguéla-Arnaud, Mathilde, Wayne Crismani, Cécile Larchevêque, Julien Mazel, Nicole Froger, Sandrine Choinard, Afef Lemhemdi та ін. "Multiple mechanisms limit meiotic crossovers: TOP3α and two BLM homologs antagonize crossovers in parallel to FANCM". Proceedings of the National Academy of Sciences 112, № 15 (30 березня 2015): 4713–18. http://dx.doi.org/10.1073/pnas.1423107112.
Повний текст джерелаPark, Youngji, Guangbin Luo, and Stanton Gerson. "Repopulation Advantage of Blm−/− Cells in the Primary Recipients Can Be Reversed by Cisplatin Treatment." Blood 104, no. 11 (November 16, 2004): 2683. http://dx.doi.org/10.1182/blood.v104.11.2683.2683.
Повний текст джерелаCheok, C. F., C. Z. Bachrati, K. L. Chan, C. Ralf, L. Wu, and I. D. Hickson. "Roles of the Bloom's syndrome helicase in the maintenance of genome stability." Biochemical Society Transactions 33, no. 6 (October 26, 2005): 1456–59. http://dx.doi.org/10.1042/bst0331456.
Повний текст джерелаGarige, Mamatha, and Sudha Sharma. "Cellular Deficiency of Werner Syndrome Protein or RECQ1 Promotes Genotoxic Potential of Hydroquinone and Benzo[a]pyrene Exposure." International Journal of Toxicology 33, no. 5 (September 2014): 373–81. http://dx.doi.org/10.1177/1091581814547422.
Повний текст джерелаGupta, Sonia Vidushi, and Kristina Hildegard Schmidt. "Maintenance of Yeast Genome Integrity by RecQ Family DNA Helicases." Genes 11, no. 2 (February 18, 2020): 205. http://dx.doi.org/10.3390/genes11020205.
Повний текст джерелаPike, Ashley C. W., Shivasankari Gomathinayagam, Paolo Swuec, Matteo Berti, Ying Zhang, Christina Schnecke, Francesca Marino, et al. "Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: Insights from DNA complex structures." Proceedings of the National Academy of Sciences 112, no. 14 (March 23, 2015): 4286–91. http://dx.doi.org/10.1073/pnas.1417594112.
Повний текст джерелаДисертації з теми "RecQ4 helicases"
THANGAVEL, SARAVANA BHAVAN. "Characterization of the Role of RecQ helicases in human DNA replication." Doctoral thesis, Scuola Normale Superiore, 2010. http://hdl.handle.net/11384/85963.
Повний текст джерелаMojumdar, Aditya. "Structural and Biochemical study of human RECQ4." Doctoral thesis, Università degli studi di Trieste, 2015. http://hdl.handle.net/10077/11141.
Повний текст джерелаRecQ helicases belong to a ubiquitous family of DNA unwinding enzymes that are essential to maintain genome stability by acting at the interface between DNA replication, recombination and repair. Humans have five different paralogues of RecQ helicases namely RecQ1, BLM, WRN, RecQ4 and RecQ5. This work focuses on the structural and biochemical study of human RecQ4. Germ-line mutations in the RECQ4 gene give rise to three distinct human genetic disorders (Rothmund-Thomson, RAPADILINO and Baller-Gerold syndromes). Despite the important roles of RecQ4 in various cellular processes, RecQ4 have never been fully characterized. In addition to the helicase domain, RecQ4 has a unique N-terminal part that is essential for viability and is constituted by a region homologous to the yeast Sld2 replication initiation factor, followed by a cysteine-rich region, predicted to fold as a Zn knuckle. A part of this work focuses on the structural and biochemical analysis of both the human and Xenopus RecQ4 cysteine-rich regions, and shows by NMR spectroscopy that the Xenopus fragment does indeed assumes the canonical Zn knuckle fold, whereas the human sequence remains unstructured, consistent with the mutation of one of the Zn ligands. Both the human and Xenopus Zn knuckles bind to a variety of nucleic acid substrates, with a preference for RNA. We also investigated the effect of an additional Sld2 homologous region upstream the Zn knuckle. In both the human and Xenopus system, the presence of this region strongly enhances binding to nucleic acids. These results reveal novel possible roles of RecQ4 in DNA replication and genome stability. Recently the catalytic core of RecQ4 has been predicted to include RecQ-like-C-terminal (RQC) domain at the C-terminus of the helicase domain, similar to other RecQ helicases. This domain is composed of a Zn-binding region and a winged helix (WH) domain. Another part of this thesis centers on the structural and biochemical characterization of the catalytic core of RecQ4 including the helicase and RQC domain. The results provide an insight in the Zn binding ligands present in the RQC domain that plays a role in DNA binding and unwinding activity of the protein. Also the presence of the characteristic aromatic residue at the tip of the WH β hairpin and its role in DNA binding and unwinding has been established. Finally, it provides a low resolution SAXS model of the catalytic core of RecQ4.
Elicasi RecQ appartengono a una famiglia ubiquitaria di DNA svolgimento enzimi che sono essenziali per mantenere la stabilità del genoma agendo all'interfaccia tra replicazione del DNA, ricombinazione e riparazione. Gli esseri umani hanno cinque diversi paralogues di RecQ elicasi cioè RecQ1, BLM, WRN, RecQ4 e RecQ5. Questo lavoro si concentra sullo studio strutturale e biochimica di RecQ4 umana. Mutazioni germinali nel gene RECQ4 danno luogo a tre malattie genetiche umane distinte (Rothmund-Thomson, RAPADILINO e sindromi Baller-Gerold). Nonostante i ruoli importanti di RecQ4 in diversi processi cellulari, RecQ4 non sono mai stati pienamente caratterizzato. In aggiunta al dominio elicasi, RecQ4 ha una parte unica N-terminale che è essenziale per la vitalità ed è costituito da una regione omologa al lievito Sld2 fattore di iniziazione replica, seguita da una regione ricca di cisteina, previsto per piegare come stinco Zn . Una parte di questo lavoro si concentra sull'analisi strutturale e biochimica sia della regioni ricche di cisteina Xenopus RecQ4 umana e, e spettacoli di spettroscopia NMR che il frammento Xenopus effettivamente assume la canonica Zn nocca volte, mentre la sequenza di resti umani non strutturato, coerente con la mutazione di uno dei ligandi Zn. Sia il nocche Xenopus Zn umana e si legano ad una varietà di substrati di acido nucleico, con una preferenza per l'RNA. Abbiamo anche studiato l'effetto di un ulteriore regione omologa Sld2 monte la nocca Zn. Sia il sistema Xenopus umano e, la presenza di questa regione migliora fortemente legame ad acidi nucleici. Questi risultati rivelano possibili ruoli nuovi di RecQ4 nella replicazione del DNA e la stabilità del genoma. Recentemente il nucleo catalitico di RecQ4 stato previsto per includere RecQ-like-C-terminale (RQC) dominio al C-terminale del dominio elicasi, simile ad altri elicasi RecQ. Questo dominio è costituito da una regione-Zn vincolanti e un'elica alato (WH) dominio. Un'altra parte di questa tesi incentrata sulla caratterizzazione strutturale e biochimica del nucleo catalitico della RecQ4 compreso il elicasi e il dominio RQC. I risultati forniscono una descrizione nel Zn ligandi presenti nel dominio RQC che svolge un ruolo nel legame al DNA e l'attività svolgimento della proteina legante. Inoltre è stata stabilita la presenza della caratteristica residuo aromatico sulla punta della forcella WH β e il suo ruolo nel legame al DNA e di svolgimento. Infine, esso fornisce una bassa risoluzione SAXS modello del nucleo catalitico di RecQ4.
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Ren, Hua. "Aspects moléculaires des hélicases de la famille de RecQ." Phd thesis, École normale supérieure de Cachan - ENS Cachan, 2009. http://tel.archives-ouvertes.fr/tel-00448084.
Повний текст джерелаKaiser, Sebastian [Verfasser], and Caroline [Gutachter] Kisker. "A RecQ helicase in disguise: Characterization of the unconventional Structure and Function of the human Genome Caretaker RecQ4 / Sebastian Kaiser ; Gutachter: Caroline Kisker." Würzburg : Universität Würzburg, 2019. http://d-nb.info/1206879246/34.
Повний текст джерелаGuo, Rongbing. "Biochemical and structural characterization of BLM Helicase." Paris 11, 2008. http://www.theses.fr/2008PA112168.
Повний текст джерелаBloom's syndrome (BS) is an autosomal recessive disorder, showing high frequency of sister chromatid exchange in lymphocyte of the patients. Since BS is preposition of a wide spectrum of cancer, the syndrome has been studied for understanding of the mechanism of cancer extensively. Ln the first part, we proved the existence of a zinc-binding domain in which a zinc ion is coordinated by four cysteines residues in RecQ-Ct domain of BLM. This conclusion is drawn from our biophysical and biochemical studies. We modeled the 3D structure of BLM protein based on that of E. Coli RecQ helicase, which revealed a similar structural domain in both helicases that coordinate zinc. The results from experiments with three mutants showed that their enzymatic activities were severely reduced or abrogated. The demetalization of zinc from BLM had no influence on the activities of BLM, but it would decrease the themostability of the protein. Ln conclusion, BLM contains a zinc binding domain with one zinc ion in each protein. The second part of our studies includes the work for understanding of causative molecular mechanism of missense mutations which happened in helicase domain of BLM found in BS patients. On the basis of the work inthe fist part, we further modeled the 3D structure of BLM in complex with A TPyS and DNA. With the model, we deduced the possible causative mechanism of mutants. We produced mutant proteins and purified them to homogeneity. The A TPase activity, A TP binding activity, DNA binding activity and helicase activity ofthe mutants were ail checked. Ln conclusion 1 showed that: 1. BLM642-129o possibly employ an "inchworm" model mechanism; 2. Amino acid residues from 861 to 901 are imprtant for DNA binding; 3. DNA binding ofBLM is mainly controlled by lobe2 and lobe3, lobel contribute to a transient ssDNA binding; 4. The annealing activity of RecQ helicase suggests a weak DNA binding activity
Budhathoki, Jagat B. "Interactions of RecQ-Family Helicases with G-quadruplex Structures at the Single Molecule Level." Kent State University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=kent1467765011.
Повний текст джерелаHuber, Michael D. "Structure-function analysis and substrate specific inhibition of RecQ helicases /." Thesis, Connect to this title online; UW restricted, 2005. http://hdl.handle.net/1773/9253.
Повний текст джерелаBajpai, Sailesh. "Analysis of human RECQ1 helicase function in cells." Thesis, Open University, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.522223.
Повний текст джерелаLevitt, Nicola C. "Role of RecQ helicases in maintenance of genome integrity." Thesis, University of Oxford, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.275469.
Повний текст джерелаLucic, Bojana. "Understanding the structural basis of the human RECQ1 helicase function." Thesis, Open University, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.536078.
Повний текст джерелаКниги з теми "RecQ4 helicases"
Lombard, David B. Biochemistry and genetics of recq-helicases. Boston, MA: Kluwer Academic Publishers, 2001.
Знайти повний текст джерелаLombard, David B. Biochemistry and Genetics of RecQ-Helicases. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1405-3.
Повний текст джерелаLombard, David B. Biochemistry and genetics of recq-helicases. Boston, MA: Kluwer Academic Publishers, 2001.
Знайти повний текст джерелаLombard, David B. Biochemistry and Genetics of RecQ-Helicases. Springer, 2012.
Знайти повний текст джерелаLombard, David B. Biochemistry and Genetics of Recq-Helicases. Springer London, Limited, 2012.
Знайти повний текст джерелаLombard, David B. Biochemistry and Genetics of RecQ-Helicases. Springer, 2000.
Знайти повний текст джерелаЧастини книг з теми "RecQ4 helicases"
Lombard, David B. "The RecQ-family helicases." In Biochemistry and Genetics of RecQ-Helicases, 3–19. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1405-3_1.
Повний текст джерелаLu, Linchao, Weidong Jin, Hao Liu, and Lisa L. Wang. "RECQ DNA Helicases and Osteosarcoma." In Advances in Experimental Medicine and Biology, 129–45. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-04843-7_7.
Повний текст джерелаLu, Linchao, Weidong Jin, and Lisa L. Wang. "RECQ DNA Helicases and Osteosarcoma." In Current Advances in the Science of Osteosarcoma, 37–54. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-43085-6_3.
Повний текст джерелаMohaghegh, Payam, and Ian D. Hickson. "Biochemical Roles of RecQ Helicases." In Molecular Mechanisms of Werner’s Syndrome, 12–21. Boston, MA: Springer US, 2004. http://dx.doi.org/10.1007/978-1-4419-9032-7_2.
Повний текст джерелаLombard, David B. "Targeting the WRN Locus in the mouse." In Biochemistry and Genetics of RecQ-Helicases, 21–41. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1405-3_2.
Повний текст джерелаLombard, David B. "Interaction of the BLM protein with Topo III alpha in Somatic and meiotic cells." In Biochemistry and Genetics of RecQ-Helicases, 43–58. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1405-3_3.
Повний текст джерелаLombard, David B. "Nijmegen Breakage Syndrome disease protein and Mre11 at PML Nuclear Bodies and meiotic telomeres." In Biochemistry and Genetics of RecQ-Helicases, 59–76. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1405-3_4.
Повний текст джерелаLarsen, Nicolai Balle, and Ian D. Hickson. "RecQ Helicases: Conserved Guardians of Genomic Integrity." In Advances in Experimental Medicine and Biology, 161–84. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5037-5_8.
Повний текст джерелаKobbe, Daniela, Manfred Focke, and Holger Puchta. "Purification and Characterization of RecQ Helicases of Plants." In Methods in Molecular Biology, 195–209. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-355-8_14.
Повний текст джерелаSeki, Masayuki, Shusuke Tada, and Takemi Enomoto. "Function of RECQ family helicase in genome stability." In Subcellular Biochemistry, 49–73. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/978-1-4020-4896-8_5.
Повний текст джерелаТези доповідей конференцій з теми "RecQ4 helicases"
Zuo, Mingxin, David Maxwell, Basvoju A. Bhanu Prasad, Zhenghong Peng, William Bornmann, and Milind M. Javle. "Abstract 5361: Development of targeted inhibitors against RecQ1 helicase." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-5361.
Повний текст джерелаLao, Victoria Valinluck, Kelly T. Carter, Peter S. Rabinovitch, Piri Welcsh, and William M. Grady. "Abstract 1157: Increased expression of RecQ helicases in sporadic primary colorectal cancers." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1157.
Повний текст джерелаChun, Stephen G., Nelson S. Yee, Fang Qi, Richard Allsopp, Philip M. Davy, Keith S. Fong, Michele Carbone, and Peter K. Bryant-Greenwood. "Abstract 3209: The WRN RecQ helicase acts as a tumor suppressor in pancreatic adenocarcinoma." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3209.
Повний текст джерелаWelcsh, Piri, Keffy Kehrli, Paul Lazarchuk, and Julia Sidorova. "Abstract POSTER-BIOL-1346: Growth-suppressive effect of WRN RECQ helicase inactivation in breast and ovarian cancer cells." In Abstracts: 10th Biennial Ovarian Cancer Research Symposium; September 8-9, 2014; Seattle, WA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1557-3265.ovcasymp14-poster-biol-1346.
Повний текст джерела