Triple helix-specific ligands

J. L. Mergny; G. Duval-Valentin; C. H. Nguyen; L. Perrouault; B. Faucon; M. Rougée; T. Montenay-Garestier; E. Bisagni; C. Hélène

doi:10.1126/science.256.5064.1681

Triple helix-specific ligands

J. L. Mergny
, G. Duval-Valentin
, C. H. Nguyen
, L. Perrouault
, B. Faucon
, M. Rougée
, T. Montenay-Garestier
, E. Bisagni
, C. Hélène

CNRS
Institut Curie

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

Résumé

A triple helix is formed upon binding of an oligodeoxynucleotide to the major groove of duplex DNA. A benzo[e]pyridoindole derivative (BePI) strongly stabilized this structure and showed preferential binding to a triplex rather than to a duplex. Energy transfer experiments suggest that BePI intercalates within the triple helix. Sequence-specific inhibition of transcription initiation of a specific gene by Escherichia coli RNA polymerase by a triplex-forming oligodeoxynucleotide is strongly enhanced when the triplex is stabilized by BePI. Upon irradiation with ultraviolet light, BePI induces covalent modifications of the target within the triple helix structure.

langue originale	Anglais
Pages (de - à)	1681-1684
Nombre de pages	4
journal	Science
Volume	256
Numéro de publication	5064
Les DOIs	https://doi.org/10.1126/science.256.5064.1681
état	Publié - 1 janv. 1992

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10.1126/science.256.5064.1681

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title = "Triple helix-specific ligands",

abstract = "A triple helix is formed upon binding of an oligodeoxynucleotide to the major groove of duplex DNA. A benzo[e]pyridoindole derivative (BePI) strongly stabilized this structure and showed preferential binding to a triplex rather than to a duplex. Energy transfer experiments suggest that BePI intercalates within the triple helix. Sequence-specific inhibition of transcription initiation of a specific gene by Escherichia coli RNA polymerase by a triplex-forming oligodeoxynucleotide is strongly enhanced when the triplex is stabilized by BePI. Upon irradiation with ultraviolet light, BePI induces covalent modifications of the target within the triple helix structure.",

author = "Mergny, \{J. L.\} and G. Duval-Valentin and Nguyen, \{C. H.\} and L. Perrouault and B. Faucon and M. Roug{\'e}e and T. Montenay-Garestier and E. Bisagni and C. H{\'e}l{\`e}ne",

year = "1992",

month = jan,

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doi = "10.1126/science.256.5064.1681",

language = "English",

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TY - JOUR

T1 - Triple helix-specific ligands

AU - Mergny, J. L.

AU - Duval-Valentin, G.

AU - Nguyen, C. H.

AU - Perrouault, L.

AU - Faucon, B.

AU - Rougée, M.

AU - Montenay-Garestier, T.

AU - Bisagni, E.

AU - Hélène, C.

PY - 1992/1/1

Y1 - 1992/1/1

N2 - A triple helix is formed upon binding of an oligodeoxynucleotide to the major groove of duplex DNA. A benzo[e]pyridoindole derivative (BePI) strongly stabilized this structure and showed preferential binding to a triplex rather than to a duplex. Energy transfer experiments suggest that BePI intercalates within the triple helix. Sequence-specific inhibition of transcription initiation of a specific gene by Escherichia coli RNA polymerase by a triplex-forming oligodeoxynucleotide is strongly enhanced when the triplex is stabilized by BePI. Upon irradiation with ultraviolet light, BePI induces covalent modifications of the target within the triple helix structure.

AB - A triple helix is formed upon binding of an oligodeoxynucleotide to the major groove of duplex DNA. A benzo[e]pyridoindole derivative (BePI) strongly stabilized this structure and showed preferential binding to a triplex rather than to a duplex. Energy transfer experiments suggest that BePI intercalates within the triple helix. Sequence-specific inhibition of transcription initiation of a specific gene by Escherichia coli RNA polymerase by a triplex-forming oligodeoxynucleotide is strongly enhanced when the triplex is stabilized by BePI. Upon irradiation with ultraviolet light, BePI induces covalent modifications of the target within the triple helix structure.

UR - https://www.scopus.com/pages/publications/0026696129

U2 - 10.1126/science.256.5064.1681

DO - 10.1126/science.256.5064.1681

M3 - Article

C2 - 1609278

AN - SCOPUS:0026696129

SN - 0036-8075

VL - 256

SP - 1681

EP - 1684

JO - Science

JF - Science

IS - 5064

ER -

Triple helix-specific ligands

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