The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer

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The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer. / Nowock, J; Borgmeyer, U; Püschel, A W; Rupp, R A; Sippel, A E.

in: NUCLEIC ACIDS RES, Jahrgang 13, Nr. 6, 25.03.1985, S. 2045-61.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Nowock, J, Borgmeyer, U, Püschel, AW, Rupp, RA & Sippel, AE 1985, 'The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer', NUCLEIC ACIDS RES, Jg. 13, Nr. 6, S. 2045-61.

APA

Nowock, J., Borgmeyer, U., Püschel, A. W., Rupp, R. A., & Sippel, A. E. (1985). The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer. NUCLEIC ACIDS RES, 13(6), 2045-61.

Vancouver

Nowock J, Borgmeyer U, Püschel AW, Rupp RA, Sippel AE. The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer. NUCLEIC ACIDS RES. 1985 Mär 25;13(6):2045-61.

Bibtex

@article{61326725c7914a68a95c10b0b2066a67,
title = "The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer",
abstract = "TGGCA-binding proteins are nuclear proteins with high affinity for double-stranded DNA homologous to the prototype recognition sequence 5'YTGGCANNNTGCCAR 3'. Their ubiquitous tissue distribution in higher vertebrates characterizes them as a class of highly conserved proteins which may exert a basic function. To obtain clues to this function, specific binding sites were mapped on three viral genomes. Recognition sites were identified in the enhancer region of the BK virus, in the LTR of the mouse mammary tumor virus, and in the origin of replication of adenovirus 12. The TGGCA-binding protein from HeLa cells appears to be identical to nuclear factor I described by others, which stimulates initiation of adenovirus DNA replication in vitro. However, data from MMTV, BKV, and from cellular genes suggest that this specific protein-DNA interaction may also be involved in the control of gene activity.",
keywords = "Adenoviruses, Human, Animals, BK Virus, Base Sequence, CCAAT-Enhancer-Binding Proteins, Chromatin, DNA, Viral, DNA-Binding Proteins, Enhancer Elements, Genetic, Gene Expression Regulation, Genes, Regulator, Humans, Mammary Tumor Virus, Mouse, Mice, NFI Transcription Factors, Nuclear Proteins, Species Specificity, Transcription Factors, Y-Box-Binding Protein 1",
author = "J Nowock and U Borgmeyer and P{\"u}schel, {A W} and Rupp, {R A} and Sippel, {A E}",
year = "1985",
month = mar,
day = "25",
language = "English",
volume = "13",
pages = "2045--61",
journal = "NUCLEIC ACIDS RES",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "6",

}

RIS

TY - JOUR

T1 - The TGGCA protein binds to the MMTV-LTR, the adenovirus origin of replication, and the BK virus enhancer

AU - Nowock, J

AU - Borgmeyer, U

AU - Püschel, A W

AU - Rupp, R A

AU - Sippel, A E

PY - 1985/3/25

Y1 - 1985/3/25

N2 - TGGCA-binding proteins are nuclear proteins with high affinity for double-stranded DNA homologous to the prototype recognition sequence 5'YTGGCANNNTGCCAR 3'. Their ubiquitous tissue distribution in higher vertebrates characterizes them as a class of highly conserved proteins which may exert a basic function. To obtain clues to this function, specific binding sites were mapped on three viral genomes. Recognition sites were identified in the enhancer region of the BK virus, in the LTR of the mouse mammary tumor virus, and in the origin of replication of adenovirus 12. The TGGCA-binding protein from HeLa cells appears to be identical to nuclear factor I described by others, which stimulates initiation of adenovirus DNA replication in vitro. However, data from MMTV, BKV, and from cellular genes suggest that this specific protein-DNA interaction may also be involved in the control of gene activity.

AB - TGGCA-binding proteins are nuclear proteins with high affinity for double-stranded DNA homologous to the prototype recognition sequence 5'YTGGCANNNTGCCAR 3'. Their ubiquitous tissue distribution in higher vertebrates characterizes them as a class of highly conserved proteins which may exert a basic function. To obtain clues to this function, specific binding sites were mapped on three viral genomes. Recognition sites were identified in the enhancer region of the BK virus, in the LTR of the mouse mammary tumor virus, and in the origin of replication of adenovirus 12. The TGGCA-binding protein from HeLa cells appears to be identical to nuclear factor I described by others, which stimulates initiation of adenovirus DNA replication in vitro. However, data from MMTV, BKV, and from cellular genes suggest that this specific protein-DNA interaction may also be involved in the control of gene activity.

KW - Adenoviruses, Human

KW - Animals

KW - BK Virus

KW - Base Sequence

KW - CCAAT-Enhancer-Binding Proteins

KW - Chromatin

KW - DNA, Viral

KW - DNA-Binding Proteins

KW - Enhancer Elements, Genetic

KW - Gene Expression Regulation

KW - Genes, Regulator

KW - Humans

KW - Mammary Tumor Virus, Mouse

KW - Mice

KW - NFI Transcription Factors

KW - Nuclear Proteins

KW - Species Specificity

KW - Transcription Factors

KW - Y-Box-Binding Protein 1

M3 - SCORING: Journal article

C2 - 2987840

VL - 13

SP - 2045

EP - 2061

JO - NUCLEIC ACIDS RES

JF - NUCLEIC ACIDS RES

SN - 0305-1048

IS - 6

ER -