Výsledky vyhledávání - "Belén Illana"

Functional Recovery in a Friedreich's Ataxia Mouse Model by Frataxin Gene Transfer Using an HSV-1 Amplicon Vector

Autor: Alfredo Giménez-Cassina, Javier Díaz-Nido, Christina Mauritz, Filip Lim, Gloria M Palomo, Francisco Wandosell, Belén Illana

Publikováno v: Molecular Therapy. 15:1072-1078

There is currently no effective treatment for Friedreich's ataxia (FA), the most common of the hereditary ataxias. The disease is caused by mutations in FRDA that drastically reduce expression levels of the mitochondrial protein frataxin. In FA anima

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f16d4c7e16653555c3950539222a6566
https://doi.org/10.1038/sj.mt.6300143

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Compartmentalization of phage phi29 DNA replication: interaction between the primer terminal protein and the membrane-associated protein p1

Autor: Alicia Bravo, Margarita Salas, Belén Illana

Publikováno v: Scopus-Elsevier

The bacteriophage phi29 replication protein p1 (85 amino acids) is membrane associated in Bacillus subtilis-infected cells. The C-terminal 52 amino acid residues of p1 are sufficient for assembly into protofilament sheet structures. Using chemical cr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cad5a49576ef56ea0c78a952c2bf6a6
https://pubmed.ncbi.nlm.nih.gov/11032825

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The putative coiled coil domain of the ø29 terminal protein is a major determinant involved in recognition of the origin of replication

Autor: Alejandro Serna-Rico, Margarita Salas, Wilfried J. J. Meijer, Belén Illana

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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The linear double-stranded genome of phage φ29 contains a terminal protein (TP) covalently linked at each 5′ DNA end, called parental TP. Initiation of φ29 DNA replication starts with the recognition of the origins of replication, constituted by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a56d9d0c61464e7a18c4bb868269b9e8
http://hdl.handle.net/10261/38519

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Phage phi29 terminal protein residues Asn80 and Tyr82 are recognition elements of the replication origins

Autor: Crisanto Gutierrez, Margarita Salas, Luis Blanco, Belén Illana, José M. Lázaro, Wilfried J. J. Meijer

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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Initiation of phage φ29 DNA replication starts with the recognition of the origin of replication, located at both ends of the linear DNA, by a heterodimer formed by the φ29 terminal protein (TP) and the φ29 DNA polymerase. The parental TP, covalen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33738fd039aef3dcc74651992ea7c910
https://pubmed.ncbi.nlm.nih.gov/10329712

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The 'RGD' sequence in phage ø29 terminal protein is required for interaction with ø29 DNA polymerase

Autor: Luis Blanco, Margarita Salas, Belén Illana, Ángel Zaballos

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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The RGD (Arg-Gly-Asp) motif functions as a recognition site for adhesive proteins responsible for a number of cell–cell interactions. Certain viruses use this sequence as a receptor-binding site by interaction with cellular integrins. To elucidate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22dff7ed215dcd07063319c4cf225ee1
http://hdl.handle.net/10261/39210

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Functional Characterization of the Genes Coding for the Terminal Protein and DNA Polymerase from Bacteriophage GA-1. Evidence for a Sliding-back Mechanism During Protein-primed GA-1 DNA Replication

Autor: Luis Blanco, Margarita Salas, Belén Illana

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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We have determined the nucleotide sequence of 2676 bp at the left part of the linear genome ofBacillus subtilisbacteriophage GA-1. Computer analysis revealed that this fragment contains two open reading frames (ORFs), ORF1 and ORF2, which contain 265

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e7feecd255e6b0e623d0b1cfa5b08e4
http://hdl.handle.net/10261/38882

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