Zobrazeno 1 - 10
of 287
pro vyhledávání: '"L, Kear"'
Autor:
Nicholas Chia, Jessica J. Saw, John C. Lieske, Matthew W. Curtis, James C. Williams, Elena M. Wilson, Mayandi Sivaguru, Bruce W. Fouke, Michael F. Romero, Jamie L. Kear-Scott, Amy E. Krambeck, Kyle W. Fouke
Publikováno v:
Nature Reviews Urology. 18:404-432
GeoBioMed — a new transdisciplinary approach that integrates the fields of geology, biology and medicine — reveals that kidney stones composed of calcium-rich minerals precipitate from a continuum of repeated events of crystallization, dissolutio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e026994f2edb56b9e571fa2febfd529f
https://doi.org/10.1038/s41585-021-00469-x
https://doi.org/10.1038/s41585-021-00469-x
Autor:
Mayandi, Sivaguru, Jessica J, Saw, Elena M, Wilson, John C, Lieske, Amy E, Krambeck, James C, Williams, Michael F, Romero, Kyle W, Fouke, Matthew W, Curtis, Jamie L, Kear-Scott, Nicholas, Chia, Bruce W, Fouke
Publikováno v:
Nature reviews. Urology. 18(7)
GeoBioMed - a new transdisciplinary approach that integrates the fields of geology, biology and medicine - reveals that kidney stones composed of calcium-rich minerals precipitate from a continuum of repeated events of crystallization, dissolution an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ca0806e498d3334991a835b75b8c102f
https://pubmed.ncbi.nlm.nih.gov/34031587
https://pubmed.ncbi.nlm.nih.gov/34031587
Autor:
Jamie L. Kear-Scott, Gail E. Fanucci, Angelo M. Veloro, Luis Galiano, Mandy E. Blackburn, Xi Huang, Zhanglong Liu, Linh Pham, Ian Mitchelle S. de Vera, Thomas M. Casey, Jeffrey D. Carter
Publikováno v:
Physical Chemistry Chemical Physics. 18:5819-5831
The conformational landscape of HIV-1 protease (PR) can be experimentally characterized by pulsed-EPR double electron-electron resonance (DEER). For this characterization, nitroxide spin labels are attached to an engineered cysteine residue in the fl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7bddb8d60797e52936147371f26634e
https://doi.org/10.1039/c5cp04556h
https://doi.org/10.1039/c5cp04556h
Autor:
Jamie L. Kear-Scott, D. Allan Drummond, Alexandra E Rojek, Edoardo M. Airoldi, Evgeny V. Pilipenko, Tao Pan, Michael F. Dion, Bogdan Budnik, Alexander Franks, Joshua A. Riback, Pawel R. Laskowski, Michael H. Schwartz, Edward W. J. Wallace, Christopher D. Katanski
Publikováno v:
Cell, vol 162, iss 6
SummaryHeat causes protein misfolding and aggregation and, in eukaryotic cells, triggers aggregation of proteins and RNA into stress granules. We have carried out extensive proteomic studies to quantify heat-triggered aggregation and subsequent disag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c784466c883714316def0e831ac407f
https://doi.org/10.1016/j.cell.2015.08.041
https://doi.org/10.1016/j.cell.2015.08.041
Autor:
Carlos Simmerling, Xi Huang, Gail E. Fanucci, Ben M. Dunn, Jamie L. Kear-Scott, Manuel D. Britto, Robert McKenna, Michael Bieri, Christopher D. Boone, Paul R. Gooley, James R. Rocca
Publikováno v:
Journal of Biological Chemistry. 289:17203-17214
HIV-1 protease is an essential enzyme for viral particle maturation and is a target in the fight against HIV-1 infection worldwide. Several natural polymorphisms are also associated with drug resistance. Here, we utilized both pulsed electron double
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8238e61b0185bc85730123f3e5622d5
https://doi.org/10.1074/jbc.m114.571836
https://doi.org/10.1074/jbc.m114.571836
Publikováno v:
Journal of Biophysical Chemistry. :137-146
Site-directed spin-labeling with continuous wave electron paramagnetic resonance spectroscopy was used to monitor autoproteolysis of HIV-1 protease, an enzyme essential for viral maturation. Two protein constructs were examined, namely subtype F and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9996f27e7b3ef2610b07ff768a04225
https://doi.org/10.4236/jbpc.2011.22017
https://doi.org/10.4236/jbpc.2011.22017
Autor:
Song, Yun1 (AUTHOR), Wang, Yaru1 (AUTHOR), Zhang, Huafang2 (AUTHOR), Saddique, Muhammad Abu Bakar2 (AUTHOR), Luo, Xiumei2 (AUTHOR), Ren, Maozhi2 (AUTHOR) renmaozhi01@caas.cn
Publikováno v:
Molecular Plant Pathology. Nov2024, Vol. 25 Issue 11, p1-19. 19p.
Publikováno v:
Analytica Chimica Acta. 478:245-258
Real-time measurement of total oil concentration in complex samples is required in wastewater discharge streams from ships and processing industries. A novel technology has been developed for the accurate quantification of a variety of single oils an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::39d10c44afaf0c6455069fd6f378bc71
https://doi.org/10.1016/s0003-2670(02)01471-x
https://doi.org/10.1016/s0003-2670(02)01471-x
Autor:
D. Allan Drummond, Tobin R. Sosnick, Jamie L. Kear-Scott, Alexandra E Rojek, Evgeny V. Pilipenko, Christopher D. Katanski, Joshua A. Riback
Publikováno v:
Cell. 168:1028-1040.e19
In eukaryotic cells, diverse stresses trigger coalescence of RNA-binding proteins into stress granules. In vitro, stress-granule-associated proteins can demix to form liquids, hydrogels, and other assemblies lacking fixed stoichiometry. Observing the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ceee2b01c7ea05ac44e27308f54dec2
https://doi.org/10.1016/j.cell.2017.02.027
https://doi.org/10.1016/j.cell.2017.02.027
Autor:
Joshua A. Riback, Jamie L. Kear-Scott, Tobin R. Sosnick, Evgeny V. Pilipenko, D. Allan Drummond, Christopher A. Katanski
Publikováno v:
Biophysical Journal. 112:5a
In eukaryotic cells, a variety of stresses trigger the coalescence of RNA-binding proteins into stress granules. In vitro, stress-granule-associated proteins can demix to form liquids, hydrogels, and other assemblies lacking fixed stoichiometry. Obse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a061493acdfeeaad723d64627672a12
https://doi.org/10.1016/j.bpj.2016.11.047
https://doi.org/10.1016/j.bpj.2016.11.047