References of "Muller, Marc"
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See detailEffect of seasonal acclimatization on the expression of the carp transcription factor Pit-1
Kausel, G.; Vera, M. I.; Figueroa, J. et al

in Biochemistry and Molecular Biology International (1998), 45(5), 813-21

We isolated a clone comprising four exons of the carp Pit-1 gene. Using synthetic oligonucleotide probes derived from the carp Pit-1 sequence Pit-1 expression was assessed by in situ hybridization in ... [more ▼]

We isolated a clone comprising four exons of the carp Pit-1 gene. Using synthetic oligonucleotide probes derived from the carp Pit-1 sequence Pit-1 expression was assessed by in situ hybridization in pituitary sections from summer- and winter-acclimatized carp. Semiquantitative analyses of the hybridization signals revealed a significant higher Pit-1 expression in the proximal pars distalis (PPD) and pars intermedia (PI) of the pituitary glands from summer-acclimatized carp, compared to the winter-acclimatized fish. In both adaptive states, relative to the PPD and PI, only a basal Pit-1 expression was detected in the rostral pars distalis. Thus, during seasonal acclimatization of an eurythermal fish, Pit-1 seems to be involved in the mechanisms that underlie the compensatory response. [less ▲]

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See detailRégulation transcriptionnelle du gène de la prolactine humaine
Muller, Marc ULg; Berwaer, Monique; Caccavelli, Laure et al

in Medecine Sciences : M/S (1998), 14(580-587),

Le gène humain de la prolactine (hPRL) est exprimé essentiellement par l'antéhypophyse. L'analyse des éléments régulateurs de la transcription sur plus de 5 000 bases en amont du site de début de ... [more ▼]

Le gène humain de la prolactine (hPRL) est exprimé essentiellement par l'antéhypophyse. L'analyse des éléments régulateurs de la transcription sur plus de 5 000 bases en amont du site de début de transcription a montré l'importance du contrôle par le facteur de transcription Pit-1, spécifique de l'hypophyse, à côté de facteurs ubiquistes. Des hormones modulent l'expression du gène hPRL, transmettant leur signal par les voies intracellulaires de l'AMP cyclique et du calcium, relayées au niveau du promoteur proximal (-250/+1) essentiellement par les facteurs de transcription Pit-1 et AP-1. Les récepteurs nucléaires contrôlent aussi en partie la transcription de hPRL: le récepteur des oestrogènes l'active en se liant aux éléments de réponse distaux ; les récepteurs nucléaires des hormones thyroïdiennes et des glucocorticoïdes la répriment en interférant respectivement avec la fonction activatrice de AP-1 et de Pit-1. [less ▲]

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See detailPro239Ser: a novel recessive mutation of the Pit-1 gene in seven Middle Eastern children with growth hormone, prolactin, and thyrotropin deficiency
Pernasetti, Flavia; Milner, Robert DG; al Ashwal, Abdullah A Z et al

in Journal of Clinical Endocrinology and Metabolism (1998), 83(6), 2079-83

Pit-1, a member of the POU-homeo domain protein family, is one of the transcription factors responsible for anterior pituitary development and pituitary-specific gene expression. Here, we describe seven ... [more ▼]

Pit-1, a member of the POU-homeo domain protein family, is one of the transcription factors responsible for anterior pituitary development and pituitary-specific gene expression. Here, we describe seven children with GH, PRL, and TSH deficiency from three, reportedly unrelated, Middle Eastern families, harboring a newly recognized Pro- > Ser recessive mutation in codon 239 of the Pit-1 gene. The mutated residue is located at the beginning of the second alpha-helix of the POU-homeodomain and is strictly conserved among all POU proteins. The Pro239Ser mutant binds DNA normally but is unable to stimulate transcription. [less ▲]

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See detailTranscription factor AP1 is involved in basal and okadaic acid-stimulated activity of the human PRL promoter
Caccavelli, Laure; Manfroid, Isabelle ULg; Martial, Joseph ULg et al

in Molecular Endocrinology (Baltimore, Md.) (1998), 12(8), 1215-27

The tumor promoter, okadaic acid (OA), an inhibitor of protein phosphatases, stimulates the activity of the human PRL (hPRL) proximal promoter. We analyzed in detail the effects of OA on transcription ... [more ▼]

The tumor promoter, okadaic acid (OA), an inhibitor of protein phosphatases, stimulates the activity of the human PRL (hPRL) proximal promoter. We analyzed in detail the effects of OA on transcription factor binding to elements P1 and P2 of this promoter, sequences known to contain at least one Pit-1 binding site each. OA treatment induces binding of an AP1-related transcription factor to the P1 site. This effect is specific, as protein binding to the P2 site is not altered by the treatment. Specific antibodies were used to confirm that the OA-induced complex is related to AP1 and to show that it contains JunD and c-fos, but not Pit-1. The increase in AP1 binding to P1 and to a canonical AP1 site correlates to an increase in cellular JunD and c-fos content. Transient transfection experiments showed that both AP1 and Pit-1 are involved in the regulation of basal and OA-stimulated promoter activity. Our results demonstrate that a member of the AP1 family, containing JunD and c-fos, can bind to the proximal element P1 within the hPRL promoter. In addition, they show that AP1 is involved in both basal and OA-stimulated expression of the hPRL gene. [less ▲]

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See detailAt Least Three Subdomains of V-Erba Are Involved in Its Silencing Function
Busch, Kerstin; Martin, Bernd; Baniahmad, Aria et al

in Molecular Endocrinology (1997), 11(3), 379-89

Several members of the thyroid hormone receptor (TR) family are able to switch from a transcriptional repressor to a transcriptional activator upon binding of their ligand. The oncogene v-erbA is a ... [more ▼]

Several members of the thyroid hormone receptor (TR) family are able to switch from a transcriptional repressor to a transcriptional activator upon binding of their ligand. The oncogene v-erbA is a variant form of the TR unable to bind hormone and thus acts as a constitutive repressor. We demonstrate, using fusion proteins between the DNA-binding domain of the yeast factor GAL4 and the silencing domains of v-erbA and TR beta, that point mutations in three different regions severely affect their repression function. Furthermore, the three regions, each as an inactive fusion protein with the GAL4 DNA-binding domain, restore silencing activity when assembled on the same promoter. These observations define at least three silencing subdomains, SSD1-SSD3, which are involved in the silencing function of v-erbA. We propose a model in which full silencing activity is brought about by the combined interaction of each silencing subdomain with corepressors and/or basal transcription factors. [less ▲]

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See detailRegulation of prolactin gene expression in fishes
Poncelet, A. C.; Yaron, Z.; Levavi-Sivan, B. et al

in Nagabhushanan, R.; Thompson, M.F.; Fingennan, M. (Eds.) Recent Advances in Marine Biotechnology (1997)

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See detailThyroid hormone inhibits the human prolactin gene promoter by interfering with activating protein-1 and estrogen stimulations
Pernasetti, Flavia; Caccavelli, L.; Van de Weerdt, Cécile ULg et al

in Molecular Endocrinology (Baltimore, Md.) (1997), 11(7), 986-96

Transcription of the human PRL (hPRL) gene in the pituitary is subject to tissue-specific and multihormonal regulation involving two main regulatory regions, a proximal promoter and a distal enhancer. In ... [more ▼]

Transcription of the human PRL (hPRL) gene in the pituitary is subject to tissue-specific and multihormonal regulation involving two main regulatory regions, a proximal promoter and a distal enhancer. In this report we show that thyroid hormone inhibits the expression of the hPRL gene in rat pituitary cells. Transient expression experiments show that thyroid hormone regulation involves a strong inhibitory element, located in the proximal (-164/-35) promoter, which is modulated by a more distal stimulatory response control region. Gel retardation experiments reveal that the thyroid hormone receptor does not bind to the proximal negative element. We show the existence of an activating protein-1 (AP-1) response element located at positions -61 to -54 of the proximal promoter, conferring AP-1 stimulation to the hPRL promoter. This AP-1 induction is abolished when hormone-bound thyroid hormone receptor is present, indicating that there is an interference between the thyroid hormone receptor and AP-1 regulatory pathways. Furthermore, using the complete hPRL upstream region, we show that estrogen induction is abolished by simultaneous thyroid hormone treatment. [less ▲]

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See detailThe glucocorticoid receptor inhibits the human prolactin gene expression by interference with Pit-1 activity
Nalda, Asunción M; Martial, Joseph ULg; Muller, Marc ULg

in Molecular & Cellular Endocrinology (1997), 134(2), 129-37

Glucocorticoids have been shown to inhibit the activity of the human prolactin (hPRL) promoter. Using transient expression experiments in rat pituitary cells, we located the sequence conferring ... [more ▼]

Glucocorticoids have been shown to inhibit the activity of the human prolactin (hPRL) promoter. Using transient expression experiments in rat pituitary cells, we located the sequence conferring glucocorticoid inhibition to a region which contains Pit-1 binding sites, responsible for pituitary-specific expression, but does not seem to contain a glucocorticoid receptor (GR) binding site. Co-transfection experiments in non-pituitary cell lines, using expression vectors for Pit-1 and different mutants of the human GR show that inhibition of the hPRL gene is seen only in the presence of Pit-1 and GR, and that the DNA binding function of the receptor is not required. Immunoprecipitation studies show that either anti-GR or anti-Pit-1 antibodies are able to co-precipitate GR and Pit-1, suggesting an interaction between these factors. We conclude that the activated GR functionally interferes with the pituitary specific factor Pit-1, thereby leading to the observed transcriptional repression. [less ▲]

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See detailA one-nucleotide difference in a cAMP and phorbol ester response element leads to differential regulation of the human chorionic somatomammotropin A and B gene transcription
Oury, Cécile ULg; Alsat, E.; Jacquemin, P. et al

in Journal of Molecular Endocrinology (1997), 18(2), 87-99

Human chorionic somatomammotropin (hCS) is encoded by two highly related genes, hCS-A and hCS-B, located in the hGH/hCS gene locus. Both genes are expressed in the syncytiotrophoblast layer of the ... [more ▼]

Human chorionic somatomammotropin (hCS) is encoded by two highly related genes, hCS-A and hCS-B, located in the hGH/hCS gene locus. Both genes are expressed in the syncytiotrophoblast layer of the placenta and hCS release from trophoblast cells is known to be increased by cAMP and phorbol esters. However, it remains unclear whether this regulation acts at the level of hCS gene expression or secretion and whether both genes are affected. We examined the effects of cAMP and phorbol 12-myristate 13-acetate (PMA) on the transcription of the hCS-A and hCS-B genes. Transient expression experiments revealed a 7 bp cAMP- and PMA-responsive element (CRElhCS-A) spanning nucleotides-1102 to -1096 upstream of the hCS-A gene. In contrast, the homologous sequence upstream of hCS-B (CRElhCS-B), differing from CRElhCS-A by a single substitution, shows little or no response to cAMP. In band-shift assays, the CRElhCS-A oligonucleotide was shown to bind two factors related to CREBP and AP-1, whereas CRElhCS-B only competes for one of these complexes. Finally, Southwestern analysis revealed that the CRElhCS-A element binds two ubiquitous proteins of 100 kDa and 47 kDa respectively, whereas CRElhCS-B interacts only with the 47 kDa protein. Taken together, these results suggest that a 47 kDa protein binding to the CRElhCS-A and CRElhCS-B elements is involved in the PMA response of the hCS-A and hCS-B genes, and a 100 kDa protein plays a crucial role in cAMP regulation of the hCS-A gene. [less ▲]

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See detailThe tilapia prolactin I gene: evolutionary conservation of the regulatory elements directing pituitary-specific expression
Poncelet, A. C.; Levavi-Sivan, B.; Muller, Marc ULg et al

in DNA & Cell Biology (1996), 15(8), 679-92

To study the elements involved in the pituitary specific transcriptional regulation of the tilapia prolactin I gene (tiPRL I), we have cloned and entirely sequenced a 3.4-kb genomic fragment immediately ... [more ▼]

To study the elements involved in the pituitary specific transcriptional regulation of the tilapia prolactin I gene (tiPRL I), we have cloned and entirely sequenced a 3.4-kb genomic fragment immediately upstream from the first exon. In footprinting experiments, three tilapia sequences are protected from DNase I digestion by rat pituitary extracts (base pair coordinates -643 to -593, -160 to -111, and -73 to -46). Computer analysis of the nucleotide sequence reveals significant homology to mammalian binding sites for Pit-1, a transcription factor that is known to mediate pituitary-specific expression of the PRL genes in mammals. The tiPRL I 5'-flanking sequences can direct transient expression of a linked luciferase reporter gene in transfected rat pituitary cell lines and tilapia pituitary primary cell cultures. Transient expression experiments with 5'-deletion mutants reveal three regulatory regions. Two have a stimulatory effect on transcription and one an inhibitory effect. Electrophoretic mobility-shift assays (EMSA) demonstrate that the rat Pit-1 factor specifically binds to tilapia DNA sequences. Several such tilapia Pit-1 binding sites mediate activation of a linked heterologous promoter in transfected rat and tilapia pituitary cells. As evidenced by EMSA, a Pit-1-like protein is present in tilapia pituitary extracts. All these data point to a high conservation of the molecular mechanisms involved in pituitary-specific expression of the PRL genes in vertebrates. [less ▲]

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See detailDNA bending by the silencer protein NeP1 is modulated by TR and RXR.
Arnold, R.; Burcin, M.; Kaiser, Bruno ULg et al

in Nucleic Acids Research (1996), 24(14), 2640-7

NeP1 binds to the F1 silencer element of the chicken lysozyme gene and, in the presence of TR, v-ERBA or RAR, synergistically represses transcriptional activity. This repression involves a silencing ... [more ▼]

NeP1 binds to the F1 silencer element of the chicken lysozyme gene and, in the presence of TR, v-ERBA or RAR, synergistically represses transcriptional activity. This repression involves a silencing mechanism acting independently of the relative promoter position. Here we show that NeP1 alone can induce a significant directed bend on DNA. The chicken homologue of human NeP1, CTCF, shows identical binding and bending properties. In contrast, the isolated DNA binding domain of CTCF efficiently binds DNA, but fails to confer bending. Similarly, the TR-RXR hetero- or homodimer, binding adjacent to NeP1 at the F2 sequence, do not show significant DNA bending. The binding of the T3 ligand to TR changes neither the magnitude nor the direction of the NeP1 induced bend. However, when all factors are bound simultaneously as a quaternary complex, the TR-RXR heterodimer changes the location of the bend center, the flexure angle and the bending direction. [less ▲]

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See detailEnhancement of nuclear receptor transcriptional signalling.
Renkawitz, Rainer; Kaltschmidt, Christian; Leers, Joerg et al

in Journal of Steroid Biochemistry & Molecular Biology (1996), 56(1-6 Spec No), 39-45

Glucocorticoids and thyroid hormones induce complex responses in about every mammalian tissue. These effects are mediated by the transcription factor function of the corresponding nuclear receptors, which ... [more ▼]

Glucocorticoids and thyroid hormones induce complex responses in about every mammalian tissue. These effects are mediated by the transcription factor function of the corresponding nuclear receptors, which in most cases achieve the observed regulatory strength in synergy with other factors. Here we describe the functional interaction of the glucocorticoid receptor (GR) with liver-specific transcription factors, the functional synergy of GR with the thyroid hormone receptor (TR), the synergizing sub-domains of the TR, and finally the direct interaction of the GR with other proteins. [less ▲]

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See detailThe enhancers of the human placental lactogen B, A, and L genes: progressive activation during in vitro trophoblast differentiation and importance of the DF-3 element in determining their respective activities
Jacquemin, P.; Alsat, E.; Oury, Cécile ULg et al

in DNA & Cell Biology (1996), 15(10), 845-54

The hCS-A and hCS-B genes encoding human chorionic somatomammotropin and the related hCS-L gene are very similar in their coding and flanking sequences. For each of these genes, downstream enhancers ... [more ▼]

The hCS-A and hCS-B genes encoding human chorionic somatomammotropin and the related hCS-L gene are very similar in their coding and flanking sequences. For each of these genes, downstream enhancers, varying in strength, have been identified with the help of cytotrophoblast-derived JEG-3 cells, which do not express the hCS genes. Here we study the activity of the hCS enhancers in human syncytiotrophoblast in primary culture, which naturally expresses the hCS genes. We show that the activity of the hCS-B gene enhancer is mediated by two elements, DF-3 and DF-4, whereas the hCS-L and hCS-A gene enhancers display weaker activity due to mutations in their respective DF-3 sites. Replacement of the hCS-B DF-3 site with the homologous hCS-A sequence causes hCS-B enhancer activity to decrease. Primary cytotrophoblasts differentiate in culture to form the syncytiotrophoblast. We show that during this process the production of hCS progressively increases and that concomitantly all three hCS enhancers are progressively activated. A targeted mutation in the 3' part of the DF-4 element abolishes the binding of a protein present only in syncytiotrophoblast extracts and inactivates the DF-4 element. Thus, a direct correlation exists between the appearance of this syncytiotrophoblast-specific protein and hCS enhancer activity. This primary culture model proves useful in studying the regulation of the hCS genes. [less ▲]

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See detailTwo silencing sub-domains of v-erbA synergize with each other, but not with RXR.
Martin, Bernd; Renkawitz, Rainer; Muller, Marc ULg

in Nucleic Acids Research (1994), 22(23), 4898-905

The thyroid hormone receptor (TR) and the retinoic acid receptor (RAR) induce gene expression in the presence of specific ligand and repress transcription in the absence of hormone. This repression is ... [more ▼]

The thyroid hormone receptor (TR) and the retinoic acid receptor (RAR) induce gene expression in the presence of specific ligand and repress transcription in the absence of hormone. This repression is mediated by an active silencing mechanism rather then by interference with DNA binding activators. V-erbA, a variant form of TR which is unable to bind hormone, represents a constitutive repressor. Here we show, using fusion proteins with the GAL4 DNA binding domain, that the minimal silencing domain of v-erbA extends from amino acids 389 to 632 and that internal deletions within this domain retain at least some repression function. Co-transfection experiments of different deletion mutants indicate that the silencing domain is composed of at least two sub-domains which are non-functional when tested individually. When combined in a heterodimeric complex, they synergize such that silencing activity is regained. In contrast to the retinoic acid receptor the retinoid X receptor does not contain a silencing domain. In addition it is unable to cooperate with the repression function of TR or v-erbA in a heterodimer. [less ▲]

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See detailA thyroid hormone receptor-dependent glucocorticoid induction.
Leers, Joerg; Steiner, Christoff; Renkawitz, Rainer et al

in Molecular Endocrinology (Baltimore, Md.) (1994), 8(4), 440-7

Glucocorticoid and thyroid hormones exert their effects in many body tissues by binding to their respective receptors. The search for possible cross-talking mechanisms in overlapping target cells led to ... [more ▼]

Glucocorticoid and thyroid hormones exert their effects in many body tissues by binding to their respective receptors. The search for possible cross-talking mechanisms in overlapping target cells led to the discovery of synergism between a thyroid hormone receptor-binding site and a cryptic glucocorticoid-responsive element. Glucocorticoid responsiveness could only be detected in the presence of thyroid hormone and its receptor. This synergism requires the glucocorticoid receptor (GR) DNA-binding domain and is mediated by the transactivation domains. We found that synergism also occurs when the thyroid hormone receptor is replaced by the retinoic acid receptor or the GR is replaced by the progesterone receptor. Synergism is qualitatively independent of the type of thyroid hormone receptor-binding site and promoter. In several combinations of promoter and response elements, including a retinoic acid response element, T3 induction was only seen in the presence of the cryptic glucocorticoid-responsive element, GR, and glucocorticoids. [less ▲]

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See detailDNase I hypersensitive sites far upstream of the rat tryptophan oxygenase gene direct developmentally regulated transcription in livers of transgenic mice.
Kaltschmidt, Christian; Muller, Marc ULg; Brem, Gottfried et al

in Mechanisms of Development (1994), 45(3), 203-10

Expression of the gene coding for tryptophan oxygenase (TO) is switched on in rat liver about two weeks after birth. We identified two clusters of DNaseI hypersensitive (HS) sites in the TO gene upstream ... [more ▼]

Expression of the gene coding for tryptophan oxygenase (TO) is switched on in rat liver about two weeks after birth. We identified two clusters of DNaseI hypersensitive (HS) sites in the TO gene upstream region; one near the promoter, the other at a distant upstream location (-8.5 kb). Hypersensitivity of upstream sites was present in adult and in 7 day old rat liver, but absent in kidney. To investigate their role in transcriptional regulation, a reporter gene controlled by both HS site regions was used to generate transgenic mice. In these animals the transgene followed the cell specific and developmental regulation of the endogenous gene: inactive after birth and active in adult liver. Transgenes containing only the promoter proximal HS site were non-functional. [less ▲]

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See detailA complex composed of at least two HeLa nuclear proteins protects preferentially one DNA strand of the simple (gt)n(ga)m containing region of intron 2 in HLA-DRB genes.
Maueler, Winfried; Frank, G.; Muller, Marc ULg et al

in Journal of Cellular Biochemistry (1994), 56(1), 74-85

Electrophoretic mobility shift assays reveal that HeLa nuclear proteins bind fast and with measurable affinity to target DNAs containing mixed simple repetitive (gt)n(ga)m stretches. Preincubation of the ... [more ▼]

Electrophoretic mobility shift assays reveal that HeLa nuclear proteins bind fast and with measurable affinity to target DNAs containing mixed simple repetitive (gt)n(ga)m stretches. Preincubation of the proteins at elevated temperature prevents the formation of the major DNA/protein complex in favour of several distinct assemblies. A similar pattern of retarded bands was observed employing higher salt concentrations in the binding reaction. Thus conformational changes of different proteins appear to influence the complex rather than alternating DNA structures. Separation of the total nuclear extract into a water soluble and an insoluble protein fraction leads to a complete loss of target DNA binding capability of the fractions. The binding capacity is restored by combining the two fractions suggesting that at least two protein components are necessary to form a complex with the target sequence. The proteins can be differentiated into heat sensitive, water soluble and temperature stable, water insoluble, respectively. Furthermore, specifically binding polypeptides are not detectable by Southwestern analyses, probably because the essential components are separated during electrophoresis. DNase I footprint analyses yield four different protein binding regions only on the (gt)n(ga)m harbouring strand. The footprints cover larger portions of the mixed simple repeat in addition to a portion 5' of the (gt)n part. Hence at least two nuclear protein components of unknown biological function have to be present simultaneously to protect preferentially the (gt)n(ga)m-containing strand of intron 2 in HLA-DRB genes. [less ▲]

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See detailA gel retardation assay system for studying protein binding to simple repetitive DNA sequences.
Maueler, W.; Muller, Marc ULg; Kohne, A. C. et al

in Electrophoresis (1992), 13(1-2), 7-10

Simple repetitive DNA sequences have been regarded as mere "junk" present in all eukaryotic genomes. In fact, mixed simple repeat (gt)n(ga)m sequences are present in major histocompatibility complex MHC ... [more ▼]

Simple repetitive DNA sequences have been regarded as mere "junk" present in all eukaryotic genomes. In fact, mixed simple repeat (gt)n(ga)m sequences are present in major histocompatibility complex MHC-DRB genes for long evolutionary times, including such distant animals as artiodactyla and man. We describe herein an unsophisticated method which reveals that at least certain simple repetitive (gt)n(ga)m sequences bind nuclear proteins and show characteristics of a specific DNA-protein interaction via gel retardation. [less ▲]

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See detailCo-operative transactivation of steroid receptors
Muller, Marc ULg; Baniahmad, Claudia; Kaltschmidt, Christian et al

in Parker, Malcolm (Ed.) Nuclear Hormone Receptors (1991)

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See detailThe glucocorticoid receptor.
Muller, Marc ULg; Renkawitz, R.

in Biochimica et Biophysica Acta (1991), 1088

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