Zobrazeno 1 - 10
of 200
pro vyhledávání: '"Saccharomyces cerevisiae/metabolism"'
Publikováno v:
mBio, vol. 14, no. 3, pp. e0010223
bioRxiv
bioRxiv
Cells stabilize intracellular inorganic phosphate (P i ) to compromise between large biosynthetic needs and detrimental bioenergetic effects of P i . P i homeostasis in eukaryotes uses Syg1/Pho81/Xpr1 (SPX) domains, which are receptors for inositol p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10302ebd3f6c7affd144bd2402a61ad3
https://serval.unil.ch/resource/serval:BIB_16840248D4A5.P001/REF.pdf
https://serval.unil.ch/resource/serval:BIB_16840248D4A5.P001/REF.pdf
Publikováno v:
Svedlund, N, Evering, S, Gibson, B & Krogerus, K 2022, ' Fruits of their labour : Biotransformation reactions of yeasts during brewery fermentation ', Applied Microbiology and Biotechnology, vol. 106, no. 13-16, pp. 4929–4944 . https://doi.org/10.1007/s00253-022-12068-w
There is a growing appreciation for the role that yeast play in biotransformation of flavour compounds during beverage fermentations. This is particularly the case for brewing due to the continued popularity of aromatic beers produced via the dry-hop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3afe93aff427183f96bd482c9ebfeb9
https://doi.org/10.1007/s00253-022-12068-w
https://doi.org/10.1007/s00253-022-12068-w
Autor:
Joka Pipercevic, Bastian Kohl, Ruta Gerasimaite, Véronique Comte-Miserez, Sarah Hostachy, Thomas Müntener, Elia Agustoni, Henning Jacob Jessen, Dorothea Fiedler, Andreas Mayer, Sebastian Hiller
Publikováno v:
Nature communications, vol. 14, no. 1, pp. 2645
Many proteins involved in eukaryotic phosphate homeostasis are regulated by SPX domains. In yeast, the vacuolar transporter chaperone (VTC) complex contains two such domains, but mechanistic details of its regulation are not well understood. Here, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2569fd84c61d62a1bd9d675c55566e5
https://serval.unil.ch/notice/serval:BIB_A3106DB32252
https://serval.unil.ch/notice/serval:BIB_A3106DB32252
Autor:
Laura Luzia, David Lao‐Martil, Philipp Savakis, Johan van Heerden, Natal van Riel, Bas Teusink
Publikováno v:
FEBS journal, 289(19), 6021-6037. Wiley-Blackwell
FEBS Journal, 289(19), 6021-6037. Wiley-Blackwell
Luzia, L, Lao-Martil, D, Savakis, P, van Heerden, J, van Riel, N & Teusink, B 2022, ' pH dependencies of glycolytic enzymes of yeast under in vivo-like assay conditions ', FEBS Journal, vol. 289, no. 19, pp. 6021-6037 . https://doi.org/10.1111/febs.16459
FEBS Journal, 289(19), 6021-6037. Wiley-Blackwell
Luzia, L, Lao-Martil, D, Savakis, P, van Heerden, J, van Riel, N & Teusink, B 2022, ' pH dependencies of glycolytic enzymes of yeast under in vivo-like assay conditions ', FEBS Journal, vol. 289, no. 19, pp. 6021-6037 . https://doi.org/10.1111/febs.16459
Under carbon source transitions, the intracellular pH of Saccharomyces cerevisiae is subject to change. Dynamics in pH modulate the activity of the glycolytic enzymes, resulting in a change in glycolytic flux and ultimately cell growth. To understand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1404819400a4ddb06ce4dcd404d2fcb
https://pure.amc.nl/en/publications/ph-dependencies-of-glycolytic-enzymes-of-yeast-under-in-vivolike-assay-conditions(4eab9001-c6b1-4f66-bebd-b06354e3a803).html
https://pure.amc.nl/en/publications/ph-dependencies-of-glycolytic-enzymes-of-yeast-under-in-vivolike-assay-conditions(4eab9001-c6b1-4f66-bebd-b06354e3a803).html
Autor:
Daiß, Julia L., Pilsl, Michael, Straub, Kristina, Bleckmann, Andrea, Höcherl, Mona, Heiss, Florian B., Abascal-Palacios, Guillermo, Ramsay, Ewan Phillip, Tlučková, Katarina, Mars, Jean-Clement, Fürtges, Torben, Bruckmann, Astrid, Rudack, Till, Bernecky, Carrie, Lamour, Valérie, Panov, Konstantin, Vannini, Alessandro, Moss, Tom, Engel, Christoph
Publikováno v:
Life Science Alliance
Life Science Alliance, 2022, 5 (11), pp.e202201568. ⟨10.26508/lsa.202201568⟩
Daiß, J L, Pilsl, M, Straub, K, Bleckmann, A, Höcherl, M, Heiss, F B, Abascal-Palacios, G, Ramsay, E P, Tlučková, K, Mars, J-C, Fürtges, T, Bruckmann, A, Rudack, T, Bernecky, C, Lamour, V, Panov, K, Vannini, A, Moss, T & Engel, C 2022, ' The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans ', Life Science Alliance, vol. 5, no. 11, e202201568 . https://doi.org/10.26508/lsa.202201568
Life Science Alliance, 2022, 5 (11), pp.e202201568. ⟨10.26508/lsa.202201568⟩
Daiß, J L, Pilsl, M, Straub, K, Bleckmann, A, Höcherl, M, Heiss, F B, Abascal-Palacios, G, Ramsay, E P, Tlučková, K, Mars, J-C, Fürtges, T, Bruckmann, A, Rudack, T, Bernecky, C, Lamour, V, Panov, K, Vannini, A, Moss, T & Engel, C 2022, ' The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans ', Life Science Alliance, vol. 5, no. 11, e202201568 . https://doi.org/10.26508/lsa.202201568
Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a major determinant of cellular growth, and dysregulation is observed in many cancer types. Here, we present the purification of human Pol I from cells carrying a genomic GFP f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98c5a494af75c77b57e597eca946ccaa
https://epub.uni-regensburg.de/52860/
https://epub.uni-regensburg.de/52860/
Autor:
Francine J. Boonekamp, Ewout Knibbe, Marcel A. Vieira-Lara, Melanie Wijsman, Marijke A.H. Luttik, Karen van Eunen, Maxime den Ridder, Reinier Bron, Ana Maria Almonacid Suarez, Patrick van Rijn, Justina C. Wolters, Martin Pabst, Jean-Marc Daran, Barbara M. Bakker, Pascale Daran-Lapujade
Publikováno v:
Cell Reports, 39(13):111010. Cell Press
Cell reports, 39(13):111010. CELL PRESS
Cell Reports, 39(13)
Cell reports, 39(13):111010. CELL PRESS
Cell Reports, 39(13)
Although transplantation of single genes in yeast plays a key role in elucidating gene functionality in metazoans, technical challenges hamper humanization of full pathways and processes. Empowered by advances in synthetic biology, this study demonst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f6c37ae17abceac71463ceb4835f8a8
https://research.rug.nl/en/publications/fd1fea1c-43e9-4bf4-94c3-16cc1942d876
https://research.rug.nl/en/publications/fd1fea1c-43e9-4bf4-94c3-16cc1942d876
Autor:
Tomoyuki Hatano, Tzer Chyn Lim, Ingrid Billault-Chaumartin, Anubhav Dhar, Ying Gu, Teresa Massam-Wu, William Scott, Sushmitha Adishesha, Bernardo Chapa-y-Lazo, Luke Springall, Lavanya Sivashanmugam, Masanori Mishima, Sophie G. Martin, Snezhana Oliferenko, Saravanan Palani, Mohan K. Balasubramanian
Publikováno v:
Journal of cell science, vol. 135, no. 18, pp. jcs260288
Tropomyosins are structurally conserved α-helical coiled-coil proteins that bind along the length of filamentous actin (F-actin) in fungi and animals. Tropomyosins play essential roles in the stability of actin filaments and in regulating myosin II
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3da7eabaef1879f618f0b13c3eff037f
https://pubmed.ncbi.nlm.nih.gov/36148799
https://pubmed.ncbi.nlm.nih.gov/36148799