Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Zikri Hasanbasri"'
Publikováno v:
Physical Chemistry Chemical Physics. 25:13275-13288
In silico approach optimizes the acquisition scheme for the measurement of distance constraints using rigid Cu(ii) labels. Such measurements are incisive probes of protein structure and dynamics.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::65df403062973243ffb7d0694aae063a
https://doi.org/10.1039/d3cp00404j
https://doi.org/10.1039/d3cp00404j
Publikováno v:
Physical Chemistry Chemical Physics. 24:14727-14739
Herein we establish a cost-efficient acquisition scheme for orientational-independent distance measurements using Cu2+–protein labels, using insights from Monte-Carlo modeling, MD simulations, and DEER EPR measurements.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3937b1052a202418f1c0fed4769cea3
https://doi.org/10.1039/d2cp01032a
https://doi.org/10.1039/d2cp01032a
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 347
Triarylmethyl (TAM)-based labels, while still underutilized, are a powerful class of labels for pulsed-Electron Spin Resonance (ESR) distance measurements. They feature slow relaxation rates for long-lasting signals, high stability for cellular exper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::42f29f2379ec6de5b66ac53fba52542d
https://pubmed.ncbi.nlm.nih.gov/36620971
https://pubmed.ncbi.nlm.nih.gov/36620971
Publikováno v:
Journal of Magnetic Resonance. 349:107413
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14b0f7bd92d8f9cfa52d4afe60c187cf
https://doi.org/10.1016/j.jmr.2023.107413
https://doi.org/10.1016/j.jmr.2023.107413
Publikováno v:
Physical chemistry chemical physics : PCCP. 24(24)
Recent advances in site-directed Cu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::65caf4c76eed05132f138ab7d713d1f9
https://pubmed.ncbi.nlm.nih.gov/35574729
https://pubmed.ncbi.nlm.nih.gov/35574729
Publikováno v:
Protein Sci
Site‐specific dynamics in proteins are at the heart of protein function. While electron paramagnetic resonance (EPR) has potential to measure dynamics in large protein complexes, the reliance on flexible nitroxide labels is limitating especially fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b1e393437399bfc03cfd707f8d700d9
https://pubmed.ncbi.nlm.nih.gov/35762707
https://pubmed.ncbi.nlm.nih.gov/35762707
Autor:
Sunil Saxena, Ivan S. Podkorytov, Sevastyan O. Rabdano, Nikolai R. Skrynnikov, Zikri Hasanbasri, Sergei A. Izmailov
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-18 (2020)
Scientific Reports
Scientific Reports
Site-directed spin labeling (SDSL) ESR is a valuable tool to probe protein systems that are not amenable to characterization by x-ray crystallography, NMR or EM. While general principles that govern the shape of SDSL ESR spectra are known, its precis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09b0f7c4ba778c99df71dd9086115ee4
http://link.springer.com/article/10.1038/s41598-019-56750-y
http://link.springer.com/article/10.1038/s41598-019-56750-y
Publikováno v:
Journal of Magnetic Resonance. 347:107363
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6c91313583c7bc4b5a7052d876ad37d7
https://doi.org/10.1016/j.jmr.2022.107363
https://doi.org/10.1016/j.jmr.2022.107363
Publikováno v:
J Phys Chem B
Sensitive in-cell distance measurements in proteins using pulsed-Electron Spin Resonance (ESR) require reduction-resistant and cleavage-resistant spin-labels. Among the reduction-resistant moieties, the hydrophilic trityl core known as OX063 is promi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8f3eb91f532fe17843bc3dea699f69e
https://europepmc.org/articles/PMC8819876/
https://europepmc.org/articles/PMC8819876/
Autor:
Richard T. Cattley, Jeffrey L. Brodsky, Pamela S. Cantrell, Diep Nguyen, Megan E. Yates, Xuemei Zeng, Teresa M. Buck, Zikri Hasanbasri, Nathan A. Yates
Publikováno v:
Mol Cell Proteomics
Studies in the yeast Saccharomyces cerevisiae have helped define mechanisms underlying the activity of the ubiquitin-proteasome system (UPS), uncover the proteasome assembly pathway, and link the UPS to the maintenance of cellular homeostasis. Howeve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16c326bde17a570d4aef3234a0a966f8
https://europepmc.org/articles/PMC7664122/
https://europepmc.org/articles/PMC7664122/