Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Hisham Mazal"'
Publikováno v:
eLife, Vol 11 (2022)
Cryogenic optical localization in three dimensions (COLD) was recently shown to resolve up to four binding sites on a single protein. However, because COLD relies on intensity fluctuations that result from the blinking behavior of fluorophores, it is
Externí odkaz:
https://doaj.org/article/07dd6f82f5db42ef8adb4e4f4077f9a5
Autor:
Hisham Mazal, Marija Iljina, Yoav Barak, Nadav Elad, Rina Rosenzweig, Pierre Goloubinoff, Inbal Riven, Gilad Haran
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Large protein machines are tightly regulated through allosteric communication channels. Here authors use single-molecule FRET and demonstrate the involvement of ultrafast conformational dynamics in the allosteric regulation of ClpB, a hexameric AAA+
Externí odkaz:
https://doaj.org/article/ec18ad5b1e2047c382aaaf3a49e43f29
Publikováno v:
eLife, Vol 9 (2020)
The thermodynamics of protein folding in bulk solution have been thoroughly investigated for decades. By contrast, measurements of protein substrate stability inside the GroEL/ES chaperonin cage have not been reported. Such measurements require stabl
Externí odkaz:
https://doaj.org/article/58d49b94fa5f4f7cb176ed685ab9b668
Autor:
Mahyar Dahmardeh, Houman Mirzaalian Dastjerdi, Hisham Mazal, Harald Köstler, Vahid Sandoghdar
Publikováno v:
Nature Methods. 20:442-447
Interferometric scattering (iSCAT) microscopy is a label-free optical method capable of detecting single proteins, localizing their binding positions with nanometer precision, and measuring their mass. In the ideal case, iSCAT is limited by shot nois
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fce86ed4f7c25655139be8a774f063cd
https://doi.org/10.1038/s41592-023-01778-2
https://doi.org/10.1038/s41592-023-01778-2
Autor:
Marija Iljina, Hisham Mazal, Ashan Dayananda, Zhaocheng Zhang, George Stan, Inbal Riven, Gilad Haran
AAA+ proteins (ATPases associated with various cellular activities) comprise a family of powerful ring-shaped ATP-dependent translocases that carry out numerous vital substrate-remodeling functions ranging from protein unfolding and disaggregation to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f0bb77ca18648e522fc6e50fb23c3e75
https://doi.org/10.1101/2023.02.02.526786
https://doi.org/10.1101/2023.02.02.526786
Autor:
Mahyar Dahmardeh, Houman Mirzaalian Dastjerdi, Hisham Mazal, Harald Köstler, Vahid Sandoghdar
Interferometric scattering (iSCAT) microscopy is a label-free optical method capable of detecting single proteins, localizing their binding positions with nanometer precision, and measuring their mass. In the ideal case, iSCAT is limited by shot nois
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c7231a29b19d67afe258782c5d50226b
https://doi.org/10.21203/rs.3.rs-1635524/v1
https://doi.org/10.21203/rs.3.rs-1635524/v1
Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain
Publikováno v:
ACS Chemical Biology
ACS chemical biology, vol. 16, no. 4, pp. 775-785
ACS chemical biology, vol. 16, no. 4, pp. 775-785
ClpB is a tightly regulated AAA+ disaggregation machine. Each ClpB molecule is composed of a flexibly attached N-terminal domain (NTD), an essential middle domain (MD) that activates the machine by tilting, and two nucleotide-binding domains. The NTD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e61a8199f3cefffb268d6a0a9d12dd5d
https://doi.org/10.1021/acschembio.1c00156
https://doi.org/10.1021/acschembio.1c00156
Publikováno v:
The FEBS journalReferences.
It has been recently shown that in some proteins, tertiary-structure dynamics occur surprisingly fast, that is on the microsecond or sub-millisecond time scales. In this State of the Art Review, we discuss how such ultrafast domain motions relate to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc50fe07a8c96b4a49ad6e033bc0d373
https://pubmed.ncbi.nlm.nih.gov/35638578
https://pubmed.ncbi.nlm.nih.gov/35638578
Publikováno v:
Journal of the American Chemical Society
A new mechanism of allostery in proteins, based on charge rather than structure, is reported. We demonstrate that dynamic redistribution of charge within a protein can control its function and affect its interaction with a binding partner. In particu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb27fcaa66f1a45e926ef6f20d2ad8e9
http://europepmc.org/articles/PMC7735699
http://europepmc.org/articles/PMC7735699