Zobrazeno 1 - 10
of 375
pro vyhledávání: '"Paul M Thomas"'
Autor:
Tatsiana Kosciuk, Ian R. Price, Xiaoyu Zhang, Chengliang Zhu, Kayla N. Johnson, Shuai Zhang, Steve L. Halaby, Garrison P. Komaniecki, Min Yang, Caroline J. DeHart, Paul M. Thomas, Neil L. Kelleher, J. Christopher Fromme, Hening Lin
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
Lysine fatty acylation is an important protein posttranslational modification but mammalian lysine fatty acyl transferases have remained unknown so far. Here the authors report that the human N-terminal glycine myristoyltransferases 1 and 2 catalyze
Externí odkaz:
https://doaj.org/article/2680a250e1e54ba7aecb1d6f4993fea7
Autor:
Benjamin Winer, Kimberly A. Edgel, Xiaoyan Zou, Julie Sellau, Sri Hadiwidjojo, Lindsey S. Garver, Christin E. McDonough, Neil L. Kelleher, Paul M. Thomas, Eileen Villasante, Alexander Ploss, Vincent R. Gerbasi
Publikováno v:
Malaria Journal, Vol 19, Iss 1, Pp 1-13 (2020)
Abstract Background Immunization with attenuated malaria sporozoites protects humans from experimental malaria challenge by mosquito bite. Protection in humans is strongly correlated with the production of T cells targeting a heterogeneous population
Externí odkaz:
https://doaj.org/article/54c91dfe7578497593d4de236d8ff4f4
Autor:
Soo Y. Ro, Luis F. Schachner, Christopher W. Koo, Rahul Purohit, Jonathan P. Remis, Grace E. Kenney, Brandon W. Liauw, Paul M. Thomas, Steven M. Patrie, Neil L. Kelleher, Amy C. Rosenzweig
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
The activity of the membrane-bound enzyme pMMO depends on copper but the location of the copper centers is still under debate. Here, the authors reconstitute pMMO in nanodiscs and use native top-down MS to localize its copper centers, providing insig
Externí odkaz:
https://doaj.org/article/7bb55c7a2850428c843bfecc0230d63e
Autor:
Simon Lax, Cesar Cardona, Dan Zhao, Valerie J. Winton, Gabriel Goodney, Peng Gao, Neil Gottel, Erica M. Hartmann, Chris Henry, Paul M. Thomas, Scott T. Kelley, Brent Stephens, Jack A. Gilbert
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Microbes inhabit built environments and could contribute to degradation of surfaces especially in damp conditions. Here the authors explore how communities of microbes and their metabolites affect four types of built surfaces under varying environmen
Externí odkaz:
https://doaj.org/article/82f881fbb39f48b1b3c155644d7c587c
Autor:
Ashley N. Ives, Henry A. Dunn, Hamid Samareh Afsari, Henrique dos Santos Seckler, Max J. Foroutan, Erica Chavez, Rafael D. Melani, Ryan T. Fellers, Richard D. LeDuc, Paul M. Thomas, Kirill A. Martemyanov, Neil L. Kelleher, Reza Vafabakhsh
Publikováno v:
Journal of the American Chemical Society. 144(50)
G protein-coupled receptors (GPCRs) are the largest family of membrane receptors in humans. They mediate nearly all aspects of human physiology and thus are of high therapeutic interest. GPCR signaling is regulated in space and time by receptor phosp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfb9ecbb39e54343f7eba929c23b7e8c
https://pubmed.ncbi.nlm.nih.gov/36475650
https://pubmed.ncbi.nlm.nih.gov/36475650
Autor:
Lindsay K. Caesar, Matthew T. Robey, Michael Swyers, Md N. Islam, Rosa Ye, Purav P. Vagadia, Gary E. Schiltz, Paul M. Thomas, Chengcang C. Wu, Neil L. Kelleher, Nancy P. Keller, Jin Woo Bok
Publikováno v:
mBio, Vol 11, Iss 4 (2020)
ABSTRACT Advances in genome sequencing have revitalized natural product discovery efforts, revealing the untapped biosynthetic potential of fungi. While the volume of genomic data continues to expand, discovery efforts are slowed due to the time-cons
Externí odkaz:
https://doaj.org/article/0c3cdc60038744a98df4944edd8388aa
Autor:
Nebiyu A Abshiru, Jacek W Sikora, Jeannie M Camarillo, Juliette A Morris, Philip D Compton, Tak Lee, Yaseswini Neelamraju, Samuel Haddox, Caroline Sheridan, Martin Carroll, Larry D Cripe, Martin S Tallman, Elisabeth M Paietta, Ari M Melnick, Paul M Thomas, Francine E Garrett-Bakelman, Neil L Kelleher
Publikováno v:
PLoS ONE, Vol 15, Iss 10, p e0240829 (2020)
Histone post-translational modifications (PTMs) create a powerful regulatory mechanism for maintaining chromosomal integrity in cells. Histone acetylation and methylation, the most widely studied histone PTMs, act in concert with chromatin-associated
Externí odkaz:
https://doaj.org/article/9fa008740c854e4ca5435d953e809e65
Autor:
Oriana S. Fisher, Grace E. Kenney, Matthew O. Ross, Soo Y. Ro, Betelehem E. Lemma, Sharon Batelu, Paul M. Thomas, Victoria C. Sosnowski, Caroline J. DeHart, Neil L. Kelleher, Timothy L. Stemmler, Brian M. Hoffman, Amy C. Rosenzweig
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Methane- and ammonia-oxidizing bacteria use the integral membrane, copper-dependent enzymes particulate methane monooxygenase (pMMO) and ammonia monooxygenase (AMO) to oxidize methane and ammonia. Here the authors structurally characterize the copper
Externí odkaz:
https://doaj.org/article/743d3e50befe40f495dd9e6768ae3eb0
Autor:
Rey W. Martin, Benjamin J. Des Soye, Yong-Chan Kwon, Jennifer Kay, Roderick G. Davis, Paul M. Thomas, Natalia I. Majewska, Cindy X. Chen, Ryan D. Marcum, Mary Grace Weiss, Ashleigh E. Stoddart, Miriam Amiram, Arnaz K. Ranji Charna, Jaymin R. Patel, Farren J. Isaacs, Neil L. Kelleher, Seok Hoon Hong, Michael C. Jewett
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Cell-free protein synthesis allows for producing proteins without the need of a host organism, thus sparing the researcher experimental hassle. Here, the authors developed a cell-free synthesis method that enables incorporating non-standard amino aci
Externí odkaz:
https://doaj.org/article/48f02766cbcf45fab8fa2795bb729a58
Autor:
Rafael D. Melani, Vincent R. Gerbasi, Lissa C. Anderson, Jacek W. Sikora, Timothy K. Toby, Josiah E. Hutton, David S. Butcher, Fernanda Negrão, Henrique S. Seckler, Kristina Srzentić, Luca Fornelli, Jeannie M. Camarillo, Richard D. LeDuc, Anthony J. Cesnik, Emma Lundberg, Joseph B. Greer, Ryan T. Fellers, Matthew T. Robey, Caroline J. DeHart, Eleonora Forte, Christopher L. Hendrickson, Susan E. Abbatiello, Paul M. Thomas, Andy I. Kokaji, Josh Levitsky, Neil L. Kelleher
Publikováno v:
Science
Human biology is tightly linked to proteins, yet most measurements do not precisely determine alternatively spliced sequences or posttranslational modifications. Here, we present the primary structures of ~30,000 unique proteoforms, nearly 10 times m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ada067d85328d35da642f74ca2b072c
https://doi.org/10.1126/science.aaz5284
https://doi.org/10.1126/science.aaz5284