Výsledky vyhledávání - "Serge Leterme"

Detection of pregnancy-associated glycoproteins in milk and blood as a test for early pregnancy in dairy cows

Autor: Serge Leterme, Christoph Egli, Anna Rice, San Pun, L. Commun, Anton Mestek, Katherine Velek, Jean-B. Barbry

Publikováno v: Journal of Veterinary Diagnostic Investigation
Journal of Veterinary Diagnostic Investigation, American Association of Veterinary Laboratory Diagnosticians, 2016, 28 (3), pp.207-213. ⟨10.1177/1040638716632815⟩

International audience; The objective of our study was to evaluate 2 pregnancy-associated glycoprotein (PAG)-based enzyme-linked immunosorbent assays (ELISAs) for use with either blood or milk. From 12 dairy farms, 116 Montbeliarde or Holstein cows w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed633fdb863d78f0665bdebedb23eeca
https://pubmed.ncbi.nlm.nih.gov/26944877

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Two distinct genes encode small isoproteolipids affecting plasma membrane H(+)-ATPase activity of Saccharomyces cerevisiae

Autor: P. Catty, Fred S. Dietrich, Serge Leterme, André Goffeau, Catherine Navarre

Publikováno v: Journal of Biological Chemistry. 269:21262-21268

A small proteolipid called PMP1 is associated with yeast plasma membrane H(+)-ATPase (Navarre, C., Ghislain, M., Leterme, S., Ferroud, C., Dufour, J.-P., and Goffeau, A. (1992) J. Biol. Chem. 267, 6425-6428). We have identified a second Saccharomyces

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe671d8bfa2cbf91c5ea52d738f47bd1
https://doi.org/10.1016/s0021-9258(17)31958-0

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PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1

Autor: André Goffeau, M Wang, L Van Dyck, Serge Leterme, Elisabetta Balzi

Publikováno v: Journal of Biological Chemistry. 269:2206-2214

The complete sequence of the pleiotropic drug resistance gene PDR5 from Saccharomyces cerevisiae is reported and analyzed. PDR5 encodes a 160-kDa protein with a predicted duplicated six membrane-span domain and a repeated putative ATP-binding domain.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78d45631d0b876ab0538602567e279f8
https://doi.org/10.1016/s0021-9258(17)42155-7

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PIF1 DNA helicase from Saccharomyces cerevisiae. Biochemical characterization of the enzyme

Autor: Serge Leterme, Françoise Foury, A. Lahaye

Publikováno v: Journal of Biological Chemistry. 268:26155-26161

Overexpressed PIF1 DNA helicase was purified from mitochondria to near homogeneity. Its ATPase and unwinding properties were characterized. The enzyme specifically utilizes ATP (or dATP) and MgCl2 (and to a lesser extent MnCl2). ATPase activity requi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b76d6878391865db0acaf610c20eca00
https://doi.org/10.1016/s0021-9258(19)74294-x

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Purification and Preliminary Characterization of Mitochondrial Complex I (NADH:Ubiquinone Reductase) from Broad Bean (Vicia faba L.)

Autor: Marc Boutry, Serge Leterme

Publikováno v: Scopus-Elsevier
Plant Physiology, Vol. 102, no. 2, p. 435-43 (1993)

NADH:ubiquinone reductase (EC 1.6.19.3), or complex I, was isolated from broad bean (Vicia faba L.) mitochondria. Osmotic shock and sequential treatment with 0.2% (v/v) Triton X-100 and 0.5% (w/v) [3-cholamidopropyl)dimethylammonio]-1-propanesulfate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee47b3839d32fcc6a789f81ce8398af1
https://doi.org/10.1104/pp.102.2.435

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Purification and complete sequence of a small proteolipid associated with the plasma membrane H(+)-ATPase of Saccharomyces cerevisiae

Autor: André Goffeau, C. Ferroud, Michel Ghislain, Catherine Navarre, Serge Leterme, Jean-Pierre Dufour

Publikováno v: Journal of Biological Chemistry. 267:6425-6428

The purified plasma membrane H(+)-ATPase of Schizosaccharomyces pombe and Saccharomyces cerevisiae display, in addition to the catalytic subunit of 100 kDa, a highly mobile component, soluble in chloroform/methanol. Chloroform/methanol extraction of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55e4e3fb4a5bda321e30177d8631a7b1
https://doi.org/10.1016/s0021-9258(18)42713-5

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The role of two small proteolipids associated to the H+-ATPase from yeast plasma membrane

Autor: Catherine Navarre, Michel Ghislain, André Goffeau, Serge Leterme

Publikováno v: Molecular and Cellular Mechanisms of H+ Transport ISBN: 9783642793035

The plasma membrane of Saccharomyces cerevisiae contains a well-characterized ATPase that pumps protons out of the cell energizing the membrane for nutrient uptake. This H+-ATPase is similar to the other members of the cation-translocating ATPase fam

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2dbd83d87702e1c56f4ecb9d32551ae5
https://doi.org/10.1007/978-3-642-79301-1_23

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Beta subunit of mitochondrial F1-ATPase from the fission yeast. Deduced sequence of the wild type protein and identification of a mutation that increases nucleotide binding

Autor: Pierre Falson, Serge Leterme, Carine Capiau, Marc Boutry

Publikováno v: European Journal of Biochemistry
European Journal of Biochemistry, Wiley, 1991, 200, pp.61-67

International audience; The Schizosaccharomyces pombe nuclear gene, atp2, encoding the beta subunit of the mitochondrial ATP synthase, was sequenced and found to contain a 1575-bp open reading frame. Two adjacent transcription-initiation sites were f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2421f3c3cf92830a2d4218ef99a023fc
https://hal.archives-ouvertes.fr/hal-00314179

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