Cargando…

Role of Flexibility in Protein-DNA-Drug Recognition: The Case of Asp677Gly-Val703Ile Topoisomerase Mutant Hypersensitive to Camptothecin

Topoisomerases I are ubiquitous enzymes that control DNA topology within the cell. They are the unique target of the antitumor drug camptothecin that selectively recognizes the DNA-topoisomerase covalent complex and reversibly stabilizes it. The biochemical and structural-dynamical properties of the...

Descripción completa

Detalles Bibliográficos
Autores principales:	D'Annessa, Ilda, Tesauro, Cinzia, Fiorani, Paola, Chillemi, Giovanni, Castelli, Silvia, Vassallo, Oscar, Capranico, Giovanni, Desideri, Alessandro
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Hindawi Publishing Corporation 2012
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3270393/ https://www.ncbi.nlm.nih.gov/pubmed/22315664 http://dx.doi.org/10.1155/2012/206083

Ejemplares similares

Replacement of the Human Topoisomerase Linker Domain with the Plasmodial Counterpart Renders the Enzyme Camptothecin Resistant
por: Arnò, Barbara, et al.
Publicado: (2013)

Molecular mechanism of the camptothecin resistance of Glu710Gly topoisomerase IB mutant analyzed in vitro and in silico
por: Tesauro, Cinzia, et al.
Publicado: (2013)

Thr729 in human topoisomerase I modulates anti-cancer drug resistance by altering protein domain communications as suggested by molecular dynamics simulations
por: Chillemi, Giovanni, et al.
Publicado: (2008)

Mutations of human DNA topoisomerase I at poly(ADP-ribose) binding sites: modulation of camptothecin activity by ADP-ribose polymers
por: Tesauro, Cinzia, et al.
Publicado: (2014)

A single mutation in the 729 residue modulates human DNA topoisomerase IB DNA binding and drug resistance
por: Losasso, Carmen, et al.
Publicado: (2008)

Structural and Dynamical Effects Induced by the Anticancer Drug Topotecan on the Human Topoisomerase I – DNA Complex
por: Mancini, Giordano, et al.
Publicado: (2010)

Binding of an Indenoisoquinoline to the Topoisomerase-DNA Complex Induces Reduction of Linker Mobility and Strengthening of Protein-DNA Interaction
por: Mancini, Giordano, et al.
Publicado: (2012)

Simulations of DNA topoisomerase 1B bound to supercoiled DNA reveal changes in the flexibility pattern of the enzyme and a secondary protein–DNA binding site
por: D'Annessa, Ilda, et al.
Publicado: (2014)

The different cleavage DNA sequence specificity explains the camptothecin resistance of the human topoisomerase I Glu418Lys mutant
por: Fiorani, Paola, et al.
Publicado: (2006)

Antisense transcripts enhanced by camptothecin at divergent CpG-island promoters associated with bursts of topoisomerase I-DNA cleavage complex and R-loop formation
por: Marinello, Jessica, et al.
Publicado: (2013)

Evidence of the crucial role of the linker domain on the catalytic activity of human topoisomerase I by experimental and simulative characterization of the Lys681Ala mutant
por: Fiorani, Paola, et al.
Publicado: (2009)

ATP independent type IB topoisomerase of Leishmania donovani is stimulated by ATP: an insight into the functional mechanism
por: Sengupta, Souvik, et al.
Publicado: (2011)

Peptide Inhibition of Topoisomerase IB from Plasmodium falciparum
por: Roy, Amit, et al.
Publicado: (2011)

Development of Derivatives of 3, 3′-Diindolylmethane as Potent Leishmania donovani Bi-Subunit Topoisomerase IB Poisons
por: Roy, Amit, et al.
Publicado: (2011)

The open state of human topoisomerase I as probed by molecular dynamics simulation
por: Chillemi, Giovanni, et al.
Publicado: (2007)

Effect on DNA relaxation of the single Thr718Ala mutation in human topoisomerase I: a functional and molecular dynamics study
por: Chillemi, Giovanni, et al.
Publicado: (2005)

Dimethylmyricacene: An In Vitro and In Silico Study of a Semisynthetic Non-Camptothecin Derivative Compound, Targeting Human DNA Topoisomerase 1B
por: Ottaviani, Alessio, et al.
Publicado: (2022)

Three different mutations in the DNA topoisomerase 1B in Leishmania infantum contribute to resistance to antitumor drug topotecan
por: Rosa-Teijeiro, Chloé, et al.
Publicado: (2021)

DNA topoisomerase I inhibition by camptothecin induces escape of RNA polymerase II from promoter-proximal pause site, antisense transcription and histone acetylation at the human HIF-1α gene locus
por: Baranello, Laura, et al.
Publicado: (2010)

Síncope como Expressão Fenotípica da Amiloidose Hereditária por Transtirretina Val142Ile (Val122Ile)
por: Nunes, Nágela S. V., et al.
Publicado: (2020)

Role of the protein in the DNA sequence specificity of the cleavage site stabilized by the camptothecin topoisomerase IB inhibitor: a metadynamics study
por: Coletta, Andrea, et al.
Publicado: (2013)

The desoxazoline asidiacyclamide analogue cyclo(Gly–Thr–D-Val–Thz–Ile–Thr–D-Val–Thz) acetonitrile monosolvate
por: Asano, Akiko, et al.
Publicado: (2011)

Characterization of DNA Topoisomerase-1 in Spodoptera exigua for Toxicity Evaluation of Camptothecin and Hydoxy-Camptothecin
por: Zhang, Lan, et al.
Publicado: (2013)

Rarity of TLR4 Asp299Gly and Thr399Ile Polymorphisms in the Korean Population
por: Kim, Yeun Sun, et al.
Publicado: (2008)

Topoisomerase I activity and sensitivity to camptothecin in breast cancer-derived cells: a comparative study
por: Tesauro, Cinzia, et al.
Publicado: (2019)

New Topoisomerase I mutations are associated with resistance to camptothecin
por: Gongora, Céline, et al.
Publicado: (2011)

Anthracyclines as Topoisomerase II Poisons: From Early Studies to New Perspectives
por: Marinello, Jessica, et al.
Publicado: (2018)

Peptides for Infectious Diseases: From Probe Design to Diagnostic Microarrays
por: Cretich, Marina, et al.
Publicado: (2019)

Natural Compounds as Therapeutic Agents: The Case of Human Topoisomerase IB
por: Ottaviani, Alessio, et al.
Publicado: (2021)

A small organic compound enhances the religation reaction of human topoisomerase I and identifies crucial elements for the religation mechanism
por: Arnò, Barbara, et al.
Publicado: (2013)

Characterization of the differences in the cyclopiazonic acid binding mode to mammalian and P. Falciparum Ca(2+) pumps: A computational study
por: Di Marino, Daniele, et al.
Publicado: (2015)

Decreased Camptothecin Sensitivity of the Stem-Cell-Like Fraction of Caco2 Cells Correlates with an Altered Phosphorylation Pattern of Topoisomerase I
por: Roy, Amit, et al.
Publicado: (2014)

Different Camptothecin Sensitivities in Subpopulations of Colon Cancer Cells Correlate with Expression of Different Phospho-Isoforms of Topoisomerase I with Different Activities
por: Tesauro, Cinzia, et al.
Publicado: (2020)

Differential induction of Leishmania donovani bi-subunit topoisomerase I–DNA cleavage complex by selected flavones and camptothecin: activity of flavones against camptothecin-resistant topoisomerase I
por: Das, Benu Brata, et al.
Publicado: (2006)

Absence of the toll-like receptor 4 gene polymorphisms Asp299Gly and Thr399Ile in Singaporean Chinese
por: Liang, Xiao Hui, et al.
Publicado: (2005)

Toll-like receptor 4 single-nucleotide polymorphisms Asp299Gly and Thr399Ile in ovarian cancers
por: WANG, AN-CONG, et al.
Publicado: (2014)

Targeting of Topoisomerase I for Prognoses and Therapeutics of Camptothecin-Resistant Ovarian Cancer
por: Lee, Yu-Chieh, et al.
Publicado: (2015)

Modulation of Colorectal Cancer Risk by Polymorphisms in 51Gln/His, 64Ile/Val, and 148Asp/Glu of APEX Gene; 23Gly/Ala of XPA Gene; and 689Ser/Arg of ERCC4 Gene
por: Dziki, L., et al.
Publicado: (2017)

Asp299Gly and Thr399Ile polymorphism of TLR-4 gene in patients with prostate cancer from North India
por: Priyadarshini, Anjali, et al.
Publicado: (2013)

Toll-like receptor 4 Asp299Gly and Thr399Ile polymorphisms: New data and a meta-analysis
por: Senhaji, Nezha, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_8ua432nrpiab6vbrd8vqc9utr4