Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Alexander Eletsky"'
Autor:
Niloofar Abolhasani Khaje, Alexander Eletsky, Sarah E. Biehn, Charles K. Mobley, Monique J. Rogals, Yoonkyoo Kim, Sushil K. Mishra, Robert J. Doerksen, Steffen Lindert, James H. Prestegard, Joshua S. Sharp
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-8 (2022)
A mass spectrometry-based method guides computational modeling for de novo protein structure prediction.
Externí odkaz:
https://doaj.org/article/c2ada858bcc842d6afa56065cc8b866e
Autor:
Alexander Eletsky, Karolina Michalska, Scott Houliston, Qi Zhang, Michael D Daily, Xiaohui Xu, Hong Cui, Adelinda Yee, Alexander Lemak, Bin Wu, Maite Garcia, Meagan C Burnet, Kristen M Meyer, Uma K Aryal, Octavio Sanchez, Charles Ansong, Rong Xiao, Thomas B Acton, Joshua N Adkins, Gaetano T Montelione, Andrzej Joachimiak, Cheryl H Arrowsmith, Alexei Savchenko, Thomas Szyperski, John R Cort
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e101787 (2014)
Bacterial species in the Enterobacteriaceae typically contain multiple paralogues of a small domain of unknown function (DUF1471) from a family of conserved proteins also known as YhcN or BhsA/McbA. Proteins containing DUF1471 may have a single or th
Externí odkaz:
https://doaj.org/article/86d6bee1feac4e90bbb12b0e86a9a3f7
Autor:
Monique J. Rogals, Alexander Eletsky, Chin Huang, Laura C. Morris, Kelley W. Moremen, James H. Prestegard
Publikováno v:
ACS chemical biology.
Glycans attached to glycoproteins can contribute to stability, mediate interactions with other proteins, and initiate signal transduction. Glycan conformation, which is critical to these processes, is highly variable and often depicted as sampling a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05cfef9352f6a52a847493be6e2ed9b6
https://pubmed.ncbi.nlm.nih.gov/36417668
https://pubmed.ncbi.nlm.nih.gov/36417668
Autor:
Robert V. Williams, Monique J. Rogals, Alexander Eletsky, Chin Huang, Laura C. Morris, Kelley W. Moremen, James H. Prestegard
Publikováno v:
Journal of Magnetic Resonance. 345:107336
Not all proteins are amenable to uniform isotopic labeling with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35998bfa3c44276d245cadb90a3ce1d0
https://doi.org/10.1016/j.jmr.2022.107336
https://doi.org/10.1016/j.jmr.2022.107336
Autor:
Alexander Eletsky, James H. Prestegard, Laura C. Morris, Jeong Yeh Yang, Robert J. Woods, Kelley W. Moremen, Fang Tian, Gordon R. Chalmers
Publikováno v:
J Mol Biol
Characterization of proteins using NMR methods begins with assignment of resonances to specific residues. This is usually accomplished using sequential connectivities between nuclear pairs in proteins uniformly labeled with NMR active isotopes. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89a3406305601f158b97778eeef00f38
https://doi.org/10.1016/j.jmb.2019.04.029
https://doi.org/10.1016/j.jmb.2019.04.029
Autor:
Christopher M. West, Alexander Eletsky, James H. Prestegard, Karen J. Gonzalez, Hyun W. Kim, Eva-Maria Strauch, Hanke van der Wel
Publikováno v:
Biochemistry
Skp1 is an adapter that links F-box proteins to cullin-1 in the Skp1/cullin-1/F-box (SCF) protein family of E3 ubiquitin ligases that targets specific proteins for polyubiquitination and subsequent protein degradation. Skp1 from the amoebozoan Dictyo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::089305b95eed28efda5d2713baf6eaf1
https://europepmc.org/articles/PMC7521599/
https://europepmc.org/articles/PMC7521599/
Autor:
Thomas Szyperski, Gaetano T. Montelione, Nourhan S. Daigham, G. V. T. Swapna, Jeffrey M. Boyd, Peter C. Kahn, Hassan Al-Tameemi, Zuelay Rosario-Cruz, Alexander Eletsky
As complications associated with antibiotic resistance have intensified, copper (Cu) is attracting attention as an antimicrobial agent. Recent studies have shown that copper surfaces decrease microbial burden, and host macrophages use Cu to increase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::441cd10c5395ebad5571c14c54fe912e
https://europepmc.org/articles/PMC6422080/
https://europepmc.org/articles/PMC6422080/
Autor:
Surya V.S.R.K. Pulavarti, Per Jr Greisen, Gabriel J. Rocklin, Colin Correnti, Thomas W. Linsky, David J. Craik, Olivier Cheneval, Lauren Carter, X. Xu, Quentin Kaas, Jason M. Gilmore, Christopher D. Bahl, Po-Ssu Huang, William A. Johnsen, Andrew M. Watkins, David Baker, Vikram Khipple Mulligan, Peta J. Harvey, Richard Bonneau, Thomas Szyperski, Gaurav Bhardwaj, Garry W. Buchko, Evangelos A. Coutsias, James M. Olson, Stephen A. Rettie, Yifan Song, Alexander Eletsky
Publikováno v:
Nature
Naturally occurring, pharmacologically active peptides constrained with covalent crosslinks generally have shapes that have evolved to fit precisely into binding pockets on their targets. Such peptides can have excellent pharmaceutical properties, co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf8778c9d2a01f5c0c9930bd5485921c
https://doi.org/10.1038/nature19791
https://doi.org/10.1038/nature19791
Autor:
Timothy M. Jacobs, J. F. Federizon, Benfeard Williams, X. Xu, Tishan Williams, Thomas Szyperski, Alexander Eletsky, Brian Kuhlman
Publikováno v:
Science. 352:687-690
Building new proteins from the old Proteins are the workhorses of biology. Designing new, stable proteins with functions desirable in biotechnology or biomedicine remains challenging. Jacobs et al. developed a computational method called SEWING that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e2cb0606ea44ea2c8745e3fd835749e
https://doi.org/10.1126/science.aad8036
https://doi.org/10.1126/science.aad8036
Autor:
Alexander Eletsky, Robert S. Haltiwanger, Atsuko Ito, Steven J. Berardinelli, Rajashri Manjunath
Publikováno v:
The FASEB Journal. 34:1-1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04d8809ee67dbd3029a77135078ca5e0
https://doi.org/10.1096/fasebj.2020.34.s1.05437
https://doi.org/10.1096/fasebj.2020.34.s1.05437