Výsledky vyhledávání - "J A, Martial"

Transcriptional regulation by triiodothyronine requires synergistic action of the thyroid receptor with another trans-acting factor

Autor: M L Voz, B Peers, M J Wiedig, P Jacquemin, A Belayew, J A Martial

Publikováno v: Molecular and Cellular Biology. 12:3991-3997

Human placental lactogen B (hCS-B) promoter activity is strongly stimulated by triiodothyronine (T3) in pituitary GC cells through interaction between the thyroid receptor and a thyroid receptor-binding element (TBE) spanning coordinates -67 to -41.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4f74a6baa6dbe51e180c28df466a7b96
https://doi.org/10.1128/mcb.12.9.3991

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Heat shock stimulation of a tilapia heat shock protein 70 promoter is mediated by a distal element

Autor: A, Molina, E, Di Martino, J A, Martial, M, Muller

Publikováno v: The Biochemical journal. 356(Pt 2)

We reported previously that a tilapia (Oreochromis mossambicus) heat shock protein 70 (HSP70) promoter is able to confer heat shock response on a reporter gene after transient expression both in cell culture and in microinjected zebrafish embryos. He

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a25b55df0bba209d42e00cf4d04e675f
https://pubmed.ncbi.nlm.nih.gov/11368761

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Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties

Autor: M, Alvarez, J P, Zeelen, V, Mainfroid, F, Rentier-Delrue, J A, Martial, L, Wyns, R K, Wierenga, D, Maes

Publikováno v: The Journal of biological chemistry. 273(4)

The purification and characterization of triose-phosphate isomerase from the psychrophilic bacterium Vibrio marinus (vTIM) is described. Crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex (at a 2.7-A resolution) ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::94653412084f488cb3082abfcedb378b
https://pubmed.ncbi.nlm.nih.gov/9442062

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Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme

Autor: S C, Mande, V, Mainfroid, K H, Kalk, K, Goraj, J A, Martial, W G, Hol

Publikováno v: Protein science : a publication of the Protein Society. 3(5)

The crystal structure of recombinant human triosephosphate isomerase (hTIM) has been determined complexed with the transition-state analogue 2-phosphoglycolate at a resolution of 2.8 A. After refinement, the R-factor is 16.7% with good geometry. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::be678e8a99d21eec650791c4a85faff7
https://pubmed.ncbi.nlm.nih.gov/8061610

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Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide

Autor: E A, Merritt, S, Sarfaty, F, van den Akker, C, L'Hoir, J A, Martial, W G, Hol

Publikováno v: Protein science : a publication of the Protein Society. 3(2)

Cholera toxin (CT) is an AB5 hexameric protein responsible for the symptoms produced by Vibrio cholerae infection. In the first step of cell intoxication, the B-pentamer of the toxin binds specifically to the branched pentasaccharide moiety of gangli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fcec6749886d4d97f99188807aa220cd
https://pubmed.ncbi.nlm.nih.gov/8003954

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Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences

Autor: F, Rentier-Delrue, S C, Mande, S, Moyens, P, Terpstra, V, Mainfroid, K, Goraj, M, Lion, W G, Hol, J A, Martial

Publikováno v: Journal of molecular biology. 229(1)

We focused on the temperature adaptation of triosephosphate isomerase (TIM; E.C. 5.3.1.1.) by comparing the structure of TIMs isolated from bacterial organisms living in either cold or hot environments. The TIM gene from psychrophilic bacteria Moraxe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5fac4dbc024a89744089b29cf73fa287
https://pubmed.ncbi.nlm.nih.gov/8421318

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Transcriptional induction of the human prolactin gene by cAMP requires two cis-acting elements and at least the pituitary-specific factor Pit-1

Autor: B, Peers, P, Monget, M A, Nalda, M L, Voz, M, Berwaer, A, Belayew, J A, Martial

Publikováno v: The Journal of biological chemistry. 266(27)

To identify the cis-acting elements responsible for cAMP stimulation of human prolactin (hPRL) promoter activity, pituitary GC cells were transfected with 5'-deleted hPRL promoters fused to the chloramphenicol acetyltransferase reporter gene. The pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1e3c97d6ca8ba3bd91f3eeaeec0e1c61
https://pubmed.ncbi.nlm.nih.gov/1655738

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Characterization of an unusual thyroid response unit in the promoter of the human placental lactogen gene

Autor: M L, Voz, B, Peers, A, Belayew, J A, Martial

Publikováno v: The Journal of biological chemistry. 266(20)

The human placental lactogen B (hCS-B) promoter activity is strongly stimulated by thyroid hormones in the rat pituitary GC cell line. The minimal DNA sequence required for stimulation, as determined by transfection with 5' and 3' deletion mutants, s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e0a0e4f87805da901e042ffcd8b5886f
https://pubmed.ncbi.nlm.nih.gov/2071609

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The possibilities of recombinant DNA technology for the elucidation of the structure of steroid receptors and their mode of action

Autor: F, Rentier-Delrue, M, Voz, J A, Martial

Publikováno v: Progress in clinical and biological research. 342

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::30f16697ebcf85dca9156cd560d7c4de
https://pubmed.ncbi.nlm.nih.gov/2199993

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Human prolactin. cDNA structural analysis and evolutionary comparisons

Autor: N E, Cooke, D, Coit, J, Shine, J D, Baxter, J A, Martial

Publikováno v: The Journal of biological chemistry. 256(8)

Prolactin (Prl), growth hormone, and chorionic sommatomammotropin form a set (the "Prl set") of hormones which is thought to have evolved from a common ancestral gene. This assumption is based on several lines of evidence: overlap in their biological

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::38135222aa67818716df1f572fc397dc
https://pubmed.ncbi.nlm.nih.gov/6260780

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