Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Jeremy J Wolff"'
SITE-SPECIFIC LABELING OF A PROTEIN LYSINE RESIDUE BY NOVEL KINETIC LABELING COMBINATORIAL LIBRARIES
Autor:
Allen Krantz, Arthur M Hanel, Ivona Strug, Andrzej Wilczynski, Jeremy J Wolff, Wolin Huang, Linda H Huang, Tina Settineri, Darren L Holmes, Margaret C Hardy, Dominique P Bridon
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 9, Iss 15 (2014)
The first example of a kinetic labeling library designed to enable the discovery of affinity labels is presented. Each library component (1) consists of a variable peptidyl component linked to a biotinyl moiety by a 4-mercaptobenzoyl linker in thioes
Externí odkaz:
https://doaj.org/article/b5781b56027b45358e4cbb98b9eca02e
Autor:
Yuchang Li, Liting Chen, Lu Li, Chantal Sottas, Stephanie K. Petrillo, Anthoula Lazaris, Peter Metrakos, Hangyu Wu, Yuji Ishida, Takeshi Saito, Lucy Golden-Mason, Hugo R. Rosen, Jeremy J. Wolff, Cristina I. Silvescu, Samuel Garza, Garett Cheung, Tiffany Huang, Jinjiang Fan, Martine Culty, Bangyan Stiles, Kinji Asahina, Vassilios Papadopoulos
Publikováno v:
iScience, Vol 24, Iss 5, Pp 102457- (2021)
Summary: Translocator protein (TSPO, 18 kDa) levels increase in parallel with the evolution of simple steatosis (SS) to nonalcoholic steatohepatitis (NASH) in nonalcoholic fatty liver disease (NAFLD). However, TSPO function in SS and NASH is unknown.
Externí odkaz:
https://doaj.org/article/d8dec988be0e41ee9ce7256bef9886c1
Autor:
Guozhang Zou, Vera B. Ivleva, Jeremy J. Wolff, Rong Sylvie Yang, Casper Alabanza, Nathan Barefoot, Cindy Cai, Yanhong Yang, Daniel B. Gowetski, Jason G. Gall, Q. Paula Lei
Publikováno v:
Journal of the American Society for Mass Spectrometry. 34:813-819
Autor:
Lin Wang, Xi Xing, Xianfeng Zeng, S. RaElle Jackson, Tara TeSlaa, Osama Al-Dalahmah, Laith Z. Samarah, Katharine Goodwin, Lifeng Yang, Melanie R. McReynolds, Xiaoxuan Li, Jeremy J. Wolff, Joshua D. Rabinowitz, Shawn M. Davidson
Publikováno v:
Nature Methods. 19:223-230
Autor:
Jeremy J. Wolff, Joseph A. Loo, Piriya Wongkongkathep, Iain Campuzano, Huilin Li, Michael Nshanian, Chawita Netirojjanakul, Carter Lantz, Chris Spahr
Publikováno v:
J Am Soc Mass Spectrom
Journal of the American Society for Mass Spectrometry, vol 31, iss 5
Journal of the American Society for Mass Spectrometry, vol 31, iss 5
Analysis of proteins and complexes under native mass spectrometric (MS) and solution conditions was typically performed using the time-of-flight analyzers, due to their routine high m/z transmission and detection capabilities. However, over recent ye
Autor:
Sara Forcisi, Franco Moritz, Christopher J. Thompson, Basem Kanawati, Jenny Uhl, Carlos Afonso, Chantal D. Bader, Aiko Barsch, Berin A. Boughton, Rosalie K. Chu, Justine Ferey, Francisco Fernandez-Lima, Céline Guéguen, Dimitri Heintz, Mario Gomez-Hernandez, Kyoung-Soon Jang, Nikolas Kessler, Vaughn Mangal, Rolf Müller, Ryo Nakabayashi, Edith Nicol, Simone Nicolardi, Magnus Palmblad, Ljiljana Paša-Tolić, Jacob Porter, Isabelle Schmitz-Afonso, Jong Bok Seo, Eduardo Sommella, Yuri E. M. van der Burgt, Claire Villette, Matthias Witt, Ashley Wittrig, Jeremy J. Wolff, Michael L. Easterling, Frank H. Laukien, Philippe Schmitt-Kopplin
Publikováno v:
J. Am. Soc. Mass Spectrom. 33, 2203–2214 (2022)
Journal of The American Society for Mass Spectrometry, 33(12), 2203-2214. AMER CHEMICAL SOC
Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, 2022, 33 (12), pp.2203-2214. ⟨10.1021/jasms.2c00082⟩
Journal of The American Society for Mass Spectrometry, 33(12), 2203-2214. AMER CHEMICAL SOC
Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, 2022, 33 (12), pp.2203-2214. ⟨10.1021/jasms.2c00082⟩
International audience; Ultrahigh resolution mass spectrometry (UHR-MS) coupled with direct infusion (DI) electrospray ionization offers a fast solution for accurate untargeted profiling. Fourier transform ion cyclotron resonance (FT-ICR) mass spectr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54d6a8f864314d5f2f165ea13bb494dd
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=66674
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=66674
Autor:
Lin, Wang, Xi, Xing, Xianfeng, Zeng, S RaElle, Jackson, Tara, TeSlaa, Osama, Al-Dalahmah, Laith Z, Samarah, Katharine, Goodwin, Lifeng, Yang, Melanie R, McReynolds, Xiaoxuan, Li, Jeremy J, Wolff, Joshua D, Rabinowitz, Shawn M, Davidson
Publikováno v:
Nature methods. 19(2)
Isotope tracing has helped to determine the metabolic activities of organs. Methods to probe metabolic heterogeneity within organs are less developed. We couple stable-isotope-labeled nutrient infusion to matrix-assisted laser desorption ionization i
Autor:
Tiffany Huang, Jinjiang Fan, Martine Culty, Bangyan L. Stiles, Peter Metrakos, Hanguy Wu, Chantal M. Sottas, Anthoula Lazaris, Liting Chen, Garett Cheung, Vassilios Papadopoulos, Lu Li, Christina Silvescu, Kinji Asahina, Jeremy J. Wolff, Stephanie Petrillo, Samuel Garza, Yuchang Li
Publikováno v:
SSRN Electronic Journal.
Translocator protein (TSPO, 18kDa) levels increase in parallel with the evolution of simple steatosis (SS) to nonalcoholic steatohepatitis (NASH) in non-alcoholic fatty liver disease (NAFLD). However, TSPO function in SS and NASH is unknown. Loss of
Autor:
Jonna Frasor, Jeremy J. Wolff, Brian P. David, Thomas E. Speltz, Laura M. Sanchez, Terry W. Moore, Oleksii Dubrovskyi
Publikováno v:
ACS medicinal chemistry letters, vol 9, iss 7
[Image: see text] Matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) imaging mass spectrometry has emerged as a powerful, label-free technique to visualize penetration of small molecules in vivo and in vitro, including in 3D cell
Autor:
Richa Sarin, Antonius Koller, Ziqing Lin, Luis F. Schachner, Wonhyeuk Jung, Lloyd M. Smith, Ljiljana Paša-Tolić, Julia Chamot-Rooke, Alexander R. Ivanov, Iain D. G. Campuzano, Carter Lantz, Ying Ge, Caroline J. DeHart, Julian P. Whitelegge, Jennifer L. Lippens, Kendall Johnson, Krishna Aluri, Catherine M. Rawlins, Yury O. Tsybin, Neil L. Kelleher, Jeffrey N. Agar, Paul O. Danis, Daniel P. Donnelly, Jared R. Auclair, Jeremy J. Wolff, Joseph A. Loo, Luca Fornelli, Bifan Chen
Publikováno v:
Nature methods, vol 16, iss 7
Nature Methods
Nature Methods, Nature Publishing Group, 2019, 16 (7), pp.587-594. ⟨10.1038/s41592-019-0457-0⟩
Nature Methods, 2019, 16 (7), pp.587-594. ⟨10.1038/s41592-019-0457-0⟩
Nature Methods
Nature Methods, Nature Publishing Group, 2019, 16 (7), pp.587-594. ⟨10.1038/s41592-019-0457-0⟩
Nature Methods, 2019, 16 (7), pp.587-594. ⟨10.1038/s41592-019-0457-0⟩
One gene can give rise to many functionally distinct proteoforms, each of which has a characteristic molecular mass. Top-down mass spectrometry enables the analysis of intact proteins and proteoforms. Here members of the Consortium for Top-Down Prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f4d2ff753f4535711f739a1916ff31f
https://escholarship.org/uc/item/72c7s81j
https://escholarship.org/uc/item/72c7s81j