Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Ayala, Shiber"'
Autor:
Johannes Venezian, Hagit Bar-Yosef, Hila Ben-Arie Zilberman, Noam Cohen, Oded Kleifeld, Juan Fernandez-Recio, Fabian Glaser, Ayala Shiber
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-17 (2024)
Abstract Protein-protein interactions are at the heart of all cellular processes, with the ribosome emerging as a platform, orchestrating the nascent-chain interplay dynamics. Here, to study the characteristics governing co-translational protein fold
Externí odkaz:
https://doaj.org/article/2ea1e80328a249b98833f76866e76e8b
Autor:
Ayala Shiber, Yoav S. Arava
Publikováno v:
Microorganisms, Vol 11, Iss 3, p 739 (2023)
Translation regulation and localized translation are essential for protein synthesis, controlling all aspects of cellular function in health and disease [...]
Externí odkaz:
https://doaj.org/article/50b1e96c081f43ac841dd05adef2d0d9
Autor:
Ayala Shiber, Tommer Ravid
Publikováno v:
Biomolecules, Vol 4, Iss 3, Pp 704-724 (2014)
Molecular chaperones were originally discovered as heat shock-induced proteins that facilitate proper folding of proteins with non-native conformations. While the function of chaperones in protein folding has been well documented over the last four d
Externí odkaz:
https://doaj.org/article/5a0bebdbcbea4e2aa18ac85577b31c3c
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2477
Selective Ribosome Profiling (SeRP) is an emerging methodology, developed to capture cotranslational interactions in vivo. To date, SeRP is the only method that can directly capture, in near-codon resolution, ribosomes in action. Thus, SeRP allows us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5aec7ca7617ac23fb7982db473f74b18
https://pubmed.ncbi.nlm.nih.gov/35524118
https://pubmed.ncbi.nlm.nih.gov/35524118
Publikováno v:
Methods in Molecular Biology ISBN: 9781071622568
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ee3e02882b928c3d4a14818b2783eb1
https://doi.org/10.1007/978-1-0716-2257-5_11
https://doi.org/10.1007/978-1-0716-2257-5_11
Autor:
Ajeet K, Sharma, Johannes, Venezian, Ayala, Shiber, Günter, Kramer, Bernd, Bukau, Edward P, O'Brien
Publikováno v:
Proc Natl Acad Sci U S A
The presence of a single cluster of nonoptimal codons was found to decrease a transcript’s half-life through the interaction of the ribosome-associated quality control machinery with stalled ribosomes in Saccharomyces cerevisiae. The impact of mult
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::267fe86aa1019bea205a8bc147d46821
https://pubmed.ncbi.nlm.nih.gov/34911752
https://pubmed.ncbi.nlm.nih.gov/34911752
Publikováno v:
Journal of Visualized Experiments.
In recent years, it has become evident that ribosomes not only decode our mRNA but also guide the emergence of the polypeptide chain into the crowded cellular environment. Ribosomes provide the platform for spatially and kinetically controlled bindin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09f3ec2578b8f9a984f6f7cb378752cd
https://doi.org/10.3791/62878
https://doi.org/10.3791/62878
Publikováno v:
Annual Review of Biochemistry
The timely production of functional proteins is of critical importance for the biological activity of cells. To reach the functional state, newly synthesized polypeptides have to become enzymatically processed, folded, and assembled into oligomeric c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3d113ca8fed49da5058ffc0fdff1248
https://pubmed.ncbi.nlm.nih.gov/30508494
https://pubmed.ncbi.nlm.nih.gov/30508494
Autor:
Günter Kramer, Kevin Klann, Bernd Bukau, Frank Tippmann, Kristina Döring, Ulrike A. Friedrich, Ayala Shiber, Mostafa Zedan, Dorina Merker
Publikováno v:
Nature
The folding of newly synthesized proteins to the native state is a major challenge within the crowded cellular environment, as non-productive interactions can lead to misfolding, aggregation and degradation1. Cells cope with this challenge by couplin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::548a2d90d3b8b6d141d8b2da1aab1e55
https://pubmed.ncbi.nlm.nih.gov/30194367
https://pubmed.ncbi.nlm.nih.gov/30194367
Autor:
Tommer Ravid, Ayala Shiber
Publikováno v:
Biomolecules, Vol 4, Iss 3, Pp 704-724 (2014)
Biomolecules
Biomolecules
Molecular chaperones were originally discovered as heat shock-induced proteins that facilitate proper folding of proteins with non-native conformations. While the function of chaperones in protein folding has been well documented over the last four d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af7521e7feec16370d92c51b80b0faff
https://doi.org/10.3390/biom4030704
https://doi.org/10.3390/biom4030704