Viral myb oncogene encodes a sequence-specific DNA-binding activity

Standard

Viral myb oncogene encodes a sequence-specific DNA-binding activity. / Biedenkapp, H; Borgmeyer, U; Sippel, A E; Klempnauer, K H.

in: NATURE, Jahrgang 335, Nr. 6193, 27.10.1988, S. 835-7.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Biedenkapp, H, Borgmeyer, U, Sippel, AE & Klempnauer, KH 1988, 'Viral myb oncogene encodes a sequence-specific DNA-binding activity', NATURE, Jg. 335, Nr. 6193, S. 835-7. https://doi.org/10.1038/335835a0

APA

Biedenkapp, H., Borgmeyer, U., Sippel, A. E., & Klempnauer, K. H. (1988). Viral myb oncogene encodes a sequence-specific DNA-binding activity. NATURE, 335(6193), 835-7. https://doi.org/10.1038/335835a0

Vancouver

Biedenkapp H, Borgmeyer U, Sippel AE, Klempnauer KH. Viral myb oncogene encodes a sequence-specific DNA-binding activity. NATURE. 1988 Okt 27;335(6193):835-7. https://doi.org/10.1038/335835a0

Bibtex

@article{5e62235c21bd429496cef41c67b2468a,
title = "Viral myb oncogene encodes a sequence-specific DNA-binding activity",
abstract = "The retroviral oncogene v-myb and its cellular progenitor c-myb encode nuclear DNA-binding proteins. Myb genes have been identified in a broad range of species, including vertebrates, the fruit fly Drosophila melanogaster and the plant Zea mays. The localization of the DNA-binding domain of the v-MYB protein to the highly conserved amino-terminal region suggests that the MYB/DNA interaction is important for MYB function. We show here that v-MYB specifically recognizes the nucleotide sequence pyAACG/TG. So like other nuclear transforming proteins, v-MYB seems to be a member of the class of sequence-specific DNA-binding factors presumably involved in gene regulation.",
keywords = "Base Sequence, Binding Sites, Cloning, Molecular, DNA, DNA-Binding Proteins, Molecular Sequence Data, Oncogene Proteins v-myb, Oncogenes, Plasmids, Retroviridae Proteins",
author = "H Biedenkapp and U Borgmeyer and Sippel, {A E} and Klempnauer, {K H}",
year = "1988",
month = oct,
day = "27",
doi = "10.1038/335835a0",
language = "English",
volume = "335",
pages = "835--7",
journal = "NATURE",
issn = "0028-0836",
publisher = "NATURE PUBLISHING GROUP",
number = "6193",

}

RIS

TY - JOUR

T1 - Viral myb oncogene encodes a sequence-specific DNA-binding activity

AU - Biedenkapp, H

AU - Borgmeyer, U

AU - Sippel, A E

AU - Klempnauer, K H

PY - 1988/10/27

Y1 - 1988/10/27

N2 - The retroviral oncogene v-myb and its cellular progenitor c-myb encode nuclear DNA-binding proteins. Myb genes have been identified in a broad range of species, including vertebrates, the fruit fly Drosophila melanogaster and the plant Zea mays. The localization of the DNA-binding domain of the v-MYB protein to the highly conserved amino-terminal region suggests that the MYB/DNA interaction is important for MYB function. We show here that v-MYB specifically recognizes the nucleotide sequence pyAACG/TG. So like other nuclear transforming proteins, v-MYB seems to be a member of the class of sequence-specific DNA-binding factors presumably involved in gene regulation.

AB - The retroviral oncogene v-myb and its cellular progenitor c-myb encode nuclear DNA-binding proteins. Myb genes have been identified in a broad range of species, including vertebrates, the fruit fly Drosophila melanogaster and the plant Zea mays. The localization of the DNA-binding domain of the v-MYB protein to the highly conserved amino-terminal region suggests that the MYB/DNA interaction is important for MYB function. We show here that v-MYB specifically recognizes the nucleotide sequence pyAACG/TG. So like other nuclear transforming proteins, v-MYB seems to be a member of the class of sequence-specific DNA-binding factors presumably involved in gene regulation.

KW - Base Sequence

KW - Binding Sites

KW - Cloning, Molecular

KW - DNA

KW - DNA-Binding Proteins

KW - Molecular Sequence Data

KW - Oncogene Proteins v-myb

KW - Oncogenes

KW - Plasmids

KW - Retroviridae Proteins

U2 - 10.1038/335835a0

DO - 10.1038/335835a0

M3 - SCORING: Journal article

C2 - 3185713

VL - 335

SP - 835

EP - 837

JO - NATURE

JF - NATURE

SN - 0028-0836

IS - 6193

ER -