Two independent routes of de novo vitamin B6 biosynthesis: not that different after all

Autor: Barbara Kappes, Peter Macheroux, Ivo Tews, Thomas Raschle, Nikolaus Amrhein, Thérésa Bridget Fitzpatrick

Publikováno v: Biochemical Journal, Vol. 407, No 1 (2007) pp. 1-13

Vitamin B6 is well known in its biochemically active form as pyridoxal 5′-phosphate, an essential cofactor of numerous metabolic enzymes. The vitamin is also implicated in numerous human body functions ranging from modulation of hormone function to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68dbd4bfb53601ea357978da880b9cb2
https://doi.org/10.1042/bj20070765

Crystal structure, biochemical and genetic characterization of yeast and E. cuniculi TAF(II)5 N-terminal domain: implications for TFIID assembly

Autor: Christophe Romier, Christian P. Vivarès, Catherine Birck, Nicole James, Dino Moras, Jean Cavarelli, Martine A. Collart

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2007, 368 (5), pp.1292-306. ⟨10.1016/j.jmb.2007.02.039⟩
Journal of Molecular Biology, Vol. 368, No 5 (2007) pp. 1292-306
Journal of Molecular Biology, 2007, 368 (5), pp.1292-306. ⟨10.1016/j.jmb.2007.02.039⟩

General transcription factor TFIID plays an essential role in transcription initiation by RNA polymerase II at numerous promoters. However, understanding of the assembly and a full structural characterization of this large 15 subunit complex is lacki

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2eca0b980b88428fc42d06e5c6933808
https://pubmed.ncbi.nlm.nih.gov/17397863

The Yeast hnRNP-Like Proteins Yra1p and Yra2p Participate in mRNA Export through Interaction with Mex67p

Autor: Patrizia Vinciguerra, Daniel Zenklusen, Françoise Stutz, Yvan Strahm

Publikováno v: Molecular and Cellular Biology, Vol. 21, No 13 (2001) pp. 4219-32

Yra1p is an essential nuclear protein which belongs to the evolutionarily conserved REF (RNA and export factor binding proteins) family of hnRNP-like proteins. Yra1p contributes to mRNA export in vivo and directly interacts with RNA and the shuttling

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9066f61b7718573da7ebd1ba3ab60d35
https://europepmc.org/articles/PMC87083/

The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest

Autor: Olivier Donzé, Toufik Abbas-Terki, Didier Picard

Publikováno v: FEBS Letters, Vol. 467, No 1 (2000) pp. 111-6

The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast. A cdc37 mutant strain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4410d8a9bf00987eba7d2bdd25d6af15
https://archive-ouverte.unige.ch/unige:4652

Functional domains of the heavy metal-responsive transcription regulator MTF-1

Autor: Freddy Radtke, Hans-Peter Müller, Walter Schaffner, Enrico Brugnera, Oleg Georgiev

Publikováno v: Nucleic acids research. 23(12)

Metallothioneins (MTs) constitute a class of low molecular weight, cysteine-rich, metal binding proteins which are regulated at the level of gene transcription in response to heavy metals and other adverse treatments. We have previously cloned a zinc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfcdf0f918c8d4c29e91b71a18a6f4f0
https://pubmed.ncbi.nlm.nih.gov/7610056