Výsledky vyhledávání - "Bernasconi, Lilia"

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H90-10 single-chain antibody recognizes Hsp90beta by immunoprecipitation and Western blotting

Autor: Abboud, Ernest, Bernasconi, Lilia, Picard, Didier

Publikováno v: Antibody reports, Vol. 4, No 1 (2021) P. e285

The recombinant antibody H90-10 detects the endogenous human heat-shock protein 90 beta (Hsp90β) by immunoprecipitation (IP) and Western blotting.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbc56b7c77bdb2d6f6d45a69c51ac9fb

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The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

Autor: Bhattacharya, Kaushik, Weidenauer, Lorenz, Luengo, Tania Morán, Pieters, Ellis C., Echeverría, Pablo C., Bernasconi, Lilia, Wider, Diana, Sadian, Yashar, Koopman, Margreet B., Villemin, Matthieu, Bauer, Christoph, Rüdiger, Stefan G. D., Quadroni, Manfredo, Picard, Didier

Publikováno v: Nature communications, vol. 11, no. 1, pp. 5975
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-21 (2020)
Nature Communications, Vol. 11, No 5975 (2020)

Hop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a number of e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86f0303de9d74f104f895a228e479a13
https://serval.unil.ch/notice/serval:BIB_A3C58F977248

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The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis

Autor: Joshi, Abhinav, Dai, Li, Liu, Yanxin, Lee, Jungsoon, Ghahhari, Nastaran Mohammadi, Segala, Gregory, Beebe, Kristin, Jenkins, Lisa M., Lyons, Gaelyn C., Bernasconi, Lilia, Tsai, Francis T. F., Agard, David A., Neckers, Len, Picard, Didier

Publikováno v: BMC Biology
BMC Biology, Vol 18, Iss 1, Pp 1-23 (2020)
BMC Biology, Vol. 18, No 10 (2020)

Background The molecular chaperone TRAP1, the mitochondrial isoform of cytosolic HSP90, remains poorly understood with respect to its pivotal role in the regulation of mitochondrial metabolism. Most studies have found it to be an inhibitor of mitocho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0b1cfd4731c77edaf19067c23e184a9c
http://europepmc.org/articles/PMC6986101

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Additional file 2 of The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis

Autor: Abhinav Joshi, Dai, Li, Yanxin Liu, Jungsoon Lee, Ghahhari, Nastaran, Segala, Gregory, Beebe, Kristin, Jenkins, Lisa, Gaelyn Lyons, Bernasconi, Lilia, Tsai, Francis, Agard, David, Neckers, Len, Picard, Didier

Additional file 2: Figure S2. Carbon flux and total quantitation of target metabolites. (a) Schematic metabolic map showing the flow and distribution of 13C atoms in metabolites of the TCA cycle when cells consume 13C-Gln. Note that most of these met

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d02c1b430bdb6e3c361d1cbe654ba09

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Additional file 12 of The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis

Additional file 12: Figure S5. An extension of Figure 5 showing TRAP1-GST pulldown MS strategy and analysis, and a control experiment for mitochondrial lysis conditions. (a) TRAP1-GST pulldown strategy. (b) Venn diagram of the proteins identified by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80f07c45678633cbfb9e70b1ffa26ee6

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