Zobrazeno 1 - 10
of 33
pro vyhledávání: '"James J, Pesavento"'
Autor:
James J. Pesavento, James G. Umen, Henna Shaghasi, Mowei Zhou, Bradley S. Evans, Sarah R Rommelfanger, Shin-Cheng Tzeng, Ljiljana Paša-Tolić
Publikováno v:
Journal of the American Society for Mass Spectrometry. 32:1671-1688
We present an updated analysis of the linker and core histone proteins and their proteoforms in the green microalga Chlamydomonas reinhardtii by top-down mass spectrometry (TDMS). The combination of high-resolution liquid chromatographic separation,
Autor:
Alessandro Costa, Ludovic Renault, Paolo Swuec, Tatjana Petojevic, James J Pesavento, Ivar Ilves, Kirsty MacLellan-Gibson, Roland A Fleck, Michael R Botchan, James M Berger
Publikováno v:
eLife, Vol 3 (2014)
The Cdc45/Mcm2-7/GINS (CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains unclear. Using electron microscopy, we have determined the structure of the CMG in the presence o
Externí odkaz:
https://doaj.org/article/1c9a75ab3cf549beafe69c123e444555
Autor:
Sarah R, Rommelfanger, Mowei, Zhou, Henna, Shaghasi, Shin-Cheng, Tzeng, Bradley S, Evans, Ljiljana, Paša-Tolić, James G, Umen, James J, Pesavento
Publikováno v:
Journal of the American Society for Mass Spectrometry. 32(7)
We present an updated analysis of the linker and core histone proteins and their proteoforms in the green microalga
Publikováno v:
Methods (San Diego, Calif.). 184
The development of universal, broadly applicable methods for histone extraction from animal cells and tissues has unlocked the ability to compare these epigenetic-influencing proteins across tissue types, healthy and diseased states, and cancerous ve
Autor:
Michael C. Jewett, Therese Wohlschlager, Vamsi K. Mootha, Jeremy Gunawardena, Steven M. Patrie, James J. Pesavento, Nicolas L. Young, Ole N. Jensen, Catherine Fenselau, Jeffrey N. Agar, Laura L. Kiessling, Sarah A. Slavoff, Evan R. Williams, Sharon J. Pitteri, Emma Lundberg, Lloyd M. Smith, Ruedi Aebersold, Alan Saghatelian, Salvatore Sechi, Marc Vidal, Nathan A. Yates, Tom W. Muir, Michael J. MacCoss, David R. Walt, Parag Mallick, Henry Rodriguez, Jennifer E. Van Eyk, Michael Snyder, Joseph A. Loo, Vicki H. Wysocki, Hartmut Schlüter, Bing Zhang, Milan Mrksich, Benjamin A. Garcia, Martin R. Larsen, Alexander R. Ivanov, Mark S. Baker, Ying Ge, Nevan J. Krogan, Catherine E. Costello, Paul J. Hergenrother, Neil L. Kelleher, I. Jonathan Amster, Rachel R. Ogorzalek Loo, Emily S. Boja, Mathias Uhlén, Benjamin F. Cravatt, Ronald C. Hendrickson, Wendy Sandoval, Paul M. Thomas, Christian G. Huber, Forest M. White, Carolyn R. Bertozzi
Publikováno v:
Nature chemical biology, vol 14, iss 3
Aebersold, R, Agar, J N, Amster, I J, Baker, M S, Bertozzi, C R, Boja, E S, Costello, C E, Cravatt, B F, Fenselau, C, Garcia, B A, Ge, Y, Gunawardena, J, Hendrickson, R C, Hergenrother, P J, Huber, C G, Ivanov, A R, Jensen, O N, Jewett, M C, Kelleher, N L, Kiessling, L L, Krogan, N J, Larsen, M R, Loo, J A, Ogorzalek Loo, R R, Lundberg, E, MacCoss, M J, Mallick, P, Mootha, V K, Mrksich, M, Muir, T W, Patrie, S M, Pesavento, J J, Pitteri, S J, Rodriguez, H, Saghatelian, A, Sandoval, W, Schlüter, H, Sechi, S, Slavoff, S A, Smith, L M, Snyder, M P, Thomas, P M, Uhlén, M, Van Eyk, J E, Vidal, M, Walt, D R, White, F M, Williams, E R, Wohlschlager, T, Wysocki, V H, Yates, N A, Young, N L & Zhang, B 2018, ' How many human proteoforms are there? ', Nature Chemical Biology, vol. 14, no. 3, pp. 206-214 . https://doi.org/10.1038/nchembio.2576
PMC
Aebersold, R, Agar, J N, Amster, I J, Baker, M S, Bertozzi, C R, Boja, E S, Costello, C E, Cravatt, B F, Fenselau, C, Garcia, B A, Ge, Y, Gunawardena, J, Hendrickson, R C, Hergenrother, P J, Huber, C G, Ivanov, A R, Jensen, O N, Jewett, M C, Kelleher, N L, Kiessling, L L, Krogan, N J, Larsen, M R, Loo, J A, Ogorzalek Loo, R R, Lundberg, E, MacCoss, M J, Mallick, P, Mootha, V K, Mrksich, M, Muir, T W, Patrie, S M, Pesavento, J J, Pitteri, S J, Rodriguez, H, Saghatelian, A, Sandoval, W, Schlüter, H, Sechi, S, Slavoff, S A, Smith, L M, Snyder, M P, Thomas, P M, Uhlén, M, Van Eyk, J E, Vidal, M, Walt, D R, White, F M, Williams, E R, Wohlschlager, T, Wysocki, V H, Yates, N A, Young, N L & Zhang, B 2018, ' How many human proteoforms are there? ', Nature Chemical Biology, vol. 14, no. 3, pp. 206-214 . https://doi.org/10.1038/nchembio.2576
PMC
Despite decades of accumulated knowledge about proteins and their post-translational modifications (PTMs), numerous questions remain regarding their molecular composition and biological function. One of the most fundamental queries is the extent to w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::112005919432b51c4f87047a1ed9bdfa
https://escholarship.org/uc/item/1r85h1h0
https://escholarship.org/uc/item/1r85h1h0
Publikováno v:
Journal of proteome research. 17(1)
The unicellular microalga Chlamydomonas reinhardtii has played an instrumental role in the development of many new fields (bioproducts, biofuels, etc.) as well as the advancement of basic science (photosynthetic apparati, flagellar function, etc.). C
Publikováno v:
Molecular Cell. 37:247-258
MCM2-7 proteins provide essential helicase functions in eukaryotes at chromosomal DNA replication forks. During the G1 phase of the cell cycle, they remain loaded on DNA but are inactive. We have used recombinant methods to show that the Drosophila M
Publikováno v:
Journal of Biological Chemistry. 283:14927-14937
Quantitative proteomics has focused heavily on correlating protein abundances, ratios, and dynamics by developing methods that are protein expression-centric (e.g. isotope coded affinity tag, isobaric tag for relative and absolute quantification, etc
Publikováno v:
Analytical Chemistry. 80:2499-2505
Recent advances in mass spectrometry instrumentation, such as FTICR and OrbiTrap, have made it possible to generate high-resolution spectra of entire proteins. While these methods offer new opportunities for performing "top-down" studies of proteins,
Publikováno v:
Molecular & Cellular Proteomics. 6:1510-1526
Recent developments in top down mass spectrometry have enabled closely related histone variants and their modified forms to be identified and quantitated with unprecedented precision, facilitating efforts to better understand how histones contribute