Zobrazeno 1 - 10
of 19
pro vyhledávání: '"John A. Buglino"'
Autor:
Samantha J. Nelson, John T. Williams, John A. Buglino, Subhalaxmi Nambi, Lisa J. Lojek, Michael S. Glickman, Thomas R. Ioerger, Christopher M. Sassetti
Publikováno v:
mSphere, Vol 8, Iss 4 (2023)
ABSTRACT Mycobacterium tuberculosis is exposed to a variety of stresses during a chronic infection, as the immune system simultaneously produces bactericidal compounds and starves the pathogen of essential nutrients. The intramembrane protease, Rip1,
Externí odkaz:
https://doaj.org/article/3ff0ef3e4c504a0da4ca3f3ee42264fd
Publikováno v:
mBio, Vol 13, Iss 5 (2022)
ABSTRACT Bacterial pathogens and their hosts engage in intense competition for critical nutrients during infection, including metals such as iron, copper, and zinc. Some metals are limited by the host, and some are deployed by the host as antimicrobi
Externí odkaz:
https://doaj.org/article/95516269ca08459390eb30900637ebd9
Publikováno v:
eLife, Vol 10 (2021)
Bacterial pathogens that infect phagocytic cells must deploy mechanisms that sense and neutralize host microbicidal effectors. For Mycobacterium tuberculosis, the causative agent of tuberculosis, these mechanisms allow the bacterium to rapidly adapt
Externí odkaz:
https://doaj.org/article/1a5a03298a9343d98fb0356fb5bd5737
Publikováno v:
eLife
Bacterial pathogens that infect phagocytic cells must deploy mechanisms that sense and neutralize host microbicidal effectors. For Mycobacterium tuberculosis, the causative agent of tuberculosis, these mechanisms allow the bacterium to rapidly adapt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d80e0e669cd5cb6eec9f15c9825599c4
https://pubmed.ncbi.nlm.nih.gov/34003742
https://pubmed.ncbi.nlm.nih.gov/34003742
Autor:
John A Buglino, Marilyn D Resh
Publikováno v:
PLoS ONE, Vol 5, Iss 6, p e11195 (2010)
Sonic hedgehog (Shh) is a palmitoylated protein that plays key roles in mammalian development and human cancers. Palmitoylation of Shh is required for effective long and short range Shh-mediated signaling. Attachment of palmitate to Shh is catalyzed
Externí odkaz:
https://doaj.org/article/10284af35d7a4a02a25e9eb605a82465
Autor:
Ryan Kniewel, Lorenzo I. Finci, Christopher D. Lima, Veronica Solorzano, John A. Buglino, Debra Dunaway-Mariano, Jin Wu, Zhihao Zhuang, Feng Song
Publikováno v:
Journal of Biological Chemistry. 281:11028-11038
The structure and biochemical function of the hot dog-fold thioesterase PaaI operative in the aerobic phenylacetate degradation pathway are examined. PaaI showed modest activity with phenylacetyl-coenzyme A, suggestive of a role in coenzyme A release
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5fb6f8634823dcc0ef50e71c08f2ed3
https://doi.org/10.1074/jbc.m513896200
https://doi.org/10.1074/jbc.m513896200
Autor:
Grant I. Miura, Jessica E. Treisman, Diego Alvarado, Marilyn D. Resh, Mark A. Lemmon, John A. Buglino
Publikováno v:
Developmental Cell. 10(2):167-176
SummaryLipid modifications such as palmitoylation or myristoylation target intracellular proteins to cell membranes. Secreted ligands of the Hedgehog and Wnt families are also palmitoylated; this modification, which requires the related transmembrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07514f1f461b8df9b540f90529074e99
Autor:
Christopher D. Lima, Julian A. Ferreras, Kenolisa C. Onwueme, Luis E. N. Quadri, John A. Buglino
Publikováno v:
Proceedings of the National Academy of Sciences. 101:4608-4613
Mycobacterium tuberculosis ( Mt ) produces complex virulence-enhancing lipids with scaffolds consisting of phthiocerol and phthiodiolone dimycocerosate esters (PDIMs). Sequence analysis suggested that PapA5, a so-called polyketide-associated protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40edba0e65b5b12f31f34ebca336a653
https://doi.org/10.1073/pnas.0306928101
https://doi.org/10.1073/pnas.0306928101
Autor:
F. Temple Burling, Ryan Kniewel, Christopher D. Lima, Tanya Chadha, Andrew Beckwith, John A. Buglino
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:73-76
The 2.0 A crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to ribose-1-phosphate and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae738ffddede5a4b7b684de99755784c
https://doi.org/10.1107/s0907444902018929
https://doi.org/10.1107/s0907444902018929