Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Andrija Finka"'
Autor:
Bruno Fauvet, Andrija Finka, Marie-Pierre Castanié-Cornet, Anne-Marie Cirinesi, Pierre Genevaux, Manfredo Quadroni, Pierre Goloubinoff
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration wit
Externí odkaz:
https://doaj.org/article/970197eb0bba44c6bea6a1507738f3d2
Autor:
Andrija Finka, Manfredo Quadroni, Pierre Goloubinoff, Bruno Fauvet, Pierre Genevaux, Anne-Marie Cirinesi, Marie-Pierre Castanié-Cornet
Publikováno v:
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences, Frontiers Media, 2021, 8 (14), pp.2914-2928.e7. ⟨10.3389/fmolb.2021.653073⟩
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in molecular biosciences, vol. 8, pp. 653073
Frontiers in Molecular Biosciences, Frontiers Media, 2021, 8 (14), pp.2914-2928.e7. ⟨10.3389/fmolb.2021.653073⟩
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in molecular biosciences, vol. 8, pp. 653073
In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa8debf440f38a0ffbd1b5695617ef1d
https://hal.archives-ouvertes.fr/hal-03364316
https://hal.archives-ouvertes.fr/hal-03364316
Publikováno v:
Plant, cell & environment, vol. 44, no. 7, pp. 2117-2133
Plant, Cell & Environment
Plant, Cell & Environment
At dawn of a scorching summer day, land plants must anticipate upcoming extreme midday temperatures by timely establishing molecular defences that can keep heat‐labile membranes and proteins functional. A gradual morning pre‐exposure to increasin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b66c8ebe5a28a9db0dbb07abb850fd2
https://serval.unil.ch/notice/serval:BIB_4641E70C783E
https://serval.unil.ch/notice/serval:BIB_4641E70C783E
Autor:
Andrija Finka
Publikováno v:
Medica Jadertina
Volume 49
Issue suplement 2
Volume 49
Issue suplement 2
21 Molecular mechanisms of acquired thermotolerance in plants Andrija Finka Department of Ecology, Agriculture and Aquaculture, University of Zadar, Trg Kneza Višeslava 1, 23000 Zadar afinka@unizd.hr Sessile organisms such as plants experience daily
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______951::87f06e72db5ad16777d1b2868e01507d
https://hrcak.srce.hr/file/328695
https://hrcak.srce.hr/file/328695
Publikováno v:
Annual Review of Biochemistry, vol. 85, pp. 715-742
Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989, groundbreaking experiments demonstrated that a purified chaperone can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54a6cf180c4f25cc28bdaff5e6fef370
https://doi.org/10.1146/annurev-biochem-060815-014124
https://doi.org/10.1146/annurev-biochem-060815-014124
Autor:
Manfredo Quadroni, Bruno Fauvet, Pierre Genevaux, Marie-Pierre Castanié-Cornet, Andrija Finka, Anne-Marie Cirinesi, Pierre Goloubinoff
Whereas in eukaryotic cells, the Hsp90s are profusely-studied molecular chaperones controlling protein homeostasis together with Hsp70s, in bacteria, the function of Hsp90 (HtpG) and its collaboration with Hsp70 (DnaK) remains unknown. To uncover phy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc398ecf9e563c9551e35a25cb99267e
https://doi.org/10.1101/451989
https://doi.org/10.1101/451989
Autor:
Andrija Finka, Pierre Goloubinoff
Publikováno v:
Cell Stress and Chaperones
Cell Stress and Chaperones, vol. 18, no. 5, pp. 591-605
Cell Stress and Chaperones, vol. 18, no. 5, pp. 591-605
In the crowded environment of human cells, folding of nascent polypeptides and refolding of stress-unfolded proteins is error prone. Accumulation of cytotoxic misfolded and aggregated species may cause cell death, tissue loss, degenerative conformati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96c671a684168b3a322475c37fcf69b5
Autor:
Andrija Finka, Manfredo Quadroni, Pierre Goloubinoff, Biana Shtaif, Galit Pinto, Galia Gat-Yablonski
Publikováno v:
Aging (Albany NY)
Aging, vol. 8, no. 8, pp. 1735-1758
Aging, vol. 8, no. 8, pp. 1735-1758
Studies in young mammals on the molecular effects of food restriction leading to prolong adult life are scares. Here, we used high-throughput quantitative proteomic analysis of whole rat livers to address the molecular basis for growth arrest and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8df9a55530d9c93b073185688750f859
https://doi.org/10.18632/aging.101009
https://doi.org/10.18632/aging.101009
Autor:
Pierre Goloubinoff, Younousse Saidi, Frans J. M. Maathuis, America Farinia Henriquez Cuendet, Andrija Finka
Publikováno v:
The Plant cell
Typically at dawn on a hot summer day land plants need precise molecular thermometers to sense harmless increments in the ambient temperature to induce a timely heat shock response (HSR) and accumulate protective heat shock proteins in anticipation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0192d216d439e2b004c1499ded00fcb9
https://doi.org/10.1105/tpc.112.095844
https://doi.org/10.1105/tpc.112.095844
Publikováno v:
Trends in biochemical sciences
In plants, the heat stress response (HSR) is highly conserved and involves multiple pathways, regulatory networks and cellular compartments. At least four putative sensors have recently been proposed to trigger the HSR. They include a plasma membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb15596626aea6d9a348d6af3bb88145