Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Sylvester M. Greer"'
Autor:
Jake T. Kline, Michael W. Belford, Jingjing Huang, Joseph B. Greer, David Bergen, Ryan T. Fellers, Sylvester M. Greer, David M. Horn, Vlad Zabrouskov, Romain Huguet, Cornelia L. Boeser, Kenneth R. Durbin, Luca Fornelli
The high-throughput quantification of intact proteoforms using a label-free approach is typically performed on proteins in the 0-30 kDa mass range extracted from whole cell or tissue lysates. Unfortunately, even when high-resolution separation of pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::675ef2afbcf9d01663649adf88f75c8b
https://doi.org/10.26434/chemrxiv-2023-2gkr3
https://doi.org/10.26434/chemrxiv-2023-2gkr3
Autor:
Chinh Q. Ngo, Emily L. Que, Sylvester M. Greer, Inês C. Santos, Radhika Mehta, Audrey G. Fikes, Kanchan Aggarwal
Publikováno v:
ChemBioChem. 20:1003-1007
One-third of all proteins are estimated to require metals for structural stability and/or catalytic activity. Desthiobiotin probes containing metal binding groups can be used to capture metalloproteins with exposed active-site metals under mild condi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a3c5bc6f205581424d9f29595b54c3c
https://doi.org/10.1002/cbic.201800613
https://doi.org/10.1002/cbic.201800613
Autor:
Sam Hughes, Nicolas L. Young, David Clarke, Frank Sobott, Anja Resemann, Kristina Srzentić, Kim F. Haselmann, Detlev Suckau, Dina L. Bai, Young Ah Goo, Christian Malosse, Mathieu Dupré, Sylvester M. Greer, Neil R. Quebbemann, Ziqing Lin, Jared B. Shaw, Alain Beck, Yury O. Tsybin, Stuart Pengelley, Timothy K. Toby, Lidong He, Paul O. Danis, Henrique S. Seckler, Robert Anthony D’Ippolito, Natalia Gasilova, Jeffrey N. Agar, Donald F. Hunt, Jennifer S. Brodbelt, Matthew V. Holt, Simone Nicolardi, Joseph A. Loo, Yuri E. M. van der Burgt, Nicholas D. Schmitt, Laure Menin, Robert J. Millikin, Ljiljana Paša-Tolić, David R. Goodlett, Mowei Zhou, Joshua D. Hinkle, Michael R. Shortreed, Christopher L. Hendrickson, Wendy Sandoval, Richa Sarin, Jeffrey Shabanowitz, Alan G. Marshall, Anton N. Kozhinov, Neil L. Kelleher, Chad R. Weisbrod, Lissa C. Anderson, Julia Chamot-Rooke, Yunqiu Chen, John R. Yates, Luca Fornelli, Konstantin O. Nagornov, Lloyd M. Smith, Sneha Chatterjee, Ying Ge, Sung Hwan Yoon, Jolene K. Diedrich, Norelle C. Wildburger
Publikováno v:
Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2020, 31 (9), pp.1783-1802. ⟨10.1021/jasms.0c00036⟩
Journal of the American Society for Mass Spectrometry
Journal of the American Society for Mass Spectrometry, vol 31, iss 9
Journal of The American Society for Mass Spectrometry, 31(9), 1783-1802. AMER CHEMICAL SOC
J Am Soc Mass Spectrom
Journal of The American Society for Mass Spectrometry, 2020, 31 (9), pp.1783-1802. ⟨10.1021/jasms.0c00036⟩
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2020, 31 (9), pp.1783-1802. ⟨10.1021/jasms.0c00036⟩
Journal of the American Society for Mass Spectrometry
Journal of the American Society for Mass Spectrometry, vol 31, iss 9
Journal of The American Society for Mass Spectrometry, 31(9), 1783-1802. AMER CHEMICAL SOC
J Am Soc Mass Spectrom
Journal of The American Society for Mass Spectrometry, 2020, 31 (9), pp.1783-1802. ⟨10.1021/jasms.0c00036⟩
International audience; The Consortium for Top-Down Proteomics (www.topdownproteomics.org) launched the present study to assess the current state of top-down mass spectrometry (TD MS) and middle-down mass spectrometry (MD MS) for characterizing monoc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce93ac618ef03bef2381fe00d09bf9cf
https://hdl.handle.net/1887/3182316
https://hdl.handle.net/1887/3182316
Publikováno v:
Journal of Proteome Research. 17:1340-1347
To extend proteome coverage obtained from bottom-up mass spectrometry approaches, three complementary ion activation methods, higher energy collision dissociation (HCD), ultraviolet photodissociation (UVPD), and negative mode UVPD (NUVPD), are used t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e940fdccfab89bbf68045f65645c3f70
https://doi.org/10.1021/acs.jproteome.7b00673
https://doi.org/10.1021/acs.jproteome.7b00673
Publikováno v:
Analytical Chemistry. 89:11772-11778
The most popular bottom-up proteomics workflow uses trypsin to enzymatically cleave proteins C-terminal to lysine and arginine residues prior to LCMS/MS analysis of the resulting peptides. The high frequency of these residues generates short peptides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2027e12fe3e46df1c5ceda10d98efb67
https://doi.org/10.1021/acs.analchem.7b03396
https://doi.org/10.1021/acs.analchem.7b03396
Publikováno v:
Journal of the American Chemical Society. 139:15681-15690
Complete structural characterization of complex lipids, such as glycerophospholipids, by tandem mass spectrometry (MS/MS) continues to present a major challenge. Conventional activation methods do not generate fragmentation patterns that permit the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::faabcc6c2ebacf70d5050f3fb1ddc62b
https://doi.org/10.1021/jacs.7b06416
https://doi.org/10.1021/jacs.7b06416
Autor:
Sylvester M. Greer, Ole N. Jensen, Mariel Coradin, Veit Schwämmle, Malena Schack Jespersen, Benjamin A. Garcia, Jennifer S. Brodbelt, Simone Sidoli
Publikováno v:
Greer, S M, Sidoli, S, Coradin, M, Schack Jespersen, M, Schwämmle, V, Jensen, O N, Garcia, B A & Brodbelt, J S 2018, ' Extensive Characterization of Heavily Modified Histone Tails by 193 nm Ultraviolet Photodissociation Mass Spectrometry via a Middle-Down Strategy ', Analytical Chemistry, vol. 90, no. 17, pp. 10425–10433 . https://doi.org/10.1021/acs.analchem.8b02320
The ability to map combinatorial patterns of post-translational modifications (PTMs) of proteins remains challenging for traditional bottom-up mass spectrometry workflows. There are also hurdles associated with top-down approaches related to limited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8a65f67495dd6cb56e228ae35e11d88
https://findresearcher.sdu.dk:8443/ws/files/143485645/E_YFBUO2.PDF
https://findresearcher.sdu.dk:8443/ws/files/143485645/E_YFBUO2.PDF
Autor:
Shanzhong Gong, Sylvester M. Greer, Meredith K Purchal, Radhika Mehta, Emily L. Que, Chinh Q. Ngo, Munaum H Qureshi
Publikováno v:
Chemical communications (Cambridge, England). 54(43)
We report the synthesis and application of a small molecule probe for carbonic anhydrase (CA) to track holo-CA in cell lysates and live-cell models of zinc dyshomeostasis. The probe displays a 12-fold increase in fluorescence upon binding to bovine C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3feb00626abab3f3471a8ebaa8b02c9
https://pubmed.ncbi.nlm.nih.gov/29745391
https://pubmed.ncbi.nlm.nih.gov/29745391
Publikováno v:
Journal of proteome research. 17(3)
The characterization of protein post-translational modifications (PTMs) remains a significant challenge for traditional bottom-up proteomics methods owing to the lability of PTMs and the difficulty of mapping combinatorial patterns of PTMs based on a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79fef1667ffed71b3a03166063f92a64
https://pubmed.ncbi.nlm.nih.gov/29343059
https://pubmed.ncbi.nlm.nih.gov/29343059
Publikováno v:
Journal of Proteome Research. 14:2626-2632
Recent mass spectrometric studies have reported enhanced proteome coverage by employing multiple proteases or by using multiple or alternative activation methods such as electron-transfer dissociation in combination with collisional-activated dissoci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6bb1ba617f89553cf928742a559fbcf
https://doi.org/10.1021/acs.jproteome.5b00165
https://doi.org/10.1021/acs.jproteome.5b00165