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Dynamics of DNA Supercoil Relaxation by Type II Topoisomerases [PDF]

open access: yesBiophysical Journal, 2011
Dynamics of DNA supercoil relaxation by type II topoisomerasesQing Shao∗, Laura Finzi∗, and David Dunlap#Dept. of Physics∗ and Cell Biology#, Emory University, Atlanta, GA 30322Type II topoisomerases are some of the main targets of anti-cancer drugs, since they catalyze DNA decatenation and unwinding which is crucial for cell division. A recent crystal
Shao, Qing, Dunlap, David, Finzi, Laura
openaire   +1 more source

Arabidopsis thaliana GYRB3 does not encode a DNA gyrase subunit.

open access: yesPLoS ONE, 2010
BackgroundDNA topoisomerases are enzymes that control the topology of DNA in all cells. DNA gyrase is unique among the topoisomerases in that it is the only enzyme that can actively supercoil DNA using the free energy of ATP hydrolysis.
Katherine M Evans-Roberts   +4 more
doaj   +1 more source

“Breaking up is hard to do”: the formation and resolution of sister chromatid intertwines [PDF]

open access: yes, 2014
The absolute necessity to resolve every intertwine between the two strands of the DNA double helix provides a massive challenge to the cellular processes that duplicate and segregate chromosomes.
Bartkova   +110 more
core   +1 more source

Alignment and phylogenetic analysis of type II DNA topoisomerases [PDF]

open access: yesJournal of Biosciences, 1996
DNA topoisomerases have been evolved to solve the topological problems of DNA during replication, transcription, recombination and segregation. Discovery of several new enzymes and their characterization has necessitated this compilation. This analysis shows the distinct evolutionary relatedness of type II DNA topoisomerases.
Madhusudan, K, Nagaraja, V
openaire   +2 more sources

Structural basis of gate-DNA breakage and resealing by type II topoisomerases.

open access: yesPLoS ONE, 2010
Type II DNA topoisomerases are ubiquitous enzymes with essential functions in DNA replication, recombination and transcription. They change DNA topology by forming a transient covalent cleavage complex with a gate-DNA duplex that allows transport of a ...
Ivan Laponogov   +5 more
doaj   +1 more source

Local selection rules that can determine specific pathways of DNA unknotting by type II DNA topoisomerases [PDF]

open access: yes, 2017
We performed numerical simulations of DNA chains to understand how local geometry of juxtaposed segments in knotted DNA molecules can guide type II DNA topoisomerases to perform very efficient relaxation of DNA knots.
Burnier, Yannis   +3 more
core  

Dammarenediol II enhances etoposide‐induced apoptosis by targeting O‐GlcNAc transferase and Akt/GSK3β/mTOR signaling in liver cancer

open access: yesMolecular Oncology, EarlyView.
Etoposide induces DNA damage, activating p53‐dependent apoptosis via caspase‐3/7, which cleaves PARP1. Dammarenediol II enhances this apoptotic pathway by suppressing O‐GlcNAc transferase activity, further decreasing O‐GlcNAcylation. The reduction in O‐GlcNAc levels boosts p53‐driven apoptosis and influences the Akt/GSK3β/mTOR signaling pathway ...
Jaehoon Lee   +8 more
wiley   +1 more source

Structural insights into the DNA topoisomerase II of the African swine fever virus

open access: yesNature Communications
Type II topoisomerases are ubiquitous enzymes that play a pivotal role in modulating the topological configuration of double-stranded DNA. These topoisomerases are required for DNA metabolism and have been extensively studied in both prokaryotic and ...
Jingyuan Cong   +8 more
doaj   +1 more source

Probabilidades de transición en diagramas de nudos [PDF]

open access: yes, 2015
Treballs Finals de Grau de Matemàtiques, Facultat de Matemàtiques, Universitat de Barcelona, Any: 2015, Director: Carles CasacubertaSome enzymes like condensins or type II topoisomerases are capable of changing the topology of cyclic DNA molecules.
Orenes Chueca, Pablo
core  

Crystallization and preliminary crystallographic analysis of the DNA gyrase B protein from B-stearothermophilus [PDF]

open access: yes, 1996
DNA gyrase B (GyrB) from B. stearothermophilus has been crystallized in the presence of the non-hydrolyzable ATP analogue, 5'-adenylpl-beta-gamma-imidodiphosphate (ADPNP), by the dialysis method.
Brannigan, J A   +4 more
core   +2 more sources

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