Výsledky vyhledávání - "DNA ligase activity"

Altered DNA ligase activity in human disease

Autor: Seema Khattri Bhandari, Tasmin Naila, Alan E. Tomkinson

Publikováno v: Mutagenesis

The joining of interruptions in the phosphodiester backbone of DNA is critical to maintain genome stability. These breaks, which are generated as part of normal DNA transactions, such as DNA replication, V(D)J recombination and meiotic recombination

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ee262aef5d5ef0fd2ae255a6068b7f6
https://doi.org/10.1093/mutage/gez026

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DNA Damage and Repair in Patients With Coronary Artery Disease: Correlation With Plaque Morphology Using Optical Coherence Tomography (DECODE Study)

Autor: Ruan M. Elliott, Paul Kolm, Nikunj Shah, Stephen P. Hoole, Mark Mariathas, Martin R. Bennett, Hector M. Garcia-Garcia, Kazuhiro Dan, Kayode O. Kuku, Nick E.J. West, Lisiane B. Meira, Nick Curzen, Michael Mahmoudi, Adam J. Brown

Publikováno v: Cardiovascular Revascularization Medicine. 20:812-818

Objective The aim of this study was to examine DNA ligase activity and expression of DNA damage response pathway (DDR) genes in patients with stable angina (SA) and non-ST elevation myocardial infarction (NSTEMI) and determine whether they correlate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d5a46474acd4b54c04ab8afc9ba1d8a
https://doi.org/10.1016/j.carrev.2019.04.028

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Deoxyribonucleic Acid Repair Activity Is Associated with Healed Coronary Plaque Rupture by Optical Coherence Tomography

Autor: Nikunj Shah, Michael Mahmoudi, Paul Kolm, Nick Curzen, Martin R. Bennett, Kazuhiro Dan, Hector M. Garcia-Garcia, Kayode O. Kuku, Omar Yacob, Ron Waksman

Publikováno v: Journal of Cardiovascular Translational Research. 12:608-610

Deoxyribonucleic acid (DNA) damage and repair signaling cascades are related to the development of atherosclerosis. Pathological studies have demonstrated that healed coronary plaque rupture (HCPR) contributes to plaque progression and predisposes to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be1c629e50ee2ed647e3c42d71d9175f
https://doi.org/10.1007/s12265-019-09904-2

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Mutational phospho-mimicry reveals a regulatory role for the XRCC4 and XLF C-terminal tails in modulating DNA bridging during classical non-homologous end joining

Autor: Abinadabe J. de Melo, Stephane Betzi, Katheryn Meek, Davide Normanno, Mauro Modesti, Aurélie Négrel

Publikováno v: eLife
eLife, eLife Sciences Publication, 2017, 6, ⟨10.7554/eLife.22900⟩
eLife, Vol 6 (2017)
eLife, 2017, 6, ⟨10.7554/eLife.22900⟩

XRCC4 and DNA Ligase 4 (LIG4) form a tight complex that provides DNA ligase activity for classical non-homologous end joining (the predominant DNA double-strand break repair pathway in higher eukaryotes) and is stimulated by XLF. Independently of LIG

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67e709d08f7af1644184b943b9f33589
https://hal.archives-ouvertes.fr/hal-01541119

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Phaeocystis globosa Virus DNA Polymerase X: A >swiss Army knife>, Multifunctional DNA polymerase-lyase-ligase for Base Excision Repair

Autor: Corina P. D. Brussaard, Miguel de Vega, Ana de Ory, José L. Fernández-García

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)

Phaeocystis globosa virus 16T is a giant virus that belongs to the so-called nucleo-cytoplasmic large DNA virus (NCLDV) group. Its linear dsDNA genome contains an almost full complement of genes required to participate in viral base excision repair (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6aa958644b366ef402324bc3f3360d8d
http://hdl.handle.net/10261/166316

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Mutations of Asp540 and the domain-connecting residues synergistically enhance Pyrococcus furiosus DNA ligase activity

Autor: Hirokazu Nishida, Maiko Tanabe, Sonoko Ishino, Yoshizumi Ishino

Publikováno v: FEBS Letters. 588:230-235

The structure of Pyrococcus furiosus DNA ligase (PfuLig), which architecturally resembles human DNA ligase I (hLigI), revealed that the C-terminal helix stabilizes the closed conformation through several ionic interactions between two domains (adenyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff5e7758a7dd469fb3cde3d21cabb543
https://doi.org/10.1016/j.febslet.2013.10.037

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A High-Throughput Fluorescence Resonance Energy Transfer-Based Assay for DNA Ligase

Autor: Ann E. Eakin, Adam B. Shapiro, Grant K. Walkup, Olga Rivin

Publikováno v: SLAS Discovery. 16:486-493

DNA ligase is the enzyme that catalyzes the formation of the backbone phosphodiester bond between the 5'-PO(4) and 3'-OH of adjacent DNA nucleotides at single-stranded nicks. These nicks occur between Okazaki fragments during replication of the laggi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::948510ead29a29f368b8f6ccaa6ee0b3
https://doi.org/10.1177/1087057111398295

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Label-Free Electrochemical Monitoring of DNA Ligase Activity

Autor: Miroslav Fojta, Jan Vacek, Richard P. Bowater, Desmond R. Bullard, Manuel Lavesa-Curto, Emil Paleček, Katerina Cahova

Publikováno v: Analytical Chemistry. 80:7609-7613

This study presents a simple, label-free electrochemical technique for the monitoring of DNA ligase activity. DNA ligases are enzymes that catalyze joining of breaks in the backbone of DNA and are of significant scientific interest due to their essen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1e5c645639a24b4dea1aabe29d180ff
https://doi.org/10.1021/ac801268p

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