A comprehensive review of the interaction between COVID-19 spike proteins with mammalian small and major heat shock proteins

Autor: Navhaya Liberty T., Blessing Dzveta Mutsawashe, Yamkela Mthembu, Godlo Sesethu, Makhoba Xolani Henry

Publikováno v: Biomolecular Concepts, Vol 15, Iss 1, Pp 3518-88 (2024)

Coronavirus disease 2019 (COVID-19) is a novel disease that had devastating effects on human lives and the country’s economies worldwide. This disease shows similar parasitic traits, requiring the host’s biomolecules for its survival and propagat

Externí odkaz: https://doaj.org/article/f748989b52f24552ba8f921c35e8671e

RNAi-dependent heterochromatin assembly in fission yeast Schizosaccharomyces pombe requires heat-shock molecular chaperones Hsp90 and Mas5

Autor: Kosuke Okazaki, Hiroaki Kato, Tetsushi Iida, Kaori Shinmyozu, Jun-ichi Nakayama, Yota Murakami, Takeshi Urano

Publikováno v: Epigenetics & Chromatin, Vol 11, Iss 1, Pp 1-15 (2018)

Abstract Background Heat-shock molecular chaperone proteins (Hsps) promote the loading of small interfering RNA (siRNA) onto RNA interference (RNAi) effector complexes. While the RNAi process is coupled with heterochromatin assembly in several model

Externí odkaz: https://doaj.org/article/c21f2b976a3141d2b4c189279221bfda

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Prospects of HSP70 as a genetic marker for thermo-tolerance and immuno-modulation in animals under climate change scenario

Autor: Chengjian Yang, Muhammad Shah Nawaz ul Rehman, Muhammad Ali, Faiz-ul Hassan, Ayesha Nawaz, Syed Muhammad Raihan Dilshad

Publikováno v: Animal Nutrition, Vol 5, Iss 4, Pp 340-350 (2019)
Animal Nutrition

Heat stress induced by long periods of high ambient temperature decreases animal productivity, leading to heavy economic losses. This devastating situation for livestock production is even becoming worse under the present climate change scenario. Str

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27efcee1fa50d25d2e013b90f8d8fe25
http://www.sciencedirect.com/science/article/pii/S2405654519300095

Tubulin folding: the special case of a beta-tubulin isotype from the Antarctic psychrophilic ciliate Euplotes focardii

Autor: Luciano Milanesi, Daniela Sparvoli, Sandra Pucciarelli, Ronald Melki, Federica Chiappori, Cristina Miceli

Publikováno v: Polar Biology
Polar Biology, Springer Verlag, 2013, 36 (12), pp.1833-1838. ⟨10.1007/s00300-013-1390-9⟩
Polar biology
36 (2013): 1833–1838. doi:10.1007/s00300-013-1390-9
info:cnr-pdr/source/autori:Pucciarelli, Sandra; Chiappori, Federica; Sparvoli, Daniela; Milanesi, Luciano; Miceli, Cristina; Melki, Ronald/titolo:Tubulin folding: the special case of a beta-tubulin isotype from the Antarctic psychrophilic ciliate Euplotes focardii/doi:10.1007%2Fs00300-013-1390-9/rivista:Polar biology (Print)/anno:2013/pagina_da:1833/pagina_a:1838/intervallo_pagine:1833–1838/volume:36

International audience; Folding assistance is a fundamental requirement of certain proteins, and it may be subjected to physicochemical constraints in case of organisms adapted to polar temperatures. Limited information is available about protein fol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60197804777dfb9a72795ac46ef58aaa
https://doi.org/10.1007/s00300-013-1390-9